UniProt ID
stringlengths 6
10
| Protein Sequence
stringlengths 2
35.2k
| Functional Description
stringlengths 5
30.7k
|
|---|---|---|
Q7N545 | MSTLITLKNVAVNFGDRRVLNNISLHLQRGNILTLLGPNGAGKSTLVRVVLGLIEPSSGTIEQTDGLKIGYVPQKLHLDPTLPLTVKRFMMLKPGVKSGDILPALERVNAAHLLQQPMQKLSGGESQRVLLARALLNQPQLLVLDEPTQGVDVNGQLALYDLINQIRTELHCAVLMVSHDLHLVMAKTDEVLCLNQHICCSGTPEVVSTHPEFIAMFGHHGAEQLAIYRHQHDHHQHNHHHDLKGKIILENNRECHS | Part of the ABC transporter complex ZnuABC involved in zinc import. Responsible for energy coupling to the transport system. ATP(in) + H2O(in) + Zn(2+)(out) = ADP(in) + H(+)(in) + phosphate(in) + Zn(2+)(in) The complex is composed of two ATP-binding proteins (ZnuC), two transmembrane proteins (ZnuB) and a solute-binding protein (ZnuA). Belongs to the ABC transporter superfamily. Zinc importer (TC 3.A.1.15.5) family. |
Q6LTB1 | MTTLVELQSVTVTFGDRHVLDQVSMKLERGQITTLIGPNGAGKSTLVKVITGLRKPSTGHVVRQKGIRIGYVPQKLQLNSTLPLTVDRFMRLAGRYDENARKEALSLVGGTHLHHSDMHSLSGGEMQRVLLARALLQKPDVLVLDEPVQGVDVNGQLELYNLIQSLRDILNCSILMVSHDLHLVMAKTDNVICLHHHICCSGEPDTITNHPSYVALFGQQQSEQLALYHHHHNHEHDLAGSPVGPCQHNKQHGHDNA | Part of the ABC transporter complex ZnuABC involved in zinc import. Responsible for energy coupling to the transport system. ATP(in) + H2O(in) + Zn(2+)(out) = ADP(in) + H(+)(in) + phosphate(in) + Zn(2+)(in) The complex is composed of two ATP-binding proteins (ZnuC), two transmembrane proteins (ZnuB) and a solute-binding protein (ZnuA). Belongs to the ABC transporter superfamily. Zinc importer (TC 3.A.1.15.5) family. |
Q48PV0 | MTDALIRLEQVAVTLSGQSVLDNIQLSVKPGEIVTLIGPNGAGKTTLVRAVLGLLKPDSGTVWRKPKLRVGYMPQKLHVDQTLPLSVLRFLRLVPGVDRMAAESALEEVGAEKVIDSPIQGISGGEMQRVLLARALLRKPELLVLDEPVQGVDVAGQAELYGLITRLRDRHQCGVLMVSHDLHLVMSTTDQVVCLNRHVCCSGHPEHVSHDPAFVELFGKNAQSLAIYHHHHDHAHDLHGAVVNDAPATSSHTHTHVHGDHCKHG | Part of the ABC transporter complex ZnuABC involved in zinc import. Responsible for energy coupling to the transport system. ATP(in) + H2O(in) + Zn(2+)(out) = ADP(in) + H(+)(in) + phosphate(in) + Zn(2+)(in) The complex is composed of two ATP-binding proteins (ZnuC), two transmembrane proteins (ZnuB) and a solute-binding protein (ZnuA). Belongs to the ABC transporter superfamily. Zinc importer (TC 3.A.1.15.5) family. |
Q02DK9 | MDNALVRLTQVGVSFNGQAVLSDVDLAIEPGQIVTLIGPNGAGKTTLVRSVLGLLKPHVGEVWRRPRLTIGYMPQKLHVDATLPLSVLRFLRLVPGVKREQALAALREVGAAHVLERPLQSISGGELQRVLLARALLRKPELLVLDEPVQGVDVAGQAELYRLIGKLRDRYGCGVLMVSHDLHLVMSATDQVVCLNRHVCCSGHPEQVSGDPAFVELFGQDARSLAIYHHHHDHAHDLHGEVVKAGPGALPPGTRFTPVHKHGPDCNHG | Part of the ABC transporter complex ZnuABC involved in zinc import. Responsible for energy coupling to the transport system. ATP(in) + H2O(in) + Zn(2+)(out) = ADP(in) + H(+)(in) + phosphate(in) + Zn(2+)(in) The complex is composed of two ATP-binding proteins (ZnuC), two transmembrane proteins (ZnuB) and a solute-binding protein (ZnuA). Belongs to the ABC transporter superfamily. Zinc importer (TC 3.A.1.15.5) family. |
Q9HT73 | MDNALVRLTQVGVSFNGQAVLSDVDLAIEPGQIVTLIGPNGAGKTTLVRSVLGLLKPHVGEVWRRPRLTIGYMPQKLHVDATLPLSVLRFLRLVPGVKREQALAALREVGAAHVLERPLQSISGGELQRVLLARALLRKPELLVLDEPVQGVDVAGQAELYRLIGKLRDRYGCGVLMVSHDLHLVMSATDQVVCLNRHVCCSGHPEQVSGDPAFVELFGQDARSLAIYHHHHDHAHDLHGEVVKAGPGALPPGTRFTPVHKHGPDCNHG | Part of the ABC transporter complex ZnuABC involved in zinc import. Responsible for energy coupling to the transport system. ATP(in) + H2O(in) + Zn(2+)(out) = ADP(in) + H(+)(in) + phosphate(in) + Zn(2+)(in) The complex is composed of two ATP-binding proteins (ZnuC), two transmembrane proteins (ZnuB) and a solute-binding protein (ZnuA). Belongs to the ABC transporter superfamily. Zinc importer (TC 3.A.1.15.5) family. |
Q1IGY7 | MSDALIRLEQVGVSFAGEAVLDSIDLAVAPGQIVTLIGPNGAGKTTLVRAVLGLLKPHRGKVWRKPKLRIGYMPQKIQVDATLPLSVLRFLRLVPGVDRAAALSALQEVGAEQVIDSPIQTISGGEMQRVLLARALLREPELLVLDEPVQGVDVVGQTELYNLITRLRDRHGCGVLMVSHDLHLVMSATDQVVCLNRHVCCSGHPEQVSNDPAFVELFGQNAKSLAVYHHHHDHSHDLHGSVIAPGAHVHGEHCKHG | Part of the ABC transporter complex ZnuABC involved in zinc import. Responsible for energy coupling to the transport system. ATP(in) + H2O(in) + Zn(2+)(out) = ADP(in) + H(+)(in) + phosphate(in) + Zn(2+)(in) The complex is composed of two ATP-binding proteins (ZnuC), two transmembrane proteins (ZnuB) and a solute-binding protein (ZnuA). Belongs to the ABC transporter superfamily. Zinc importer (TC 3.A.1.15.5) family. |
Q4KKK4 | MSNALIRLEQVGVTFAGQNVLENIQLSVEPGQIVTLIGPNGAGKTTLVRAVLGLLKPDTGSVWRKPKLRVGYMPQKLHVDPTLPLSVLRFLRLVPGVDRTRALAALKEVGAEQVIDSPVQSISGGEMQRVLLARALLREPELLVLDEPVQGVDVAGQAELYSLITRLRDRHGCGVLMVSHDLHLVMSTTDQVVCLNRHVCCSGHPEQVSGDPAFVELFGKNAPSLAIYHHHHDHAHDLHGSVVTQPASGHAHVHGENCKHG | Part of the ABC transporter complex ZnuABC involved in zinc import. Responsible for energy coupling to the transport system. ATP(in) + H2O(in) + Zn(2+)(out) = ADP(in) + H(+)(in) + phosphate(in) + Zn(2+)(in) The complex is composed of two ATP-binding proteins (ZnuC), two transmembrane proteins (ZnuB) and a solute-binding protein (ZnuA). Belongs to the ABC transporter superfamily. Zinc importer (TC 3.A.1.15.5) family. |
Q3KKA1 | MSDALIRLEKVAVRFAGQNVLDNIHLSVEPGQIVTLIGPNGAGKTTLVRAVLGLLKPDSGSVWRKPKLRVGYMPQKLHVDPTLPLSVLRFLRLVPGVDRPRALAALKEVGAEHVIDSPVQSVSGGEMQRVLLARALLREPELLVLDEPVQGVDVAGQAELYSLITRLRDRHGCGVLMVSHDLHLVMSTTDQVVCLNRHVCCSGHPEQVSGDPAFVELFGNNAPSLAIYHHHHDHAHDLHGSVVKGPVTGQPHVHGDSCKHG | Part of the ABC transporter complex ZnuABC involved in zinc import. Responsible for energy coupling to the transport system. ATP(in) + H2O(in) + Zn(2+)(out) = ADP(in) + H(+)(in) + phosphate(in) + Zn(2+)(in) The complex is composed of two ATP-binding proteins (ZnuC), two transmembrane proteins (ZnuB) and a solute-binding protein (ZnuA). Belongs to the ABC transporter superfamily. Zinc importer (TC 3.A.1.15.5) family. |
Q88RL1 | MSDALIRLDQVGVTFGGEAVLDSIDLSVAPGQIVTLIGPNGAGKTTLVRAVLGLLKPHRGKVWRKPKLRIGYMPQKIQVDATLPLSVLRFLRLVPGVDRAAALSALQEVGAEQVIDSPIQTISGGEMQRVLLARALLREPQLLVLDEPVQGVDVVGQTELYNLITRLRDRHGCGVLMVSHDLHLVMSATDQVVCLNRHVCCSGHPEQVSGDPAFVELFGKTAPSLAIYHHHHDHSHDLHGSVVAPGTHVHGEHCKHG | Part of the ABC transporter complex ZnuABC involved in zinc import. Responsible for energy coupling to the transport system. ATP(in) + H2O(in) + Zn(2+)(out) = ADP(in) + H(+)(in) + phosphate(in) + Zn(2+)(in) The complex is composed of two ATP-binding proteins (ZnuC), two transmembrane proteins (ZnuB) and a solute-binding protein (ZnuA). Belongs to the ABC transporter superfamily. Zinc importer (TC 3.A.1.15.5) family. |
