wanglab/gogpt-training-data huggingface dataset:
Protein: DCN1-like protein 5 (DCUN1 domain-containing protein 5) (Defective in cullin neddylation protein 1-like protein 5) (Squamous cell carcinoma-related oncogene 5) (Q1RMX9)
Organism: Bos taurus (Bovine)
Function: Contributes to the neddylation of all cullins by transferring NEDD8 from N-terminally acetylated NEDD8-conjugating E2s enzyme to different cullin C-terminal domain-RBX complexes which is necessary for the activation of cullin-RING E3 ubiquitin ligases (CRLs). May play a role in DNA damage response and may participate in cell proliferation and anchorage-independent cell growth.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9BTE7}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q9BTE7}. Note=Subcellular localization is independent of the interaction with cullins. {ECO:0000250|UniProtKB:Q9BTE7}.
Interaction partners:
- NEDD8-conjugating enzyme Ubc12
- NEDD8-conjugating enzyme UBE2F
- Ubiquitin-like protein NEDD8
- NEDD8-activating enzyme E1 catalytic subunit
- Cullin-2
- RING-type domain-containing protein.
- Cullin-3
- Cullin-associated NEDD8-dissociated protein 1
Sequence:
MPVKKKRKSGVAAAAAEDGGLKKCKISSYCRSQPPARLISGEEHFSSKKCLAWFYEYAGPDEVVGPEGMEKFCEDIGVEPENIIMLVLAWKLEAESMGFFTKEEWLKGMTSLQCDCTEKLQNKFDFLRSQLNDISSFKNIYRYAFDFARDKDQRSLDIDTAKSMLALLLGRTWPLFSVFYQYLEQSKYRVMNKDQWYNVLEFSRTVHADLSNYDEDGAWPVLLDEFVEWHKVRQAS
Protein: Asparagine--tRNA ligase, mitochondrial (EC 6.1.1.22) (Asparaginyl-tRNA synthetase) (AsnRS) (Q9P6I0)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Mitochondrion {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Glutamyl-tRNA
- Glutamyl-tRNA
- Probable proline--tRNA ligase, mitochondrial
- Putative proline--tRNA ligase C19C7.06
- Isoleucine--tRNA ligase, cytoplasmic
- Isoleucine--tRNA ligase, mitochondrial
- Probable glutamine--tRNA ligase
- Serine--tRNA ligase, mitochondrial
- Probable asparagine--tRNA ligase, cytoplasmic
- Serine--tRNA ligase, cytoplasmic
Sequence:
MNKFQLPKTLKSLWHHPHNGELISINGWVRSIRKLKNVCFAMVSDGTCQQALQVVTSPEQSKKLSYGASVNIEGQLAVSKNAKLGLQQYELLAEKIKIYGQINDDNYPIQKKHLTTEMLRQIPHLRLRTAKQGEIFRLRSDSLKALRQFFSSKDFTETNPPIITSSDCEGAGEVFTLTPQETHKNKSFERDDQKHFFDRPAFLTVSTQLHLEALALGLSRVYTISPAFRAEQSHTSRHLAEFWMLEAEVAFMTSLSQLTSLMEDMIKYTLNSLMEQNYHRDHWDQLLKPWKCMTYSEAIEELSAVKKTWKYPPKWGNDLSSEHEKYLCEILHKTPVFVTDYPQKIKPFYMKSSGPDTVAAVDLLVPQVGELAGGSLRKDHLDEYKTYPPELQWYLDLMKYSNAPHGGFGLGIERLIAFLEGENTNVKETIPFPRSVGSIFA
Protein: H-caldesmon (Q8VD79)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
KLKGGNLGENQVEKMVEEKTPEIQEEAVLMVLENGQVSAEESKIEGDGEQDMEEIARRKKMGEEERERAEAERLRLEVEGQEQERIKAEQDRKLAEERARVEAEQKAAAEERERREAEERERREAEERERREAEERAEQARIQEEQRRVAEAQKKAKAEEEEKARIEEQRQKQQLEEQRSEKREAKDKGEKGAEKADRKGVNEREAPDDRLQTAVPKTQEKEEEKGVKGQAQRQKPQDDKPAFRKEEIKDEKIKKDKEPKEEVKSFLDRKKGFTEVKAQNGEFMTHKLKQTENAFSPSRSGGRASGDKEAEGAPQVEAGKR
Protein: Ribose-phosphate pyrophosphokinase 1 (EC 2.7.6.1) (Phosphoribosyl pyrophosphate synthase I) (PRS-I) (Q9D7G0)
Organism: Mus musculus (Mouse)
Function: Catalyzes the synthesis of phosphoribosylpyrophosphate (PRPP) that is essential for nucleotide synthesis.
