wanglab/gogpt-training-data huggingface dataset:
Protein: Zinc finger FYVE domain-containing protein 9 isoform X1 (Zinc finger, FYVE domain-containing 9a) (A5PMI2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Mothers against decapentaplegic homolog 2
- Mothers against decapentaplegic homolog
- Mothers against decapentaplegic homolog.
- Zinc finger FYVE domain-containing protein
- Zinc finger, FYVE domain-containing 9b.
- ATP-dependent RNA helicase SUPV3L1, mitochondrial
Sequence:
MENYFQAEAFNLDKVLDEFEQNEDETDTPILSDAKWTQILAPPSHLLSLNPALTHSDLSPRDSPISFKPLLDTQTSDGPSLVEVTRLNGKQGLGQQQEGKSEERPADVYSPPLPQPNIGKLVSTDGQLADLPSFNSGVLENGYPASPDHTVQSDIIRFNDDETNQPVIDKKCLKDTGPCELKLEQNGHISDAGRDFISTEEESEDKPSILKNGVKMETSKDESVSPSCKVGIRDNSNGLCPEGSSSHKGVLHKSVNGGGELDCGRENDEGAFQNGVMVENENTEKDNSASNQEEKEKMLKTDHKGMHKESLEGERCLSDGLVEDLDGDAQNQLAVSSKEDSVTEEKEIEESKQETCDPVRQLESGRTGKLNNSRLQPVSIPYGGARPKQPVNLKLQIPQPLSNQVQNEFGTNSKNKNMEPQSRTGGLDASSEATESGVVQINGEHGNGSSGLIIPSESPDNDLQAGQQGAFSKKPLSSLGEVAPVWVPDSQAPICMKCEVKFTFTKRRHHCRACGKVFCAACCSLKSRLMYMDRKEARVCVTCHCALINAQTWENTGSGCNQSPNPNNPAEYCSTIPPLQQAQASGALSSPPPTVMVPVGVLKQPGSEGSLPREQRRVWFADGILPNGEATDSSKAPAANPNPSQPVATSQNSNKSSGANASEAVHGSGALTTSPVGSSFSLIPEDGLPPILISTGVKGGTGGHITDYAVEERPSEIALMQQLEEGCPDPLVFVLNANLLAMVKLVNYVNRKCWYMTTKGMHAVGQAEVVVLLQCLPDEKTIPKDIFTHFVQLYREALAGNVLGHLGHSFFTQSFLGSKEHGGFLYVNPTFQTLQDLPLPNSPYLFGILVQKWETPWAKVFPIRLMLRLGAEYRFYPCPLFSVRFRKPLFGETGHTIMNLLADFRNYQYTLPVVKGLVVDMEVRKTCIKIPSNRYNELMKAMNKSNEHVLAMGACFNDRADSHLVCVQNDDGNYQTQAISIHHQPRKVTGASFFVFSGALKASSGYLAKTSIVEDGVMVQITAETMEALRQALREMKDFSIACGKADQEENQEHVQVQWVDDDHNVNKGVISPIDGKSMESVTSVKIFHGSEYKANGKVIKWTEVFFLRSEDQNNGLSDPADHSRLAENVARAFCMALCPHLKLLKEDGMAKLGLRVTLDSDQVGYLAGSNGQPLLPQYLSELDSALIPVIHSGACQLSEGPVVMELIFYILEIIS
Protein: BZIP domain-containing protein (A7RWP1)
Organism: Nematostella vectensis (Starlet sea anemone)
Interaction partners:
- BZIP domain-containing protein
- BZIP domain-containing protein
- BZIP domain-containing protein
- BZIP domain-containing protein
- Uncharacterized protein
- Stress-activated protein kinase JNK
- Stress-activated protein kinase JNK
- BZIP domain-containing protein
- BZIP domain-containing protein
- BZIP domain-containing protein
Sequence:
LRSPDFSLLKLASPDIEKMLMSLQSGISASNFKLESQTTESGVLQPIDLEIQEVVKRERKKQRNRIASSKCRKRKLEREARLENRVKDLKERNIELNAVANALKQQVCDLKQRVMDHVSEGCQVMLAHQSRMSPS
Protein: Epidermal growth factor-binding protein type B (EGF-BP B) (EC 3.4.21.119) (Glandular kallikrein K13) (mGK-13) (Prorenin-converting enzyme 1) (PRECE-1) (Tissue kallikrein 13) (P36368)
Organism: Mus musculus (Mouse)
Function: Cleaves REN2 at a dibasic site to yield mature renin.