Q87UN0 | MAEALIRLEQVAVTLSGQSVLDNIQLSVRPGEIVTLIGPNGAGKTTLVRAVLGLLKPDSGTVWRKPKLRVGYMPQKLHVDQTLPLSVLRFLRLVPGVDRVAAQSALEEVGAEKVIDSPLQGISGGEMQRVLLARALLRKPELLVLDEPVQGVDVAGQAELYSLITRLRDRHQCGVLMVSHDLHLVMSTTDQVVCLNRHVCCSGHPEQVSHDPAFVELFGKNAQSLAIYHHHHDHAHDLHGAVVNDAPTASPPHTHVHGDSCKHG | Part of the ABC transporter complex ZnuABC involved in zinc import. Responsible for energy coupling to the transport system. ATP(in) + H2O(in) + Zn(2+)(out) = ADP(in) + H(+)(in) + phosphate(in) + Zn(2+)(in) The complex is composed of two ATP-binding proteins (ZnuC), two transmembrane proteins (ZnuB) and a solute-binding protein (ZnuA). Belongs to the ABC transporter superfamily. Zinc importer (TC 3.A.1.15.5) family. |
Q4ZZS2 | MSDALIRLDKVAVTLSGQNVLDDIQLSVKPGEIVTLIGPNGAGKTTLVRAVLGLLKPDSGTVWRKPKLRVGYMPQKLHVDQTLPLSVLRFLRLVPGVDRTAAASALEEVGAGKVIDSPIQGISGGEMQRVLLARALLRKPELLVLDEPVQGVDVAGQAELYSLITRLRDRHRCGVLMVSHDLHLVMSTTDQVVCLNRHVCCSGHPEQVSHDPAFVELFGKNAQSLAIYHHHHDHAHDLHGAVVNDAAPLSHTHVHGDSCKHG | Part of the ABC transporter complex ZnuABC involved in zinc import. Responsible for energy coupling to the transport system. ATP(in) + H2O(in) + Zn(2+)(out) = ADP(in) + H(+)(in) + phosphate(in) + Zn(2+)(in) The complex is composed of two ATP-binding proteins (ZnuC), two transmembrane proteins (ZnuB) and a solute-binding protein (ZnuA). Belongs to the ABC transporter superfamily. Zinc importer (TC 3.A.1.15.5) family. |
Q4FQ27 | MNNTSKLLNLSNVSYYIGQQRLLSHINIDIAVNETISVIGPNGAGKSTLVKLILGLIEPTSGQVTPSAPLQIGYVPQRFSVPPILPLRVSDLLAQAHKKRLMAEQRQFIFDKLSLTHLLSRQMLHLSGGETQRVLLARALLDKPNLLILDEPMQGLDPETEVWLYQFIDELPEFLRCAMLVVSHDLHWVMKGSRRVICLNKHICCEGQPSELAISSEFQKLFGHHYEQPYVHQPHACEHHAPS | Part of the ABC transporter complex ZnuABC involved in zinc import. Responsible for energy coupling to the transport system. ATP(in) + H2O(in) + Zn(2+)(out) = ADP(in) + H(+)(in) + phosphate(in) + Zn(2+)(in) The complex is composed of two ATP-binding proteins (ZnuC), two transmembrane proteins (ZnuB) and a solute-binding protein (ZnuA). Belongs to the ABC transporter superfamily. Zinc importer (TC 3.A.1.15.5) family. |
Q1Q889 | MNNTSKLLNLSNVSYYIGQQRLLSNINIDIAVNETVSVIGPNGAGKSTLVKLILGLIVPTSGQVTPSEPLQIGYVPQRFSVPPILPLRVSDLLAQACKKRLTAEQRQFIFDKLSLTHLLSRQMLHLSGGETQRVLLARALLDKPNLLILDEPMQGLDPETEVWLYQFIDELPEFLRCAMLVVSHDLHWVMKGSRRVICLNKHICCEGQPSELAISSEFQKLFGHHYEQPYVHQPHACEHHAPS | Part of the ABC transporter complex ZnuABC involved in zinc import. Responsible for energy coupling to the transport system. ATP(in) + H2O(in) + Zn(2+)(out) = ADP(in) + H(+)(in) + phosphate(in) + Zn(2+)(in) The complex is composed of two ATP-binding proteins (ZnuC), two transmembrane proteins (ZnuB) and a solute-binding protein (ZnuA). Belongs to the ABC transporter superfamily. Zinc importer (TC 3.A.1.15.5) family. |
Q2K6Q4 | MLSPANAKNQRLVSLEDVGVLRGGRWLVRGVEFSVSRGEIVTLIGPNGSGKSTSAKAAIGVLKPDEGRVERLSGLKVGYVPQKLSIDWTLPLTVRRLMTLTGPLPERDMQAALEAAGIAHMIGAEVQHLSGGEFQRALMARAIARKPDLLVLDEPVQGVDFSGEIALYHLIKSIRNASGCGILLISHDLHVVMAETDTVICLNGHVCCRGTPEAVSRSPEYVRLFGSRAAQTLAVYSHHHDHTHLPDGRVLHADGSVTDHCHPEDGHHAHDSQEHAHGQDHVHAHEHSHDDHHGHDHAHEHAHSRSGEGRHA | Part of the ABC transporter complex ZnuABC involved in zinc import. Responsible for energy coupling to the transport system. ATP(in) + H2O(in) + Zn(2+)(out) = ADP(in) + H(+)(in) + phosphate(in) + Zn(2+)(in) The complex is composed of two ATP-binding proteins (ZnuC), two transmembrane proteins (ZnuB) and a solute-binding protein (ZnuA). Belongs to the ABC transporter superfamily. Zinc importer (TC 3.A.1.15.5) family. |
Q1MEG2 | MLSPAKTPAGIRAEPLVSLENVGVLRNGRWLVRGVDFSVSRGEIVTLIGPNGSGKSTSAKAAIGVLKPDEGRVERKAGLKVGYVPQKLSIDWTLPLSVRRLMTLTGPLPERDMLSALESAGIAHMLDAEVQHLSGGEFQRALMARAIARKPDLLVLDEPVQGVDFSGEIVLYDLIKSIRNATGCGILLISHDLHVVMAETDTVICLNGHVCCRGTPESVSRSPEYVRLFGSRAAQTLAVYSHHHDHTHLPDGRVQHADGTVTDHCHPDDGHHAHEHGHAGHEHDHDHPDHAHPHAHEAGERHA | Part of the ABC transporter complex ZnuABC involved in zinc import. Responsible for energy coupling to the transport system. ATP(in) + H2O(in) + Zn(2+)(out) = ADP(in) + H(+)(in) + phosphate(in) + Zn(2+)(in) The complex is composed of two ATP-binding proteins (ZnuC), two transmembrane proteins (ZnuB) and a solute-binding protein (ZnuA). Belongs to the ABC transporter superfamily. Zinc importer (TC 3.A.1.15.5) family. |
Q92P76 | MLNFRSPETMPLVSLANAGVRRNGRWLVRGVDFSISRGEIVTLIGPNGSGKSTTAKTAIGVLKPDEGHVERLAGLKVGYVPQKLAVDWTLPLTVERLMTLTGPLKGREIEESLAATGMLHMAKAEVQHLSGGEFQRALLARAIARKPDLLVLDEPVQGVDFSGEIALYELIKQIRNRTGCGILLISHDLHIVMAETDTVVCLNGHVCCRGTPQVVSQSPEYLKLFGRRAAGALAVYSHHHDHTHLPDGRVLHADGSITESCFPGDGHHHHEEADNIHDHDPDCGCGHHARLQGYDGTEKRDA | Part of the ABC transporter complex ZnuABC involved in zinc import. Responsible for energy coupling to the transport system. ATP(in) + H2O(in) + Zn(2+)(out) = ADP(in) + H(+)(in) + phosphate(in) + Zn(2+)(in) The complex is composed of two ATP-binding proteins (ZnuC), two transmembrane proteins (ZnuB) and a solute-binding protein (ZnuA). Belongs to the ABC transporter superfamily. Zinc importer (TC 3.A.1.15.5) family. |
Q1RGL1 | MKKPIIEFHNVSKKFGNKLPINNVSFTVKKNNITTLIGPNGAGKTTIVRLMLGLEKPTSGEIIIDPRLKIGYVPQKFNLSSDLPITVKKFLDLLAPNNLTNDIKEIHSFIDLERLKDQKISTLSGGQFQKIVLASSLLSKPDLIILDEPLQSLDVTSQQEFYQLISLIRKKLDITVFMISHDLFTVIKNSDQVICLNGHICCTGTPNAITPNSDFSNALSSLGFYTHHHDHKH | Part of the ABC transporter complex ZnuABC involved in zinc import. Responsible for energy coupling to the transport system. ATP(in) + H2O(in) + Zn(2+)(out) = ADP(in) + H(+)(in) + phosphate(in) + Zn(2+)(in) The complex is composed of two ATP-binding proteins (ZnuC), two transmembrane proteins (ZnuB) and a solute-binding protein (ZnuA). Belongs to the ABC transporter superfamily. Zinc importer (TC 3.A.1.15.5) family. |
Q92G36 | MQKPIIEFRNVSKKFGNKLPINNVSFTVKKNNITTLIGPNGAGKTTIVRLMLGLEKPTSGEIIIDPKLKIGYVPQKFGLTPDLPITVKNFLELLAPSNFNNNIKEINSFIDLEHIKDQEISKLSGGQFQKVVLACSIVNNPDLIILDEPLQSLDVTSQQEFYQLINLIRKKLNITVFMISHDLFTVIKNSDQVICLNGHICCSGIPNEITPNSEFSNALSALGFYTHHHDHKH | Part of the ABC transporter complex ZnuABC involved in zinc import. Responsible for energy coupling to the transport system. ATP(in) + H2O(in) + Zn(2+)(out) = ADP(in) + H(+)(in) + phosphate(in) + Zn(2+)(in) The complex is composed of two ATP-binding proteins (ZnuC), two transmembrane proteins (ZnuB) and a solute-binding protein (ZnuA). Belongs to the ABC transporter superfamily. Zinc importer (TC 3.A.1.15.5) family. |
Q4UJW5 | MEKPIIEFRNVSKKFGNKLPINNVSFTVKKNNITTLIGPNGAGKTTIVRLMLGLEKPTNGEIIIDPKLKIGYVPQKFGLTPDLPITVKKFLDLLAPSNFNSNIKEINSFIDLEHIKDQEISKLSGGQFQKVVLACSIVNKPDLIILDEPLQSLDVTSQQEFYQLINLIRKKLNITVFMISHDLFTVIKNSDQVICLNGHICCSGVPNEITPNSEFSNALSSLGFYTHHHDHRH | Part of the ABC transporter complex ZnuABC involved in zinc import. Responsible for energy coupling to the transport system. ATP(in) + H2O(in) + Zn(2+)(out) = ADP(in) + H(+)(in) + phosphate(in) + Zn(2+)(in) The complex is composed of two ATP-binding proteins (ZnuC), two transmembrane proteins (ZnuB) and a solute-binding protein (ZnuA). Belongs to the ABC transporter superfamily. Zinc importer (TC 3.A.1.15.5) family. |