Interaction partners:
- Amidophosphoribosyltransferase
- Ribose-5-phosphate isomerase
- Transketolase
- Ribokinase
- Phosphopentomutase
- Transketolase-like protein 1
- Transketolase-like protein 2
- ADP-ribose pyrophosphatase, mitochondrial
- Uridine 5'-monophosphate synthase
- ADP-sugar pyrophosphatase
Sequence:
MPNIKIFSGSSHQDLSQKIADRLGLELGKVVTKKFSNQETCVEIGESVRGEDVYIVQSGCGEINDNLMELLIMINACKIASASRVTAVIPCFPYARQDKKDKSRAPISAKLVANMLSVAGADHIITMDLHASQIQGFFDIPVDNLYAEPAVLKWIRENISEWRNCTIVSPDAGGAKRVTSIADRLNVDFALIHKERKKANEVDRMVLVGDVKDRVAILVDDMADTCGTICHAADKLLSAGATRVYAILTHGIFSGPAISRINNACFEAVVVTNTIPQEDKMKHCSKIQVIDISMILAEAIRRTHNGESVSYLFSHVPL
Protein: Protein FLUORESCENT IN BLUE LIGHT, chloroplastic (Q940U6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Negative regulator of tetrapyrrole biosynthesis (including chlorophyll) in chloroplasts, probably via HEMA1 repression. Inhibits especially the magnesium ion Mg(2+) branch of tetrapyrrole biosynthesis, but independently of heme.
Subcellular location: Plastid, chloroplast membrane {ECO:0000269|PubMed:18431481}; Single-pass membrane protein. Plastid, chloroplast thylakoid membrane; Single-pass membrane protein.
Interaction partners:
- Glutamyl-tRNA reductase 1, chloroplastic
- Glutamyl-tRNA reductase-binding protein, chloroplastic
- Light-harvesting complex-like protein 3 isotype 2, chloroplastic
- Light-harvesting complex-like protein 3 isotype 1, chloroplastic
- Probable cysteine protease RD21B
Sequence:
MAALIRCCSSFSHTSGGQPPPRDKSRAPEIGKFATSIGYSVVRKPGDHPPFSKIIHSSSQPKERQGKGILQTPFASVGSLDKFSAFEGIGRLKLPVMAVLLTNSLQMATPLEALAAEICEPESSMFSMPILLLVALIGATVGGLLARQRKGELQRLNEQLRQINAALRRQAKIESYAPSLSYAPVGARIPDSEIIVEPKKQELISKLKTGKTFLRNQEPEKAYTEFKIALELAQSLKDPTEEKKAARGLGASLQRQGKYREAIQYHSMVLAISKRESEDSGITEAYGAIADCYTELGDLEKAGKFYDTYIARLETD
Protein: RING-type E3 ubiquitin transferase (EC 2.3.2.27) (A0AR23)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MLSTVSPDLSPETLGSVPLATPPRPQTASSAPLPRPIRKHSEAGPSGQPARGSMEVGMRVVRGADWKWANQDDGEGHVGTVVEIGRQGSTTTPDKTVVVQWDSGTRTNYRSGYQGAFDLLLYDNAQIGVRHSNIICDSCKKHGIMGMRWKCKVCFDYDLCTQCYMNNKHGLTHAFERYETAHSQPVSLTPRQNLSRIILKGIFQGVKVVRGPDWDWGNQDGGEGKVGKVVDIRGWDQESGRSVASVTWSNSTTNVYRMGHKGKVDLKYVSDVQGGFYYKEHLPKLGEHAELQRQESADSHSFQQGDKVKCLLEVDILRQMQEGHGGWNPKMAEYISRIGTVHRITDRGDVRVQYSNNIRWTFHPGALTKVNTFAVGELVKVLDDIDSVKRLQVGHGEWTDSMAPALGQVGKVLKVYADGDLRVAFGGQTWTFNPACLSAQPGEVDANLMTVENASESSSTVISVLEKLLSQSTEQDNPGRLVIEAAHGSAAKVRELLQKHPDKVDIKNQGKTALQVAAHQGHVEVVKVLLQANSSIEAKDEDGDAALHYTAFGNQAEIARLLLSKGASVNLLNNSMCTALHIAVNKGFTDVVRVLTEHSADVNLQDSYGDTPLHDAIAKDFRSIIEILTVVPNIDFTQQNNRGFNLLHHAALKGNKLATEMILSRARQLADVKKEDGFSALHLAALNNHRDVAEILLKEGRCDINIRNNRNQTPLQLAVTQGHMALVALLVMEGADVNAEDEDGDTAMHTSLSRQQLTTVISSAEGDGAVLYGRLCSSGLMGNTELNVGAAIACFLAQEGADISYANHKGKSPLDLVTDSSVQTLIRSFAEKHRLHAVSCGTGSSSSSSSLRRVHTTPNTMTNLAVPSVTGPSECLICSELALLVLFSPCQHSVACEECAHRMKKCIRCQVTITKKIRQDQTEVECSPSSENSEQHHLLEQLQSRYRQMEERITCPICIDNHIRLVFQCGHASCIDCSSALKTCPICRQTIRERIQLFV
