wanglab/gogpt-training-data huggingface dataset:
Protein: Late cornified envelope protein 3B (Late envelope protein 14) (Q5TA77)
Organism: Homo sapiens (Human)
Function: A structural component of the cornified envelope of the stratum corneum involved in innate cutaneous host defense (Probable). Possesses defensin-like antimicrobial activity against a broad spectrum of Gram-positive and Gram-negative bacteria, both aerobic and anaerobic species. Upon inflammation, may regulate skin barrier repair by shaping cutaneous microbiota composition and immune response to bacterial antigens.
Interaction partners:
- Late cornified envelope protein 1A
- Late cornified envelope protein 1D
- Involucrin
- Loricrin
- Late cornified envelope protein 1E
- Late cornified envelope protein 1C
- Peptidoglycan recognition protein 4
- Late cornified envelope protein 1B
- Repetin
- Late cornified envelope protein 3A
Sequence:
MSCQQNQQQCQPLPKCPSPKCPPKSSAQCLPPASSCCAPRPGCCGGPSSEGGCCLSHHRCCRSHRCRRQSSNSCDRGSGQQDGASDCGYGSGGCC
Protein: Polyubiquitin-B [Cleaved into: Ubiquitin] (P0CG53)
Organism: Bos taurus (Bovine)
Function: Exists either covalently attached to another protein, or free (unanchored) (By similarity). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in proteotoxic stress response and cell cycle; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, DNA-damage responses as well as in signaling processes leading to activation of the transcription factor NF-kappa-B (By similarity). Linear polymer chains formed via attachment by the initiator Met lead to cell signaling (By similarity). Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed (By similarity). When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling (By similarity).
Subcellular location: [Ubiquitin]: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Mitochondrion outer membrane {ECO:0000250|UniProtKB:P0CG47}; Peripheral membrane protein {ECO:0000250|UniProtKB:P0CG47}.
Interaction partners:
- Ubiquitin-ribosomal protein eL40 fusion protein
- Polyubiquitin-C
- Ubiquitin-ribosomal protein eS31 fusion protein
- 26S proteasome non-ATPase regulatory subunit 4
- TNF receptor-associated factor 6
- Ubiquitin carboxyl-terminal hydrolase 7
- Ubiquitin-conjugating enzyme E2 N
- Ubiquitin-conjugating enzyme E2 variant 2
- Proteasomal ubiquitin receptor ADRM1
- [histone H3]-dimethyl-L-lysine
Sequence:
MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGC
Protein: Plexin-A4 (Q6BEA0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Involved in the development of primary sensory neurons especially in branching of the peripheral axons. Interacts with the SLIT2 signaling specifically to promote axonal branching of Rohon-Beard neurons and the trigeminal sensory ganglion neurons.
Subcellular location: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
- Neuropilin-1a
- Sema domain, transmembrane domain
- Sema domain, immunoglobulin domain
- Semaphorin-2A
- Semaphorin 7A
- Semaphorin-3aa
- Semaphorin-3ab
- Sema domain, immunoglobulin domain
- Neuropilin 1b.
- Dihydropyrimidinase-related protein 3
Sequence:
MAFHNRRWNFTFSCCVVVLLLPLVAARPQQPSAATRVHEEYSTFRVENTEWTFNHLAVDHRNGNVYLGAVNRIYKLSPGLDIQVSHQTGPDEDNRNCYPPRIVQPCSEPLTLTNNVNKMLLMDYRENRLLACGSLYQGICKLLRLDDLFKLGEPFHKKEHYLSGVNESGSVFGVIVSYGDASPDKLFVATAVDGRPEYFPTISSRKLTRNSEEDGMFAYVFHDEFVASMIKIPSDTFTVVPDFDIYYVYGFSSGNFVYFLTLQPEMGGGPTTGSSSAGREQVYTSKLVRLCKDDTAFNSYVEVPLGCVKGGVEYRLLQAAYLSKAGTILARSLGIGPDDDILYAVFSKGQKRRPKESSQESALCVFTLKEINERIKDRLQSCYKGEGTLDLAWLKVKDISCSSALLTIDDNFCGLDMNAPLGVSEMVRGIPLFSESKDKMTSVIAYVYKNHSLAFVGTRGGRLKKIRVDGPTYGALQYETIQVVDNGPILRDMAFSSDQHFLYVMSESQLTRVPVEACEQYSSCNECLGSGDPHCGWCVLHSMCTRKEKCERSSEPRRFASNIKQCVRLSVHPNNISVSQYSVMLVLEAHNVPELSAGVNCTFEDLAEMDGLVEGNRITCSSPAEKEVPRIIVDQGDHQIVQLYLKSKETGLAFANTSFVFYNCSVHKSCLSCVGSPYQCHWCKYRHTCTHDPSSCSFQEGRVKQPEECPQLLPADRILVPVNVVKPITLRAKNLPQPQSGQRGYECVLTIQGVEQRVPALRFNSSSVQCQNTSYMYDGMEMSSLPVDLTVIWNGDFSIDNPAQNKVHLYKCDARRESCGLCLKADPLFGCVWCKGENRCSLKQHCSYPQSMWLEHNGINSKCTHPRITKITPLRGPREGGTLVTIRGENLGLEFSEIKDHVKVADVECTPVPEGYIPAEQIVCEMGKAERSQFAGNVQVCVGECRPEFMAKSSKYYYFVIPQLLSLKPSRGPISGGTIVNITGGNLDAGSNVSIMFKDQKCTYQRRGGQWITCRSHASMQGYGNVSVSVYVDKAHIHKDLKFEYVEDPTITKLEPEWSIFSGNTPLTVSGTNLDIIHTPLIRAKYKNLETINICQVLSPTTMQCMAPELPYSISKHKDVPERPDEFGFILDNVQSVLALNNTNFVYYPNPVFEPLSVSGVQELKPGSPIILKGRNFLPPTPGGNGKLNYTVLIGDKPCALTVSDTQLLCESPNLTGRHKVLARVGGIEFSPGVVHITSDSPLSSTAVISIAGAGGLLIFFIVIVLIAYKRKSRESDLTLKRLQMQMDNLESRVALECKEAFAELQTDIHELTSDLDGAGIPFLDYRTYTMRVLFPGIEEHPVLRDLEVPGYRQEQVEKGLKLFGQLINNKVFLLSFIRTLESQRGFSMRDRGNVASLIMTVLQSKLEYATDVLKHLLSDLIDKNLESKNHPKLLLRRTESVAEKMLTNWFTFLLYKFLKECAGEPLFSLFCAIKQQMEKGPIDSITGEARYSLSEDKLIRQQIDYKTLVVNCMHPDNEKSPEVQVKVLNCDTVSQVKEKILDAIYKNVPYSHRPKASDMDLEWRQGRVVRVILQDEDVTTKIEADWKRLNMLSHYQVTDNAVVALVPKQVTAYNSVNNSTVSRTSASKYENMIKYTGSPDSLRSRTPMITPDLESGVKVWHLVKNHEHGDQKEGDRGSKMVSEIYLTRLLATKGTLQKFVDDLFETIFSTAHRGSALPLAIKYMFDFLDEQADKHNIHDPHVRHTWKSNCLPLRFWVNVIKNPQFVFDIHKSSITDACLSVVAQTFMDSCSTSEHRLGKDSPSNKLLYAKDIPSYKSWVERYYSDISKMPAISDQDMNAYLAEQSRMHMNEFNTMSSLSEIYSYIGKYTEEIVSALEQDDGARKQRLAYKLEQVVAFMSLES
Protein: Rothein 1 (P86508)
Organism: Litoria rothii (Roth's tree frog) (Hyla rothii)
Function: Induces contraction of intestinal smooth muscle in isolated guinea pig ileum. Induces proliferation of mouse splenocytes.
Subcellular location: Secreted {ECO:0000269|PubMed:16124032}.
Interaction partners:
Sequence:
SVSNIPESIGF
Protein: Alpha-1B adrenergic receptor (Alpha-1B adrenoreceptor) (Alpha-1B adrenoceptor) (P15823)
Organism: Rattus norvegicus (Rat)
Function: This alpha-adrenergic receptor mediates its action by association with G proteins that activate a phosphatidylinositol-calcium second messenger system. Its effect is mediated by G(q) and G(11) proteins. Nuclear ADRA1A-ADRA1B heterooligomers regulate phenylephrine (PE)-stimulated ERK signaling in cardiac myocytes (By similarity).
Subcellular location: Nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell membrane {ECO:0000250|UniProtKB:P35368}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000250|UniProtKB:P35368}. Membrane, caveola {ECO:0000250|UniProtKB:P35368}. Note=Location at the nuclear membrane facilitates heterooligomerization and regulates ERK-mediated signaling in cardiac myocytes. Colocalizes with GNAQ, PLCB1 as well as LAP2 at the nuclear membrane of cardiac myocytes (By similarity). {ECO:0000250}.