Q9ZCC4 | MQKPIIEFRNVSKKFGNKTPISKVSFIVKKNNITTLIGPNGAGKTTIVRLMLGLEKPTSGEVIIDRKLKIGYVPQKFGLTTDIPITVKKFLDLLAPSHFNKNIKEISSFIDLEHIKKQEISKLSGGQFQKVVLACSIINNPDLIILDEPLQSLDVTSQQEFYQLIHFIRKKLNITVFMISHDLFTVIKNSDQVICLNGHICCSGVPHEITPNSEFSNALSSLGFYTHNHDHKH | Part of the ABC transporter complex ZnuABC involved in zinc import. Responsible for energy coupling to the transport system. ATP(in) + H2O(in) + Zn(2+)(out) = ADP(in) + H(+)(in) + phosphate(in) + Zn(2+)(in) The complex is composed of two ATP-binding proteins (ZnuC), two transmembrane proteins (ZnuB) and a solute-binding protein (ZnuA). Belongs to the ABC transporter superfamily. Zinc importer (TC 3.A.1.15.5) family. |
A6ZQY2 | MRSFIKAHKKSTSFDESPKRHSNFSGNTNNSSQRSSDDSLDFLPSTPSQMNYDSIPPPAKHSPGFESFHRLANKTSKLFKKTSNSNLNSHLASTPTTSTNQTTSNSFVLQNPPTKNTGPPPPLPPPLFPSSSTSSFSRHDNESEYTAYKKTSPAKDFNRTTDSLPAIKGTITHSWGDSKVESHVIILNDPASPASNTSEATSSKQFKTPIIGNENLTSTTSPSNLEPAIRILNKNKGKQQENIDDAEDGSSKKEHHVYKALALAKNRNRQARIHSHDDIINLGKASQMDMSLLAAAFSGNSTTTINNDQSSNEQTDEKILDIERVTTTSTLTSSETTSPINKSPCFYSQTLSLSPKIRHGDLQSSPSKVNKNDSQNETLNKKKVRISLNRKEEEKVYSLNNNSDEYSVNEKETHKANDCNDESSENGDGDNDHDDDYDDDDDDDDDDDESEFSFEYAGINVRTSSVKYYSKPEPAANVYIDDLYEDENFDDDMNCIEDDESGNEGNEICGLSTRFEETSLKSNKVKKFNDLFNLSDDDEEEDGKDNSNNGDENESDNLYQKRLENGKETFNGNHGGHHDDASLGETVDNKEQFLINDNVKKPIQKYNDLFDLSDEDDNDDKEMSEAESYMFSDEAPSIESGPANAKSTRGIYSQSNKNIIRDGKPNYSFSLKRNNSDDETEHTSAIKASLTGTTGSTKPTVKSFSDIFNVDDSASDAESDSGTGGNNSNGLVSNDSERQVSLQSSLYETKSESHPPNHPHSQILQTPAKIVITPSVSDAQSQALAITDDDGEDDDDDTSSILRTPFQLIDSSHSQQPHYASPQYTAVLNSPPLPPPARSQSLKYHDLNCDLDSEVPRPMSNLFFIDEAEEDEYNQKSKFFDFDHYDIDEINGIPEDFNFSDSERDDLNRRTLKSPLRGGSKNREVSPFSSVSSSFRSTHSFNGKLTINQGAKELAPMKNKIELTNKTVTFFNSNNWNTYDCNSLSRKTSSQMRDSKYQNHNVGQNVEPSSVRSPQHQISNGLDGKCNDNYVISPNLPTTITPTNSFTKPTPEFSNDYSLSPIQETPSSVQSSPKRA | Involved in the integrity functions of RAM, a conserved signaling network that regulates maintenance of polarized growth and daughter-cell-specific transcription. Interacts with BUD27, GIS1 and SSD1. Localized to the cortex of small and large buds during bud growth, to the bud neck during mitotic exit and to the tips of mating projections in pheromone-treated cells. Repressed by zinc. Belongs to the ZRG8 family. |
D3DLT2 | MRSFIKAHKKSTSFDESPKRHSNFSGNTNNSSQRSSDDSLDFLPSTPSQMNYDSIPPPAKHSPGFESFHRLANKTSKLFKKTSNSNLNSHLASTPTTSTNQTTSNSFVLQNPPTKNTGPPPPLPPPLFPSSSTSSFSRHDNESEYTAYKKTSPAKDFNRTTDSLPAIKGTITHSWGDSKVESHVIILNDPASPASNTSEATSSKQFKTPIIGNENLTSTTSPSNLEPAIRILNKNKGKQQENIDDAEDGSSKKEHHVYKALALAKNRNRQARIHSHDDIINLGKASQMDMSLLAAAFSGNSTTTINNDQSSNEQTDEKILDIERVTTTSTLTSSETTSPINKSPCFYSQTLSLSPKIRHGDLQSSPSKVNKNDSQNETLNKKKVRISLNRKEEEKVYSLNNNSDEYSVNEKETHKANDCNDESSENGDGDNDHDDDYDDDDDDDDDDDESEFSFEYAGINVRTSSVKYYSKPEPAANVYIDDLYEDENFDDDMNCIEDDESGNEGNEICGLSTRFEETSLKSNKVKKFNDLFNLSDDDEEEDGKDNSNNGDENESDNLYQKRLENGKETFNGNHGGHHDDASLGETVDNKEQFLINDNVKKPIQKYNDLFDLSDEDDNDDKEMSEAESYMFSDEAPSIESGPANAKSTRGIYSQSNKNIIRDGKPNYSFSLKRNNSDDETEHTSAIKASLTGTTGSTKPTVKSFSDIFNVDDSASDAESDSGTGGNNSNGLVSNDSERQVSLQSSLYETKSESHPPNHPHSQILQTPAKIVITPSVSDAQSQALAITDDDGEDDDDDTSSILRTPFQLIDSSHSQQPHYASPQYTAVLNSPPLPPPARSQSLKYHDLNCDLDSEVPRPMSNLFFIDEAEEDEYNQKSKFFDFDHYDIDEINGIPEDFNFSDSERDDLNRRTLKSPLRGGSKNREVSPFSSVSSSFRSTHSFNGKLTINQGAKELAPMKNKIELTNKTVTFFNSNNWNTYDCNSLSRKTSSQMRDSKYQNHNVGQNVEPSSVLSPQHQISNGLDGKCNDNYVISPNLPTTITPTNSFTKPTPEFSNDYSLSPIQETPSSVQSSPKRA | Involved in the integrity functions of RAM, a conserved signaling network that regulates maintenance of polarized growth and daughter-cell-specific transcription. Interacts with BUD27, GIS1 and SSD1. Localized to the cortex of small and large buds during bud growth, to the bud neck during mitotic exit and to the tips of mating projections in pheromone-treated cells. Repressed by zinc. Belongs to the ZRG8 family. |
Q8GWC4 | MGWWRKKKKPKSEIASERGAKLLKDLIECCDGKSNPIKFFSADEIRKATNNFGVSNLVSELSHDFDYKWYSGKNENHDMILVRKAFSQSVYYKDTFFRDIAVSSMVSGHKNFLKLIGYCLEFEEPVMVYHGVKKHYHLESSEQPWKRRMKIAEDIATALAYLHTAFPRPFVYRCLSLTNILLDEDGVAKLMDFSFCVSIPEGETFVQVDYIAGTVDYLKPNYLKHGVVSEETDVFAVGHSMQMLLMGEKIFDRIMRRPFPTSKFMEEPKMDEIADPEMGEISEEELCQMKAFLLLSLRCTGHVGEVPTMVEVAKELKSIQRCLHNDTFSPSVETQFDSHQDISSSVILSNQTKDTRALLRCIACHVFDEMFQWVMMNWFRFFRRNRRIC | Together with RPP13L4/ZAR1, involved in the regulation of the ambient temperature-sensitive intersection of growth and immune response in the absence of pathogens. Induced by elevated temperature (e.g. at 25 degrees Celsius). The protein kinase domain is predicted to be catalytically inactive. Slightly shortened inflorescence stem when grown at 25 degrees Celsius (PubMed:28499073). The double mutant zed1-6 zrk12-1 exhibits short inflorescence stem and autoimmunity symptoms when grown at 25 degrees Celsius (PubMed:28499073). Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. |
Q9SVX8 | MEWWKKKSLRAIIKRERLVRGHERGGTLLEEIIKSCNGKANPIKIFSADQILEATDTFSESNRVSELFDEIPYDWYYSGKNNNHHHHHKLLLIKKWRYRFSEHNGGNFCRDIAISSIVSGHKNFMQLVGCCLESEHPVLVYRASKKPTSLDLKMVVSWRQRLKIAEEIATALAYLHTAFPRPFVYRILRLEDILLDDEDGVAKLCNFSYCVSIPQGETFVKLGNGCIGGDYDYMDDNYLINGIVSEKTDAFGFGIFMQKLLMGEERFHELCYDRSDLTTFENRRKFAKCIDEIVDSNMLEKIGDVTEEERCRMEAFIVLSERCIGLRGEVPKMVEVAKELKRFLRDSSSSCGETSL | Interacts with RPP13L4/ZAR1. The protein kinase domain is predicted to be catalytically inactive. Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. ZRK subfamily. |
U5LR94 | MKKQYLKSGSGTRKEKDKAKRWFLDNGSIFLRELVADCNGKSIPIRSFSPEQILKATNNFDSSCFVSQDVYYKWYRGEIEDRSYMIKRFSEDEITGKRHRVKEVYNDIVLSARMSNHSNFLQLLGCCLEFPFPVLVFEFAEHGAMNQRGGVIVNGEESLLPWSVRLKIGKEIANAVTYLHTAFPKIIIHRDVKPMHVFLDKNWTAKLSDLSFSISLPEGKSRIEAEWVLGTFGYIDPLYHKTCFVTEYTDVYSFGICLLVIITGKPAIMTISDGDLQGILSLVRELCENGKLDEVIDPRLMKDITSGQRLQVEACVVLALRCCKERDEDRPKMIQVAKELKQIEASLKNSS | Serine/threonine-protein kinase that confers a broad-spectrum quantitative disease resistance (QDR) to the pathogenic biotrophic bacteria Xanthomonas campestris (e.g. pv. campestris (Xcc), pv. raphani, pv. armoriaceae and pv. incanae) by restricting bacterial spread to the vascular system from the infection site; X.campestris causes black rot disease in crops (PubMed:24068949, PubMed:26355215, PubMed:30948526). Seems to not have any kinase activity (PubMed:24068949). ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein] ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein] Component of a stable high-order oligomeric complex made of RKS1 and RPP13L4/ZAR1 which recruits Xanthomonas campestris effector XopAC/AvrAC-mediated uridylylated PBL2 in the presence of ATP to form a wheel-like pentameric resistosome; this complex triggers immunity toward X.campestris in vascular tissues (PubMed:26355215, PubMed:30948527, PubMed:30948526). Interacts with RPP13L4/ZAR1 and uridylylated PBL2 (PubMed:26355215, PubMed:30948526). Expressed at high levels in germinating seeds and at lower levels in adult leaves. Induced by elevated temperature (e.g. at 25 degrees Celsius). Increased sensitivity to the pathogenic biotrophic bacteria Xanthomonas campestris pv. campestris (Xcc). Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. ZRK subfamily. |