Protein: TBC1 domain family, member 4 (D3ZGN0)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- RAC-beta serine/threonine-protein kinase
- RAC-alpha serine/threonine-protein kinase
- RAC-gamma serine/threonine-protein kinase
- Solute carrier family 2, facilitated glucose transporter member 4
- Ras-related protein Rab-8A
- Insulin receptor substrate 1
Sequence:
MESPSCIQDEPFPHPLEPEPIALAQPGATKPGDKRFRLWYVGGSCLDRRTTLPMLPWLMAEIRRRSLKPEAGGCGAPAAREVLLVLSAPFLRCVPAPGVGVGGGAGSGAVQPNTGVFIFEHKAQHISRFIHNSHDLTYFAYLIKAQPDDPESQMACHVFRATDPNQVPDVISSIRQLSKAAMKEDAKPSKDNEDAFYNSQKFEVLYCGRVIVTHKKAPSSLIDDCKDKFSLHEQQRLKLQGERGGDPGDGDEMGVLEAESPVSPDDGLPEKPDGLVNCPRALPSLASLPALASQPALASSRVCFPERILEDCGFDEQQEFRSRCSSVTGVMQKKVHENNQKTQPRRRHASAPSHVQPSDSEKNRTMLFQVGRFEINLISPDTKSVVLEKNFKDISSCSQGIKHVDHFGFICRESLEPGLSQYICYVFQCANESLVDEVMLTLKQAFSTAAALQSAKTQIKLCEACPMHSLHKLCERIEGLYPPRAKLVIQRHLSSLTDNEQADIFERVQKMKPISDQEENELVILHLRQLCEAKQKTHVHIGEGQAIISNSTIPENSTSGGRFKLDVLKNKAKRSLTSSLENIFSRGANRMRGRLGSVDSFERSNSLASEKDFSPGGSPPGTPPASPLSSAWHTFPEEDSDSPQFRRRAHTFSHPPSSSRRKLNLQDGKAHGLRSPLLRQNSSEQCSVLPSARRMCKESNSSSSLPSLHTSFSAPSFTASSFLKSFYQSSGRLSPQYENEIRQDTASESSDGEGRKRTSSTCSNESLSAGGTPVTPRRISWRQRIFLRVASPVNKSPSAMQQQKDGLDRTELLPLSPLSPTMEEEPLVIFLSGDEDTEKVEEKKKSKEIKSLWKKAIHQQILLLRMEKENQKLEARRDELQSRKVKLDYEEVGTCQKEVLIAWDKKLLNCRTKIRCDMEDIHTSLKEGVPKSRRGEIWQFLALQYRLRHRLPNKHQPPDTSYKELLKQLTAQQHAILVDLGRTFPTQPYFSVQLGAGQLSLFNLLKAYSLLDKEVGYCQGISFVAGVLLLHMSEEQAFEMLKFLMYDLGFRKQYRPDMMSLQIQMYQLSRLLHDYHRDLYNHLEENEISPSLYAAPWFLTLFASQFPLGFVARVFDIIFLQGTEVIFKVALSLLSSQEALVMECENFENIVEFLKSTLPDMNTTEMEKIITQVFEMDISKQLHAYEVEYHVLQDELLESSYACEDNESLEKLERANNQLKRQNMDLLEKLQVAHAKIQALESNLETLLTRETKMKALIRTLEQDKMAYQKTVEQIRKLLPADALANCELLLKDLSYPTNDKAKAGNKP
Protein: Wee1-like protein kinase (EC 2.7.10.2) (Wee1A kinase) (P47810)
Organism: Mus musculus (Mouse)
Function: Acts as a negative regulator of entry into mitosis (G2 to M transition) by protecting the nucleus from cytoplasmically activated cyclin B1-complexed CDK1 before the onset of mitosis by mediating phosphorylation of CDK1 on 'Tyr-15'. Specifically phosphorylates and inactivates cyclin B1-complexed CDK1 reaching a maximum during G2 phase and a minimum as cells enter M phase. Phosphorylation of cyclin B1-CDK1 occurs exclusively on 'Tyr-15' and phosphorylation of monomeric CDK1 does not occur. Its activity increases during S and G2 phases and decreases at M phase when it is hyperphosphorylated. A correlated decrease in protein level occurs at M/G1 phase, probably due to its degradation (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P30291}.