Interaction partners:
Sequence:
MWFLILFLALSLGGIDAAPPLQSRVVGGFNCKKNSQPWQVAVYYQKEHICGGVLLDRNWVLTAAHCYVDQYEVWLGKNKLFQEEPSAQHRLVSKSFPHPGFNMSLLMLQTIPPGADFSNDLMLLRLSKPADITDVVKPIALPTKEPKPGSKCLASGWGSITPTRWQKPDDLQCVFITLLPNENCAKVYLQKVTDVMLCAGEMGGGKDTCRDDSGGPLICDGILQGTTSYGPVPCGKPGVPAIYTNLIKFNSWIKDTMMKNA
Protein: Cyclin-T1 (A0A0G2JXM2)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Cyclin-dependent kinase 9
- ALF transcription elongation factor 4
- Bromodomain containing 4
- ALF transcription elongation factor 1
- Elongation factor for RNA polymerase II 2
- Protein HEXIM1
- MLLT3, super elongation complex subunit
- Cyclin-dependent kinase 7
- Elongation factor for RNA polymerase II
- Cyclin-dependent kinase 12
Sequence:
MEGERKNNNKRWYFTREQLENSPSRRFGVDSDKELSYRQQAANLLQDMGQRLNVSQLTINTAIVYMHRFYMIQSFTQFHRYSMAPAALFLAAKVEEQPKKLEHVIKVAHTCLHPQESLPDTRSEAYLQQVQDLVILESIILQTLGFELTIDHPHTHVVKCTQLVRASKDLAQTSYFMATNSLHLTTFSLQYTPPVVACVCIHLACKWSNWEIPVSTDGKHWWEYVDATVTLELLDELTHEFLQILEKTPSRLKRIRNWRAYQAAMKTKPDDRGADENTSEQTILNMISQTSSDTTIAGLMSMSAASTGAVPSLPASEESSSSLTSVDMLQGERWLSSQPPFKLEASQGHRTSENLALIGVDHSLQHDGSNAFVSQKQTSKSVPSAKVSLKEYRAKHAEELAAQKRQLENMEANVKSQYAYAAQNLLSHDSHSSVILKMPIEGSENPERPFLDKADKSALKMRLPVAGGDKAASSKPEEIKMRIKVHSAGDKHNSVEDSVAKSREHKEKQRTHPSNHHHHHNHHSHKHSHLQLPVGPVSKRPSDPKHSSQTSTLAHKTYSLSSTLSSSSSTRKRGPPEETGAAVFDHPAKIAKSTKSSSLNFPFPPLPTMTQLPGHSSDTSGLPFSQPSCKTRVPHVKLDKGPPGANGHNTTQSIDYQDTVNMLHSLLSAQGVQPTQPPAFEFVHSYGEYMNPRAAGISRSGNTDKPRPPPLPSEPPPPLPPLPK
Protein: Cytokine-like nuclear factor N-PAC (Glyoxylate reductase 1 homolog) (Nuclear protein NP60) (Putative oxidoreductase GLYR1) (K7EMM8)
Organism: Homo sapiens (Human)
Subcellular location: Chromosome {ECO:0000256|ARBA:ARBA00004286}.
Interaction partners:
Sequence:
XGKLGRYPPWPGKIVNPPKDLKKPRGKKCFFVKFFGTEDHAWIKVEQLKPYHAHKEEMIKINKGKRFQQAVDAVEEFLRRAKGKDQTSSHNSSDDKNRRNSSEERSRPNSGDEKRKLSLSEGKVKKNMGEGKKRVSSGSSERGSKSPLKRAQEQSPRKRGRPPKDEKDLTIPESSTVKGMMAGPMAAFKWQPTASEPVKDADPHFHHFLLSQTEKETGSTSIQAADSTAVNGSITPTDKKIGFLGLGLMGSGIVSNLLKMGHTVTVWNRTAEKCDLFIQEGARLGRTPAEVVSTCDITFACVSDPKAAKDLVLGPSGVLQGIRPGKCYVDMSTVDADTVTELAQVIVSRGGRFLEAPVSGNQQLSNDGMLVILAAGDRGLYEDCSSCFQAMGKTSFFLGEVGNAAKMMLIVNMVQGSFMATIAEGLTLAQVTGQSQQTLLDILNQGQLASIFLDQKCQNILQGNFKPDFYLKYIQKDLRLAIALGDAVNHPTPMAAAANEVYKRAKALDQSDNDMSAVYRAYIH
Protein: Class I SAM-dependent methyltransferase (Q9HTB3)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- Glycosyltransferase
- Glycosyltransferase
- Acyltransferase 3 domain-containing protein
- Glycosyltransferase WbpX
- D-rhamnosyltransferase WbpZ
- Methyltransferase type 11 domain-containing protein
- ABC subunit of A-band LPS efflux transporter
- Glycosyltransferase WbpY
- DUF1127 domain-containing protein
- Alginate biosynthesis protein AlgA
Sequence:
MIRALLQRWRSRPAAASEPVSPRMCGLRDAVLDGWFRSETGELLAGFAIGAQDTLLDLGCGEGVATLFAARQGASVIFTDSEEDKVRSLAQQVEAVARRPFTGLVSDSDPLPLRDACADKLVCMEVLEHVANPARVMAELVRLGRPGAQYLLSVPDPVGEHLQQGIAPADYFRAPNHIHIFSRDDFARLVQDAGLVIEHRQASGFFWVMGMIFFWASERAAGRELGGAVRDRIQPPYPALMEDWARLWENLLARPDGLEIKHLLDHFMPKSQVIIARKPLDPGSSRT
Protein: FMRFamide-like neuropeptides 16 [Cleaved into: AQTFVRF-amide 1; AQTFVRF-amide 2; GQTFVRF-amide] (Q7YX32)
