wanglab/gogpt-training-data huggingface dataset:
Protein: Microtubule-associated protein 7 (A0A0G2KB52)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Transient receptor potential cation channel subfamily V member 4
Sequence:
MDSGGSCFPWSKAEWIVKPHEDLDSLYFLAFASDGYKIQGKRPAPSRPTSTLSGQTSNHSGNKPDPPPVLRVDDRQRLARERREEREKQLAARETVWLEREERARQHYERHLEARKKKLEDQRLKEERRRAAVEEKRRQRLEEDKERHEAVVRRTMERSQKPKQKYNRWSWGSPLHGSSSIHSGDPDRRSVSTMNLSKHVDPVISKRLSSSSATLLNSPDRARRLQLSPWESSVVSRLLTPTHSFLARSKSTAALSGDTASCSPITTPFKTAHSRNPVDRPKLFITPPEGSARRRTIHGISSYKREREHIPFHVSPGVRRTLSPSNLKARSPAPARLWPPSKSMPHLPGTPRPASSLTPGPVRAAASSSSPGNIRPVKREVKVEPEKKDPEKKVTNDPTIKGRVPLVKVEEGTVEEGTPVKPPDPAVPAPTPATDPAPAPPSPSSVSVGVIPKTSAGTTDPEEATRLLAEKRRLAREQREKEERERKEKEELERQKIEELARRVAEERSRREEEARRLEAEQARKREELALRLAEEERERWEREEVERAQKQKEEEARAREEAEKARQEREKHFQKEEQERLERKKRLEEIMRRTRRTETADKKTTGQSNGDMVKGVLAGETEVSALPGVNSPGHVESAGSTHGVALQQSKVTIESSPDLEKQPNENGMSTQNENFEEIINLPVGSKASRLDVSNENPEIPLKPILAFNDEGTLGPLPQVDGVQTQQTTEVI
Protein: GTP-binding protein (GTPase cRhoA) (RhoA GTPase) (O93467)
Organism: Gallus gallus (Chicken)
Interaction partners:
- Rho-associated protein kinase
- Actin, cytoplasmic 1
- Rho associated coiled-coil containing protein kinase 2
- Uncharacterized protein.
- Uncharacterized protein.
- Uncharacterized protein.
- Rho GTPase activating protein 35.
- Rho guanine nucleotide exchange factor 11.
- Serine/threonine-protein kinase N2
- Rhotekin.
Sequence:
MAAIRKKLVIVGDGACGKTCLLIVFSKDQFPEVYVPTVFENYVADIEVDGKQVELALWDTAGQEDYDRLRPLSYPDTDVILMCFSIDSPDSLENIPEKWTPEVKHFCPNVPIILVGNKKDLRNDEHTRRELAKMKQEPVKPEEGRDMANRIGAFGYMECSAKTKDGVREVFEMATRAALQARRGKKKSGCLLL
Protein: CACN subunit beta associated regulatory protein (F1MAS1)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Zinc finger protein 316
Sequence:
MQPTATMATAAATTATVALTTSWDNATNRPTAEPDPILDNYVLLVVVMSLFVGGTLVVLSGVLLLCKRCWEVHQRFNRAMEETEKTTTTYLDNGTHPIQDPDCRGEDPEGQDTETERFLATTSTGRRVSFNEAALFEQSRKAQDKGRRYTLTEGDFHHLKNARLTHLHLPPLKIATIHECDSGEASAAATPHPHPASTPKDSLAIFQPPGKSLTGHSVGPSSALPGDPYSSVDFSEISPSASSDSGEGTSLDAGTRGTKAAGPETAPGEMGTGSSGAGTVLQFFTRLRRHASLDGASPYFKVKKWKLESSQRASSLDTRGSPKRHHFQRQRAASESMEQEGDIPHADFIQYIASAGDSVAFPPPRPFLASPTSPPPTLGRLEAAEAAGGGSPETPPEHGISLGPEHAQQQDPQQEQDAEHAQCSYRDLWSLRASLELHAATASDHSSSGNDRDSVRSGDSSGSGSGGGGAAPAFPPPPESPPALRPKDGEARRLLQMDSGYASIEGRGAGDEVSELPAPARSPPRSPRAWPRRPRRDYSIDEKTDALFHEFLRHDPHFDDAPRHRARAHPHTHARKQWQQRGRQHSDPGGARVATPPGATRPTRAPLRRGDSVDCPPEGRAPPITGDDPSIPVIEEEPGGGGSGCPGSGLCVEPAGALLDKLAASLDERLFSPRLAEPVASSPVLIVAAAAPTSPDHSPA
Protein: pH-regulated antigen PRA1 (58 kDa fibrinogen-binding mannoprotein) (P87020)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Cell surface protein involved in the host-parasite interaction during candidal infection. With MP65, represents a major component of the biofilm matrix. Sequesters zinc from host tissue and mediates leukocyte adhesion and migration. As a surface protein, binds the two human complement regulators CFH and CFHR1, as well as plasminogen PLG, mediates complement evasion and extra-cellular matrix interaction and/or degradation. As a released protein, enhances complement control in direct vicinity of the yeast and thus generates an additional protective layer which controls host complement attack, assisting the fungus in escaping host surveillance. Binds to host fluid-phase C3 and blocks cleavage of C3 to C3a and C3b, leading to inhibition of complement activation. Mediates also human complement control and complement evasion through binding to C4BPA, another human complement inhibitor, as well as through binding to host integrin alpha-M/beta-2. Decreases complement-mediated adhesion, as well as uptake of C.albicans by human macrophages.