Interaction partners:
- G2/mitotic-specific cyclin-B1
- Cyclin-dependent kinase 1
- Serine/threonine-protein kinase PLK1
- Cyclin-dependent kinase 2
- Serine/threonine-protein kinase Chk1
- M-phase inducer phosphatase 1
- Wee1-like protein kinase 2
- Cyclin-A2
- M-phase inducer phosphatase 3
- Cyclin-A1
Sequence:
MSFLSRQQPPPTRRVGAAYSLRQKLIFSPGSDCEEEEEEEEEGSGHSTGEDSAFQEPDSPLPSARSPAEAEAERRRRSPGAEPSSPGELEDDLLLQGGGGGAQAAGGGAEGDSWEEEGFGSSSPVKSPSTAYFLSSPFSPVRCGGPGDASPQGCGAPRAMDDPCSPQPDYPSTPPHKTFRKLRLFDTPHTPKSLLSKARVIDSGSVKLRGSSLFMDTEKSGKREFDTRQTPQVNINPFTPDPVLLHSSGRCRGRKRAYFNDSSEDMEASDYEFEDETRPAKRITITESNMKSRYTTEFHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDEQNALREVYAHAVLGQHPHVVRYFSAWAEDDHMLIQNEYCNGGSLADAISENYRVMSYLTEVELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRTSIPNAVSEEGDEDDWISNKVMFKIGDLGHVTRISSPQVEEGDSRFLANEVLQENYSHLPKADIFALALTVVCAAGAEPLPRNGEQWHEIRQGRLPRIPQVLSQEVTELLRVMIHPDPERRPSAMELVKHSVLLSASRKSAEQLRIELNAEKFKNSLLQKELKKAQMAAKVAAEERALFTDRMATRSTTQSNRTSRLIGKKMNRSVSLTIY
Protein: Transmembrane protein (Q384E9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MINQTGFASALASRTALRHSALRMLPVRRDCFTLFSCRRCFSFSRARAPRVNLEEVRFDKQSARYAGTVFGVPTDAVVFYAKVGAAVVGVLIVFCIFVKGYGILARLNLGTVARLGFTSGFLSCMVLNAVFIGIARRFRISPNAVYNQSIAIVMQNEKVVQHLGPHPRTGDFKAYCQTGGFRLPLIRRIRSGSYELSDLLGLKPQKLQMMFVLRNQANGGEGFVTCEVRRETTGFLSSANTFRSLAVTLTDPSRSSARTIVLIGKPEDVVYRGLMNL
Protein: Serine/threonine-protein kinase sck2 (EC 2.7.11.1) (Q10364)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Protein kinase that is part of growth control pathway which is at least partially redundant with the cAMP pathway.
Interaction partners:
- Serine/threonine-protein kinase tor2
- Serine/threonine-protein kinase sck1
- cAMP-dependent protein kinase regulatory subunit
- Serine/threonine-protein kinase ksg1
- Tuberous sclerosis 2 protein homolog
- Serine/threonine-protein kinase tor1
- Small ribosomal subunit protein eS6B
- Small ribosomal subunit protein eS6A
- Serine/threonine-protein kinase psk1
- Uncharacterized protein C1739.01
Sequence:
MMNKWAKNWFGLSKKSVSTNSAKGSLPRSPLASIQTNQPVEEGEGGSLPSVSNLGPSSIDHPMEEFASDQSTVGNRNSNDILPEVDHEPSGYLKLQIGSLVLGGPHTDAALAMECSRLNQLFVVVQFGTTEFVSPPLKWESPGRDIGTSSRDSANVSRSSSMMSSHPIPTPAIQRTSSIPNPLTPSYVVFDVAKPVPIDVNIYDHGNNNEFVGRTYIHPSYNYGQFEQFCNSVEVSPAYNRMVDLRLSLNTVFQPLSQHSYGPDDFVPLKLIGKGTFGQVYLVRKKDTERVYAMKVLSKKVIVRRKEVAHTVGERDILVQTSAADSPFIVALRFSFQTPKDLYLVTDYMAGGELFWHLQKSVRFPEERAKFYIAELLLALQALHKRGIVYRDLKPENILLDVQGHIALCDFGLSKANLSVGTTTRTFCGTTDYLAPEVILDEAGYDMMVDFWSLGVLLYEMTCGWSPFYADNTQQLYKNIVFGKVRFPRGLLSVEARDLIKLLLNRNPKHRLGAHGDVEEVMKHPFFDGIDWKKLAAKEISPPFKPIVEGEIDVSNFDVEFTNKAIDRDFSSTDEMSTSAPLSSTVQNGFKGFTYIDASAMDEAFGYHNSNDSASSISSQDDYSKDNSDMDLNRANDEVFMGQIDP
Protein: Mitogen-activated protein kinase kinase 1 (AtMKK1) (MAP kinase kinase 1) (EC 2.7.12.2) (AtMEK1) (NMAPKK) (Q94A06)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: MEKK1, MKK1/MKK2 and MPK4/MPK6 function in a signaling pathway that modulates the expression of genes responding to biotic and abiotic stresses and also plays an important role in pathogen defense by negatively regulating innate immunity. Activates by phosphorylation the downstream MPK4. Acts redundantly with MKK2. MKK1-MPK6 module mediates abscisic acid (ABA)-dependent CAT1 expression with H(2)O(2) production and response to drought and salt stress. MKK1-MPK6 module is also involved in sugar signaling during the process of seed germination.