A1A6H5 | MKSMVKKLKQSLRSGSLEKRKEKEKDIQEEKWFLDNGSIFLKELIADCNGKSIPIRNFSSDQILKATSNFGSSCFVTAEGFYVWYKGIIEDRSYMIKRFSEYKVTQYRVAEVYNEIVLSARMSNHNNFLKLIGFCLEFSLPVLVFEYAEHGVLNHRGGVIVNGEEVILPLSLRLKIGKEIANAVTYLHMAFPKILIHRHIKPRNVFLDENWTPKLSDFSISINLPEGKSRIEVECVQGTIGYLDPVYYTTKMVTEYTDVYSFGVFLMVILTGKPALASTSSDGDYKHIASYVKGFHENGQLDGVIDPKVMEDITSAQKVHVEACVVLALRCCELRDENRPKMIQIAKELKQIETLFRRS | The protein kinase domain is predicted to be catalytically inactive. Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. ZRK subfamily. Truncated N-terminus. Truncated N-terminus. Truncated N-terminus. Truncated N-terminus. Truncated N-terminus. Truncated N-terminus. Truncated N-terminus. Truncated N-terminus. Truncated N-terminus. Truncated N-terminus. Truncated N-terminus. Truncated N-terminus. Truncated N-terminus. Truncated N-terminus. Truncated N-terminus. Truncated N-terminus. Truncated N-terminus. Truncated N-terminus. Truncated N-terminus. Truncated N-terminus. Truncated N-terminus. Truncated N-terminus. Truncated N-terminus. Truncated N-terminus. Truncated N-terminus. Truncated N-terminus. Truncated N-terminus. Truncated N-terminus. Truncated N-terminus. Truncated N-terminus. Truncated N-terminus. Truncated N-terminus. Truncated N-terminus. Truncated N-terminus. Truncated N-terminus. Truncated N-terminus. Truncated N-terminus. Truncated N-terminus. Truncated N-terminus. Truncated N-terminus. Truncated N-terminus. Truncated N-terminus. Truncated N-terminus. |
Q9SVY7 | MESMVKKLKQNLRTGSWKKKEKSMKKERWFLENGSIFLKELIVDCNGKSIPIRSFTSSQIRKATKNFDLSCFVAEEGFYIWYKGVIEDRSYMIKRFSEYKVTDYRVSEVYKDIVLSARMSNHNNFLKLLGCCLEFPFPVLVFEFAEHGVLNYRGGITVNGEESLLPLSLRLKIGKEIANALAYLHMAFPKIIIYRDVKPLHVFLDNNWTAKLSDLSFSISLEEGKSQIEAEDVLGTYGYLDPLYFATRIVTEYTDVYSFGVFLMVVITGISVYFTGSDGYPVGILGYMKGLAENGKLNEIVYPMIMKEMTSAQRLQVEACVLLALRCCEERVEDRPKMIQVAKELKRIEHHVLRS | Required for RPP13L4/ZAR1 recognition of the Pseudomonas syringae type III effector (T3E) HopF2a. ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein] ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein] Interacts with RPP13L4/ZAR1. Reduced resistance to Pseudomonas syringae expressing HopZ1a. Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. ZRK subfamily. Truncated N-terminus. |
Q9SVY8 | MNDQKMSCWRKKSKKKNSEANQRQRWFQENGKVLLEDLIELCNGKSNPIKTFSAEEILQATDNFSESNLVIRFNFMYRGILQNRPVLIKRATWNYYKSDTLEKICRDIAVSSMVSGHKNFLKLLGCCLEFEHPVLVCEYAERIPFNTPNPEMLLPWRMRIKIAKEIAIAVSYLHTALSRTMIHTDIQPFNIFVDSNGTAKLSDFCLCIAIPEGETFVKVHADRVEGTLDYLEYNYAATGLITEYTDVFSFGVLLQNFFTRTYGVVDCCCSEDESLFEEFEDKQNVMNLRISDRISKFVEEGRIFDMLDPKMLESMGDDETEEHKIRRMKAVLMLSLRCTGHRGDVPKMMEVAKELKRIERWT | ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein] ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein] Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. ZRK subfamily. |
B9DHG2 | MDWLRTKRIRAKKRKRNVKENGEVVLKELIECCDGKCNPIKNFSYDQIIKATNNFCQSNRASRIDVYYRCYKGMLDDRPVLIKKGKYTLDMKEICRDIAISSMVSGHKNFLKLLGCCLEFTPPVLVFEYAEVITLGPLLTSHPGYLRRIKIAREVANALTYLHTAFSRVFIHSNLDPFTIFLDGNGVAKLGNFCNCITIPEGETFVHDDTLQKYHELRHNTLKGTHGLGVCNLPVIDPDYKSTGKVTTKTDMHSFGGFMLALVQIREVDDELSLSSDMLRALADLFIKPYDDVRYVHFPLHHHVSKILRKFGYAEVVDSDMSEVAAWPIKAFLRLALRCIGCKLGDPLSSMIQVTKELRLIEKSAYYPSNNRSQMSSI | Interacts with RPP13L4/ZAR1. Induced by elevated temperature (e.g. at 25 degrees Celsius). The protein kinase domain is predicted to be catalytically inactive. Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. ZRK subfamily. |
Q9SVZ1 | MAHISDIKLIRTDTTLDLSQKAEKGMIWTMGGASYLYYNAYDHGSLTCRCGTLLIASSGGKYNPIRTFSSHQILEATNNFDWSYAIGVDRFVWYKGTIENRAVLIKYYKGEPFNFDPDNFYRDIAVSSMMSSHKNVLKLLGCCLEFPRPVLVCEYPEKGALAYIGGAGEVIKPLAWSVRLKIAKEIADAVTYLHTEFPRTIIHRDLKLTNIFLDENWTAKLSSFSLSIPIPEGELGVEDIVCGTQGFGEPHYMENMDSIKNRLMVTVIT | ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein] ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein] Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. ZRK subfamily. |
Q5U595 | MTEHGIKWGCEYCTYENWPSAIKCTMCRAPRPSGAIITEEPFKNSTPDVGSMERDIGSPLICPDSSARPRVKSSYSMEPSSKWSCQICTYLNWPRAIRCTQCLSQRRTRSPTESPQSSGSGLRSIPSPIDPCEEYNDRNKLNIKGQHWTCSACTYENCAKAKKCVVCDHPTPNNMDAIELANTDEASSIINEQDRARWRGGCSSSNSQRRSPPTSKRDSDMDFQRIELAGAVGSKEEFELDLKKLKQIKNRMRKTDWLFLNACVGIVEGDLSAVESYKTSGGDIARQLSADEVRLLNRPSAFDVGYTLVHLSIRFQRQDMLAILLTEVSQHAAKCIPAMVCPELTEQIRREIAASVHQRKGDFACYFLTDLVTFTLPADIEDLPPTVQEKLFDEVLDRDVQKELEEESPIINWSLELGTRLDSRLYALWNRTAGDCLLDSVLQATWGIYDKDSVLRKALHDSLHDCSHWFYSRWKEWESWYSQSFGLHFSLREEQWQEDWAFILSLASQPGASLEQTHIFVLAHILRRPIIVYGVKYYKSFRGETLGYTRFQGVYLPLLWEQSFCWKSPIALGYTRGHFSALVAMENDGFDNRGAGANLNTDDDITVTFLPLVDSERKLLHIHFLSAQELGNEDQQEKLLREWMDCCVTEGGVLVAMQKSSRRRNHPLVTQMVEKWLDGYRQIRPCTALSDGEEDEDDEDE | Ubiquitin thioesterase, which specifically hydrolyzes 'Lys-29'-linked and 'Lys-33'-linked diubiquitin (By similarity). Also cleaves 'Lys-63'-linked chains, but with 40-fold less efficiency compared to 'Lys-29'-linked ones (By similarity). Positive regulator of the Wnt signaling pathway that deubiquitinates apc protein, a negative regulator of Wnt-mediated transcription (By similarity). Acts as a regulator of autophagy by mediating deubiquitination of pik3c3/vps34, thereby promoting autophagosome maturation (By similarity). Plays a role in the regulation of cell morphology and cytoskeletal organization (By similarity). Required in the stress fiber dynamics and cell migration (By similarity). Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal). Enriched in punctate localization in the cytoplasm. The RanBP2-type zinc fingers, also called NZFs, mediate the interaction with ubiquitin and determine linkage specificity. RanBP2-type zinc fingers 1 and 2 (also named NZF1 and NZF2) specifically recognize and bind 'Lys-29'- and 'Lys-33'-linked ubiquitin. RanBP2-type zinc finger 3 (also named NZF3) binds 'Lys-33'-linked ubiquitin and shows weak binding to 'Lys-6'-, 'Lys-48'- and 'Lys-63'-linked ubiquitin chains but it does not interact with 'Lys-29'-linked chains. The OTU domain mediates the deubiquitinating activity. The second ankyrin repeat ANK 2 is termed AnkUBD, it interacts with ubiquitin hydrophobic patch and contributes to linkage specificity. Belongs to the peptidase C64 family. |
