wanglab/gogpt-training-data huggingface dataset:
Protein: Uncharacterized protein YML079W (Q03629)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Interaction partners:
- Secreted protein CSS3
Sequence:
MSANVQEAANAAIEPASFVKVPMPEPPSSLQQLINDWQLIKHREGGYFKETDRSPYTMEVEKPVNGGSGNTEMVTRNQSTLIYYLLTPDSPIGKFHKNINRIIHILQRGKGQYVLVYPDGQVKSFKVGFDYKNGEVSQWVVPGGVFKASFLLPNEEFDNGFLISEVVVPGFDFEDHTFLKGEDELKHLVGPEKAAELAFLA
Protein: AP-2 complex subunit alpha-1 (Adaptor protein complex AP-2 subunit alpha-1) (Adaptor-related protein complex 2 subunit alpha-1) (Alpha-adaptin 1) (Clathrin assembly protein complex 2 alpha large chain 1) (At-a-Ad) (At-alpha-Ad) (Q8LPL6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Subunit of the adaptor protein complex 2 (AP-2). Adaptor protein complexes function in protein transport via transport vesicles in different membrane traffic pathways. Adaptor protein complexes are vesicle coat components and appear to be involved in cargo selection and vesicle formation. AP-2 is involved in clathrin-dependent endocytosis in which cargo proteins are incorporated into vesicles surrounded by clathrin (clathrin-coated vesicles, CCVs) which are destined for fusion with the early endosome. The complex binds polyphosphoinositides (By similarity).
Subcellular location: Membrane, coated pit {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Component of the coat surrounding the cytoplasmic face of coated vesicles in the plasma membrane. {ECO:0000250}.
Interaction partners:
- AP-2 complex subunit mu
- AP-2 complex subunit sigma
- Adaptin ear-binding coat-associated protein 1 NECAP-1
- Calcium-binding EF hand family protein
- Clathrin heavy chain 1
- Beta-adaptin-like protein B
- Clathrin heavy chain 2
- Calcium sensing receptor, chloroplastic
- Beta-adaptin-like protein C
- Clathrin interactor EPSIN 2
Sequence:
MTGMRGLSVFISDVRNCQNKEAERLRVDKELGNIRTCFKNEKVLTPYKKKKYVWKMLYIHMLGYDVDFGHMEAVSLISAPKYPEKQVGYIVTSCLLNENHDFLKLAINTVRNDIIGRNETFQCLALTLVGNIGGRDFAESLAPDVQKLLISSSCRPLVRKKAALCLLRLFRKNPDAVNVDGWADRMAQLLDERDLGVLTSSTSLLVALVSNNHEAYSSCLPKCVKILERLARNQDVPQEYTYYGIPSPWLQVKAMRALQYFPTIEDPSTRKALFEVLQRILMGTDVVKNVNKNNASHAVLFEALSLVMHLDAEKEMMSQCVALLGKFISVREPNIRYLGLENMTRMLMVTDVQDIIKKHQSQIITSLKDPDISIRRRALDLLYGMCDVSNAKDIVEELLQYLSTAEFSMREELSLKAAILAEKFAPDLSWYVDVILQLIDKAGDFVSDDIWFRVVQFVTNNEDLQPYAASKAREYLDKIAIHETMVKVSAYILGEYGHLLARQPGCSASELFSILHEKLPTISTPTIPILLSTYAKLLMHAQPPDPELQKKVWAVFKKYESCIDVEIQQRAVEYFELSKKGPAFMDVLAEMPKFPERQSSLIKKAENVEDTADQSAIKLRAQQQPSNAMVLADQQPVNGAPPPLKVPILSGSTDPESVARSLSHPNGTLSNIDPQTPSPDLLSDLLGPLAIEAPPGAVSNEQHGPVGAEGVPDEVDGSAIVPVEEQTNTVELIGNIAERFHALCLKDSGVLYEDPHIQIGIKAEWRGHHGRLVLFMGNKNTSPLTSVQALILPPAHLRLDLSPVPDTIPPRAQVQSPLEVMNIRPSRDVAVLDFSYKFGANVVSAKLRIPATLNKFLQPLQLTSEEFFPQWRAISGPPLKLQEVVRGVRPLALPEMANLFNSFHVTICPGLDPNPNNLVASTTFYSESTGAILCLARIETDPADRTQLRMTVGTGDPTLTFELKEFIKEQLITVPMGSRALVPAAGPAPPVAQPPSPAALADDPGAMLAGLL
Protein: Nonsense-mediated mRNA decay factor SMG8 (Amplified in breast cancer gene 2 protein) (Protein smg-8 homolog) (Q8ND04)
Organism: Homo sapiens (Human)
Function: Involved in nonsense-mediated decay (NMD) of mRNAs containing premature stop codons. Is recruited by release factors to stalled ribosomes together with SMG1 and SMG9 (forming the SMG1C protein kinase complex) and, in the SMG1C complex, is required to mediate the recruitment of SMG1 to the ribosome:SURF complex and to suppress SMG1 kinase activity until the ribosome:SURF complex locates the exon junction complex (EJC). Acts as a regulator of kinase activity.