Subcellular location: Secreted {ECO:0000269|PubMed:1398933, ECO:0000269|PubMed:17277107, ECO:0000269|PubMed:17905924, ECO:0000269|PubMed:19098294, ECO:0000269|PubMed:22074954, ECO:0000269|PubMed:7768591, ECO:0000269|PubMed:8300229, ECO:0000269|PubMed:8759797, ECO:0000269|PubMed:9440517}. Note=Found primarily on the cell surface of filamentous forms and enriched at hyphal tips. {ECO:0000269|PubMed:8300229}.
Interaction partners:
- Zinc-regulated transporter 1
- Low-affinity Zn
- Csr1p
Sequence:
MNYLLFCLFFAFSVAAPVTVTRFVDASPTGYDWRADWVKGFPIDSSCNATQYNQLSTGLQEAQLLAEHARDHTLRFGSKSPFFRKYFGNETASAEVVGHFDNVVGADKSSILFLCDDLDDKCKNDGWAGYWRGSNHSDQTIICDLSFVTRRYLTQLCSSGYTVSKSKTNIFWAGDLLHRFWHLKSIGQLVIEHYADTYEEVLELAQENSTYAVRNSNSLIYYALDVYAYDVTIPGEGCNGDGTSYKKSDFSSFEDSDSGSDSGASSTASSSHQHTDSNPSATTDANSHCHTHADGEVHC
Protein: Large ribosomal subunit protein bL20c (50S ribosomal protein L20, chloroplastic) (P0C448)
Organism: Oryza sativa subsp. indica (Rice)
Function: Binds directly to 23S ribosomal RNA and is necessary for the in vitro assembly process of the 50S ribosomal subunit. It is not involved in the protein synthesizing functions of that subunit (By similarity).
Subcellular location: Plastid, chloroplast.
Interaction partners:
- Uncharacterized protein
- 50S ribosomal protein L31
- Large ribosomal subunit protein bL33c
- 50S ribosomal protein L21
- Small ribosomal subunit protein uS2c
- Small ribosomal subunit protein uS14c
- Small ribosomal subunit protein uS12cz/uS12cy
- Large ribosomal subunit protein uL3m
- Large ribosomal subunit protein uL16c
- Uncharacterized protein
Sequence:
MTRVPRGYIARRRRAKMRSFASNFRGAHLRLNRMITQQVRRAFVSSHRDRVRQKRDFRRLWISRINAATRIHKVFDNYSKLIHNLYKKELILNRKILAQVAVLNPNNLYTISNKIKIIN
Protein: tRNA uridine(34) hydroxylase (EC 1.14.-.-) (ORF39.9) (tRNA hydroxylation protein O) (P24188)
Organism: Escherichia coli (strain K12)
Function: Catalyzes oxygen-dependent 5-hydroxyuridine (ho5U) modification at position 34 in tRNAs, the first step in 5-carboxymethoxyuridine (cmo5U) biosynthesis. May be part of an alternate pathway, which is able to bypass cmo5U biogenesis in a subset of tRNAs under aerobic conditions.
Interaction partners:
- Dual-specificity RNA pseudouridine synthase RluA
Sequence:
MPVLHNRISNDALKAKMLAESEPRTTISFYKYFHIADPKATRDALYQLFTALNVFGRVYLAHEGINAQISVPASNVETFRAQLYAFDPALEGLRLNIALDDDGKSFWVLRMKVRDRIVADGIDDPHFDASNVGEYLQAAEVNAMLDDPDALFIDMRNHYEYEVGHFENALEIPADTFREQLPKAVEMMQAHKDKKIVMYCTGGIRCEKASAWMKHNGFNKVWHIEGGIIEYARKAREQGLPVRFIGKNFVFDERMGERISDEIIAHCHQCGAPCDSHTNCKNDGCHLLFIQCPVCAEKYKGCCSEICCEESALPPEEQRRRRAGRENGNKIFNKSRGRLNTTLCIPDPTE
Protein: Small ribosomal subunit protein uS12 (40S ribosomal protein S23) (Q8T3U2)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P62266}. Cytoplasm {ECO:0000305|PubMed:23636399}. Rough endoplasmic reticulum {ECO:0000250|UniProtKB:Q6SA96}. Note=Detected on cytosolic polysomes (By similarity). Detected in ribosomes that are associated with the rough endoplasmic reticulum (By similarity). {ECO:0000250|UniProtKB:P62266, ECO:0000250|UniProtKB:Q6SA96}.