Interaction partners:
Sequence:
MNPDLDTGHNTSAPAHWGELKDDNFTGPNQTSSNSTLPQLDVTRAISVGLVLGAFILFAIVGNILVILSVACNRHLRTPTNYFIVNLAIADLLLSFTVLPFSATLEVLGYWVLGRIFCDIWAAVDVLCCTASILSLCAISIDRYIGVRYSLQYPTLVTRRKAILALLSVWVLSTVISIGPLLGWKEPAPNDDKECGVTEEPFYALFSSLGSFYIPLAVILVMYCRVYIVAKRTTKNLEAGVMKEMSNSKELTLRIHSKNFHEDTLSSTKAKGHNPRSSIAVKLFKFSREKKAAKTLGIVVGMFILCWLPFFIALPLGSLFSTLKPPDAVFKVVFWLGYFNSCLNPIIYPCSSKEFKRAFMRILGCQCRGGRRRRRRRRLGACAYTYRPWTRGGSLERSQSRKDSLDDSGSCMSGTQRTLPSASPSPGYLGRGTQPPVELCAFPEWKPGALLSLPEPPGRRGRLDSGPLFTFKLLGDPESPGTEGDTSNGGCDTTTDLANGQPGFKSNMPLAPGHF
Protein: Phosphotransferase (EC 2.7.1.-) (Q38C41)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- ATP-dependent 6-phosphofructokinase
- Glucose-6-phosphate isomerase
- Glucosamine 6-phosphate N-acetyltransferase
- mannose-6-phosphate isomerase
- glutamine--fructose-6-phosphate transaminase
- Glucosamine-6-phosphate isomerase
- Fructose-bisphosphate aldolase
- fructose-bisphosphatase
- Phosphomannomutase
- glucose-6-phosphate 1-epimerase
Sequence:
MSRRLNNILEHISIQGNDGETVRAVKRDVAMAALTNQFTMSVESMRQIMTYLLYEMVEGLEGRESTVRMLPSYVYKADPKRATGVFYALDLGGTNFRVLRVACKEGAVVDSSTSAFKIPKYALEGNATDLFDFIASNVKKTMETRAPEDLNRTVPLGFTFSFPVEQTKVNRGVLIRWTKGFSTKGVQGNDVIALLQAAFGRVSLKVNVVALCNDTVATMISHYFKDPEVQVGVIIGTGSNACYFETASAVTKDPAVAARGSALTPISMESGNFDSKYRFVLPTTKFDLDIDDASLNKGQQALEKMISGMYLGEIARRVIVHLSSINCLPAALQTALGNRGSFESRFAGMISADRMPGLQFTRSTIQKVCGVDVQSIEDLRIIRDVCRLVRGRAAQLSASFCCAPLVKTQTQGRATIAIDGSVFEKIPSFRRVLQDNINRILGPECDVRAVLAKGGSGVGAALISAIVADGK
Protein: Serine/threonine-protein kinase PknH (EC 2.7.11.1) (P9WI71)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: May regulate bacterial growth in response to external signals to facilitate adaptation to the host environment. In vitro, phosphorylates several substrates such as EmbR, DevR (DosR), DacB1 and Rv0681.
Subcellular location: Cell membrane {ECO:0000269|PubMed:15043876}; Single-pass membrane protein {ECO:0000269|PubMed:15043876}.
Interaction partners:
- Transcriptional regulatory protein EmbR
- Serine/threonine protein phosphatase PstP
- Glycogen accumulation regulator GarA
- FHA domain-containing protein FhaA
Sequence:
MSDAQDSRVGSMFGPYHLKRLLGRGGMGEVYEAEHTVKEWTVAVKLMTAEFSKDPVFRERMKREARIAGRLQEPHVVPIHDYGEVDGQMFLEMRLVEGTDLDSVLKRFGPLTPPRAVAIITQIASALDAAHADGVMHRDVKPQNILITRDDFAYLVDFGIASATTDEKLTQLGTAVGTWKYMAPERFSNDEVTYRADIYALACVLHECLTGAPPYRADSAGTLVSSHLMGPIPQPSAIRPGIPKAFDAVVARGMAKKPEDRYASAGDLALAAHEALSDPDQDHAADILRRSQESTLPAPPKPVPPPTMPATAMAPRQPPAPPVTPPGVQPAPKPSYTPPAQPGPAGQRPGPTGQPSWAPNSGPMPASGPTPTPQYYQGGGWGAPPSGGPSPWAQTPRKTNPWPLVAGAAAVVLVLVLGAIGIWIAIRPKPVQPPQPVAEERLSALLLNSSEVNAVMGSSSMQPGKPITSMDSSPVTVSLPDCQGALYTSQDPVYAGTGYTAINGLISSEPGDNYEHWVNQAVVAFPTADKARAFVQTSADKWKNCAGKTVTVTNKAKTYRWTFADVKGSPPTITVIDTQEGAEGWECQRAMSVANNVVVDVNACGYRITNQAGQIAAKIVDKVNKE
Protein: Poly(U) binding splicing factor 60 (E9PMU7)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MEQLNLADSGLVGKEARRCRRASPPMGMPSAWWLQNEAGCLFAARQVNGQQGGGSEPAAAAAVVAAGDKWKPPQGTDSIKMENGQSTAAKLGLPPLTPEQQEALQKAKKYAMEQSIKSVLVKQTIAHQQQQLTNLQMAAQRQRALAIMCRVYVGSIYYELGEDTIRQAFAPFGPIKSIDMSWDSVTMKHKGFAFVEYEVPEAAQLALEQMNSVMLGGRNIKVGRPSNIGQAQPIIDQLAEEARAFNR
Protein: BolA-like protein 1 (hBolA) (Q9Y3E2)
Organism: Homo sapiens (Human)
Function: Acts as a mitochondrial iron-sulfur (Fe-S) cluster assembly factor that facilitates (Fe-S) cluster insertion into a subset of mitochondrial proteins (By similarity). Probably acts together with the monothiol glutaredoxin GLRX5. May protect cells against oxidative stress.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:22746225}.