Interaction partners:
- Serine/threonine-protein kinase SMG1
- Nonsense-mediated mRNA decay factor SMG9
- Regulator of nonsense transcripts 1
- Regulator of nonsense transcripts 2
- Eukaryotic peptide chain release factor subunit 1
- Nonsense-mediated mRNA decay factor SMG5
- Regulator of nonsense transcripts 3A
- Telomerase-binding protein EST1A
- Nonsense-mediated mRNA decay factor SMG7
- Eukaryotic peptide chain release factor GTP-binding subunit ERF3A
Sequence:
MAGPVSLRDLLMGASAWMGSESPGGSPTEGGGSAAGGPEPPWREDEICVVGIFGKTALRLNSEKFSLVNTVCDRQVFPLFRHQDPGDPGPGIRTEAGAVGEAGGAEDPGAAAGGSVRGSGAVAEGNRTEAGSQDYSLLQAYYSQESKVLYLLLTSICDNSQLLRACRALQSGEAGGGLSLPHAEAHEFWKHQEKLQCLSLLYLFSVCHILLLVHPTCSFDITYDRVFRALDGLRQKVLPLLKTAIKDCPVGKDWKLNCRPCPPRLLFLFQLNGALKVEPPRNQDPAHPDKPKKHSPKRRLQHALEDQIYRIFRKSRVLTNQSINCLFTVPANQAFVYIVPGSQEEDPVGMLLDQLRSHCTVKDPESLLVPAPLSGPRRYQVMRQHSRQQLSFHIDSSSSSSSGQLVDFTLREFLWQHVELVLSKKGFDDSVGRNPQPSHFELPTYQKWISAASKLYEVAIDGKEEDLGSPTGELTSKILSSIKVLEGFLDIDTKFSENRCQKALPMAHSAYQSNLPHNYTMTVHKNQLAQALRVYSQHARGPAFHKYAMQLHEDCYKFWSNGHQLCEERSLTDQHCVHKFHSLPKSGEKPEADRNPPVLYHNSRARSTGACNCGRKQAPRDDPFDIKAANYDFYQLLEEKCCGKLDHINFPVFEPSTPDPAPAKNESSPAPPDSDADKLKEKEPQTQGESTSLSLALSLGQSTDSLGTYPADPQAGGDNPEVHGQVEVKTEKRPNFVDRQASTVEYLPGMLHSNCPKGLLPKFSSWSLVKLGPAKSYNFHTGLDQQGFIPGTNYLMPWDIVIRTRAEDEGDLDTNSWPAPNKAIPGKRSAVVMGRGRRRDDIARAFVGFEYEDSRGRRFMCSGPDKVMKVMGSGPKESALKALNSDMPLYILSSSQGRGLKPHYAQLMRLFVVVPDAPLQIILMPQVQPGPPPCPVFYPEKQEITLPPDGLWVLRFPYAYVTERGPCFPPKENVQLMSYKVLRGVLKAVTQ
Protein: Nuclear pore complex protein Nup50 (50 kDa nucleoporin) (Q7K0D8)
Organism: Drosophila melanogaster (Fruit fly)
Function: Component of the nuclear pore complex that has a direct role in nuclear protein import (By similarity). Actively displaces NLSs from importin-alpha, and facilitates disassembly of the importin-alpha:beta-cargo complex and importin recycling (By similarity). Binds to transcriptionally active chromatin sites when located in the nucleoplasm and is involved in transcriptional activation.