Interaction partners:
- 40S ribosomal protein S15
- Large ribosomal subunit protein eL30
- Ribosomal protein S30, isoform A
- Large ribosomal subunit protein uL16
- Small ribosomal subunit protein uS2
- Large ribosomal subunit protein eL14
- Large ribosomal subunit protein uL3
- Large ribosomal subunit protein eL13
- Large ribosomal subunit protein uL5
- Small ribosomal subunit protein eS19A
Sequence:
MGKPRGLRTARKHVNHRRDQRWADKDYKKAHLGTRWKANPFGGASHAKGIVLEKVGVEAKQPNSAIRKCVRVQLIKNGKKITAFVPRDGSLNYIEENDEVLVAGFGRKGHAVGDIPGVRFKVVKVANVSLLALYKEKKERPRS
Protein: Ribosomal protein S6 kinase (EC 2.7.11.1) (E9PGT3)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MPLAQLKEPWPLMELVPLDPENGQTSGEEAGLQPSKDEGVLKEISITHHVKAGSEKADPSHFELLKVLGQGSFGKVFLVRKVTRPDSGHLYAMKVLKKATLKVRDRVRTKMERDILADVNHPFVVKLHYAFQTEGKLYLILDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALGLDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKEAIDHEKKAYSFCGTVEYMAPEVVNRQGHSHSADWWSYGVLMGKDRKETMTLILKAKLGMPQFLSTEAQSLLRALFKRNPANRLGSGPDGAEEIKRHVFYSTIDWNKLYRREIKPPFKPAVAQPDDTFYFDTEFTSRTPKDSPGIPPSAGAHQLFRGFSFVATGLMEDDGKPRAPQAPLHSVVQQLHGKNLVFSDGYVVKETIGVGSYSECKRCVHKATNMEYAVKVIDKSKRDPSEEIEILLRYGQHPNIITLKDVYDDGKHVYLVTELMRGGELLDKILRQKFFSEREASFVLHTIGKTVEYLHSQGVVHRDLKPSNILYVDESGNPECLRICDFGFAKQLRAENGLLMTPCYTANFVAPEVLKRQGYDEGCDIWSLGILLYTMLAGYTPFANGPSDTPEEILTRIGSGKFTLSGGNWNTVSETAKDLVSKMLHVDPHQRLTAKQVLQHPWVTQKDKLPQSQLSHQDLQLVKGAMAATYSALNSSKPTPQLKPIESSILAQRRVRKLPSTTL
Protein: Glycine--tRNA ligase, mitochondrial 1 (EC 6.1.1.14) (Diadenosine tetraphosphate synthetase) (Ap4A synthetase) (EC 2.7.7.-) (Glycyl-tRNA synthetase 1) (GlyRS-1) (O23627)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the ATP-dependent ligation of glycine to the 3'-end of its cognate tRNA, via the formation of an aminoacyl-adenylate intermediate (Gly-AMP). Also produces diadenosine tetraphosphate (Ap4A), a universal pleiotropic signaling molecule needed for cell regulation pathways, by direct condensation of 2 ATPs. Thereby, may play a special role in Ap4A homeostasis.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:11278923}. Cytoplasm, cytosol {ECO:0000269|PubMed:11278923}.
