wanglab/gogpt-training-data huggingface dataset:
Protein: Pre-rRNA-processing protein pro-1 (Proximal proliferation in germline protein 1) (Q22006)
Organism: Caenorhabditis elegans
Function: Component of the PELP1 complex involved in the nucleolar steps of 28S rRNA maturation and the subsequent nucleoplasmic transit of the pre-60S ribosomal subunit (By similarity). Required for processing ITS2 sequences from rRNA intermediates during 26S rRNA maturation. Required in the soma to promote normal proliferation and prevent germline tumor formation.
Subcellular location: Nucleus, nucleolus {ECO:0000250|UniProtKB:Q9BV38}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q4VBE8}.
Interaction partners:
- Pre-rRNA-processing protein Ipi1 N-terminal domain-containing protein
- Protein SDA1 homolog
- Peptidase M24 domain-containing protein
- NLE domain-containing protein
- Nucleolar GTP-binding protein 2
- Polynucleotide 5'-hydroxyl-kinase nol-9
- Guanine nucleotide-binding protein-like 3 homolog
- Ribosome biogenesis protein BOP1 homolog
- RRM domain-containing protein
- Nucleolar complex protein 2 homolog
Sequence:
MAYLGVDTSRIAGTQPLEMLLVSSGSPDPHSTIIIDPRTGVSSWSYKGSELQGASTGLVEPLGHDGEHVVITTKERPLVHVLAVHPKDRFHQKCVLPGPVSAIVSDNSGHFVFMSIKRQLYCWLLSTGELLSVIDAHYQNITKIVISDDDSMIFTASKDGAVHGYLVTDLVSADRDHTVAPFRKWASHTLSISDLKITNGSNPRVLSAGADHIACLHSISMDSVILKASSDRPLTACAIDPAETRIFIGTEVGNIAQINLFQLAPEERDLLVQAGDEHNTKFRVLNGHSDEISRLAINTDGTLLASGDASGKYCIWEISSHQCLKVSTMRSVINTLRFIPFWKTISGGEHVAKFRPVWDLKREPTKCDRFAIEVSTEFNSDQKHWNDVIEETIDQLLLESGSKSSAQLQWDAEGPARNEAAKAEKAAENTIKNIITLGDDEDDAPEVGNQRRKSGKKNKKNRKNQKKNDFEAAVIEKKQVEPIVIDDEEEVNSSLQKKFDALKAENEKLKEINKQMYEFVAKEIVDSEK
Protein: Uncharacterized protein (Q584U4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MTGADRFNSRSLVKALDHPEPFEDWLQGTRYMQKYLLSLKFQTCRAPYVPTRQEHSKASYLTMSKRKCVDGSQRSRKADELTTETTGAAVGVATPLQHAASAGGDSQGSVRKHSAPQRKGRKSSDNCADTAAVDGVASCDRDLRGSLLRSYNRIKGTYTSSFPAMLTPYRRSYWTYKQREMTKDSYSGGSGGPAVTGECVSGGSDPQQKSKRCPAGARSDGLPSTTERTFLTGPPRFSPTPLPVTLRRKR
Protein: Syntaxin binding protein 1 (A0A0D9SG72)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MHDVIKKVKKKGEWKVLVVDQLSMRMLSSCCKMTDIMTEGITIVEDINKRREPLPSLEAVYLITPSEKSVHSLISDFKDPPTAKYRAAHVFFTDSCPDALFNELVKSRAAKVIKTLTEINIAFLPYESQVYSLDSADSFQSFYSPHKAQMKNPILERLAEQIATLCATLKEYPAVRYRGEYKDNALLAQLIQDKLDAYKADDPTMGEGPDKARSQLLILDRGFDPSSPVLHELTFQAMSYDLLPIENDVYKYETSGIGEARVKEVLLDEDDDLWIALRHKHIAEVSQEVTRSLKDFSSSKRMNTGEKTTMRDLSQMLKKMPQYQKELSKYSTHLHLAEDCMKHYQGTVDKLCRVEQDLAMGTDAEGEKIKDPMRAIVPILLDANVSTYDKIRIILLYIFLKNGITEENLNKLIQHAQIPPEDSEIITNMAHLGVPIVTDSTLRRRSKPERKERISEQTYQLSRWTPIIKDIMEDTIEDKLDTKHYPYISTRSSASFSTTAVSARYGHWHKNKAPGEYRSGPRLIIFILGGVSLNEMRCAYEVTQANGKWEVLIGSTHILTPQKLLDTLKKLNKTDEEISS
Protein: Somatostatin receptor subtype 1 (Q866U3)