Organism: Caenorhabditis elegans
Function: FMRFamides and FMRFamide-like peptides are neuropeptides. AQTFVRF-amide inhibits the activity of dissected pharyngeal myogenic muscle system.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- FMRF-Like Peptide
- FMRFamide-like neuropeptides 14
- FMRFamide-like neuropeptides 5
- FMRFamide-like neuropeptides 7
- FMRFamide-like neuropeptides 1
- FMRFamide-like neuropeptides 22
- FMRFamide-like neuropeptides 6
- FMRFamide-like neuropeptides 11
- FMRFamide-like neuropeptide 18
- FMRFamide-like neuropeptides 9
Sequence:
MNFSGFEFSSIVAFFLLILQLSTAAVLPADYAYGVADEMSALPDSGSLFAEQRPSKRAQTFVRFGKRAQTFVRFGKRGQTFVRFGRSAPFEQ
Protein: Peptidoglycan recognition protein 6 (A0A060VTM4)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Interaction partners:
- Uncharacterized protein
- Peptidoglycan-recognition protein
- Phosphatidylinositol glycan anchor biosynthesis class U protein
- Phosphatidylinositol glycan anchor biosynthesis class U protein
- L-serine ammonia-lyase
- L-serine ammonia-lyase
- L-serine deaminase
- L-serine deaminase
- L-serine dehydratase/L-threonine deaminase
- L-serine deaminase
Sequence:
MSGAQGVEDSMISPMEPHWKWCLTLLVVLVSAHTDTKVTSSQHMDDFIRVLEQVEYRNPGLQPVNACAGQLVSDEFMQHFLGTIREDSTSEAPVMDSNLSDFIGRAVRHQVTERGREEGVVLTADGTTVAMSPVLLGIEAGLVSKTRCQVRGLYPLTLARNLGLSFQRFHSSLLSHRLGPDGCWDDVTSPQVFTLSDKPSLATDALVNGGMDGVILGMEVSAQSQRPLKLSSLLRTYYCHHLEVEGLDTAPRLISRLRRENFRELARPPLLQRQVVRSLVLQRRLIDHSTMLSQEKEELTAVVREGIKEFVHKYMDCPAIIPRCQWGAAPYRGTPTPLSLPLSFMYIHHTYQPGQPCLTFQQCSADMRSMQRFHQDDRGWDDIGYSFVAGSDGYLYEGRGWHWQGAHTKGYNSKGYGVSFIGDYTSRLPSQQTMELVKDRLASCAVGGGRLVGNFTLYGHRQLVKTSCPGDALYSEITGWEHFGCVQYVQM
Protein: UDP-glucuronosyltransferase 1A1 (UGT1A1) (EC 2.4.1.17) (B1) (UDP-glucuronosyltransferase 1-1) (UDPGT 1-1) (UGT1*1) (UGT1-01) (UGT1.1) (Q64550)
Organism: Rattus norvegicus (Rat)
Function: UDP-glucuronosyltransferase (UGT) that catalyzes phase II biotransformation reactions in which lipophilic substrates are conjugated with glucuronic acid to increase the metabolite's water solubility, thereby facilitating excretion into either the urine or bile. Essential for the elimination and detoxification of drugs, xenobiotics and endogenous compounds. Catalyzes the glucuronidation of endogenous estrogen hormones such as estradiol, estrone and estriol (By similarity). Involved in the glucuronidation of bilirubin, a degradation product occurring in the normal catabolic pathway that breaks down heme in vertebrates (By similarity). Also catalyzes the glucuronidation the isoflavones genistein, daidzein, glycitein, formononetin, biochanin A and prunetin, which are phytoestrogens with anticancer and cardiovascular properties (By similarity). Involved in the glucuronidation of the AGTR1 angiotensin receptor antagonist losartan, a drug which can inhibit the effect of angiotensin II (By similarity). Involved in the biotransformation of 7-ethyl-10-hydroxycamptothecin (SN-38), the pharmacologically active metabolite of the anticancer drug irinotecan (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P22309}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Cytochrome P450 1A1