A0JMQ9 | MTDLGLKWSCEYCTYENWPSAIKCTMCRAQRHNAPIITEEPFKSSSSLDPSLCTTQGGSTLLICPDSSARPRVRIADELPETSSKWSCHMCTYLNWPRAIRCTQCLSQRQQGSQQHSPLSPSETPQTSGSRPSPVTSDPCEEYNDRNRLNMHAQRWPCSACTYENWPKSLRCVVCDHPKPSGSPETPQQDSEAESATSPSIVNEQERENVRTAGGGGGGSRGRLRKLSPPMCKGQAEVKIELASGAVGSDNEQEADFKKLKQIRNRMRRSDWLFLNACAGVVEGDLAAVEAYKSSGGDIARQLTADEVRILNRPSAFDAGFTLVHLAIRFQRQDMLAVLLTEVSQQTAKCIPALVCPELTEQIRREVAAALHRRKGEFPCYFFTDLVTFTLPADIEDLPPNVQEKLFDEVLDRDVQKELEEESPIINWSLELGTRLDSRLYALWNRTAGDCLLDSVLQATWGIYDKDSVLRKSLNDSLHDCSHWFYTRWKEWESWYSQSFGLHFSLREEQWQEDWAFILSLASQPGASLEQTHVFVLAHILRRPIIVYGVKYYKSFRGETLGYTRFQGVYLPLLWEQSFCWKSPIALGYTRGHFSALVAMENDGYDNRGAGANLNTDDDVTVTFLPLVDSERKLLHIHFLSAQEMGTEEQQERMLRQWMDCCVTEGGVLVAMQKSSRRRNHPLVTQMVEKWLDGYRQLAACPTLSDGEEEEEDEDE | Ubiquitin thioesterase, which specifically hydrolyzes 'Lys-29'-linked and 'Lys-33'-linked diubiquitin (By similarity). Also cleaves 'Lys-63'-linked chains, but with 40-fold less efficiency compared to 'Lys-29'-linked ones (By similarity). Positive regulator of the Wnt signaling pathway that deubiquitinates apc protein, a negative regulator of Wnt-mediated transcription (By similarity). Acts as a regulator of autophagy by mediating deubiquitination of pik3c3/vps34, thereby promoting autophagosome maturation (By similarity). Plays a role in the regulation of cell morphology and cytoskeletal organization (By similarity). Required in the stress fiber dynamics and cell migration (By similarity). Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal). Enriched in punctate localization in the cytoplasm. The RanBP2-type zinc fingers, also called NZFs, mediate the interaction with ubiquitin and determine linkage specificity. RanBP2-type zinc fingers 1 and 2 (also named NZF1 and NZF2) specifically recognize and bind 'Lys-29'- and 'Lys-33'-linked ubiquitin. RanBP2-type zinc finger 3 (also named NZF3) binds 'Lys-33'-linked ubiquitin and shows weak binding to 'Lys-6'-, 'Lys-48'- and 'Lys-63'-linked ubiquitin chains but it does not interact with 'Lys-29'-linked chains. The OTU domain mediates the deubiquitinating activity. The second ankyrin repeat ANK 2 is termed AnkUBD, it interacts with ubiquitin hydrophobic patch and contributes to linkage specificity. Belongs to the peptidase C64 family. |
Q6NUB7 | MTEDGIKWACEYCTFENWPSAIKCTMCRAPRPSGAIITEEPFKNRTPDVGSMEREIGSPLICPDSSARPRVKSSYSMETSSKWSCQICTYLNWPRAIRCTQCLSQRRTRSPTESPQSSGSGLRSIPGPIDPCEEYNDRNKLNIKGQHWTCSACTYENCAKAKKCVVCDHPTPNNMDAIELANTDEASSIINEQDRARWRGGCSSSNSQRRSPPTSKRDSDMDFQRIELAGAVGSKEEFELDLKKLKQIKNRMRKTDWLFLNACVGVVEGDLSAVEAYKTSGGDIARQLSADEVRLLNRPSAFDVGYTLVHLSIRFQRQDMLAILLTEVAQHAAKCIPAMVCPELTEQIRREIAASVHQRKGDFACYFLTDLVTFTLPADIEDLPPTVQEKLFDEVLDRDVQKELEEESPIINWSLELGTRLDSRLYALWNRTAGDCLLDSVLQATWGIYDKDSVLRKALHDSLRDCSHWFYSRWKEWESWYSQSFGLHFSLREEQWQEDWAFILSLASQPGASLEQTHIFVLAHILRRPIIVYGVKYYKSFRGETLGYTRFQGVYLPLLWEQSFCWKSPIALGYTRGHFSALVAMENDGFDNRGAGANLNTDDDVTVTFLPLVDSERKLLHVHFLSAQELGNEDQQEKLLREWMDCCVTEGGVLVAMQKSSRRRNHPLVTQMVEKWLDGYRQIRPCTALSDGEEDEDDEDE | Ubiquitin thioesterase, which specifically hydrolyzes 'Lys-29'-linked and 'Lys-33'-linked diubiquitin (By similarity). Also cleaves 'Lys-63'-linked chains, but with 40-fold less efficiency compared to 'Lys-29'-linked ones (By similarity). Positive regulator of the Wnt signaling pathway that deubiquitinates apc protein, a negative regulator of Wnt-mediated transcription (By similarity). Acts as a regulator of autophagy by mediating deubiquitination of pik3c3/vps34, thereby promoting autophagosome maturation (By similarity). Plays a role in the regulation of cell morphology and cytoskeletal organization (By similarity). Required in the stress fiber dynamics and cell migration (By similarity). Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal). Enriched in punctate localization in the cytoplasm. The RanBP2-type zinc fingers, also called NZFs, mediate the interaction with ubiquitin and determine linkage specificity. RanBP2-type zinc fingers 1 and 2 (also named NZF1 and NZF2) specifically recognize and bind 'Lys-29'- and 'Lys-33'-linked ubiquitin. RanBP2-type zinc finger 3 (also named NZF3) binds 'Lys-33'-linked ubiquitin and shows weak binding to 'Lys-6'-, 'Lys-48'- and 'Lys-63'-linked ubiquitin chains but it does not interact with 'Lys-29'-linked chains. The OTU domain mediates the deubiquitinating activity. The second ankyrin repeat ANK 2 is termed AnkUBD, it interacts with ubiquitin hydrophobic patch and contributes to linkage specificity. Belongs to the peptidase C64 family. |
P47917 | MELSPNNSTDQSLLDAQLELWHTTFAFMKSMALKSAIHLRIADAIHLHGGAASLSQILSKVHLHPSRVSSLRRLMRVLTTTNVFGTQPLGGGSDDDSEPVYTLTPVSRLLIGSQSSQLAQTPLAAMVLDPTIVSPFSELGAWFQHELPDPCIFKHTHGRGIWELTKDDATFDALVNDGLASDSQLIVDVAIKQSAEVFQGISSLVDVGGGIGAAAQAISKAFPHVKCSVLDLAHVVAKAPTHTDVQFIAGDMFESIPPADAVLLKSVLHDWDHDDCVKILKNCKKAIPPREAGGKVIIINMVVGAGPSDMKHKEMQAIFDVYIMFINGMERDEQEWSKIFSEAGYSDYRIIPVLGVRSIIEVYP | May be involved in the O-methylation of suberin phenylpropanoid precursors. Homodimer. Accumulates preferentially in the roots and is located predominantly in the region of the endodermis, low levels are seen in the leaves, stems and other shoot organs. Belongs to the class I-like SAM-binding methyltransferase superfamily. Cation-independent O-methyltransferase family. COMT subfamily. |
Q9JP79 | MIDYRDRHILSLLQANAEMPLSEIAERVALSVSACSRRVARLREEGYIKGTIALLDRKKINLPTTIFLLVKTGLHTGNYLEQFHAAVSAIPEIVEVHRLTGNFDYILKLALPNVEYYDVIYKQILKHVAFYDMSAYISMETVKISPALPTNYI | Extended N-terminus. |
O94639 | MSLNNLSNSYNQYLAQESHQILRHLFLNKQYSPLVKRDDDSSATVTCGGDANEFNEYGHLGYRIGAIFVILATSLIGMNLPLVLSKITKNRPNVYIEYLYLFARYFGSGVILATAFIHLLAPACNKLYDPCLDDLFGGYDWAPGICLISCWFILLLEVLLNRYVEWRFGMEIGDHHGPTLGAKQHSHSHEDGAHGVHEHPVYDIEECADGVEHECVKDDLEEVKLEPYTNTDSTDLTTKEEARSFLLKQQLTAFIILESSIILHSVIIGLTTAVSGEEFKTLFPVIIFHQAFEGCGLGSRLAGMAWGPKTAWVPWVLGVIYSLVTPIGMAAGLGVREHWDPLAHGSYAAQGVLDAISSGILVYAGLVELLAHDFLFSPERERNWYKLIYLLACSMAGTGVMALLGKWA | High-affinity zinc transport protein. Regulates intracellular zinc levels. Belongs to the ZIP transporter (TC 2.A.5) family. |
D6VV80 | MSNVTTPWWKQWDPSEVTLADKTPDDVWKTCVLQGVYFGGNEYNGNLGARISSVFVILFVSTFFTMFPLISTKVKRLRIPLYVYLFAKYFGSGVIVATAFIHLMDPAYGAIGGTTCVGQTGNWGLYSWCPAIMLTSLTFTFLTDLFSSVWVERKYGLSHDHTHDEIKDTVVRNTAAVSSENDNENGTANGSHDTKNGVEYYEDSDATSMDVVQSFQAQFYAFLILEFGVIFHSVMIGLNLGSVGDEFSSLYPVLVFHQSFEGLGIGARLSAIEFPRSKRWWPWALCVAYGLTTPICVAIGLGVRTRYVSGSYTALVISGVLDAISAGILLYTGLVELLARDFIFNPQRTKDLRELSFNVICTLFGAGIMALIGKWA | High-affinity zinc transport protein. Induced in activity >100-fold in response to zinc-limiting growth conditions. Not expressed in zinc-replete cells. Inhibited by Cu(2+) and Fe(3+) ions. Belongs to the ZIP transporter (TC 2.A.5) family. |