Interaction partners:
- BolA-like protein 3
- Glutaredoxin-3
- Glutaredoxin-related protein 5, mitochondrial
- Anamorsin
- NFU1 iron-sulfur cluster scaffold homolog, mitochondrial
- Ferredoxin-2, mitochondrial
- Iron-sulfur cluster assembly enzyme ISCU
- BolA-like protein 2
- Iron-sulfur cluster assembly 2 homolog, mitochondrial
- LYR motif-containing protein 4
Sequence:
MLSGRLVLGLVSMAGRVCLCQGSAGSGAIGPVEAAIRTKLEEALSPEVLELRNESGGHAVPPGSETHFRVAVVSSRFEGLSPLQRHRLVHAALAEELGGPVHALAIQARTPAQWRENSQLDTSPPCLGGNKKTLGTP
Protein: RUN and FYVE domain-containing protein 4 (Q6ZNE9)
Organism: Homo sapiens (Human)
Function: Positively regulates macroautophagy in primary dendritic cells. Increases autophagic flux, probably by stimulating both autophagosome formation and facilitating tethering with lysosomes. Binds to phosphatidylinositol 3-phosphate (PtdIns3P) through its FYVE-type zinc finger.
Subcellular location: Cytoplasmic vesicle, autophagosome {ECO:0000269|PubMed:26416964}. Lysosome {ECO:0000269|PubMed:35314674}. Note=In the presence of ARL8, recruited to endolysosomes. {ECO:0000269|PubMed:35314674}.
Interaction partners:
Sequence:
MAEEGAILKVTKDLRAAVSAILQGYGDGQGPVTDTSAELHRLCGCLELLLQFDQKEQKSFLGPRKDYWDFLCTALRRQRGNMEPIHFVRSQDKLKTPLGKGRAFIRFCLARGQLAEALQLCLLNSELTREWYGPRSPLLCPERQEDILDSLYALNGVAFELDLQQPDLDGAWPMFSESRCSSSTQTQGRRPRKNKDAPKKIPAAYGGPENVQIEDSHTSQAICLQDAPSGQQLAGLPRSQQQRHLPFFLEKKGESSRKHRYPQSMWEPEGKELQLDQEERAPWIEIFLGNSTPSTQGQGKGAMGTQKEVIGMEAEVTGVLLVAEGQRTTEGTHKKEAEWSHVQRLLMPSPRGAVEGAVSGSRQGSGGSSILGEPWVLQGHATKEDSTVENPQVQTEVTLVARREEQAEVSLQDEIKSLRLGLRKAEEQAQRQEQLLREQEGELQALREQLSRCQEERAELQAQLEQKQQEAERRDAMYQEELGGQRDLVQAMKRRVLELIQEKDRLWQRLQHLSSMAPECCVACSKIFGRFSRRYPCRLCGGLLCHACSMDYKKRDRCCPPCAQGREAQVT
Protein: Activator of 90 kDa heat shock protein ATPase homolog 1 (AHA1) (p38) (O95433)
Organism: Homo sapiens (Human)
Function: Acts as a co-chaperone of HSP90AA1. Activates the ATPase activity of HSP90AA1 leading to increase in its chaperone activity. Competes with the inhibitory co-chaperone FNIP1 for binding to HSP90AA1, thereby providing a reciprocal regulatory mechanism for chaperoning of client proteins. Competes with the inhibitory co-chaperone TSC1 for binding to HSP90AA1, thereby providing a reciprocal regulatory mechanism for chaperoning of client proteins.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:11554768}. Endoplasmic reticulum {ECO:0000269|PubMed:11554768}. Note=May transiently interact with the endoplasmic reticulum.