Interaction partners:
- Mitogen-activated protein kinase 4
- Mitogen-activated protein kinase kinase kinase 1
- Mitogen-activated protein kinase 6
- Mitogen-activated protein kinase 10
- Disease resistance protein SUMM2
- Mitogen-activated protein kinase kinase 2
- Mitogen-activated protein kinase 11
- Probable WRKY transcription factor 33
- Protein MKS1
- Mitogen-activated protein kinase 17
Sequence:
MNRGSLCPNPICLPPLEQSISKFLTQSGTFKDGDLRVNKDGIQTVSLSEPGAPPPIEPLDNQLSLADLEVIKVIGKGSSGNVQLVKHKLTQQFFALKVIQLNTEESTCRAISQELRINLSSQCPYLVSCYQSFYHNGLVSIILEFMDGGSLADLLKKVGKVPENMLSAICKRVLRGLCYIHHERRIIHRDLKPSNLLINHRGEVKITDFGVSKILTSTSSLANSFVGTYPYMSPERISGSLYSNKSDIWSLGLVLLECATGKFPYTPPEHKKGWSSVYELVDAIVENPPPCAPSNLFSPEFCSFISQCVQKDPRDRKSAKELLEHKFVKMFEDSDTNLSAYFTDAGSLIPPLAN
Protein: Oxidant-induced cell-cycle arrest protein 5 (A0A1D8PGP6)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Ras family GTPase
- Serine/threonine-protein kinase
- Serine/threonine protein kinase
- Bfa1p
- Tyrosine-protein phosphatase CDC14
- Protein phosphatase PP2A regulatory subunit B
- DNA damage-inducible protein 1
- Uncharacterized protein
- Mitotic regulator
- Spindle assembly checkpoint component MAD2
Sequence:
MEQELLLKGRKKDSIEQFISGSQLFLENGLSQLRYMVLVEGLSTPEGYDQCPYRSYVWSILCRVPPFPTEQYLQLLETSSQTLPDELLIKIKNDTFRTLMNDKKFHSKVNEESLIRILSCIGITTEVGYVQGLNVLLAPIAYVCHKSEPQAFAILHNLITKQIPLYITPNMEGVHTGLQLVDAVLKIIDPVLSDYLDSKFLKAKIYAFPSILTLCACTPPLKSVLKLWDFLFAYGTHINVLFVVAQLIICRSSILESEQPMKILRTWPNLEENEIIKLSLSFIPELPEKLYDLIARHGYDRKVPKELARFLEEK
Protein: TNFAIP3 interacting protein 2 (D6RGJ2)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MSRDPGSGGWEEAPRAAAALCTLYHEAGQRLRRLQDQLAARDALIARLRARLAALEGDAAPSLVDALLEQVARFREQLRRQEGGAAEAQMRQEIERLTERLEEKEREMQQLLSQPQHEREKEVVLLRRSMAEGERARAASDVLCRSLANETHQLRRTLTATAHMCQHLAKCLDERQHAQRNVGERSPDQSEHTDGHTSVQSVIEKLQEENRLLKQKVTHILAYKDDFMSERADRERAQSRIQELEEKVASLLHQVSWRQDSREPDAGRIHAGSKTAKYLAADALELMVPGGWRPGTGSQQPEPPAEGGHPGAAQRGQGDLQCPHCLQCFSDEQGEELLRHVAECCQ
Protein: Nuclear autoantigenic sperm protein (NASP) (P49321)
Organism: Homo sapiens (Human)
Function: Required for DNA replication, normal cell cycle progression and cell proliferation. Forms a cytoplasmic complex with HSP90 and H1 linker histones and stimulates HSP90 ATPase activity. NASP and H1 histone are subsequently released from the complex and translocate to the nucleus where the histone is released for binding to DNA.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q99MD9}. Nucleus {ECO:0000250|UniProtKB:Q99MD9}.