D6VYC5 | MVDLIARDDSVDTCQASNGYNGHAGLRILAVFIILISSGLGVYFPILSSRYSFIRLPNWCFFIAKFFGSGVIVATAFVHLLQPAAEALGDECLGGTFAEYPWAFGICLMSLFLLFFTEIITHYFVAKTLGHDHGDHGEVTSIDVDAPSSGFVIRNMDSDPVSFNNEAAYSIHNDKTPYTTRNEEIVATPIKEKEPGSNVTNYDLEPGKTESLANELVPTSSHATNLASVPGKDHYSHENDHQDVSQLATRIEEEDKEQYLNQILAVFILEFGIIFHSVFVGLSLSVAGEEFETLFIVLTFHQMFEGLGLGTRVAETNWPESKKYMPWLMGLAFTLTSPIAVAVGIGVRHSWIPGSRRALIANGVFDSISSGILIYTGLVELMAHEFLYSNQFKGPDGLKKMLSAYLIMCCGAALMALLGKWA | Low-affinity zinc transport protein. Active in zinc-replete cells and is time-, temperature- and concentration-dependent and prefers zinc over other metals as its substrate. Inhibited by Cu(2+) and Fe(3+) ions. Belongs to the ZIP transporter (TC 2.A.5) family. |
D6VX25 | MEKIPRWLLFSLISSVLCILGALCVPLLSVAFDSKRNSQSKLVNYGLSLSAGSMITTSLYMLLPRIEKSNRFKVFPGLLLGICLSFFLNYLVHAFASESLVHCADSGDHATGSHIHSKSHSHSHSHSHADSHSNFSNDHDLENAPSEHGYATSSSSVSENDPLITKDSDRPQMKKKMSLIDLLTRRKSEGECCDLNKCTPLLQSEQPEYIACVPPVIKSSQSERNVPHGCEGSEDNGQSDDKDHRGLVCVENNIGYDLENLSLYRKNFLSSRHHHSSESPENYGSNQLSHSFSSPLGNDVTENPAALADTQYHPENGSLYPHHHHLETPFSKLLSIGMQTCLVLALHKFPEGFIIFYTNRSDSSKSLGFSIFLSLTIHNFVEGFAMTLPFYTVFESKWVAILITAVLGGGSQPLGALIGYFIFKGSTPRDHEPNMDFLLSVTAGFLLVIGLQMFQTGIGFSDGHHHHQGEGDEEMKQSHSSGTTCLKWCCTGVLLILASALFT | Transports zinc from storage in the vacuole to the cytoplasm. Belongs to the ZIP transporter (TC 2.A.5) family. |
Q6IRM9 | MWAERHRAAVELQQFLSSVYEQVKKEESLGPFQFKDDIQVHVVCDGHCKPLESFCSGSEVLYILEKKPLTLEDNVLDETENNEGISFYTSLQEIPQPQAIPTMRARQFLTSYTLTHNPNMVQLNSGAPVKVLPPLWVRCDCSDAEGTCWLGAEPIKSSRNEITGMSFRTVTCAGPTADKSTFPSLDSLRQAHKERHYSSVMQTRGFAQYDLFGCNTVENSVIESQSSVTVDFVWNGVERILQLPPLASAATLNIKVESGDLRSPVYSVYKELDFLLVLAEGLKTGVTEWPETGETKSAVDLVQLLLNDLKNKVDGLTSSVSKKDNEKIKSDTAAVDCSIQSFITERGDLDFAEMLWCRMRKSVSSYQDVVNCFSLVIQSLKNGEVHPWIHRGSSSALSKLIQQSYHGKMQSVSLTGLTPMRMLLEIGLDKMKKDYISCFIGQDLATFNYLDYFISSSVDIQEQVQRVKKLHHMLEVVVVCNAFLSLGHENLFPLTQSCLKYYKENPWNEQHVFQLPIRPSVISTFYQNSHPQTWRVEIISGHGQKEVKTTWQLTSRRPVDHVSFAVPDVPIDMTISGENEEIVYYPTQVSCSQVNFC | Essential component of the mitotic checkpoint, which prevents cells from prematurely exiting mitosis. Required for the assembly of the dynein-dynactin and mad1-mad2 complexes onto kinetochores (By similarity). Component of the RZZ complex composed of kntc1/rod, zw10 and zwilch. Belongs to the ZWILCH family. |
Q0IJ01 | MWAERHRAAVELQQFLSSIYEQVKKGESLGPFQYKDDVQVHVVCDGHCKPLENFCSGSEVLYIMEKKPLTLEDNALDETENNEGISFYMSLQESPQPQAIPTMSARQFLTSYTLTHNPNMIQLNSGVPVKVLPPLWVRCDSSDAEGTCWLGAEPIKSNRNEITGMSFRTVTCAGPTADKSTFPSLDSLRQAHKERHYSSAMQTRGFAQYDLFGSNTVENSVIESQSSVTVDFVWNGVERILQLPPLTSAATLNIKVESGDLRSPVYSVYKELDFLLVLAEGLKTGVTEWPETSETKSAVDLVQHLLNDLKNKVDGLSTSVSKKDNEKIKSDTAAVDCSIQSFITERGDLDFAEMLWCKMRKSVSSYQDVVNCFSLVIQSLKHGEMHPWIHRGSSSTLSKLIQESYHGDMQSLSLTGLTPMRMLLEIGLDKMKKDYINCFIGQDLATFNYLDYFICTSVDLQEQVQRVKKLHHMLEVVVVCNAFLSLGHENLFPLTQSCLKYYKENPWNEQHVFQLPIRPSVISTFYQNSHPQTWRVEIISGHGQKEVKTTWQLTSRRPVDHVSFAVPDVPIDMTISGDNEELVYYPTQVSCSQVHFC | Essential component of the mitotic checkpoint, which prevents cells from prematurely exiting mitosis. Required for the assembly of the dynein-dynactin and mad1-mad2 complexes onto kinetochores (By similarity). Component of the RZZ complex composed of kntc1/rod, zw10 and zwilch. Belongs to the ZWILCH family. |
Q2TBH8 | MGAAESEVETAAREVLAKVADIQEPVGFQEEAELPAQILAEFVMDSRKKDKLLCSQLQVVDFLQNFLVQEGTAQDQNPLASEDTSRQKALEAKEQWKELKATYQEHVEVITNSLTEALPKVEEAQIKQAQLQEALKQLQAKKQMAMEKLRIAQKQWQLEQEKHLQNLAEASSEVRERQTGAQQELQRLYQELGTLKQQAGQEKDKLQRHQTFLQLLYTLQGKQLFNEAEAEIPQELDLPKDKLQQVTQPQEQNTQDTMGREADNPQPVGDAGLPWLPGRQQHKEES | Part of the MIS12 complex, which is required for kinetochore formation and spindle checkpoint activity. Required to target ZW10 to the kinetochore at prometaphase (By similarity). Interacts with ZW10 and MIS12. Interacts with the NDC80 subunit of the NDC80 complex specifically during mitosis. Also interacts with KNL1, CETN3, DSN1 and PMF1 (By similarity). Localizes to kinetochores from late prophase to anaphase. |
Q9BWD0 | MEAAETEAEAAALEVLAEVAGILEPVGLQEEAELPAKILVEFVVDSQKKDKLLCSQLQVADFLQNILAQEDTAKGLDPLASEDTSRQKAIAAKEQWKELKATYREHVEAIKIGLTKALTQMEEAQRKRTQLREAFEQLQAKKQMAMEKRRAVQNQWQLQQEKHLQHLAEVSAEVRERKTGTQQELDRVFQKLGNLKQQAEQERDKLQRYQTFLQLLYTLQGKLLFPEAEAEAENLPDDKPQQPTRPQEQSTGDTMGRDPGVSFKAVGLQPAGDVNLP | Part of the MIS12 complex, which is required for kinetochore formation and spindle checkpoint activity. Required to target ZW10 to the kinetochore at prometaphase. Interacts with ZW10 and MIS12. Interacts with the NDC80 subunit of the NDC80 complex specifically during mitosis. Also interacts with KNL1, CETN3, DSN1 and PMF1. Localizes to kinetochores from late prophase to anaphase. |
Q9D0W9 | MADAEKNAVAEKNNAVATKEVLAEAAAILEPVGLQEEAELPAKIMEEFMRNSRKKDKLLCSQLQVVNFLQTFLAQEDTEQSPDALASEDASRQKATETKEQWKDMKATYMDHVDVIKCALSEALPQVKEAHRKYTELQKAFEQLEAKKRVLEEKLQLAQKQWVLQQKRLQNLTKISAEVKRRRKRALEKLDGSHQELETLKQQAGQEQEKLQRNQSYLQLLCSLQNKLVISEGKAEDKDVKGRALTAKSKSP | Part of the MIS12 complex, which is required for kinetochore formation and spindle checkpoint activity. Required to target ZW10 to the kinetochore at prometaphase (By similarity). Interacts with ZW10 and MIS12. Interacts with the NDC80 subunit of the NDC80 complex specifically during mitosis. Also interacts with KNL1, CETN3, DSN1 and PMF1 (By similarity). Localizes to kinetochores from late prophase to anaphase. |
Q546Y5 | MADAEKNAVAEKNAVAEENAVAEENAVADKNATKEVLAEAASVLEPVGLPEEAELPAKIMEEFMRNSRKKDKLLCSQLQVVNFLQTFLAQEDNTDQNPDALASEDTSRQKATETKEQWKELKATYMDHVDVIKCALSEALPQVKEAHRKYTELQKAFEQLEAKKRVLEEKLQLAQKQWVLQQKRLQNLTKISAEVKRRRKRALEKLDGSHQELETLKQQAGQEQEKLQRNQSYLQLLCSLQNKLVISESKADDKDVKGPALPPKSP | Part of the MIS12 complex, which is required for kinetochore formation and spindle checkpoint activity. Required to target ZW10 to the kinetochore at prometaphase (By similarity). Interacts with ZW10 and MIS12. Interacts with the NDC80 subunit of the NDC80 complex specifically during mitosis. Also interacts with KNL1, CETN3, DSN1 and PMF1 (By similarity). Interacts with SNAP25. Localizes to kinetochores from late prophase to anaphase. Expressed abundantly in brain and at lower levels in testis and kidney. |
Q84TI0 | MTDPYSNFFTDWFKSNPFHHYPNSSTNPSPHPLPPVTPPSSFFFFPQSGDLRRPPPPPTPPPSPPLREALPLLSLSPANKQQDHHHNHDHLIQEPPSTSMDVDYDHHHQDDHHNLDDDDHDVTVALHIGLPSPSAQEMASLLMMSSSSSSSRTTHHHEDMNHKKDLDHEYSHGAVGGGEDDDEDSVGGDGGCRISRLNKGQYWIPTPSQILIGPTQFSCPVCFKTFNRYNNMQMHMWGHGSQYRKGPESLRGTQPTGMLRLPCYCCAPGCRNNIDHPRAKPLKDFRTLQTHYKRKHGIKPFMCRKCGKAFAVRGDWRTHEKNCGKLWYCICGSDFKHKRSLKDHIKAFGNGHGAYGIDGFDEEDEPASEVEQLDNDHESMQSK | Transcriptional regulator required for normal differentiation of the ovary transmitting tract cells and pollen tube growth. In Arabidopsis, the transmitting tract facilitates the transport of pollen tubes to the ovules for fertilization (PubMed:17600712). May play a role in the regulation of AGL8/FUL, which is required for normal pattern of cell division, expansion and differentiation during morphogenesis of the silique (PubMed:23515580). Plays a role in replum development by the activation of the homeobox protein KNAT1 (PubMed:25039392). Can form homodimers. Interacts with BLH9, STM, AGL8/FUL, AGL1/SHP1 and AGL5/SHP2. Expressed in developing carpels (PubMed:17600712). Expressed in the shoot apical meristem and the replum (PubMed:25039392). Reduced fertility, fruit length and seed set (PubMed:17600712). Reduced replum width and cell number (PubMed:25039392). The fruits of the gain-of-function mutant ntt-3D (T-DNA tagging) fail to dehisce. Belongs to the WIP C2H2-type zinc-finger protein family. |