Interaction partners:
- Heat shock protein HSP 90-beta
- Heat shock protein HSP 90-alpha
- Stress-induced-phosphoprotein 1
- Prostaglandin E synthase 3
- Peptidyl-prolyl cis-trans isomerase FKBP4
- Heat shock 70 kDa protein 4
- Hsp90 co-chaperone Cdc37
- Peptidyl-prolyl cis-trans isomerase D
- Heat shock cognate 71 kDa protein
- Endoplasmin
Sequence:
MAKWGEGDPRWIVEERADATNVNNWHWTERDASNWSTDKLKTLFLAVQVQNEEGKCEVTEVSKLDGEASINNRKGKLIFFYEWSVKLNWTGTSKSGVQYKGHVEIPNLSDENSVDEVEISVSLAKDEPDTNLVALMKEEGVKLLREAMGIYISTLKTEFTQGMILPTMNGESVDPVGQPALKTEERKAKPAPSKTQARPVGVKIPTCKITLKETFLTSPEELYRVFTTQELVQAFTHAPATLEADRGGKFHMVDGNVSGEFTDLVPEKHIVMKWRFKSWPEGHFATITLTFIDKNGETELCMEGRGIPAPEEERTRQGWQRYYFEGIKQTFGYGARLF
Protein: Uncharacterized protein (Q8C9W2)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MCIMVHVYACKEHISSWCLSIHKFKSVIVYLGASTMPVNLCTFVCIWYKAACHVSLCSYMCMVVYDGLYMSLCVQNMYLRKEKRETDSIPATVKESKQSEWAPHSFF
Protein: SUFU negative regulator of hedgehog signaling (A0A8I5ZN76)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MAELRPSVAPGPAAPPASGPSAPPAFASLFPPGLHAIYGECRRLYPDQPNPLQVTAIVKYWFTGTDGPSGFGFELTFRLKRETGESAPPTWPAELMQGLARYVFQSENTFCSGDHVSWHSPLDNSESRIQHMLLTEDPQMQPVQTPFGVVTFLQIVGVCTEELHSAQQWNGQGILELLRTVPIAGGPWLITDMRRGETIFEIDPHLQQERVDKGIETDGSNLSGVSAKCAWDDLSRPPEDDEDSRSICLGTQPRRLSGKDTEQIRETLRRGLEINSKPVLPPINSQRQNGLTYDRAP
Protein: Tyrosine specific protein phosphatase, putative (EC 3.1.3.48) (Q38AT7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- SH3 domain-containing protein
- BRCT domain-containing protein
- EGF-like domain-containing protein
Sequence:
MSTAKSFPMAQLSTRAQYSRMQREFVQLQRQENPRNINFTTSLKNRHKNRYLDILANEETIYPPVLKAVGAQPGRYPYINGNLIDLDLPHTFVACQAPVPQGVPDFLETLSEKKVDLVVMLTKLREGGVLKAERYWPEEEEDSLSFPESGHDAIKVTRDAEASYEVDAELDIVRRPLVIHVPGKPMHRVLQVQYVGWPDHGVPESAASFDELLSVIKNCVTTSPILVHCSAGIGRTGTLIGAYAALLHIERGILTDSTVYSIVAAMKQKRFGMVQRLEQYAVIYMTVLGRLGVDISGLVSTLNLKA
Protein: Elongation of very long chain fatty acids protein (EC 2.3.1.199) (Very-long-chain 3-oxoacyl-CoA synthase) (Q9VCY7)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Very long chain fatty acid elongase 7
Sequence:
MTNYIKIVEERISGLSKGVDETVDSWFLMSSPMPVVAVVLVYLAFVLKIGPEYMKNRKPMDLKRIMVFYNAFQVLYSIWMCRTSIQESNVMASIFSKKCEINRTREQNLTLYSGAWFYFFSKIIDLLDTTFFVLRKKDNQVSFLHVYHHTITVLFSWGYLKYAPGEQGVIIGILNSGVHIIMYFYYMVAAMGPQYQKYLWWKKYMTSIQLIQFVLILGYMLTVGAKGCNMPKTLTFFFVGNTVIFLYLFGNFYRKTYKKAKSVDGGSRTTGSSLAQSALRAAGGMGCMPQTMNAGKHLLQNGQVGKAYIDLNNNSVKPMKLE
Protein: EF-hand calcium-binding domain-containing protein 3 (Q8N7B9)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAVSEIKPKLKLNPLTKVPISHNKRDRDLPGSLQCQLQHKEKKLSASQMAAFQDAYNFFYKDKTGCIDFHGLMCTVAKLGMNLTKHDVYNELKCADIDRDGKVNFSDFIKVLTDKNLFLKAVVPEKETCLDLAGNPGILLFEILSRLLETSALPRKSIIEIVSYFQRKFQHTGPGMLWSPYTMGYGKRTLKPDICTPPSSSMAAFANAARIAIMKEKDLFKFLEELKRCNSGSDSPYSKIPIFPLFPNVDGVVMGKPFKDMQKLEMLRIKEPLHFFEDYFFHKRDWKTQAANIKSMDPASGYSNNIFTIDQMLKKKQTCTVADATAIKQHVKRATDTYNLGIALEHRKEMLNLWQKIRGDLIGMDSRNESFYDTFSTYTWSWNVCQELLSPKDLRLYDAYVNRNSSHNSRSSSSSDTSECYTDSGRKRKRKGLKGFQQ