Organism: Sus scrofa (Pig)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MFPNGTASSPSSPSPCPGSCGEGSGSRGPGAGTADGMEEPGRNASQNGTLSEGQGSAILISFIYSVVCLVGLCGNSMVIYVILRYAKMKTATNIYILNLAIADELLMLSVPFLVTSTLLRHWPFGALLCRLVLSVDAVNMFTSIYCLTVLSVDRYVAVVHPIKAARYRRPTVAKVVNLGVWVLSLLVILPIVVFSRTAANSDGTVACNMLMPEPAQRWLVGFVLYTFLMGFLLPVGAICLCYVLIIAKMRMVALKAGWQQRKRSERKITLMVMMVVMVFVICWMPFYVVQLVNVFAEQDDATVSQLSVILGYANSCANPILYGFLSDNFKRSFQRILCLSWMDNAAEEPVDYYATALKSRAYSVEDFQPENLESGGVFRNGTCTSRITTL
Protein: Par-2 protein (Q21610)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MTDLDTSSAQIRASQSDLSIANSSPRLLESNATTSTACINDVQQPVRRDLSSELLCPLCDQLFDRPVMVTCGHSYCEPCIERHTRDTRACVICKLDVGPFAAMIPSITLDNMVRKLKNQENIESSYDDLFICEEKLQKAPTPPISEEIPAQKMTRSLSQRSKRRLFFSIAGPTICSSPITPHRRRPLSPSARPAKSSLKIPPEPLNHSLSPPGFHNSHHRDDSLVLAGGNFRRNGFGRRSERFTAATTSAQSFAESSQISTGNSSKIDDESDGTKLKRNSFLRRSLNAFRSKSSGKEQKSFRVFAQIPEHPTEHHDVPEGDVEHLLPEKPTKSSIRSLWKRLFMPKKVSKVSPAAVQLLSQSPSTTDERSHHHTTISFVRLENEHDDPEYDEPLQLSKFSALGYYTGIGRKFERVASGCEITLVVFGHSGAGKTTFVRAIRQLFLEGTDRIRIIPMPERYRLAGIGMMPFPEGDNRLPHIVSMVLNNDETDMEYVLDIIDPEYDNSNLPQAYMDACDAAYLLVDTRNPASILSAHQIHRNMKHAQHIHVECEMLMNVPSEASGQTRVLSANALETTMKTIPIRDVCANQLDKGVLEEMLLSICERVTTARNPQTPTSSPIATSSSPS
Protein: Zinc finger and SCAN domain-containing protein 25 (Zinc finger protein 498) (Q6NSZ9)
Organism: Homo sapiens (Human)
Function: May be involved in transcriptional regulation.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00187}.
Interaction partners:
Sequence:
MLKEHPEMAEAPQQQLGIPVVKLEKELPWGRGREDPSPETFRLRFRQFRYQEAAGPQEALRELQELCRRWLRPELHTKEQILELLVLEQFLTILPREFYAWIREHGPESGKALAAMVEDLTERALEAKAVPCHRQGEQEETALCRGAWEPGIQLGPVEVKPEWGMPPGEGVQGPDPGTEEQLSQDPGDETRAFQEQALPVLQAGPGLPAVNPRDQEMAAGFFTAGSQGLGPFKDMALAFPEEEWRHVTPAQIDCFGEYVEPQDCRVSPGGGSKEKEAKPPQEDLKGALVALTSERFGEASLQGPGLGRVCEQEPGGPAGSAPGLPPPQHGAIPLPDEVKTHSSFWKPFQCPECGKGFSRSSNLVRHQRTHEEKSYGCVECGKGFTLREYLMKHQRTHLGKRPYVCSECWKTFSQRHHLEVHQRSHTGEKPYKCGDCWKSFSRRQHLQVHRRTHTGEKPYTCECGKSFSRNANLAVHRRAHTGEKPYGCQVCGKRFSKGERLVRHQRIHTGEKPYHCPACGRSFNQRSILNRHQKTQHRQEPLVQ
Protein: Aklaviketone reductase DauE (EC 1.1.1.362) (Q53882)
Organism: Streptomyces sp. (strain C5)
Function: Involved in the biosynthesis of aklavinone which is an important precursor common to the formation of the clinically significant anthracyclines such as carminomycin, daunorubicin (daunomycin), rhodomycin, aclacinomycin T (aklavin) and aclacinomycin A (aclarubicin). These compounds are aromatic polyketide antibiotics that exhibit high cytotoxicity and are widely applied in the chemotherapy of a variety of cancers. Catalyzes the NADPH-specific conversion of aklaviketone to yield aklavinone. It can also convert maggiemycin and 7-oxodaunomycinone to epsilon-rhodomycinone and daunomycinone, respectively.