Interaction partners:
- Glycine--tRNA ligase, chloroplastic/mitochondrial 2
- Putative glycine--tRNA ligase, cytoplasmic
- Class II aaRS and biotin synthetases superfamily protein
- Arginine--tRNA ligase, chloroplastic/mitochondrial
- Methionine--tRNA ligase, cytoplasmic
- At1g61690
- RING/FYVE/PHD-type zinc finger family protein
- Valine--tRNA ligase, mitochondrial 1
- 2'-phosphotransferase
- Omega-amidase, chloroplastic
Sequence:
MRIFSTFVFHRRQQIFNLRQFQTTTILRNPISIAPIQIPMDATEQSLRQSLSEKSSSVEAQGNAVRALKASRAAKPEIDAAIEQLNKLKLEKSTVEKELQSIISSSGNGSLNREAFRKAVVNTLERRLFYIPSFKIYSGVAGLFDYGPPGCAIKSNVLSFWRQHFILEENMLEVDCPCVTPEVVLKASGHVDKFTDLMVKDEKTGTCYRADHLLKDYCTEKLEKDLTISAEKAAELKDVLAVMEDFSPEQLGAKIREYGITAPDTKNPLSDPYPFNLMFQTSIGPSGLIPGYMRPETAQGIFVNFKDLYYYNGKKLPFAAAQIGQAFRNEISPRQGLLRVREFTLAEIEHFVDPENKSHPKFSDVAKLEFLMFPREEQMSGQSAKKLCLGEAVAKGTVNNETLGYFIGRVYLFLTRLGIDKERLRFRQHLANEMAHYAADCWDAEIESSYGWIECVGIADRSAYDLRAHSDKSGTPLVAEEKFAEPKEVEKLVITPVKKELGLAFKGNQKNVVESLEAMNEEEAMEMKATLESKGEVEFYVCTLKKSVNIKKNMVSISKEKKKEHQRVFTPSVIEPSFGIGRIIYCLYEHCFSTRPSKAGDEQLNLFRFPPLVAPIKCTVFPLVQNQQFEEVAKVISKELASVGISHKIDITGTSIGKRYARTDELGVPFAITVDSDTSVTIRERDSKDQVRVTLKEAASVVSSVSEGKMTWQDVWATFPHHSSAAADE
Protein: Glycosyltransferase, putative (EC 2.4.1.-) (Q388S6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004389}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004389}.
Interaction partners:
- Dolichol-phosphate mannosyltransferase subunit 1
- Dolichol phosphate-mannose biosynthesis regulatory protein
- Alpha-1,3/1,6-mannosyltransferase ALG2
- UDP-N-acetylglucosamine transferase subunit ALG13
- mannose-1-phosphate guanylyltransferase
- Cytoplasmic tRNA 2-thiolation protein 2
- GDP-mannose 4,6-dehydratase
- Probable methyltransferase BMT2 homolog
Sequence:
MFSYDDLVWTISFPTFCFLAIWFSITVSLVVRAESGRKKWKQAREHIAEIESRGDKATGAQHRNSKAVLRRVVVVVGGDFARSPRMQYHALSLAKCGMFQEVVLVGFDMGNRLSEELKLREKKKNIDGSYDDSSVEKFECVVETAYLIPPITPPLWFRILFPHPKLHWLASTFYRACACAVVFTWVLVRASMMFVNSRGQLMLVDLILMQSPPAVPFVPVVKYIVQPCAFVANAVTYYCIILTGSWLSTALKEITEGIKLQRQRQLPVEKNPTKKGPTNSNSCPKFVLSPALVVDWHNFGYTVLRSDGRPAVAVWLYRLLECNLCFGDRNITVSKAMRRALLDVSKQSKVANRVDDVWVMYDCAPSFFGLVPRSRFVQEVIRPVMSAHSQDGEEVIGCSLPPDWVLQSTAATDSRGIFIVASTSWTPDDDYTMVVEALKQVDEKLQECSQGKDSKPTASKSVWLLVTGKGVARKRFEMAVAEAHLSSLVVVTTMYMQSYKHYAMALGAADVGLCMHNSSSGLDLPMKAVDMLGSGLPVVALRYKSLHELLDDKRGWFFSNAEELGQVMWKQLILTNGPLLEKRRQVAQNEPGTWDENWGEVLMPLLANLL
Protein: Mitogen-activated protein kinase sakA (MAP kinase hog1) (EC 2.7.11.24) (Q4WSF6)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Function: Mitogen-activated protein kinase involved in a signal transduction pathway that is activated by changes in the osmolarity of the extracellular environment. Controls osmotic regulation of transcription of target genes (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:26878695, ECO:0000269|PubMed:27538790}. Nucleus {ECO:0000269|PubMed:26878695, ECO:0000269|PubMed:27538790}. Note=Translocates to the nucleus upon osmotic stress and cell wall damage. {ECO:0000269|PubMed:26878695, ECO:0000269|PubMed:27538790}.