Q9SGD1 | MNSYETKGLSFESPSFIEWLKPQSSTTSSKSVLYRGKTRDAISRSNHHQSQMNMLERSLFLYQPQEPLNTSIQCLPLLNKLMENNSQASDIKEENKDDVVTLQIGFPKYHRGSSEDGSDITFDHQKKPIKREIIEDGVVMMKKRRKMKFDEEIIDSDVEVCGKRFWIPSPAQIHVGPMQFACSICSKTFNRYNNMQMHMWGHGSEFRKGADSLKGTIQPAAILRLPCYCCAEGCKNNINHPRSKPLKDFRTLQTHYKRKHGSKPFSCGKCGKALAVKGDWRTHEKNCGKLWYCTCGSDFKHKRSLKDHIRSFGSGHSPHPSLLFDGFEEDTECVTTE | Probable transcriptional regulator. Belongs to the WIP C2H2-type zinc-finger protein family. |
Q9LT33 | MLFSTVLSHRTLYILTCPNTLIHSYTHPHIHAYLAFTGFLTQLHHLEISCLLLLFFSLSSLLKLMADPDCIFRNGYVDYYNYSFNYATSLSRIYNSHDSFYYPHQTTNPNINENPNLTSPDSPPLREALPLLSLSPIHKHQEPTANHHEYYFMETTETSSNSNFLDQCQDSYRHDVTVDLHLGLPNLGDGGSSSSDVVLDSTDHQEGHHDHHQDQGLEVTMASDHDDEHGGLQRGNHLHHFWIPTPSQILMGPTQFSCPLCFKTFNRYNNMQMHMWGHGSQYRKGPESLRGTQPTAMLKLPCYCCAPGCKNNIDHPRARPLKDFRTLQTHYKRKHGVRPFACRRCGKAFAVKGDWRTHEKNCGKLWYCSCGSDFKHKRSLKDHVKAFGNGHVPCCGIDHEEEEAASDVEQQE | Probable transcriptional regulator. Belongs to the WIP C2H2-type zinc-finger protein family. Truncated N-terminus. |
Q9SYC5 | MSNPACSNLFNNGCDHNSFNYSTSLSYIYNSHGSYYYSNTTNPNYINHTHTTSTSPNSPPLREALPLLSLSPIRHQEQQDQHYFMDTHQISSSNFLDDPLVTVDLHLGLPNYGVGESIRSNIAPDATTDEQDQDHDRGVEVTVESHLDDDDDHHGDLHRGHHYWIPTPSQILIGPTQFTCPLCFKTFNRYNNMQMHMWGHGSQYRKGPESLRGTQPTGMLRLPCFCCAPGCKNNIDHPRAKPLKDFRTLQTHYKRKHGSKPFACRMCGKAFAVKGDWRTHEKNCGKLWYCSCGSDFKHKRSLKDHVKAFGNGHVPCGIDSFGGDHEDYYDAASDIEQ | Probable transcriptional regulator. Belongs to the WIP C2H2-type zinc-finger protein family. |
Q9FX68 | MYNNNQYSFSGDEDSVVLSLGPPGQQYPSHNKPTSTKPSSDHEFNHPLTNPNGVTVALHIGPPSSDKETLSGGNNQEGLTARQGQYWIPSLSQILVGPTQFSCSVCNKTFNRFNNMQMHMWGHGSQYRKGPESLRGTKSSSSILRLPCYCCAEGCKNNIDHPRSKPLKDFRTLQTHYKRKHGAKPFRCRKKCEKTFAVRGDWRTHEKNCGKLWFCVCGSDFKHKRSLKDHVRAFGDGHAAHTVSDRVVGIGDADEDDEEEEEEEEDDVEEEDAHEENVRGEKNYGIRYDHFRRYGQISDDNY | Probable transcriptional regulator (Probable). Involved in leaf vasculature patterning (PubMed:18643975). Defects in venation pattern in leaves and cotyledons, altered phyllotaxy of vegetative leaves, short roots, delay in leaf initiation and reduced apical dominance. Belongs to the WIP C2H2-type zinc-finger protein family. |
Q9UJP7 | MEIPKLLPARGTLQGGGGGGIPAGGGRVHRGPDSPAGQVPTRRLLLPRGPQDGGPGRRREEASTASRGPGPSLFAPRPHQPSGGGDDFFLVLLDPVGGDVETAGSGQAAGPVLREEAKAGPGLQGDESGANPAGCSAQGPHCLSAVPTPAPISAPGPAAAFAGTVTIHNQDLLLRFENGVLTLATPPPHAWEPGAAPAQQPRCLIAPQAGFPQAAHPGDCPELRSDLLLAEPAEPAPAPAPQEEAEGLAAALGPRGLLGSGPGVVLYLCPEALCGQTFAKKHQLKMHLLTHSSSQGQRPFKCPLGGCGWTFTTSYKLKRHLQSHDKLRPFGCPAEGCGKSFTTVYNLKAHMKGHEQENSFKCEVCEESFPTQAKLGAHQRSHFEPERPYQCAFSGCKKTFITVSALFSHNRAHFREQELFSCSFPGCSKQYDKACRLKIHLRSHTGERPFLCDFDGCGWNFTSMSKLLRHKRKHDDDRRFMCPVEGCGKSFTRAEHLKGHSITHLGTKPFVCPVAGCCARFSARSSLYIHSKKHLQDVDTWKSRCPISSCNKLFTSKHSMKTHMVKRHKVGQDLLAQLEAANSLTPSSELTSQRQNDLSDAEIVSLFSDVPDSTSAALLDTALVNSGILTIDVASVSSTLAGHLPANNNNSVGQAVDPPSLMATSDPPQSLDTSLFFGTAATGFQQSSLNMDEVSSVSVGPLGSLDSLAMKNSSPEPQALTPSSKLTVDTDTLTPSSTLCENSVSELLTPAKAEWSVHPNSDFFGQEGETQFGFPNAAGNHGSQKERNLITVTGSSFLV | Cooperates with CIITA to promote transcription of MHC class I and MHC class II genes. Self-associates. Interacts with ZXDC and CIITA. May be expressed in brain, heart, kidney, liver, lung, muscle and placenta. Belongs to the ZXD family. |
Q9UBB3 | MEIPKLLPARGTLQGGGGGGIPAGGGRVHRGPDSPAGQVPTRRLLLLRGPQDGGPGRRREEASTASRGPGPSLLAPRTDQPSGGGGGGGDDFFLVLLDPVGGDVETAGSGQAAGPVLREEAEEGPGLQGGESGANPAGPTALGPRCLSAVPTPAPISAPGPAAAFAGTVTIHNQDLLLRFENGVLTLATPPPHAWEPGAAPAQQPGCLIAPQAGFPHAAHPGDCPELPPDLLLAEPAEPAPAPAPEEEAEGPAAALGPRGPLGSGPGVVLYLCPEAQCGQTFAKKHQLKVHLLTHSSSQGQRPFKCPLGGCGWTFTTSYKLKRHLQSHDKLRPFGCPAEGCGKSFTTVYNLKAHMKGHEQENSFKCEVCEESFPTQAKLSAHQRSHFEPERPYQCAFSGCKKTFITVSALFSHNRAHFREQELFSCSFPGCSKQYDKACRLKIHLRSHTGERPFLCDFDGCGWNFTSMSKLLRHKRKHDDDRRFMCPVEGCGKSFTRAEHLKGHSITHLGTKPFVCPVAGCCARFSARSSLYIHSKKHLQDVDTWKSRCPISSCNKLFTSKHSMKTHMVKRHKVGQDLLAQLEAANSLTPSSELTSQRQNDLSDAEIVSLFSDVPDSTSAALLDTALVNSGILTIDVASVSSTLAGHLPANNNNSVGQAVDPPSLMATSDPPQSLDTSLFFGTAATGFQQSSLNMDEVSSVSVGPLGSLDSLAMKNSSPEPQALTPSSKLTVDTDALTPSSTLCENSVSELLTPTKAEWNVHPDSDFFGQEGETQFGFPNAAGNHGSQKETDLITVTGSSFLV | Cooperates with CIITA to promote transcription of MHC class I and MHC class II genes. Self-associates. Interacts with ZXDC and CIITA (By similarity). May be expressed in brain, heart, kidney, liver, lung, muscle and placenta. Belongs to the ZXD family. |
Q8CEQ1 | MEIPRLLPARGTPQGAGGGGCPAGGGGVHRAPASLACQAPTRRLLLLRGAQDGGPGPRSAEAQRASRGLGPSLNRLAPRPDHRSSGGGRGGGAGGGGGGSGGGGGGGGGGGGGGGGGGSRGGSDDFFLLLLDPVGGDVETVGTEQAGAPVRREEAGAGPRPERRQSAGPPAGRPEPGPRCLSAVPAASPLPAAGPGPAAAAAAAAAAAFAGTITIHNQDLLLRFENGVLTLTTPPLPAWEPGVAPFPQPQPPPQPGALIAPQAAAAGFPPAAAAAAAAAAAGAQLGDCPELPPDLLLAEPAEPAACPAPPEEEAEAPAAAAAQSPRGPAGPGPGPGVVLYLCPEAQCGQTFAKKHQLKVHLLTHSSSQGQRPFKCPLSGCGWTFTTSYKLKRHLQSHDKLRPFGCPVQGCGKSFTTVYNLKAHMKGHEQENSFKCEVCEESFPTQAKLSTHQRSHFEPERPYQCAFSGCKKTFITVSALFSHNRAHFREQELFACSFPGCSKQYDKACRLKIHLRSHTGERPFLCDFDGCGWNFTSMSKLLRHKRKHEDDRRFTCPVEGCGKSFTRAEHLKGHSITHLGTKPFVCPVEGCCARFSARSSLYIHSKKHLQDVGAWKSRCPVPTCNKLFTSKHSMKTHMTKRHNLSQDLLAQLEAANSLTPSSELTSPGQSDLSGAELVSLFSDVPGHGSAAVLDTALVNSGILTIDVASVNSSLAGSLPADNNSNNHSLGQAAEPRALRGAPSDLPQSLDTSLFFGTSVAGYQHSPLDMDDVSAGNVGLFGSLALKNSSLEPQALTPSNKLTVDTEALTPSSTLCENSVSELLTPAKAEWNVHPESDFFGHEEETQFGFSHPTGSHGSQKDTDLITVTGTPFLV | Cooperates with CIITA to promote transcription of MHC class I and MHC class II genes. Self-associates. Interacts with ZXDC and CIITA (By similarity). Belongs to the ZXD family. |