Interaction partners:
Sequence:
MENTQRSVIVTGGGSGIGRAVARAFAARGDRVLVVGRTAGPLAETVDGHKEAHTLAVDITDPAAPQAVVREVRERLGGVVDVLVNNAATAVFGHLGELDRTAVEAQVATNLVAPVLLTQALLDPLETASGLVVNIGSAGALGRRAWPGNAVYGAAKAGLDLLTRSWAVELGPRGIRVIGVAPGVIETGAGVRAGMSQEAYDGFLEAMGQRVPLGRVGRPEDVAWWVVRLADPEAAYASGAVLAVDGGLSVT
Protein: N6-mAMP deaminase (AtMAPDA) (EC 3.5.4.-) (Adenosine deaminase-like protein) (Q8LPL7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the hydrolysis of the free cytosolic methylated adenosine nucleotide N(6)-methyl-AMP (N6-mAMP) to produce inositol monophosphate (IMP) and methylamine. Is required for the catabolism of cytosolic N6-mAMP, which is derived from the degradation of mRNA containing N6-methylated adenine (m6A). Does not possess deaminase activity toward adenosine, AMP, N6-methyladenosine, or N6-mATP in vitro.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:29884623}.
Interaction partners:
- Adenosine kinase 2
- Adenosine kinase 1
- Cytidine deaminase 6
- Cytidine deaminase 5
- Cytidine deaminase 7
- Cytidine deaminase 8
- Cytidine deaminase 3
- Cytidine deaminase 2
- tRNA
- Cytidine deaminase 1
Sequence:
MEWIQSLPKIELHAHLNGSIRDSTLLELARVLGEKGVIVFADVEHVIQKNDRSLVEVFKLFDLIHKLTTDHKTVTRITREVVEDFALENVVYLELRTTPKRSDSIGMSKRSYMEAVIQGLRSVSEVDIDFVTASDSQKLHNAGDGIGRKKIYVRLLLSIDRRETTESAMETVKLALEMRDVGVVGIDLSGNPLVGEWSTFLPALQYAKDNDLHITLHCGEVPNPKEIQAMLDFKPHRIGHACFFKDEDWTKLKSFRIPVEICLTSNIVTKSISSIDIHHFADLYNAKHPLILCTDDFGVFSTSLSNEYALAVRSLGLSKSETFALARAAIDATFAEDEVKQQLRFIFDSASPEHV
Protein: Protein lin-3 (Abnormal cell lineage protein 3) (Lethal protein 94) (Q03345)
Organism: Caenorhabditis elegans
Function: Probable ligand for tyrosine kinase receptor let-23. Essential for vulval induction, where it acts downstream of the synthetic multivulva (synMuv) class genes. Probably by activating let-23, phospholipase plc-3 and inositol 1,4,5-trisphosphate receptor itr-1 signaling cascade, plays a role in ovulation by promoting gonadal sheath cell contractions and spermatheca dilatation during ovulation. Probably by regulating neuronal transmission in ALA neurons, mediates the decrease in pharyngeal pumping and locomotion during the quiescent state that precedes each larval molt, by activating receptor lin-23-mediated signaling cascade.
Subcellular location: Membrane; Single-pass type I membrane protein.