Interaction partners:
- Basic leucine zipper
- mitogen-activated protein kinase kinase
- protein-tyrosine-phosphatase
- Protein phosphatase 2C, putative
- High osmolarity signaling protein sho1
- Mitogen-activated protein kinase mpkC
- Protein arginine N-methyltransferase
- Calmodulin
- Transcription factor
- F-box domain-containing protein
Sequence:
MAEFVRAQIFGTTFEITSRYTDLQPVGMGAFGLVCSARDQLTGQPVAVKKIMKPFSTPVLSKRTYRELKLLKHLRHENIISLSDIFISPLEDIYFVTELLGTDLHRLLTSRPLEKQFIQYFLYQILRGLKYVHSAGVVHRDLKPSNILINENCDLKICDFGLARIQDPQMTGYVSTRYYRAPEIMLTWQKYDVEVDIWSAGCIFAEMLEGKPLFPGKDHVNQFSIITELLGTPPDDVIQTICSENTLRFVKSLPKRERQPLANKFKNADPEAVDLLERMLVFDPKKRIRAGEALAHEYLSPYHDPTDEPEAEEKFDWSFNDADLPVDTWKIMMYSEILDFHNIDQGNDAGQVLMEGGVAQAQQNYA
Protein: LIM domain containing preferred translocation partner in lipoma (C9JUT4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSHPSWLPPKSTGEPLGHVPARMETTHSFGNPSISVSTQQPPKKFAPVVAPKPKYNPYKQPGGEGDFLPPPPPPLDDSSALPSISGNFPPPPPLDEEAFKVQGNPGGKTLEERRSSLDAEIDSLTSILADLECSSPYKPRPPQSSTGSTASPPVSTPVTGHKRMVIPNQPPLTATKKSTLKPQPAPQAGPIPVAPIGTLKPQPQPVPASYTTASTSSRPTFNVQVKSAQPSPHYMAAPSSGQIYGSGPQGYNTQPVPVSGQCPPPSTRGGMDYAYIPPPGLQPEPGYGYAPNQGRYYEGYYAAGPGYGGRNDSDPTYGQQGHPNTWKREPGYTPPGAGNQNPPGMYPVTGPKKTYITDPVSAPCAPPLQPKGGHSGQLGPSSVAPSFRPEDELEHLTKKMLYDMENPPADEYFGEWGLELTSEVTILL
Protein: LP03286p (Q960J1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MESDKVAASRALTQNVEMKNQLDELQQRFVQLTNDKAELVIRLDSEEFANREIRQNYNSMEQKLQANEERFKFKDEEMIRLSHENVELQRQQLMLQQQLDRLRHYEAKAYHAGEETEKENGADAPENEAEEAKEVGLLHNHSHDHSHQHSDGHCHDNDHDHSHEHNHHNAGDHGHPHDHPHDHTHDHSHSHPHDHQHDHPHDHGQNHAHRQAAETLPTAEAVERLQSRFTTLISQVADLTEEKHSLEHLVLQLQSETETIGEYIALYQTQRRMLKQREYEKAAQMRLLQAEREQLREKIEALNKLVVSLGVELPADAAQAKQPEAAAGSEHTPGEGENSQQIINKIQDIISEIKENTEQPSHNHAGDHLNCCMGKFEVV
Protein: Polycomb protein sop-2 (Suppressor of pal-1 protein 2) (Q965H3)
Organism: Caenorhabditis elegans
Function: Polycomb group (PcG) protein. PcG proteins act by forming multiprotein complexes, which are required to maintain the transcriptionally repressive state of homeotic genes throughout development. PcG proteins are not required to initiate repression, but to maintain it during later stages of development. Also required to repress expression of other genes and for localization of sor-1. Binds RNA.
Subcellular location: Nucleus {ECO:0000269|PubMed:12791274, ECO:0000269|PubMed:15107848}. Note=Forms subnuclear bodies.
Interaction partners:
- Sop-2-related protein 1
- Homeobox protein egl-5
- Sop-2-related protein 3
Sequence:
MSSNLTSNEMSSTSAIVEPPEAVKGNERDKSTRRSTSQVVRPEKHEVENALEDQCSSSSLPKEAQYYAKLDKKLEGKDPRSQFYEAVRLSADIFAHKFEKAVCSRQTFEPTNSIIKVLNTAEEEMLHEKVVPLPVSSKLQYYLNRGRYDTIFDRDEQLQRTADPMADEPDHVEKRVTSILEQASREMEEGEVEPVFYDGSDEDQELPIDLGAMRNLQRTNKFAARSSRMAARRGGRPGYRGAFRGAARGAPSRRPAPAAEVAPETPVAAPMAPAAPAAPATPEAAPAAEVMDTSIATEMPQESAVDLSNVSAATEMDTSKEGEASRPTSEKKKKIRTTEMDRLMSMDLGPKDGGRVGELGHMWPESRRRPAAPLPETPAAQPRKSLPRRAAEKKKPEDSDAAEEQEVEMEVDNDASTSTPRNARGGRGGGNRRGSRRGQKRTSGGSGKLVEPKKEPVDEPAEKIPKRSEAAPEVPATATTKEAPPSTSSSPPDAPATPATPASSDSRDSPRKIRAMIFSLTGSPPESETPPVLQQEQVISTAAPTAGRHPNIIQQVPHINRIPPQPLRRLTAPQAPPASQPEEPPVQQTVPVVKVELASAPAPIVRDPQSTEPVPPAMPTLVENNHEATLILPPNKTSDYTRWNAQDLINWVRLLITNNVDSTIAIMVREEFDGETLACLVLDDDFRKEVPIPYGHYKKMKIYGTEVLNHYRTEKYQADLRKFHEELAAWKAQQR
Protein: B9 domain-containing protein 1 (Q21191)
Organism: Caenorhabditis elegans
Subcellular location: Cytoplasm, cytoskeleton, cilium basal body {ECO:0000256|ARBA:ARBA00004120}.