Q8NAU2 | MDLPALLPAPTARGGQHGGGPGPLRRAPAPLGASPARRRLLLVRGPEDGGPGARPGEASGPSPPPAEDDSDGDSFLVLLEVPHGGAAAEAAGSQEAEPGSRVNLASRPEQGPSGPAAPPGPGVAPAGAVTISSQDLLVRLDRGVLALSAPPGPATAGAAAPRRAPQASGPSTPGYRCPEPQCALAFAKKHQLKVHLLTHGGGQGRRPFKCPLEGCGWAFTTSYKLKRHLQSHDKLRPFGCPVGGCGKKFTTVYNLKAHMKGHEQESLFKCEVCAERFPTHAKLSSHQRSHFEPERPYKCDFPGCEKTFITVSALFSHNRAHFREQELFSCSFPGCSKQYDKACRLKIHLRSHTGERPFICDSDSCGWTFTSMSKLLRHRRKHDDDRRFTCPVEGCGKSFTRAEHLKGHSITHLGTKPFECPVEGCCARFSARSSLYIHSKKHVQDVGAPKSRCPVSTCNRLFTSKHSMKAHMVRQHSRRQDLLPQLEAPSSLTPSSELSSPGQSELTNMDLAALFSDTPANASGSAGGSDEALNSGILTIDVTSVSSSLGGNLPANNSSLGPMEPLVLVAHSDIPPSLDSPLVLGTAATVLQQGSFSVDDVQTVSAGALGCLVALPMKNLSDDPLALTSNSNLAAHITTPTSSSTPRENASVPELLAPIKVEPDSPSRPGAVGQQEGSHGLPQSTLPSPAEQHGAQDTELSAGTGNFYLESGGSARTDYRAIQLAKEKKQRGAGSNAGASQSTQRKIKEGKMSPPHFHASQNSWLCGSLVVPSGGRPGPAPAAGVQCGAQGVQVQLVQDDPSGEGVLPSARGPATFLPFLTVDLPVYVLQEVLPSSGGPAGPEATQFPGSTINLQDLQ | Cooperates with CIITA to promote transcription of MHC class I and MHC class II genes. Self-associates. Interacts with ZXDA and CIITA. Expressed at high levels in heart, kidney, liver and testis, at moderate levels in brain and stomach, and at low levels in lung, muscle, placenta, small intestine and spleen. Sumoylated at Lys-660 with SUMO1, SUMO2 and SUMO3; sumoylation enhances the activity of the transcriptional activation domain. Doesn't interact with CIITA. Represses MHC class II transcription possibly via dominant-negative association with isoform 1. Belongs to the ZXD family. Truncated N-terminus. |
Q99J65 | MDLPAVLAAPATRGDQHGGGPSRLRRGAGPSLGAGPGRRRLLLLRGPEDGGPGPRPEEAPGPSPPPPEDGGDSFVVLLEVPRAADTHGQEEAEPDSGASPTEQVPAAAPGAALAGTVTIHNQDLLVRFDRGVFTLAAAPAPAAPSLHPATTPGLEPSSAAASRRGPVAASAGSPAYRCPEPQCALSFAKKHQLKVHLLTHGSLQGRRPFKCPLDGCGWAFTTSYKLKRHLQSHDKLRPFSCPVGGCGKKFTTVYNLKAHMKGHEQESLFKCEVCAERFPTHAKLNSHQRSHFEPERPYKCDFPGCEKTFITVSALFSHNRAHFREQELFSCSFPGCNKQYDKACRLKIHLRSHTGERPFICDSDSCGWTFTSMSKLLRHKRKHDDDRRFTCPVEGCGKSFTRAEHLKGHSITHLGTKPFECPVEGCCARFSARSSLYIHSKKHLQDVGTPKSRCPVSSCNRLFTSKHSMKAHVVRQHSRRQDLVPQLEAPSSLTPSSELSSPGQSELTNIDLAALFSDTPANSSSSTAGSDEALNSGILTIDVTSVSSSLGGNLPTNNNSLGPMDPLVLVAHGDMPPSLDSPLVLGTSATVLQPGSFSADDSQAMSTGAVGCLVALPVRNLNQDSPALTPSNNLTAPGTTPTSSDTTQETGSVPDLLVPIKVEQDLSPVPDVVQGQKESHGPSQSVLSSSTERPGAQKDSELSAGTGSLYLESGGSARTDYRAIQLVKKKKQKGTGSDEGASDSAHRKVKGGTINPPHVHSGQHSCFCGTLMVPSGGLTVPAPAAGLQCVQIPVLQDDPSGEGGLPLGLSPQRSAFHPYFTVDLPVYVLQEVLPAPGGFAGLETAQVPGSTINLRDLE | Cooperates with CIITA to promote transcription of MHC class I and MHC class II genes. Self-associates. Interacts with ZXDB and CIITA (By similarity). Sumoylated at Lys-661 with SUMO1, SUMO2 and SUMO3; sumoylation enhances the activity of the transcriptional activation domain. Belongs to the ZXD family. Extended N-terminus. Extended N-terminus. |
A6NCK5 | MVHFLHPGHTPRNIVPPDAQKDALGCCVVQEEASPYTLVNICLNVLIANLEKLCSERPDGTLCLPEHWSFPQEVAERFLRVMTWQGKLTDRTASIFRGNQMKLKLVNIQKAKISTAAFIKAFCRHKLIELNATAVHADLPVPDIISGLCSNRWIQQNLQCLLLDSTSIPQNSRLLFFSQLTGLRILSVFNVCFHTEDLANVSQLPRLESLDISNTLVTDISALLTCKDRLKSLTMHYLKCLAMTKSQILAVIRELKCLLHLDISDHRQLKSDLAFHLLQQKDILPNVVSLDISGGNCITDEAVELFIRLRPAMQFVGLLATDAGSSDFFTTKQGLRVAGGASMSQISEALSRYRNRSCFVKEALHRLFTETFSMEVTMPAILKLVAIGMRNHPLDLRVQFTASACALNLTRQGLAKGMPVRLLSEVTCLLFKALKNFPHYQQLQKNCLLSLTNSRILVDVPFDRFDAAKFVMRWLCKHENPKMQTMAVSVTSILALQLSPEQTAQLEELFMAVKELLAIVKQKTTENLDDVTFLFTLKALWNLTDGSPAACKHFIENQGLQIFIQVLETFSESAIQSKVLGLLNNIAEVRELSSKLVTEDVLKHINSLLCSREMEVSYFAAGIIAHLTSDRQLWISRDFQRRTLLQDLHATIQNWPSSSCKMTALVTYRSFKTFFPLLGNFSQPEVQLWALWAMYHVCSKNPSKYCKMLVEEEGLQLLCDIQEHSEATPKAQQIAASILDDFRMHFMNYQRPTLCQMPF | Probably acts as target recruitment subunit in an E3 ubiquitin ligase complex ZYGA-CUL2-elongin BC. Belongs to the zyg-11 family. |
Q8VC01 | MAWQGKLTDRTASIFQGKQMSLKLINIPRVKLSAAAFTKAFCHHKLIEVNATSVDSELLAPDIIHALQSSAWIQKNLQCLVLDSVSIPPNSGLVALSHFTGLHTLSVANVSFCNEDLVSVSQLPNLGSLDISNTLVTNISALLSCKNRLRSLTMHYLKCLAMNSPQVLAVIRQLKCLLHLDISDHQQLRSDLAFYLLQQKDILPNLTSLDISGGTDVTDQAVESFLQHRPAMRFVGLLYTDAGYSDFFTAKQGLKVAGGANMSQISEALSRYRNRSCFVKEALFRLFTETLSLRAVLPVMLKLVAIGMRNHPLDLPVQFTASACALNLTRQELARGMPVRLLAEITDLLFKATKNFPYYQQLQKNCLLSLTSSRILMDVPFDRFDAAKLALRWVCRRESPKLRTMAVSITSILALKLSPEEMGQLQEELIMAIKELLTIIRQKLAENLDDVTFLFTLKALWNLTDECPLACKYFMENEGLATVIRVLETFSISVIQSKVLGLLNNVAEVRELSSKLVTEDVIERIISLLHSSNLEVSFLAAGVLAHLTCDRQHWLSRDLQRTDLLRYLHLAIQNWPSSRCDMSVLVTYRSFKAFSPLLVNFSQPEVQRWALWAIHHVCSKNPRPKDV | Probably acts as target recruitment subunit in an E3 ubiquitin ligase complex ZYGA-CUL2-elongin BC. Belongs to the zyg-11 family. |
Q9H8L8 | MPEDQAGAAMEEASPYSLLDICLNFLTTHLEKFCSARQDGTLCLQEPGVFPQEVADRLLRTMAFHGLLNDGTVGIFRGNQMRLKRACIRKAKISAVAFRKAFCHHKLVELDATGVNADITITDIISGLGSNKWIQQNLQCLVLNSLTLSLEDPYERCFSRLSGLRALSITNVLFYNEDLAEVASLPRLESLDISNTSITDITALLACKDRLKSLTMHHLKCLKMTTTQILDVVRELKHLNHLDISDDKQFTSDIALRLLEQKDILPNLVSLDVSGRKHVTDKAVEAFIQQRPSMQFVGLLATDAGYSEFLTGEGHLKVSGEANETQIAEALKRYSERAFFVREALFHLFSLTHVMEKTKPEILKLVVTGMRNHPMNLPVQLAASACVFNLTKQDLAAGMPVRLLADVTHLLLKAMEHFPNHQQLQKNCLLSLCSDRILQDVPFNRFEAAKLVMQWLCNHEDQNMQRMAVAIISILAAKLSTEQTAQLGTELFIVRQLLQIVKQKTNQNSVDTTLKFTLSALWNLTDESPTTCRHFIENQGLELFMRVLESFPTESSIQQKVLGLLNNIAEVQELHSELMWKDFIDHISSLLHSVEVEVSYFAAGIIAHLISRGEQAWTLSRSQRNSLLDDLHSAILKWPTPECEMVAYRSFNPFFPLLGCFTTPGVQLWAVWAMQHVCSKNPSRYCSMLIEEGGLQHLYNIKDHEHTDPHVQQIAVAILDSLEKHIVRHGRPPPCKKQPQARLN | Serves as substrate adapter subunit in the E3 ubiquitin ligase complex ZYG11B-CUL2-Elongin BC. Acts redudantly with ZER1 to target substrates bearing N-terminal glycine degrons for proteasomal degradation (PubMed:33093214). Involved in the clearance of proteolytic fragments generated by caspase cleavage during apoptosis since N-terminal glycine degrons are strongly enriched at caspase cleavage sites. Also important in the quality control of protein N-myristoylation in which N-terminal glycine degrons are conditionally exposed after a failure of N-myristoylation (PubMed:31273098). Interacts with ELOC/Elongin C. Part of an E3 ubiquitin ligase complex including ZYG11B, CUL2 and Elongin BC. Belongs to the zyg-11 family. Extended N-terminus. |
Q80TA0 | MPEDQAHAAMEEASPYSLLDICLSFLTTNLEKFCSARQDGTLCLQEPGVFPQEVADRLLQTIAFHGLLNDGTVGIFRGNQMRLKRACIRKAKISAVAFRKAFCHHKLVELDATGVNADITITDIISGLGSNKWIQQNLQCLVLNSLTLSLEDPYERCFSRLSGLRALSITNVLFYNEDLAEVASLPRLESLDISNTSITDITALLACKDRLKSLTMHHLKCLKMTTTQILDVVRELKHLNHLDISDDKQFTSDIALRLLEQKDILPNLVSLDVSGRKHVTDKAVEAFIQQRPSMQFVGLLATDAGYSEFLMGKGHLKVSGEANETQIAEALRRYSERAFFVREALFHLFSLTHVMEKTKPDILKLVVTGMRNHPMNLPVQLAASACVFNLTKQDLALGMPVRLLADVTHLLLKAMEHFPNHQQLQKNCLLSLCSDRILQDVPFNRFEAAKLVMQWLCNHEDQNMQRMAVAIISILAAKLSTEQTAQLGAELFIVRQLLQIVKQKTNQNSVDTTLKFTLSALWNLTDESPTTCRHFIENQGLELFMRVLESFPTESSIQQKVLGLLNNIAEVQELHSELMWKDFIDHISSLLHSVEVEVSYFAAGIIAHLISRGEQAWTLSRSQRNSLLDDLHSAILKWPTPECEMVAYRSFNPFFPLLGCFTTPGVQLWAVWAMQHVCSKNPSRYCSMLIEEGGLQHLYNIKEHEQTDPYVQQIAVAILDSLEKHIVRHGRPPPCKKQPQARLN | Serves as substrate adapter subunit in the E3 ubiquitin ligase complex ZYG11B-CUL2-Elongin BC. Acts redudantly with ZER1 to target substrates bearing N-terminal glycine degrons for proteasomal degradation. Involved in the clearance of proteolytic fragments generated by caspase cleavage during apoptosis since N-terminal glycine degrons are strongly enriched at caspase cleavage sites. Also important in the quality control of protein N-myristoylation in which N-terminal glycine degrons are conditionally exposed after a failure of N-myristoylation. Interacts with ELOC/Elongin C. Part of an E3 ubiquitin ligase complex including ZYG11B, CUL2 and Elongin BC. Belongs to the zyg-11 family. |