Interaction partners:
- Receptor tyrosine-protein kinase let-23
- Ras protein let-60
- Protein lin-12
- Mitogen-activated protein kinase mpk-1
- Raf homolog serine/threonine-protein kinase
- EGL-17
- Sex muscle abnormal protein 5
- Protein lin-2
- Protein lin-31
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma plc-3
Sequence:
MRKMLLFCILLLFMPQFTVSESCLPSWFRQERSAPEQLQSAENAAENSGSVPPDTSRNSLETNEIGDAPSSTSTPETPTETTISEAGDDEKRTEEVAKELIEKEAEYEGEYEDEKVDEEVEEALKYNEDATQDATSTLKPAVRKEIEKLKEAKCKDYCHHNATCHVEVIFREDRVSAVVPSCHCPQGWEGTRCDRHYVQAFYAPINGRYNVRLSTMSSTAQLLVQQSSTSAIPAFAFLIVMLIMFITIVVYAYRRMSKRSDDMTYTMSHMCPPEAFNVLKTPNGRHIPVHQIPSCSYTIPTPGTVPPNISSTPGSRIPTRQQAIRNNEQARNNFFSILRSQGTIPSRSINDDDTPKHYKSVPRVEVSAINYSGHIDFSTVSYQSTESEVSKASVTCPPPAHTVINIELDSADTNFRSPSRSSGEQGSPATCEPMIRHT
Protein: Placenta growth factor (PlGF) (P49763)
Organism: Homo sapiens (Human)
Function: Growth factor active in angiogenesis and endothelial cell growth, stimulating their proliferation and migration. It binds to the receptor FLT1/VEGFR-1. Isoform PlGF-2 binds NRP1/neuropilin-1 and NRP2/neuropilin-2 in a heparin-dependent manner. Also promotes cell tumor growth.
Subcellular location: Secreted. Note=The three isoforms are secreted but PlGF-2 appears to remain cell attached unless released by heparin.
Interaction partners:
- Vascular endothelial growth factor receptor 2
- Vascular endothelial growth factor receptor 1
- Vascular endothelial growth factor receptor 3
- Neuropilin-1
- Neuropilin-2
- Vascular endothelial growth factor B
- Fibronectin
- Angiopoietin-1 receptor
- High affinity nerve growth factor receptor
- Platelet-derived growth factor receptor beta
Sequence:
MPVMRLFPCFLQLLAGLALPAVPPQQWALSAGNGSSEVEVVPFQEVWGRSYCRALERLVDVVSEYPSEVEHMFSPSCVSLLRCTGCCGDENLHCVPVETANVTMQLLKIRSGDRPSYVELTFSQHVRCECRHSPGRQSPDMPGDFRADAPSFLPPRRSLPMLFRMEWGCALTGSQSAVWPSSPVPEEIPRMHPGRNGKKQQRKPLREKMKPERCGDAVPRR
Protein: Ubiquitin carboxyl-terminal hydrolase MINDY-1 (EC 3.4.19.12) (Deubiquitinating enzyme MINDY-1) (Protein FAM63A) (Q8N5J2)
Organism: Homo sapiens (Human)
Function: Hydrolase that can specifically remove 'Lys-48'-linked conjugated ubiquitin from proteins. Has exodeubiquitinase activity and has a preference for long polyubiquitin chains. May play a regulatory role at the level of protein turnover.
Interaction partners:
- Polyubiquitin-C
- Ubiquitin-ribosomal protein eL40 fusion protein
- Polyubiquitin-B
- Ubiquitin-ribosomal protein eS31 fusion protein
- Na
Sequence:
MEYHQPEDPAPGKAGTAEAVIPENHEVLAGPDEHPQDTDARDADGEAREREPADQALLPSQCGDNLESPLPEASSAPPGPTLGTLPEVETIRACSMPQELPQSPRTRQPEPDFYCVKWIPWKGEQTPIITQSTNGPCPLLAIMNILFLQWKVKLPPQKEVITSDELMAHLGNCLLSIKPQEKSEGLQLNFQQNVDDAMTVLPKLATGLDVNVRFTGVSDFEYTPECSVFDLLGIPLYHGWLVDPQSPEAVRAVGKLSYNQLVERIITCKHSSDTNLVTEGLIAEQFLETTAAQLTYHGLCELTAAAKEGELSVFFRNNHFSTMTKHKSHLYLLVTDQGFLQEEQVVWESLHNVDGDSCFCDSDFHLSHSLGKGPGAEGGSGSPETQLQVDQDYLIALSLQQQQPRGPLGLTDLELAQQLQQEEYQQQQAAQPVRMRTRVLSLQGRGATSGRPAGERRQRPKHESDCILL