Interaction partners:
- Histone chaperone ASF1B
- Histone H4
- Histone H3.1
- Histone acetyltransferase type B catalytic subunit
- Histone chaperone ASF1A
- Histone H3.2
- Histone H3.3
- Histone H3.3C
- Histone-binding protein RBBP4
- Histone H3.1t
Sequence:
MAMESTATAAVAAELVSADKIEDVPAPSTSADKVESLDVDSEAKKLLGLGQKHLVMGDIPAAVNAFQEAASLLGKKYGETANECGEAFFFYGKSLLELARMENGVLGNALEGVHVEEEEGEKTEDESLVENNDNIDEEAREELREQVYDAMGEKEEAKKTEDKSLAKPETDKEQDSEMEKGGREDMDISKSAEEPQEKVDLTLDWLTETSEEAKGGAAPEGPNEAEVTSGKPEQEVPDAEEEKSVSGTDVQEECREKGGQEKQGEVIVSIEEKPKEVSEEQPVVTLEKQGTAVEVEAESLDPTVKPVDVGGDEPEEKVVTSENEAGKAVLEQLVGQEVPPAEESPEVTTEAAEASAVEAGSEVSEKPGQEAPVLPKDGAVNGPSVVGDQTPIEPQTSIERLTETKDGSGLEEKVRAKLVPSQEETKLSVEESEAAGDGVDTKVAQGATEKSPEDKVQIAANEETQEREEQMKEGEETEGSEEDDKENDKTEEMPNDSVLENKSLQENEEEEIGNLELAWDMLDLAKIIFKRQETKEAQLYAAQAHLKLGEVSVESENYVQAVEEFQSCLNLQEQYLEAHDRLLAETHYQLGLAYGYNSQYDEAVAQFSKSIEVIENRMAVLNEQVKEAEGSSAEYKKEIEELKELLPEIREKIEDAKESQRSGNVAELALKATLVESSTSGFTPGGGGSSVSMIASRKPTDGASSSNCVTDISHLVRKKRKPEEESPRKDDAKKAKQEPEVNGGSGDAVPSGNEVSENMEEEAENQAESRAAVEGTVEAGATVESTAC
Protein: Xylan O-acetyltransferase 3 (EC 2.3.1.-) (Protein trichome birefringence-like 9) (OsTBL9) (Q2QYW3)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Xylan acetyltransferase required for 2-O- and 3-O-monoacetylation of xylosyl residues in xylan. Catalyzes the 2-O-acetylation of xylan, followed by nonenzymatic acetyl migration to the O-3 position, resulting in products that are monoacetylated at both O-2 and O-3 positions (By similarity).
Subcellular location: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q2QYU2}; Single-pass type II membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MSKPQQQSPPSTTTTSPPPPPPSTPPPASSSRSLLSALRRSPVTTLVAAFFLLALFMYGEDVRTLAELSIDDYLYPDADFYNVSALPPLLLPPPTCDLSRGRWVFDNTSLPAYREKECTFLTKQVSCLANGRPDDLWQYWRWQPNNCSLPTFDARRFMEKMRGKRMMFVGDSLNRNQWESLVCLVQPILSKGRKKIVKRGSFNIFYAKEYRATLEFYWAPFLVESNSDNPNFHHIDQRIISPERIESHANNWKDVDYLIFNTYIWWMNNEDIKVRRPNSTSWSDHDEVPRIETYGRVFKTWSTWLEQNVDPARTSVFFMTISPLHNSPAQWGNPNGIKCVKETLPVLNYTKPLDLNHDMRMYDLVAKVAKNMKNVPVSLIDITRMSDYRKDAHTSLYSIRQGKLLTPEQKADPQKYADCIHWCLPGVPDVWNQILYTRILSKSSPPSTHPSLPPQ
Protein: Nuclear migration protein nudC (Nuclear distribution protein C homolog) (Q7ZVD2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm, cytoskeleton, spindle {ECO:0000256|ARBA:ARBA00004186}. Midbody {ECO:0000256|ARBA:ARBA00004214}.
Interaction partners:
Sequence:
MGDDDERFDGMLLAMAQQHEGGVQELVNTFFSFLRRKTDFFTGGESGAPEKLVKEAFAHHNQLALQVQKEKQSRQEKERKEKAERAAKLKEEEMKKRKIDAEEPRIKELTDEEAERLQSQLQTKQEEPKNSEVAEKTDADSKDKKGSDSEGEEDEKDKDKVKPNAGNGADLPNYRWTQSLSEVDLVVPFDVSFRLKGKDVVVDVQRRTLKVGLKGHPPLIDGQLFNEVKVEESSWLIEDGKVVTIHFEKINKMEWWNKLVTTDPEINTKKICPENSKLSDLDGETRSMVEKMMYDQRQKSMGLPTSEEQKKQDILKKFMAQHPEMDFSKAKFS
Protein: Pectinesterase B (PE B) (EC 3.1.1.11) (Pectin methylesterase B) (Q47474)
Organism: Dickeya dadantii (strain 3937) (Erwinia chrysanthemi (strain 3937))
Function: Probably involved in the degradation of methylated oligogalacturonides present in the periplasm. More active on methylated oligogalacturides than on pectin.