- Cytochrome P450 1A2
- Cytochrome P450 2E1
- Cytochrome P450 1B1
- Catechol O-methyltransferase
- Estrogen sulfotransferase Ste2
- Transmembrane O-methyltransferase homolog
- Cytochrome P450 4A10
- Beta-glucuronidase
- UDP-glucose 6-dehydrogenase
Sequence:
MSVVCRSSCSLLLLPCLLLCVLGPSASHAGKLLVIPIDGSHWLSMLGVIQQLQQKGHEVVVIAPEASIHIKEGSFYTMRKYPVPFQNENVTAAFVELGRSVFDQDPFLLRVVKTYNKVKRDSSMLLSGCSHLLHNAEFMASLEQSHFDALLTDPFLPCGSIVAQYLSLPAVYFLNALPCSLDLEATQCPAPLSYVPKSLSSNTDRMNFLQRVKNMIIALTENFLCRVVYSPYGSLATEILQKEVTVKDLLSPASIWLMRNDFVKDYPRPIMPNMVFIGGINCLQKKALSQEFEAYVNASGEHGIVVFSLGSMVSEIPEKKAMEIAEALGRIPQTVLWRYTGTRPSNLAKNTILVKWLPQNDLLGHPKARAFITHSGSHGIYEGICNGVPMVMMPLFGDQMDNAKRMETRGAGVTLNVLEMTADDLENALKTVINNKSYKENIMRLSSLHKDRPIEPLDLAVFWVEYVMRHKGAPHLRPAAHDLTWYQYHSLDVIGFLLAIVLTVVFIVYKSCAYGCRKCFGGKGRVKKSHKSKTH
Protein: Protein phosphatase 2B regulatory subunit cnb-1 (Calcineurin subunit B) (G5EDN6)
Organism: Caenorhabditis elegans
Function: Regulatory subunit of tax-6/calcineurin A, a calcium-dependent, calmodulin-stimulated protein phosphatase. Confers calcium sensitivity. Plays a role in egg-laying, fertility, growth, movement and cuticle development. Plays a role in sensitivity to CO2 levels. Regulates expression of tax-6 inhibitor rcn-1. Negatively regulates nicotinic acetylcholine receptor (nAChR) sensitivity to nicotine. Negatively regulates lifespan. Involved in endocytic processes including coelomocyte endocytosis, intestine apical endocytosis and synaptic vesicle recycling. May negatively regulate autophagy.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12221132}.
Interaction partners:
- Serine/threonine-protein phosphatase 2B catalytic subunit
- EF-hand domain-containing protein
- Calmodulin
- EF-hand domain-containing protein
- Calcipressin-like protein
- EF-hand domain-containing protein
- Calmodulin-like protein
- Uncharacterized calcium-binding protein B0563.7
- Calmodulin-like protein
- EF-hand domain-containing protein
Sequence:
MGADASLPMEMCSNFDAYELRRLTRRFKKLDVDGSGSLSVEEFMSLPELQQNPLVQRVIDIFDEDGNGEVDFREFIQGISQFSVKGDKNTKLKFAFRIYDMDRDGFISNGELFQVLKMMVGNNLKDSQLQQIVDKTILFHDKDGDGKISFQEFCDVVEHTEVHKKMVLENI
Protein: Kinesin-associated protein (H2KZP1)
Organism: Caenorhabditis elegans
Interaction partners:
- Kinesin-like protein klp-20
- Kinesin-like protein
- Osmotic avoidance abnormal protein 3
- Intraflagellar transport protein 52 C-terminal domain-containing protein
- Intraflagellar transport protein 88 homolog
- WD_REPEATS_REGION domain-containing protein
- Intraflagellar transport protein che-13
- Cytoplasmic dynein 2 light intermediate chain 1
- Similar to Transporter Of divalent Cations
- Kinesin-like protein
Sequence:
MNQVSIDAHPSDQAIIVRFEQSPSSSAGISIKKRASSANVESLGHQKIIHLKEMSLDVDIRALSNVILQKCLFIPATSRSQLEQVLFYIQKRGNQRISARSRSSSAVSFDRRPIHSPTISAELGKIDEYIECFYGETSVEKNKGAVALYELSKNPQNLTQLVNNETLMMALARVFREDWKKHFEVGTNIMNLFVNISKFSCLHGILLHHKIGTLCVNAMEHETKRYDFWIAEMKKTDQETLRKLKTAIRKQAMLLAACVTFLTNLATDISVELKMVRRNLVALLVKCLQMSSESTSSLTTATIKFLLKLSIFDENKIVMEQNGTIEKLLKLFPIQDPELRKAVIMLLFNFSFDSKNLPKMVNGGLVPHMASLLDSDTKALNMMYLLSCNDDAKAMLAYTDAIKLLMKDVLSGTGSEVTKAVLLNICLEKRNAQLVCGQRGQGLDLLMEMSINSRDLMLIKVVRAISSHEGATQNMFLKWIETLIGIAKNEGADNSESKSSFGLECMGTVAELKVAPWAKIIQSENLVPWMKTQLQEGIDESEEVTVLRDIKPLQLQIVIACGTMARQLDAARLLAPLIDTFVQLLQSCQIDDEFVVQLLYVFLQFLKHKELSARLMTQDSALGAHMIDLMHDANAVVREVCDNALLIMGEHSKEWAKRIAGERFKWHNAQWLEMVERDDSEFVDYDDEDFGADLKFDHYDDGFDMNEPLF
Protein: Phytyl ester synthase 2, chloroplastic (EC 2.3.1.-) (Q9LW26)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Acyltransferase involved in fatty acid phytyl ester synthesis in chloroplasts, a process required for the maintenance of the photosynthetic membrane integrity during abiotic stress and senescence. Exhibits phytyl ester synthesis and diacylglycerol acyltransferase activities with broad substrate specificities, and can employ acyl-CoAs, acyl carrier proteins, and galactolipids as acyl donors.
Subcellular location: Plastid, chloroplast, plastoglobule {ECO:0000269|PubMed:16461379, ECO:0000269|PubMed:22274653, ECO:0000269|PubMed:22623494}.
Interaction partners:
- Midasin
- Peroxisomal 2,4-dienoyl-CoA reductase [
- Diacylglycerol O-acyltransferase 3
- Peroxidase 6
- Strigolactones hydrolase CXE15
Sequence:
MAVTVLPSVSGLSAVASSSNLRRLTSASNHRLTAIKSVTSTSSPPTPSSGVQRRRKNNDENRATVAKVVENPYSKVEAARPDLQKRLSDFLEEAREFVGDGGGPPRWFSPLECGAQATNSPLLLYLPGIDGTGLGLIRHHKKLGEIFDIWCLHIPVSDRTPVKDLVKLIEETVKSENFRLPNRPIYLVGESIGACLALDVAARNPNIDLSLILVNPATHVNNFMVQPLSGMLNVLPDGLPTLLEDIFDFGFKQGDPLTGMLDALSNEFSVQRMGGVGGGMLRDVLAVSANLPTLSRMFPKDTLLWKLEMLKYAIASVNSHIYSVRAETLILLSGRDHWLLKEEDIDRYSRTLPKCIVRKLDDNGQFPLLEDGVDLATIIKCTCFYRRGKSHDHITDYIMPTTFELKQQVDDHRLLMDGTSPVMLSTLEDGTVVRSLEGLPSEGPVLYVGYHMILGFELAPMVIQLMTERNIHLRGLAHPMLFKNLQDSLVDTKMFDKYKIMGGVPVSHFNIYKLLREKAHVLLYPGGVREALHRKGEEYKLFWPERSEFVRVASKFGAKIVPFGVVGEDDICEIVLDSNDQRNIPILKDLMEKATKDAGNIREGDESELGNQECYFPGLVPKIPGRFYYYFGKPIETAGKEKELKDKEKAQELYLQVKSEVEQCIDYLKVKRESDPYRHLLPRMLYQASHGWSSEIPTFDL
Protein: General transcription factor IIH subunit 2 (Basic transcription factor 2 44 kDa subunit) (BTF2 p44) (General transcription factor IIH polypeptide 2) (TFIIH basal transcription factor complex p44 subunit) (Q13888)
Organism: Homo sapiens (Human)
Function: Component of the general transcription and DNA repair factor IIH (TFIIH) core complex, which is involved in general and transcription-coupled nucleotide excision repair (NER) of damaged DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. In NER, TFIIH acts by opening DNA around the lesion to allow the excision of the damaged oligonucleotide and its replacement by a new DNA fragment. In transcription, TFIIH has an essential role in transcription initiation. When the pre-initiation complex (PIC) has been established, TFIIH is required for promoter opening and promoter escape. Phosphorylation of the C-terminal tail (CTD) of the largest subunit of RNA polymerase II by the kinase module CAK controls the initiation of transcription. The N-terminus of GTF2H2 interacts with and regulates XPD whereas an intact C-terminus is required for a successful escape of RNAP II form the promoter.