Subcellular location: Nucleus, nucleoplasm {ECO:0000269|PubMed:20144760}. Nucleus envelope {ECO:0000269|PubMed:20144760}. Chromosome {ECO:0000269|PubMed:20144760}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:O08587}. Nucleus membrane; Peripheral membrane protein; Nucleoplasmic side {ECO:0000250|UniProtKB:O08587}. Note=Associates with chromatin (PubMed:20144760).
Interaction partners:
- Nuclear pore complex protein Nup153
- Nuclear pore complex protein Nup214
- Nuclear pore complex protein Nup98-Nup96
- Nuclear pore complex protein Nup107
- Nuclear pore complex protein Nup88
- Nuclear pore complex protein Nup205
- Nuclear pore glycoprotein p62
- Nuclear pore protein
- Nuclear pore complex protein Nup154
- Nuclear pore membrane glycoprotein 210
Sequence:
MAGKRQATSNLNHENWDLEEEPEERGTFRTATEEELKTRVIKKARRKIAGGSSAAEEDGAEEKTAEPKSVFSGFSGFGKPAASPAAGSPFSFLANVTAPATTSSSEPKKSAFSFGFSSSSSSADRPVSTSICGTASTSSTAPSPLPAKESTSTVDGAKPTTSIFGNISAAKKESSEAKTSSSSTSLTSTMETSEYRESVADLNRSVIKFLQDQMGKSPYCILTPVFKNYDEHLKDLQDEESARTNSTKSKTAQARSQEPVAKVSRASSPPKAATTFTFGKPSAPIGASVSPLAKKPNCTITSGGTTTTTATPLVSFGSTASFTAPVPSSSSIFSLTAKPTGEAKSDDTPKSSIFSFGAKDTTTKKDEPNFSAPKTNGFSFGLKSNNDDKPSTSLFAGFGKAPGGAGDGAKGFSFTNSATPFSLGNIHPPAAAAAPAEEEKEEDTPPKVEFKQVVEDDAIYSKRCKVFIKKDKDFGDRGVGTLYLKPVKDSEKIQLLVRADTNLGNILVNLILSKGIPCQRMGKNNVLMVCVPTPEDSKATSLLLRVKTGDEADDLLEKIKEHIK
Protein: DUF1564 family protein (Q72PB3)
Organism: Leptospira interrogans serogroup Icterohaemorrhagiae serovar copenhageni (strain Fiocruz L1-130)
Interaction partners:
Sequence:
MDILLLDDGQKIQSSLIEGSVGTDSLLVPGVYWNRLNLQEKKALRNKLPFLLRKYSKQIASMKRLHNKAGKIKYNRGVGKMKKLSIRVHSGVWATLGVLAAAHGVSRCYLFNYMLWLDEQGDFFVKTLNRGVPIFHWTYKMIWKIDRRQNFISRELQFEPNPMTNQYPYYLKE
Protein: Matrix metalloproteinase-15 (MMP-15) (EC 3.4.24.-) (Membrane-type matrix metalloproteinase 2) (MT-MMP 2) (MTMMP2) (Membrane-type-2 matrix metalloproteinase) (MT2-MMP) (MT2MMP) (SMCP-2) (P51511)
Organism: Homo sapiens (Human)
Function: Endopeptidase that degrades various components of the extracellular matrix. May activate progelatinase A.
Subcellular location: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}; Extracellular side {ECO:0000305}.