Subcellular location: Cell outer membrane {ECO:0000269|PubMed:8830237}; Lipid-anchor {ECO:0000269|PubMed:8830237}. Note=Probably active in the periplasm. {ECO:0000305|PubMed:8830237}.
Interaction partners:
- Pectate lyase C
- Pectinesterase A
- Pectate lyase B
- Pectate lyase A
- Pectate disaccharide-lyase
- Pectate lyase D
- Pectate lyase E
- Exopolygalacturonate lyase PelX
- Exo-poly-alpha-D-galacturonosidase
- Exo-poly-alpha-D-galacturonosidase
Sequence:
MSLTHYSGLAAAVSMSLILTACGGQTPNSARFQPVFPGTVSRPVLSAQEAGRFTPQHYFAHGGEYAKPVADGWTPTPIDTSRVTAAYVVGPRAGVAGATHTSIQQAVNAALRQHPGQTRVYIKLLPGTYTGTVYVPEGAPPLTLFGAGDRPEQVVVSLALDSMMSPADYRARVNPHGQYQPADPAWYMYNACATKAGATINTTCSAVMWSQSNDFQLKNLTVVNALLDTVDSGTHQAVALRTDGDRVQLENVRLLSRQDTFFVNTSDRQNSYVTDHYSRAYIKDSYIEGDVDYVFGRATAVFDRVRFHTVSSRGSKEAYVFAPDSIPSVKYGFLVINSQLTGDNGYRGAQKAKLGRAWDQGAKQTGYLPGKTANGQLVIRDSTIDSSYDLANPWGAAATTDRPFKGNISPQRDLDDIHFNRLWEYNTQVLLHE
Protein: Tetratricopeptide repeat domain 39A (E9PAZ4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MTALDLFLTNQFSEALSYLKPRTKESMYHSLTYATILEMQAMMTFDPQDILLAGNMMKEAQMLCQRHRRKSSVTDSFSSLVNRPTLGQFTEEEIHAEVCYAECLLQRAALTFLQDENMVSFIKGGIKVRNSYQTYKELDSLVQSSQYCKGENHPHFEGGVKLGVGAFNLTLSMLPTRILRLLEFVGFSGNKDYGLLQLEEGASGHSFRSVLCVMLLLCYHTFLTFVLGTGNVNIEEAEKLLKPYLNRYPKGAIFLFFAGRIEVIKGNIDAAIRRFEECC
Protein: Protein lin-52 (Abnormal cell lineage protein 52) (Q10120)
Organism: Caenorhabditis elegans
Function: Synthetic multivulva class B (synMuvB) protein. SynMuvB proteins are required to repress the induction of vulval development by Ras signaling and probably act by forming the multiprotein DRM complex that represses transcription. In association with the zinc finger protein ztf-11, negatively regulates the expression of non-neuronal genes during neurogenesis.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Protein lin-9
- Protein lin-54
- Retinoblastoma-like protein homolog lin-35
- Probable histone-binding protein lin-53
- Uncharacterized protein
- Transcription factor dpl-1
- E2F/DP family winged-helix DNA-binding domain-containing protein
- Rabphilin-1
- Probable histone-binding protein rba-1
- Protein lin-61
Sequence:
MSRPLGFIGYEFGDDEMFVQQMIEKKSNAEQAKMLEQQKKMLECTETMPEESEPVPMKCLDFEEAFQSESVSKGYESPYKNISFLKEDAVTVNTMSHCPADDIAKLIRNIQNSVYTLGIEEARQCRRGKLLNVLKPTGSASPRYLQPTPPKNVAEETTGSQ
Protein: Protein FAM204A (Q9H8W3)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MWSGLLPPGLNESDAESNSEDEATLENSGLNLQEDKEDESIRKTEIIDFSTDEPKTETESNVNAYEECPSGIPIDMWNKFQELHKKHSEQKSTTSRFRGKRRKRSRKDKLKNEKELHSEPSSNETQWKELTQYFGVNDRFDPPVKRKKVEKSGLEKRIDQAVEEWNIEKAEELSNQLATRELGVKIAKAVACHNFVKAKKEVENSQAARKKKKLAWGFEAKKRWETKSNMGYM