Subcellular location: Nucleus {ECO:0000269|PubMed:27193682}.
Interaction partners:
- General transcription factor IIH subunit 4
- General transcription factor IIH subunit 3
- General transcription factor IIH subunit 5
- Cyclin-H
- General transcription and DNA repair factor IIH helicase/translocase subunit XPB
- Cyclin-dependent kinase 7
- General transcription factor IIH subunit 1
- CDK-activating kinase assembly factor MAT1
- General transcription and DNA repair factor IIH helicase subunit XPD
- General transcription factor IIE subunit 1
Sequence:
MDEEPERTKRWEGGYERTWEILKEDESGSLKATIEDILFKAKRKRVFEHHGQVRLGMMRHLYVVVDGSRTMEDQDLKPNRLTCTLKLLEYFVEEYFDQNPISQIGIIVTKSKRAEKLTELSGNPRKHITSLKKAVDMTCHGEPSLYNSLSIAMQTLKHMPGHTSREVLIIFSSLTTCDPSNIYDLIKTLKAAKIRVSVIGLSAEVRVCTVLARETGGTYHVILDESHYKELLTHHVSPPPASSSSECSLIRMGFPQHTIASLSDQDAKPSFSMAHLDGNTEPGLTLGGYFCPQCRAKYCELPVECKICGLTLVSAPHLARSYHHLFPLDAFQEIPLEEYNGERFCYGCQGELKDQHVYVCAVCQNVFCVDCDVFVHDSLHCCPGCIHKIPAPSGV
Protein: Protein dpy-30 homolog (Dpy-30-like protein) (Dpy-30L) (Q9C005)
Organism: Homo sapiens (Human)
Function: As part of the MLL1/MLL complex, involved in the methylation of histone H3 at 'Lys-4', particularly trimethylation. Histone H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. May play some role in histone H3 acetylation. In a teratocarcinoma cell, plays a crucial role in retinoic acid-induced differentiation along the neural lineage, regulating gene induction and H3 'Lys-4' methylation at key developmental loci. May also play an indirect or direct role in endosomal transport.
Subcellular location: Nucleus {ECO:0000269|PubMed:19651892}. Golgi apparatus, trans-Golgi network {ECO:0000269|PubMed:19651892}. Note=Associated with chromatin at regions enriched in histone H3 trimethylated at 'Lys-4. Highly enriched in gene promoter regions and 5' UTRs, but not in downstream regions of genes or 3' UTRs (By similarity). {ECO:0000250}.
Interaction partners:
- Histone-lysine N-methyltransferase 2C
- Set1/Ash2 histone methyltransferase complex subunit ASH2
- Retinoblastoma-binding protein 5
- Histone-lysine N-methyltransferase SETD1B
- WD repeat-containing protein 5
- Histone-lysine N-methyltransferase SETD1A
- CXXC-type zinc finger protein 1
- Host cell factor 1
- PAX-interacting protein 1
- PAXIP1-associated glutamate-rich protein 1
Sequence:
MEPEQMLEGQTQVAENPHSEYGLTDNVERIVENEKINAEKSSKQKVDLQSLPTRAYLDQTVVPILLQGLAVLAKERPPNPIEFLASYLLKNKAQFEDRN
Protein: Killer cell lectin-like receptor subfamily H, member 1 (A0A8I6AJ99)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
Sequence:
MNEGRLTYAELKSLKSKDKPQPTQKKREYPWRISVVILGTVCLCLLISSIVFGYLFFQGTSKFKIQCEKDANKNAVSSKEVVDPSALPPTTGKGCYKCQGRWFCCGEKCYYFSEEEKTWDESEASCRLLGSHLAKIDNREEQNFIQSRLNYSYWVGLRKKGGQFLWVHQEDEKISSDL
Protein: CAAX prenyl protease 2 (EC 3.4.26.1) (Intramembrane protease Rce1) (IMP Rce1) (Prenyl protein-specific endoprotease 2) (Ras and a-factor-converting enzyme 1) (Q6LZY8)
Organism: Methanococcus maripaludis (strain DSM 14266 / JCM 13030 / NBRC 101832 / S2 / LL)
Function: Endopeptidase which proteolytically removes the C-terminal three residues of farnesylated peptides containing the CAAX motif where C is cysteine, A is an aliphatic amino acid and X is any amino acid. Cleaves the CAAX motif C-terminal to both P1 and P1' positions. Hydrolysis depends on a farnesylated cysteine residue and no activity is shown towards geranylgeranylated peptides.