Protein: Cytidine/uridine monophosphate kinase 2 (D3ZC63)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- UMP-CMP kinase
- S-adenosylmethionine-dependent nucleotide dehydratase RSAD2
- Adenylate kinase 9
- Ribonucleoside-diphosphate reductase
- Deoxycytidylate deaminase
- 5',3'-nucleotidase, mitochondrial
- Deoxycytidine kinase
- Uracil phosphoribosyltransferase homolog.
- Uridine monophosphate synthetase, isoform CRA_a.
- Nucleoside diphosphate kinase A
Sequence:
MALISCPRAPLWLGRLSRRLCARHRACTGTMARPRRFTVELPDCSLTHFVLGDAAGHRDARLTELLGPPGRSYALCVPLVPGEGCGPRVQAARVYQRLQLQLRQGPLQRCELSKLLGYGPGDQASEAQHGFLLRDPSDHPDTRQDLLQLLGSCQEATRLHLAEFQADSQGLLWQRLWELQGDRQVQVDCACVLPAPEPHLHPLLPDLLNSAVFQDRDAARAVLEECTSFIPEAREVLDLVDQCPREIQKGKFQVIAIEGLDATGKTTLTQSVSESLQAVLLQSPPPCISQWRKLFDDEPTIIRRAFYSLGNYLVASEIAKQSAKFPVIVDRYWHSTATYAIATEVSGGLQYLPPAHHPVYQWPRDLLKPDLVLLLTVNSEERVRRLQGRGQEKTKEEAELEVNSVFRQKVEATYQRMENPSCRLVDASPSRETVLQTVLQLIQRAGH
Protein: Spindle assembly abnormal protein 6 homolog (Q6NRG6)
Organism: Xenopus laevis (African clawed frog)
Function: Central scaffolding component of the centrioles ensuring their 9-fold symmetry. Required for centrosome biogenesis and duplication: required both for mother-centriole-dependent centriole duplication and deuterosome-dependent centriole amplification in multiciliated cells (By similarity).
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q7ZVT3}. Note=Component of the centrosome (By similarity). Component of the deuterosome, a structure that promotes de novo centriole amplification in multiciliated cells that can generate more than 100 centrioles. {ECO:0000250|UniProtKB:Q7ZVT3, ECO:0000269|PubMed:24075808}.
Interaction partners:
Sequence:
MADELFCKVLSIGIKCRECEDRRANVRLTVESRSSSNPVHKKELVVRLSDDTDPFFLYNLTLGEEDFQSLKNQQGLLVEFSAFPQRFIDLLEQCILEQEKPVPRFLLQLAMSSNALDCMPASLNIIETNPFKHLIHLSLKLLAGSDSDVKKYLATCIKNLKLENCTLKEKLHKSEEDLSKRLGVTQQALAEKCKELDKLRNEWASQTSLLTSKHTQEIGAEREKALQIQTQYQLQYEQQKKELETTSSRTVHHLESRVSELEAVNKDLTERKYKSESCIRELKGKLSGIEEEYHRAKQEVTSLRRENATLDSECHEKEKLINQLKTKTAVLEQEVKDKEHVIIRSVDACESAQEHKKKLEDSLEQKQMQTGKLETTVKSLSEELIKANEIIKKLQTDMKKLMEKIKLKNAVTMQQEKLLGEKEQTLQKEKLELTNVKHLLKIKEEEMLKLKEQLDSTTEKLEESKQQLKTNENVIAWLNKQLNENKIATLQGPHGLHEMPSSLKTVGSASNVGVMQSTQPQFTIGNDPYMVSPITQPIGSAFVSNFYPKNFAPGMSAPSSISLGTRLNPQAAFKANVRFNQSPTALCSPAVEPRPAPSTSTPILPSTSCDPVGLDMKYLKKNGSVPVKGQRNGSSAGTVPVRPALPKSGSSPILSAYFPGQQSRLPAS
Protein: Rho guanine nucleotide exchange factor 15 (Ephexin-5) (E5) (Q5FWH6)
Organism: Mus musculus (Mouse)
Function: Specific GEF for RhoA activation. Does not activate RAC1 or CDC42. Regulates vascular smooth muscle contractility. Negatively regulates excitatory synapse development by suppressing the synapse-promoting activity of EPHB2.