Protein: Geranylgeranyl transferase type-1 subunit beta (EC 2.5.1.59) (Geranylgeranyl transferase type I subunit beta) (O18197)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MCDISTEDQLLEFARKAAESGDQTQTFEFKKHIGFLIRHLNVFPQPYNTLETSRNTIFLFAISSLDLLGELDNLLTPERRQAYIDWIYGLQFTNGNVCGFRGSHSCENSGYDEANLAQTYSALLSLAILGDDLKKVDRKAILKTVKTAQRDNGCFWSQGVGSESDMRFVFCAVAISHILDGDKEQTIDWTKLAGFLRQSLNIDGGIGQAPGDESHGGSTFCAIASLALSNRLWTEEVLTRRDIDRLIRWAIQKQDIGFHGRAHKPDDSCYAFWIGATLKILNAYHLVSKQHLREFLMICQHPHIGGFCKYPEPGGYSDILHTYFSIAALSLLGEPAVNPVHPSLNVSMRVAERIARLQFD
Protein: Alpha/beta-Hydrolases superfamily protein (Q9T0G1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Monogalactosyldiacylglycerol synthase 1, chloroplastic
- Digalactosyldiacylglycerol synthase 1, chloroplastic
Sequence:
MSAVSCSTASSSGGCAFRFRSKTSIHSPNFIRIGTNSQSDRFCNHRLELVHGTRKVKGASVRMALVEERQSTSKDVAEPPRVLAYDLVQGALVKWRWKDDKSVPDTPTAVLLHGILGSGKNWGTFARRLAHEFPTWQFLLVDLRCHGDSTSLKKRGPHSVATTASDVLKLVGQLRLTPRVLVGHSFGGKVVLSMVEQAAKPLPRPVRAWVLDATPGKVRAGGDGEDHPRELISFLRKLPKVVLSKREVLKALINEGFSNDVAQWVITNLRPTGPSASSFSWTFDLDGIAELYQSYEETNLWNFVENLPRGVHVNFLKAERSLHRWALEDLQRIHAAEELASEEGGGVEMHVLEDAGHWVHTDNPDGLFRILSSSFQVLRA
Protein: D-mannonate dehydratase CC0532 (ManD) (EC 4.2.1.8) (Q9AAR4)
Organism: Caulobacter vibrioides (strain ATCC 19089 / CIP 103742 / CB 15) (Caulobacter crescentus)
Function: Catalyzes the dehydration of D-mannonate. Has no detectable activity with a panel of 70 other acid sugars (in vitro).
Interaction partners:
- Mannitol 2-dehydrogenase
- SAF domain-containing protein
- D-mannonate dehydratase CC2812
- 2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase
- 2-dehydro-3-deoxygluconokinase
- Uronate isomerase
- Carbohydrate kinase, pfkB family
- Ribulose-phosphate 3-epimerase
- Ribose-5-phosphate isomerase A
- 4-deoxy-L-threo-5-hexosulose-uronate ketol-isomerase
Sequence:
MLKIIDAKVIVTCPGRNFVTLKITTEDGITGVGDATLNGRELSVVSFLQDHMVPSLIGRDAHQIEDIWQFFYRGSYWRGGPVAMTALAAVDMALWDIKGKVAGLPVYQLLGGACRTGVTVYGHANGETIEDTIAEAVKYKAMGYKAIRLQTGVPGLASTYGVSKDKMFYEPADNDLPTENIWSTAKYLNSVPKLFERAREVLGWDVHLLHDVHHRLTPIEAARLGKDLEPYRLFWLEDSVPAENQAGFRLIRQHTTTPLAVGEIFAHVWDAKQLIEEQLIDYLRATVLHAGGITNLKKIAAFADLHHVKTGCHGATDLSPVTMAAALHFDMSITNFGLQEYMRHTPETDAVFPHAYTFSDGMLHPGDKPGLGVDIDEDLAAKHPYKRAYLPVNRLEDGTMFNW
Protein: Ashwin (Q9I8G4)
Organism: Xenopus laevis (African clawed frog)
Function: May regulate cell survival and anterior-posterior patterning.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9BVC5}.
Interaction partners:
Sequence:
MAKAVGSAGILVKESALLLHPELLSRDFLLLSLERRNIPVEDALNNKEKLTEIFVQHAMPLPQRDLPRNRWGRMMESKRGENKIATVLKSAGTEGGRKRPPIVFDGCSTSTTIKVKRTENGDASQRLNPSPKESTNSTQNSNPAPRLGSPTPNKEAKVATTGNHGQLDSLPVTDSALVSPKSAKLQQSMIINAVKLKRNAPKEEFDVANDTKPTEAKKKIQHVTWP