Protein: Amino acid transporter 1, putative (Q57V85)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MTSIKTKSPTSVTYPQDDHGSAEAGQANAEVERPQPEERKDGGGCFARVSLFMATIIPPGGIAASAFNIGSTTIGAGIFGLPAAANSSGLVMAMIYLIIITAMTIFSIYALGVAAERTNIRTYEGVARALLGPWGAFCTAAARTFFSFSACVAYVISVGDILSATLKGTNAPDFLKQKSGNRLLTSLMWLCFMLPLVIPRHIDSLRHVSTIAFILMIYTVVVVVVHSCMNGLPENIKNVSVGKDDNAEIILFNSGNRAIEGLGVFIFSYLFHITAYEVYMDMTNRSVGKFVLVVIIAMGMCLPMYALTAFFGYMDFGRNVTGSVLLQYDPVNYPAIMVGFVGVLVMLFVSYALLGLACRNALYDVIGWDFREVAFWKHCIAVVTLSVVMLLCGLFIPKITTVLGFAGSFCGGLLGFILPALFFMYSGGFTWQKVGPFYYISTYVLLITGVIAAVFGTGATIWAVTVG
Protein: Polypeptide N-acetylgalactosaminyltransferase 2 (EC 2.4.1.41) (Polypeptide GalNAc transferase 2) (GalNAc-T2) (pp-GaNTase 2) (Protein-UDP acetylgalactosaminyltransferase 2) (UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 2) [Cleaved into: Polypeptide N-acetylgalactosaminyltransferase 2 soluble form] (Q10471)
Organism: Homo sapiens (Human)
Function: Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Has a broad spectrum of substrates for peptides such as EA2, Muc5AC, Muc1a, Muc1b. Probably involved in O-linked glycosylation of the immunoglobulin A1 (IgA1) hinge region. Involved in O-linked glycosylation of APOC-III, ANGPTL3 and PLTP. It participates in the regulation of HDL-C metabolism.
Subcellular location: Golgi apparatus, Golgi stack membrane {ECO:0000269|PubMed:9394011}; Single-pass type II membrane protein {ECO:0000269|PubMed:9394011}. Secreted {ECO:0000269|PubMed:37453717, ECO:0000269|PubMed:9394011}. Note=Resides preferentially in the trans and medial parts of the Golgi stack. A secreted form also exists.
Interaction partners:
- Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase
- Alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 1
- Acetylgalactosaminyl-O-glycosyl-glycoprotein beta-1,3-N-acetylglucosaminyltransferase
- Glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase 1
- C1GALT1-specific chaperone 1
- Beta-1,4 N-acetylgalactosaminyltransferase 1
- Voltage-dependent P/Q-type calcium channel subunit alpha-1A
- Mucin-5AC
- Mucin-7
Sequence:
MRRRSRMLLCFAFLWVLGIAYYMYSGGGSALAGGAGGGAGRKEDWNEIDPIKKKDLHHSNGEEKAQSMETLPPGKVRWPDFNQEAYVGGTMVRSGQDPYARNKFNQVESDKLRMDRAIPDTRHDQCQRKQWRVDLPATSVVITFHNEARSALLRTVVSVLKKSPPHLIKEIILVDDYSNDPEDGALLGKIEKVRVLRNDRREGLMRSRVRGADAAQAKVLTFLDSHCECNEHWLEPLLERVAEDRTRVVSPIIDVINMDNFQYVGASADLKGGFDWNLVFKWDYMTPEQRRSRQGNPVAPIKTPMIAGGLFVMDKFYFEELGKYDMMMDVWGGENLEISFRVWQCGGSLEIIPCSRVGHVFRKQHPYTFPGGSGTVFARNTRRAAEVWMDEYKNFYYAAVPSARNVPYGNIQSRLELRKKLSCKPFKWYLENVYPELRVPDHQDIAFGALQQGTNCLDTLGHFADGVVGVYECHNAGGNQEWALTKEKSVKHMDLCLTVVDRAPGSLIKLQGCRENDSRQKWEQIEGNSKLRHVGSNLCLDSRTAKSGGLSVEVCGPALSQQWKFTLNLQQ