Subcellular location: Cell projection, dendrite {ECO:0000269|PubMed:21029865}. Note=Expressed exclusively in dendrites of the developing hippocampus.
Interaction partners:
- FYVE, RhoGEF and PH domain-containing protein 5
Sequence:
MSAQSLPAATPPTLKPPRIIRPRPPSRHRAPHSPGPLHNGSSPKALPQISNDASASVCTSIFWEPPTASLKPPALLPPSVSRTSLDSQTSPDSPSSTPSPSPVSRRSISPEPAPCSPVPPPKPSGSSRTPLPSGPTPLQDGSASAPGTVRRLAGKFEWGAEGKAQSSDSLERCSQGSTEVNGEKETPEAALSGNGSQENGTPDAALACPPCCPCVCHVAKPGLELRWVPVGSSEDILRIPCRASPLRASRSRINPPVISHPPVVLTSYRSTAERKLLPPLKPPKPTKVRQDISTSEELPQPDLKLPSEDGIQTATKAWEGDRPEGAPLNAPPVALEGREEEGLDGLKGLQWELPLQDEPLYQTYRAAVLSEELWGVGEDGGPSPANPGEAPTFSRLPGPRNTLWQELPAVRGSGLLESLSPQERRMQESLFEVVTSEASYLRSLRLLTDTFVLSQALRDTLTPRDHHTLFSNVQRVQSVSERFLGTLLSRVRSSPHITDLCDVVHAHAVGPFFVYVDYVRNQQYQEETYSRLMDTNVRFSAELRRLQSLPKCERLPLPSFLLLPFQRITRLRMLLQNILSQTEEGSSRQENAQKALGAVSKIIERCSAEVGRMKQTEELIRLTQRLRFHKVKALPLVSWSRRLELQGELTELGCRRGGVLFTSRPRFTPLCLLLFSDLLLITQPKSGQRLQVLDYAHRSLVQAQQVPDPSGPPTFRLSLLSNHQGRPTHRLLQAASLSDMQRWLGAFPTPGPLPCSPDTIYEDCECSQELCSEPSTPSKTEGQSLESKAPRKHLHKNPEGWLKGLPGAFPAQLVCEVTGEHERRKHLRQHQKLLEAVGPSSGTPDTPQP
Protein: DNA-directed RNA polymerase subunit, putative (EC 2.7.7.6) (Q387N1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- DNA-direcetd RNA polymerase II, subunit 9, putative
- DNA-directed RNA polymerases I, II, and III subunit RPABC5
- Plastid-encoded RNA polymerase subunit alpha
- Plastid-encoded RNA polymerase subunit alpha
- DNA-dependent RNA polymerases, putative
- DNA-directed RNA polymerase subunit beta
- DNA-directed RNA polymerase subunit beta
- DNA-directed RNA polymerase I subunit RPA1
- DNA-directed RNA polymerase subunit beta
- DNA-directed RNA polymerases I, II, and III subunit RPABC3
Sequence:
MIQSDIVSYVGEMGDVPDALLITPLKDRKSSVYLTKYEVARIIGERARQIVNGTSVLLDSQNGCGTGNSLELAEGCADPFAASVDPIHITKLELLQGRIPMIVRRTWPDGRTENIPVNELKVDKMLLDVQH
Protein: Uncharacterized protein C115.02c (O42895)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
- ATPase family gene 2 protein
Sequence:
MLQVLRVSAPCFAFVDTIGSIGVCRVVRFTTFHNTPIEVYNKKVNDGVWKRDPYQETAVKAINRLYTELESYTQPPITQDSMPAEKGSILSWISPLKKMFSRKKSPTLTSSLPVPGMPKGIYLYGDVGCGKTALMDLFYHNLPPNVTRSQRIHFHAFMMQVHRTSHDLQDRYGFEIDFIDHIASGIAKETTVLCFDELQVTDVADALLLRRLFEALMKYGVVIFITSNRAPSDLYKNGIQRESFIPCIKLLEHRLQVICLDSPNDYRRLKSKTEDTYLYPANSPEVKKALENWFLCYADEKDPAHQDEVEVFGRKIIVPKASGNVAWFTFEQLCGEPKSAADYLSLASRYHVFIVSDIPKLSIESKDLIHRFITFIDALYDTHGKLILSSEVPVQEIYPTAPSEVLSSTADPAAKGKIESHYHGAFGGIEEVFTFTRCLSRLSEMKKQSWIHSP