Subcellular location: Cell membrane {ECO:0000269|PubMed:24291792}; Multi-pass membrane protein {ECO:0000269|PubMed:24291792}.
Interaction partners:
- Possible sodium/proton antiporter
- Conserved hypothetical archaeal protein
- Conserved hypothetical archaeal protein
- Conserved hypothetical archeal protein
- YcaO domain-containing protein
- Uncharacterized protein
- Uncharacterized protein
- Biotin synthase
- Uncharacterized protein
- 4Fe-4S ferredoxin-type domain-containing protein
Sequence:
MISSYKYNPKLYFLSTFVVTYILWFTGAYLSFSSTYSGIYMLIMLPGLMAPFIISTILIAKSKNNELKKDFINRLFNLKLINLKTIPVVFLLMPAVILLSILLSIPFGGSISQFQFSGGFSFSTDFVPVLFLLLLAATFEELGWRGYAFDSLQSRYSLFKASILFGIFWSLWHFPLIFVNNSYQYEIFNQSIWYGLNFFLSILPMGIIITWMCLKNRKSIILAIIFHFLINLNQELLAITQDTKIIETGVLFLVAAAIILYDKKMFFEKLG
Protein: N-acetylglucosamine-6-phosphate deacetylase (GlcNAc 6-P deacetylase) (EC 3.5.1.25) (Amidohydrolase domain-containing protein 2) (Q9Y303)
Organism: Homo sapiens (Human)
Function: Hydrolyzes the N-glycolyl group from N-glycolylglucosamine 6-phosphate (GlcNGc-6-P) in the N-glycolylneuraminic acid (Neu5Gc) degradation pathway. Although human is not able to catalyze formation of Neu5Gc due to the inactive CMAHP enzyme, Neu5Gc is present in food and must be degraded.
Interaction partners:
- Glucosamine-6-phosphate deaminase 1
- Glucosamine-6-phosphate deaminase 2
- Bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase
- GDH/6PGL endoplasmic bifunctional protein
- Glucokinase regulatory protein
- N-acetylglucosaminyl-phosphatidylinositol de-N-acetylase
- N-acetyl-D-glucosamine kinase
- Glutamine--fructose-6-phosphate aminotransferase 2
- 6-phosphogluconolactonase
- Glutamine--fructose-6-phosphate aminotransferase 1
Sequence:
MRGEQGAAGARVLQFTNCRILRGGKLLREDLWVRGGRILDPEKLFFEERRVADERRDCGGRILAPGFIDVQINGGFGVDFSQATEDVGSGVALVARRILSHGVTSFCPTLVTSPPEVYHKVVPQIPVKSGGPHGAGVLGLHLEGPFISREKRGAHPEAHLRSFEADAFQDLLATYGPLDNVRIVTLAPELGRSHEVIRALTARGICVSLGHSVADLRAAEDAVWSGATFITHLFNAMLPFHHRDPGIVGLLTSDRLPAGRCIFYGMIADGTHTNPAALRIAHRAHPQGLVLVTDAIPALGLGNGRHTLGQQEVEVDGLTAYVAGTKTLSGSIAPMDVCVRHFLQATGCSMESALEAASLHPAQLLGLEKSKGTLDFGADADFVVLDDSLHVQATYISGELVWQADAARQ
Protein: RPGR-interacting protein 1 (F1PKQ6)
Organism: Canis lupus familiaris (Dog) (Canis familiaris)
Subcellular location: Cell projection, cilium {ECO:0000256|ARBA:ARBA00004138}.
Interaction partners:
- Nephrocystin 4.
- Centrosomal protein 290.
- X-linked retinitis pigmentosa GTPase regulator
- Aryl hydrocarbon receptor interacting protein like 1.