Protein: Homocysteine S-methyltransferase 2 (EC 2.1.1.10) (S-adenosylmethionine metabolism protein 4) (S-methylmethionine:homocysteine methyltransferase 2) (SMM:Hcy S-methyltransferase 2) (Q08985)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Homocysteine S-methyltransferase involved in the conversion of S-adenosylmethionine (AdoMet) to methionine to control the methionine/AdoMet ratio. Converts also S-methylmethionine (SMM) to methionine.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- 5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase
- S-adenosylmethionine synthase 1
- Adenosylhomocysteinase
- S-adenosylmethionine synthase 2
- Cystathionine gamma-synthase
- Cystathionine beta-lyase
- Putative cystathionine beta-lyase
- Cystathionine beta-synthase
- Homocysteine/cysteine synthase
- Putative cystathionine gamma-synthase YML082W
Sequence:
MARLPLKQFLADNPKKVLVLDGGQGTELENRGIKVANPVWSTIPFISESFWSDESSANRKIVKEMFNDFLNAGAEILMTTTYQTSYKSVSENTPIRTLSEYNNLLNRIVDFSRNCIGEDKYLIGCIGPWGAHICREFTGDYGAEPENIDFYQYFKPQLENFNKNDKLDLIGFETIPNIHELKAILSWDESILSRPFYIGLSVHEHGVLRDGTTMEEIAQVIKDLGDKINPNFSFLGINCVSFNQSPDILESLHQALPNMALLAYPNSGEVYDTEKKIWLPNSDKLNSWDTVVKQYISSGARIIGGCCRTSPKDIQEISAAVKKYT
Protein: Very-long-chain aldehyde decarbonylase CER3 (EC 4.1.99.5) (Protein ECERIFERUM 3) (Protein FACELESS POLLEN 1) (Protein WAX2) (Protein YORE-YORE) (Q8H1Z0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in cuticule membrane and wax production, and in the typhine and sporopollenin biosynthesis of pollen. Core components of a very-long-chain alkane synthesis complex. May be the fatty acid reductase responsible for aldehyde formation.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:19892830}; Multi-pass membrane protein {ECO:0000269|PubMed:19892830}.
Interaction partners:
- 3-ketoacyl-CoA synthase 6
- Fatty acyl-CoA reductase 3
- Protein ECERIFERUM 2
- 3-ketoacyl-CoA synthase 1
- Cytochrome b5 isoform B
- Ethylene-responsive transcription factor WIN1
- Cytochrome P450 86A2
- ABC transporter G family member 11
- Cytochrome b5 isoform A
- Cytochrome B5 isoform C
Sequence:
MVAFLSAWPWENFGNLKYLLYAPLAAQVVYSWVYEEDISKVLWCIHILIICGLKALVHELWSVFNNMLFVTRTLRINPKGIDFKQIDHEWHWDNYIILQAIIVSLICYMSPPLMMMINSLPLWNTKGLIALIVLHVTFSEPLYYFLHRSFHRNNYFFTHYHSFHHSSPVPHPMTAGNATLLENIILCVVAGVPLIGCCLFGVGSLSAIYGYAVMFDFMRCLGHCNVEIFSHKLFEILPVLRYLIYTPTYHSLHHQEMGTNFCLFMPLFDVLGDTQNPNSWELQKKIRLSAGERKRVPEFVFLAHGVDVMSAMHAPFVFRSFASMPYTTRIFLLPMWPFTFCVMLGMWAWSKTFLFSFYTLRNNLCQTWGVPRFGFQYFLPFATKGINDQIEAAILRADKIGVKVISLAALNKNEALNGGGTLFVNKHPDLRVRVVHGNTLTAAVILYEIPKDVNEVFLTGATSKLGRAIALYLCRRGVRVLMLTLSMERFQKIQKEAPVEFQNNLVQVTKYNAAQHCKTWIVGKWLTPREQSWAPAGTHFHQFVVPPILKFRRNCTYGDLAAMKLPKDVEGLGTCEYTMERGVVHACHAGGVVHMLEGWKHHEVGAIDVDRIDLVWEAAMKYGLSAVSSLTN
Protein: Polyadenylate-binding protein (PABP) (H0YAR2)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|RuleBase:RU362004}.