Protein: Ferric uptake regulation protein (Ferric uptake regulator) (P33117)
Organism: Vibrio vulnificus (strain CMCP6)
Function: Fur acts as a repressor, employing Fe(2+) as a cofactor to bind the operator of the iron transport operon.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
Sequence:
MSDNNQALKDAGLKVTLPRLKILEVLQQPDCQHISAEDLYKKLIDLGEEIGLATVYRVLNQFDDAGIVTRHHFEGGKSVFELSTQHHHDHLVCLDCGEVIEFSDDIIEERQKEIAAAYNVQLTNHSLYLYGKCGDGSCKGNPDAHKRKN
Protein: Large ribosomal subunit protein uL10 (60S acidic ribosomal protein P0) (F8VU65)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MPREDRATWKSNYFLKIIQLLDDYPKCFIVGADNVGSKQMQQIRMSLRGKAVVLMGKNTMMRKAIRGHLENNPALEKLLPHIRGNVGFVFTKEDLTEIRDMLLANKVPAAARAGAIAPCEVTVPAQNTGLGPEKTSFFQALGITTKISRGTIEILSDVQLIKTGDKVGASEATLLNMLNISPFSFGLVIQQVFDNGSIYNPEVLDITEETLHSRFLEGVRNVASVCLQIGYPTVASVPHSIINGYKR
Protein: RB-associated KRAB zinc finger protein (RB-associated KRAB repressor) (hRBaK) (Zinc finger protein 769) (Q9NYW8)
Organism: Homo sapiens (Human)
Function: May repress E2F-dependent transcription. May promote AR-dependent transcription.
Subcellular location: Nucleus {ECO:0000269|PubMed:10702291}.
Interaction partners:
- Importin-8
- Zinc finger protein 12
- Retinoblastoma-associated protein
Sequence:
MNTLQGPVSFKDVAVDFTQEEWQQLDPDEKITYRDVMLENYSHLVSVGYDTTKPNVIIKLEQGEEPWIMGGEFPCQHSPEAWRVDDLIERIQENEDKHSRQAACINSKTLTEEKENTFSQIYMETSLVPSSIIAHNCVSCGKNLESISQLISSDGSYARTKPDECNECGKTYHGEKMCEFNQNGDTYSHNEENILQKISILEKPFEYNECMEALDNEAVFIAHKRAYIGEKPYEWNDSGPDFIQMSNFNAYQRSQMEMKPFECSECGKSFCKKSKFIIHQRAHTGEKPYECNVCGKSFSQKGTLTVHRRSHLEEKPYKCNECGKTFCQKLHLTQHLRTHSGEKPYECSECGKTFCQKTHLTLHQRNHSGERPYPCNECGKSFSRKSALSDHQRTHTGEKLYKCNECGKSYYRKSTLITHQRTHTGEKPYQCSECGKFFSRVSYLTIHYRSHLEEKPYECNECGKTFNLNSAFIRHRKVHTEEKSHECSECGKFSQLYLTDHHTAHLEEKPYECNECGKTFLVNSAFDGHQPLPKGEKSYECNVCGKLFNELSYYTEHYRSHSEEKPYGCSECGKTFSHNSSLFRHQRVHTGEKPYECYECGKFFSQKSYLTIHHRIHSGEKPYECSKCGKVFSRMSNLTVHYRSHSGEKPYECNECGKVFSQKSYLTVHYRTHSGEKPYECNECGKKFHHRSAFNSHQRIHRRGNMNVLDVENL
Protein: Interferon, alpha-inducible protein 27 (Q8C6G0)
Organism: Mus musculus (Mouse)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MAFSGTGTLVASIVSKMTSSAAMVKAGGAVSGTILAGSKGLILLTQSALGSATSALGALKVGTILSGFSASTLAASPIGEEPALVGREKKSDFRFSFPAAGKAARRQRKEGQSKIYLKGFEFSRAKAVVAVLGGAMTVAAVPPALSAVGFTASGIAASSLAAKMMSLSAIANGGGVPAGGLVAILQSAGAAGLSVPSTVIVGSAGSAVVASVMNICESFYPFLMGSEVADMATEVADMAIEVADISTEEALPNLSNTEKD