Interaction partners:
- B9 domain-containing protein 2
- MecKel-Gruber Syndrome
- Transmembrane protein 231
- Meckelin
- Nephrocystin-1-like protein
- Transmembrane protein 107
- NePHronoPhthisis
- TMEM
- Transmembrane protein 237 homolog
- MecKel-Gruber Syndrome
Sequence:
MEKADSIVLTIHGNVRTTEFPEESNVCVKLSTVATGDWKIINGETVSLSSFSFRGADNQIFIDLPFECGLKGSSPFMWPRLVLNCFSKDHSGKDCVTGYGMLPIPTEPGKHVCRVHCFLPEPSSTVQQLIAKLRRVNAEFVDPMLPANADGRYACRTSTKGYVDLEINVSIKCSDTAYKFTSTSTEIKSSNSHATNNVSTTIADLAGIEAVGNEETFNAQEDNDEESKR
Protein: Ent-atiserene synthase KSL4, chloroplastic (EC 4.2.3.185) (Kaurene synthase 4) (IrKSL4) (A0A1Z3GBK8)
Organism: Isodon rubescens (Rabdosia rubescens)
Function: Involved in the biosynthesis of ent-kaurene diterpenoids natural products such as oridonin, miltiradiene, eriocalyxin B and nezukol, known to exhibit antitumor, anti-inflammatory and antibacterial activities. Catalyzes the conversion of ent-copalyl diphosphate (ent-CPP) to ent-atiserene.
Subcellular location: Plastid, chloroplast {ECO:0000255}.
Interaction partners:
Sequence:
MGIVALILIKAAMSLILSSFPLFRSSRSSPASASLAGSGLPKTTPPKTASLQSHSPMFEETKGRIAKLFKKNEVCISTYDTAWVGMVPSPFSSDQPCFPDSLFWLLDNQCPDGSWAQPHHHSHSHSPSLLNKDVLSSTLASILALHKWGLGQHHIAKGLHFLELNFASATDNSQITPLGFDIVFPAMLDHAADLSLNLRLDPTTLNDLMNRRDLELQRCTENGSAETEVYMAYIGEGMGKLHDWESVMKYQRKNGSLFNSPSTTAAAFIALRNSDCLNYLYSALNKFGSAVPAVYPLDIYSQLCIVDNLERLGISRFFSTEIQSVLDETYRCWLQGDEEIIMDASTCGLAFRTLRMNGYKVTSDSFIKVVQDCFSSPGHMRDVNTTLELYRASELMLYPHEIELEKQNSRLRSLLEQELSGGSIQSSQLNAEVKQALDYPFYAALDRMVKKKTIEHYNIDDSRILKTSFRLPSFGNKDLLSLSVQDYNRCQAIHREELREFDRWFVENRLDELEFARHKSAYYYCYFAAAATFFAPELSDARMSWAKNALMTTMVDDLFDVTGSVEEMKNLIQLVELWDVDVSTECCSHKVQILFSALKRTICEVGDRAHQLQGRSIRSHIIVIWLDLLHSMMKEVEWTRDKFVPTMDEYVSNAHVSFALGPIVLPALYLVGPKLSEEMVNHSEYHNLFKLMSMCGRLMNDIRGYEREHDDGKLNAMSLYIMNNGGEITPEVAILEIKSWNDRHRRDLLRLVLEEKSVIPKACKDLFWHMCSVVHLFYNKDDGFWSQELIEVVNQVIHQPILLNHF
Protein: A-type potassium channel modulatory protein DPP6 (DPPX) (Dipeptidyl aminopeptidase-like protein 6) (Dipeptidyl aminopeptidase-related protein) (Dipeptidyl peptidase 6) (Dipeptidyl peptidase IV-like protein) (Dipeptidyl peptidase VI) (DPP VI) (P42658)
Organism: Homo sapiens (Human)
Function: Promotes cell surface expression of the potassium channel KCND2. Modulates the activity and gating characteristics of the potassium channel KCND2. Has no dipeptidyl aminopeptidase activity.