Interaction partners:
Sequence:
MNPSAPSYPMASLYVGDLHPDVTEAMLYEKFSPAGPILSIRVCRDMITRRSLGYAYVNFQQPADAERALDTMNFDVIKGKPVRIMWSQRDPSLRKSGVGNIFIKNLDKSIDNKALYDTFSAFGNILSCKVVCDENGSKGYGFVHFETQEAAERAIEKMNGMLLNDRKVFVGRFKSRKEREAELGARAKEFTNVYIKNFGEDMDDERLKDLFGKFGPALSVKVMTDESGKSKGFGFVSFERHEDAQKAVDEMNGKELNGKQIYVGRAQKKVERQTELKRKFEQMKQDRITRYQGVNLYVKNLDDGIDDERLRKEFSPFGTITSAKVMMEGGRSKGFGFVCFSSPEEATKAVTEMNGRIVATKPLYVALAQRKEERQAHLTNQYMQRMASVRAVPNPVINPYQPAPPSGYFMAAIPQTQNRAAYYPPSQIAQLRPSPRWTAQGARPHPNTSTQTMGPRPAAAAAAATPAVRTVPQYKYAAGVRNPQQHLNAQPQVTMQQPAVHVQGQEPLTASMLASAPPQEQKQMLGERLFPLIQAMHPTLAGKITGMLLEIDNSELLHMLESPESLRSKVDEAVAVLQAHQAKEAAQKAVNSATGVPTV
Protein: Schwannomin-interacting protein 1 (SCHIP-1) (P0DPB3)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10669747}.
Interaction partners:
Sequence:
MERSGQRVTTWDCDQGKHSDSDYREDGMDLGSDAGSSSSSSRASSQSNSTKVTPCSECKSSSSPGGSLDLVSALEDYEEPFPVYQKKVIDEWAPEEDGEEEEEEDERDQRGYRDDRSPAREPGDVSARTRSGGGGGRSATTAMPPPVPNGNLHQHDPQDLRHNGNVVVAGRPSCSRGPRRAIQKPQPAGGRRSGRGPAAGGLCLQPPDGGTCVPEEPPVPPMDWEALEKHLAGLQFREQEVRNQGQARTNSTSAQKNERESIRQKLALGSFFDDGPGIYTSCSKSGKPSLSSRLQSGMNLQICFVNDSGSDKDSDADDSKTETSLDTPLSPMSKQSSSYSDRDTTEEESESLDDMDFLTRQKKLQAEAKMALAMAKPMAKMQVEVEKQNRKKSPVADLLPHMPHISECLMKRSLKPTDLRDMTIGQLQVIVNDLHSQIESLNEELVQLLLIRDELHTEQDAMLVDIEDLTRHAESQQKHMAEKMPAK
Protein: Large ribosomal subunit protein uL1 (60S ribosomal protein L10a) (P62907)
Organism: Rattus norvegicus (Rat)
Function: Component of the large ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P62906}.
Interaction partners:
- Large ribosomal subunit protein eL18
- Large ribosomal subunit protein uL18
- Large ribosomal subunit protein uL4
- Large ribosomal subunit protein eL27
- Large ribosomal subunit protein uL5
- Large ribosomal subunit protein uL14
- Large ribosomal subunit protein eL24
- Large ribosomal subunit protein eL32
- Large ribosomal subunit protein eL13
- Large ribosomal subunit protein eL19
Sequence:
MSSKVSRDTLYEAVREVLHGNQRKRRKFLETVELQISLKNYDPQKDKRFSGTVRLKSTPRPKFSVCVLGDQQHCDEAKAVDIPHMDIEALKKLNKNKKLVKKLAKKYDAFLASESLIKQIPRILGPGLNKAGKFPSLLTHNENMVAKVDEVKSTIKFQMKKVLCLAVAVGHVKMTDDELVYNIHLAVNFLVSLLKKNWQNVRALYIKSTMGKPQRLY
Protein: F-actin-capping protein subunit alpha-2 (CapZ alpha-2) (P47755)
Organism: Homo sapiens (Human)
Function: F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments.
Interaction partners:
- F-actin-capping protein subunit beta
- F-actin-capping protein subunit alpha-1
- Protein S100-B
- Dynactin subunit 2
- Dynactin subunit 1
- Actin-related protein 10
- Alpha-centractin
- Dynactin subunit 5
- F-actin-uncapping protein LRRC16A
- Dynactin subunit 4
Sequence:
MADLEEQLSDEEKVRIAAKFIIHAPPGEFNEVFNDVRLLLNNDNLLREGAAHAFAQYNLDQFTPVKIEGYEDQVLITEHGDLGNGKFLDPKNRICFKFDHLRKEATDPRPCEVENAVESWRTSVETALRAYVKEHYPNGVCTVYGKKIDGQQTIIACIESHQFQAKNFWNGRWRSEWKFTITPSTTQVVGILKIQVHYYEDGNVQLVSHKDIQDSLTVSNEVQTAKEFIKIVEAAENEYQTAISENYQTMSDTTFKALRRQLPVTRTKIDWNKILSYKIGKEMQNA
Protein: Ephrin-A2 (CEK7-ligand) (CEK7-L) (ELF-1) (EPH-related receptor tyrosine kinase ligand 6) (LERK-6) (P52801)
Organism: Mus musculus (Mouse)
Function: Cell surface GPI-bound ligand for Eph receptors, a family of receptor tyrosine kinases which are crucial for migration, repulsion and adhesion during neuronal, vascular and epithelial development. Binds promiscuously Eph receptors residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. With the EPHA2 receptor may play a role in bone remodeling through regulation of osteoclastogenesis and osteoblastogenesis.