- Retinal guanylyl cyclase 1
- Cone-rod homeobox protein
- Nephrocystin-1
- Retinal rod rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit delta
- Tubby-like protein
- Retinoid isomerohydrolase
Sequence:
MVPVSKGKNMKAQPPLSRMSREELEDSLFRLREEHMLVKELSWKQQDEIKRARTALLRLTAARRDPRAPGDPRDPSTPGAEAERPARRRQVQRPAGPPAPPGRLPRARGVHRGLHSVRGPDRGRREPRDRPSYTAPPTFRDQATSEKTGGEIPSEPNTLLVEEPPKSLEKMWSKGEEFEQRSSLECAQKAAELRASIKDNIELIRLKKLLRERNTSLVATKAQLTEVQEAYETLLQKNQGILSAAHDALVGQVSELRAELKEESKKAVSLKSQLEDVSILQITLKEFQERVEDLEKERKLLNDNYDKLLENMLASSNQPHWSSELVGEQLRQKVSQLQDQLDAELEEKTNILLQLSREKAQSQGLRLEVASLRGEQAREAELAPSGDRLCRGPHRPAGVQDVGLAEPRDPGDQGDKTLAQVVSELQASQAETALELEKARDMLALQRAINVCYQEELEAVMTKADNDSKDHTETLQRLTRLLDLKSHRIRQLEEQLKDVVYGTRQLSLCLETQPAHGDEDNVDISLLHKSENLFELHIHQAFLTSAALAQAADTQPTTFCTYYFYDFETHCTPLAVGPQPLYDFTSQYVVETDSLFLNYLHGASARLDLHQAVASEHHTLAAGWICFERVLETVERVHGSTTLTGAGGEDFGVLEYWMRLRFPVGSSLQASNKRKKAQAYLSANVPGAWEAQEDKSRLETWKHQNELRVEIIRCHGLRSRRLGTQPSPYVMYRFFTFSDHDTAIIPASNNPYFGDQARFPVLVTSDLDKYLRREALSVYVFDDEDSEPGSYLGRVQVPLLPLAQNKSIKGDFNLTDPAGNPNGFVEAQLDWKSFYQPPESFLKPEAQPEENSTKDSLESSSKEDQMAFAEIPTEAGQYQAKQKPPQVGERKEREHQVASYSRRKHGKRTGIQGKSRMEYLSRNIITGNTLQQVNYTEWKFSGLKSSIDDGLKYQQKDKEMTSSHSVVMQKEALNPVNDKESCEQASEASEAQTTDSDDIVTPVSLKCPKADSEKMCIEVISLAFNPEAEVMGDETVRQVYVEYKFCDVPLSETETPVSLRKPRAGEEIHFHFSKVIHLDPLTHAARRQFLRDALSGRGREQGRLKFTVVSDPLDDEKECQEVGYAFLELRQVMESGDLVEQELEILSPAERAPIGRLKVGVRAAVALRAVCAEMRPPGAEGAEGAEGAVRKQQPRRQGTLPQPSDPATP
Protein: Uncharacterized protein C2C4.10c (O14043)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Uncharacterized protein C3H7.13
- Putative serine/threonine-protein phosphatase C22H10.04
- Uncharacterized WD repeat-containing protein C1773.01
- Factor arrest protein 11
- Protein phosphatase PP2A regulatory subunit A
- Spindle pole body protein ppc89
- Uncharacterized protein C323.03c
Sequence:
MTELHPDEQHVFLQCLNKMQKELDLSFERYERLFKTTQELQEKVKFSSSRFYNKDSTYSKDQGLAKESAALELQKLKQENVLLRKDLNNLEQISDCYAKGMDDIMKHVATYTATMNERMNACHKEYIKMYEALASERNSLYKINEQNVQSLNKVKEWLLKSLEEEP
Protein: Paraneoplastic antigen-like protein 6A (P0CW24)
Organism: Homo sapiens (Human)
Interaction partners:
- Paraneoplastic antigen Ma1
Sequence:
MAVTMLQDWCRWMGVNARRGLLILGIPEDCDDAEFQESLEAALRPMGHFTVLGKAFREEDNATAALVELDREVNYALVPREIPGTGGPWNVVFVPRCSGEEFLGLGRVFHFPEQEGQMVESVAGALGVGLRRVCWLRSIGQAVQPWVEAVRCQSLGVFSGRDQPAPGEESFEVWLDHTTEMLHVWQGVSERERRRRLLEGLRGTALQLVHALLAENPARTAQDCLAALAQVFGDNESQATIRVKCLTAQQQSGERLSAFVLRLEVLLQKAMEKEALARASADRVRLRQMLTRAHLTEPLDEALRKLRMAGRSPSFLEMLGLVRESEAWEASLARSVRAQTQEGAGARAGAQAVARASTKVEAVPGGPGREPEGLLQAGGQEAEELLQEGLKPVLEECDN