Subcellular location: Cell membrane {ECO:0000269|PubMed:18364354, ECO:0000269|PubMed:19441798}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
- A-type voltage-gated potassium channel KCND2
- A-type potassium channel modulatory protein KCNIP1
- A-type voltage-gated potassium channel KCND3
- Sodium channel protein type 5 subunit alpha
- Voltage-gated potassium channel KCNC1
- IgLON family member 5
- Leucine-rich glioma-inactivated protein 1
- Contactin-associated protein-like 2
- A-type potassium channel modulatory protein KCNIP2
- Paraneoplastic antigen Ma2
Sequence:
MASLYQRFTGKINTSRSFPAPPEASHLLGGQGPEEDGGAGAKPLGPRAQAAAPRERGGGGGGAGGRPRFQYQARSDGDEEDELVGSNPPQRNWKGIAIALLVILVICSLIVTSVILLTPAEDNSLSQKKKVTVEDLFSEDFKIHDPEAKWISDTEFIYREQKGTVRLWNVETNTSTVLIEGKKIESLRAIRYEISPDREYALFSYNVEPIYQHSYTGYYVLSKIPHGDPQSLDPPEVSNAKLQYAGWGPKGQQLIFIFENNIYYCAHVGKQAIRVVSTGKEGVIYNGLSDWLYEEEILKTHIAHWWSPDGTRLAYAAINDSRVPIMELPTYTGSIYPTVKPYHYPKAGSENPSISLHVIGLNGPTHDLEMMPPDDPRMREYYITMVKWATSTKVAVTWLNRAQNVSILTLCDATTGVCTKKHEDESEAWLHRQNEEPVFSKDGRKFFFIRAIPQGGRGKFYHITVSSSQPNSSNDNIQSITSGDWDVTKILAYDEKGNKIYFLSTEDLPRRRQLYSANTVGNFNRQCLSCDLVENCTYFSASFSHSMDFFLLKCEGPGVPMVTVHNTTDKKKMFDLETNEHVKKAINDRQMPKVEYRDIEIDDYNLPMQILKPATFTDTTHYPLLLVVDGTPGSQSVAEKFEVSWETVMVSSHGAVVVKCDGRGSGFQGTKLLHEVRRRLGLLEEKDQMEAVRTMLKEQYIDRTRVAVFGKDYGGYLSTYILPAKGENQGQTFTCGSALSPITDFKLYASAFSERYLGLHGLDNRAYEMTKVAHRVSALEEQQFLIIHPTADEKIHFQHTAELITQLIRGKANYSLQIYPDESHYFTSSSLKQHLYRSIINFFVECFRIQDKLLTVTAKEDEEED
Protein: Adagio protein 1 (Clock-associated PAS protein ZTL) (F-box only protein 2b) (FBX2b) (Flavin-binding kelch repeat F-box protein 1-like protein 2) (FKF1-like protein 2) (LOV kelch protein 1) (Protein ZEITLUPE) (Q94BT6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of an E3 ubiquitin ligase complex that plays a central role in blue light-dependent circadian cycles. Acts as a blue light photoreceptor, due to the presence of FMN, that mediates light-regulated protein degradation of critical clock components by targeting them to the proteasome complex. The SCF(ADO1) E3 ubiquitin ligase complex is involved in the regulation of circadian clock-dependent processes including the transition to flowering time, hypocotyl elongation, cotyledons and leaf movement rhythms. APRR1/TOC1 and APRR5, but not 'GIGANTEA', are proteolytic substrates of this ubiquitin ligase complex. Blue light enhances cooperative stabilization of 'GIGANTEA' and ADO1/ZTL, leading to amplification and sharpening of the expression profile of APRR1/TOC1. ADO1/ZTL interacts with ADO3, preventing the interaction of ADO3 with CDF1.
Subcellular location: Nucleus. Cytoplasm. Note=Nuclear after 9 hours of illumination (afternoon of long days). Cytoplasmic when plant have been subsequently grown 16 hours in light and 5 hours in dark (early morning of long days).
Interaction partners:
- Protein GIGANTEA
- Two-component response regulator-like APRR1
- Two-component response regulator-like APRR3
- Cryptochrome-1
- Two-component response regulator-like APRR5
- Phytochrome B
- Protein EARLY FLOWERING 3
- UPF0235 protein At5g63440
- Protein CCA1
- Protein LHY
Sequence:
MEWDSGSDLSADDASSLADDEEGGLFPGGGPIPYPVGNLLHTAPCGFVVTDAVEPDQPIIYVNTVFEMVTGYRAEEVLGGNCRFLQCRGPFAKRRHPLVDSMVVSEIRKCIDEGIEFQGELLNFRKDGSPLMNRLRLTPIYGDDDTITHIIGIQFFIETDIDLGPVLGSSTKEKSIDGIYSALAAGERNVSRGMCGLFQLSDEVVSMKILSRLTPRDVASVSSVCRRLYVLTKNEDLWRRVCQNAWGSETTRVLETVPGAKRLGWGRLARELTTLEAAAWRKLSVGGSVEPSRCNFSACAVGNRVVLFGGEGVNMQPMNDTFVLDLNSDYPEWQHVKVSSPPPGRWGHTLTCVNGSNLVVFGGCGQQGLLNDVFVLNLDAKPPTWREISGLAPPLPRSWHSSCTLDGTKLIVSGGCADSGVLLSDTFLLDLSIEKPVWREIPAAWTPPSRLGHTLSVYGGRKILMFGGLAKSGPLKFRSSDVFTMDLSEEEPCWRCVTGSGMPGAGNPGGVAPPPRLDHVAVNLPGGRILIFGGSVAGLHSASQLYLLDPTEDKPTWRILNIPGRPPRFAWGHGTCVVGGTRAIVLGGQTGEEWMLSELHELSLASYLT
Protein: DNA topoisomerase 2 (EC 5.6.2.2) (A0A8I5Y7L4)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus, nucleolus {ECO:0000256|ARBA:ARBA00004604}. Nucleus, nucleoplasm {ECO:0000256|ARBA:ARBA00004642}.