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-anchor {ECO:0000305}.
Interaction partners:
- Ephrin type-A receptor 4
- Ephrin type-A receptor 2
- Ephrin type-A receptor 1
- Ephrin type-A receptor 10
- Ephrin type-A receptor 3
- Ephrin type-A receptor 5
- Ephrin type-A receptor 8
- Disintegrin and metalloproteinase domain-containing protein 10
- Ephrin type-A receptor 7
- Tyrosine-protein kinase Fyn
Sequence:
MAPAQRPLLPLLLLLLPLRARNEDPARANADRYAVYWNRSNPRFQVSAVGDGGGYTVEVSINDYLDIYCPHYGAPLPPAERMERYILYMVNGEGHASCDHRQRGFKRWECNRPAAPGGPLKFSEKFQLFTPFSLGFEFRPGHEYYYISATPPNLVDRPCLRLKVYVRPTNETLYEAPEPIFTSNSSCSGLGGCHLFLTTVPVLWSLLGS
Protein: Enolase-phosphatase E1 (EC 3.1.3.77) (2,3-diketo-5-methylthio-1-phosphopentane phosphatase) (Unknown transcript 4 protein) (P32626)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Bifunctional enzyme that catalyzes the enolization of 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P) into the intermediate 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HK-MTPenyl-1-P), which is then dephosphorylated to form the acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene).
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03117, ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03117, ECO:0000269|PubMed:14562095}.
Interaction partners:
- Methylthioribulose-1-phosphate dehydratase
- Acireductone dioxygenase-requiring))
- Methylthioribose-1-phosphate isomerase
- Protein UTR5
- Polyol phosphate phosphatase PYP1
- S-methyl-5'-thioadenosine phosphorylase
Sequence:
MGDNYSTYLLDIEGTVCPISFVKETLFPYFTNKVPQLVQQDTRDSPVSNILSQFHIDNKEQLQAHILELVAKDVKDPILKQLQGYVWAHGYESGQIKAPVYADAIDFIKRKKRVFIYSSGSVKAQKLLFGYVQDPNAPAHDSLDLNSYIDGYFDINTSGKKTETQSYANILRDIGAKASEVLFLSDNPLELDAAAGVGIATGLASRPGNAPVPDGQKYQVYKNFETL
Protein: Chitinase 4 (EC 3.2.1.14) (RE62779p) (Q9W2M6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- N-acetyl-D-glucosamine kinase
- beta-N-acetylhexosaminidase
- beta-N-acetylhexosaminidase
Sequence:
MKLVSIWALAALCLCLGQVASSEKLLNCYWGTWANYRPGDGKFTPSDIDPSLCTHISYTFFGISDAGEFKSLDTWLDMDDGLGFISQTIALKQRNPNLKILAVVGGWNEGSTKYSAMAADPAKRATFVSTSLAFIQQYSFDGLDLDWEYPGQRGGSEADRENFVTLLREIKETYDQYGLELGIAVGASEKSASISYDIPAISQHLTFINVMTYDFHMALDGYLGLNAPLPEVAESIDYWLSHGAPAEKLILGIGFYGHSYQMSDSSQNWPGAACIGPGTAGVYTRENGFLGYHEICLNNWQTVFDQENGAPYAFQGDQWIGYDNPESIQLKMQLVESRNLGGAMMWSIETDDFRGLCGESYPLLKTMNRALGREVSGGSGGGGGGGGEGSVTPAPTAAPTSSPTPAPTPGGGSGGNECAQDGFFVLESDCNKFYQCVGGVRYDFQCGAGLCFNTITLNCDWP