Interaction partners:
Sequence:
MAKSSLAGVDGALTWVNNAAKKEELETANKNDSSKKLSVERVYQKKTQLEHILLRPDTYIGSVEPLTQLMWVYDEDVGMNCREVTFVPGLYKIFDEILVNAADNKQRDKNMTCIKVSIDPESNIISIWNNGKGIPVVEHKVEKVYVPALIFGQLLTSSNYDDDEKKVTGGRNGYGAKLCNIFSTKFTVETACKEYKHSFKQTWMNNMMKTSEAKIKHFDGEDYTCITFQPDLAKFKMEKLDKDIVALMTRRAYDLAGSCKGVKVMFNGKKLPVNGFRSYVDLYVKDKLDETGVALKVIHELANERWDVCLTLSEKGFQQISFVNSIATTKGGRHVDYVVDQVVGKLIEVVKKKNKAGVSVKPFQVKNHIWVFINCLIENPTFDSQTKENMTLQPKSFGSKCQLSEKFFKAASNCGIVESILNWVKFKAQTQLNKKCSSVKYSKIKGIPKLDDANDAGGKHSLECTLILTEGDSAKSLAVSGLGVIGRDRYGVFPLRGKILNVREASHKQIMENAEINNIIKIVGLQYKKSYDDAESLKTLRYGKIMIMTDQDQDGSHIKGLLINFIHHNWPSLLKHGFLEEFITPIVKASKNKQELSFYSIPEFDEWKKHIENQKAWKIKYYKGLGTSTAKEAKEYFADMERHRILFRYAGPEDDAAITLAFSKKKIDDRKEWLTNFMEDRRQRRLHGLPEQFLYGTATKHLTYNDFINKELILFSNSDNERSIPSLVDGFKPGQRKVLFTCFKRNDKREVKVAQLAGSVAEMSAYHHGEQALMMTIVNLAQNFVGSNNINLLQPIGQFGTRLHGGKDAASPRYIFTMLSSLARLLFPAVDDNLLKFLYDDNQRVEPEWYIPIIPMVLINGAEGIGTGWACKLPNYDAREIVNNVRRMLEGLDPHPMLPNYKNFKGTIQELGQNQYAVSGEIFVVDRNTVEITELPVRTWTQVYKEQVLEPMLNGTDKTPALISDYKEYHTDTTVKFVVKMTEEKLAQAEAAGLHKVFKLQTTLTCNSMVLFDHMGCLKKYETVQDILKEFFDLRLSYYGLRKEWLVGMLGAESTKLNNQARFILEKIQGKITIENRSKKDLIQMLVQRGYESDPVKAWKEAQEKAAEEEDAQNPHDDSSSDSGTPSGPDFNYILNMSLWSLTKEKVEELIKQRDTKGREVNDLKRKSPSDLWKEDLAAFVEELDKVEAQEREDILAGMSGKAVKGKVGKAKVKKLQLEETMPSPYGRRIVPEITAMKADASRKLLKKKKGDPDTTVVKVEFDEEFSGTPAEGTGEETLTPSAPVNKGPKPKREKKEPGTRVRKTPASTGKPNTKKVKKRNPWSDDESKSESDLEEAEPVVIPRDSLLRRAAAERPKYTFDFSEEEEDDADDDDDNNDLEELKVKASPITNDGEDEFVPSDGIDKDEYAFSPGKSKATPEKSSHDKKSQDFGNLFSFPSYSQKSEDDSAKFDSNEEDTTSVFAPSFGLKQTDKVPSQTVAAKKGKAPSDAAAPKAKRAPRQRKVVEPANSDSDSELGNIPKKTAAPKGKGRGAKKRKASGSENEGDYNPGRKPSKTASKKPKKTSFDQDSDVDIFPSDFTSEPPALPRTGRARKEVKYFAESDEEEDVDFAMFN