Interaction partners:
- Proheparin-binding EGF-like growth factor
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Metalloproteinase inhibitor 2
- Basement membrane-specific heparan sulfate proteoglycan core protein
- Nidogen-1
- Metalloproteinase inhibitor 3
- Matrix metalloproteinase-14
Sequence:
MGSDPSAPGRPGWTGSLLGDREEAARPRLLPLLLVLLGCLGLGVAAEDAEVHAENWLRLYGYLPQPSRHMSTMRSAQILASALAEMQRFYGIPVTGVLDEETKEWMKRPRCGVPDQFGVRVKANLRRRRKRYALTGRKWNNHHLTFSIQNYTEKLGWYHSMEAVRRAFRVWEQATPLVFQEVPYEDIRLRRQKEADIMVLFASGFHGDSSPFDGTGGFLAHAYFPGPGLGGDTHFDADEPWTFSSTDLHGNNLFLVAVHELGHALGLEHSSNPNAIMAPFYQWKDVDNFKLPEDDLRGIQQLYGTPDGQPQPTQPLPTVTPRRPGRPDHRPPRPPQPPPPGGKPERPPKPGPPVQPRATERPDQYGPNICDGDFDTVAMLRGEMFVFKGRWFWRVRHNRVLDNYPMPIGHFWRGLPGDISAAYERQDGRFVFFKGDRYWLFREANLEPGYPQPLTSYGLGIPYDRIDTAIWWEPTGHTFFFQEDRYWRFNEETQRGDPGYPKPISVWQGIPASPKGAFLSNDAAYTYFYKGTKYWKFDNERLRMEPGYPKSILRDFMGCQEHVEPGPRWPDVARPPFNPHGGAEPGADSAEGDVGDGDGDFGAGVNKDGGSRVVVQMEEVARTVNVVMVLVPLLLLLCVLGLTYALVQMQRKGAPRVLLYCKRSLQEWV
Protein: Hoxa10 protein (B2RYB5)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
Interaction partners:
Sequence:
MMDFDERGPCSSNMYLPSCTYYVSGPDFSSLPSFLPQTPSSRPMTYSYSSNLPQVQPVREVTFREYAIEPATKWHPRGNLAHCYSAEELVHRDCLQAPSAAGVPGDVLAKSSANVYHHPTPAVSSNFYSTVGRNGVLPQAFDQFFETAYGTPENLASSDYPGDKNAEKGPPTAAATSAAAVAAAATGAPATSSSDGGGGGGCQEAAAEEKEQRRRPESSSSPESSSGHTEDKAGGSGGQRTRKKRCPYTKYQIRELEREFFFSVYINKEKRLQLSRMLNLTDRQVKIWFQNRRMKEKKINRDRLQYYSANPLL
Protein: Putative trypsin-6 (EC 3.4.21.4) (Serine protease 3 pseudogene 2) (Trypsinogen C) (Q8NHM4)
Organism: Homo sapiens (Human)
Function: May regulate cell migration.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
Sequence:
MNPLLILAFVGAAVAVPFDDDDKIVGGYTCEENSVPYQVSLNSGSHFCGGSLISEQWVVSAGHCYKPHIQVRLGEHNIEVLEGNEQFINAAKIIRHPKYNRIILNNDIMLIKLSTPAVINAHVSTISLPTAPPAAGTECLISGWGNTLSSGADYPDELQCLDAPVLTQAKCKASYPLKITSNMFCVGFLEGGKDSCQGDSGGPVVCNGQLQGIVSWGYGCAQKRRPGVYTKVYNYVDWIKDTIAANS
Protein: Protein lifeguard 4 (Golgi anti-apoptotic protein) (Protein S1R) (Transmembrane BAX inhibitor motif-containing protein 4) (Z-protein) (Q9HC24)
Organism: Homo sapiens (Human)
Function: Anti-apoptotic protein which can inhibit apoptosis induced by intrinsic and extrinsic apoptotic stimuli. Can modulate both capacitative Ca2+ entry and inositol 1,4,5-trisphosphate (IP3)-mediated Ca2+ release.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:17319741, ECO:0000269|PubMed:22418439}; Multi-pass membrane protein {ECO:0000269|PubMed:17319741, ECO:0000269|PubMed:22418439}.
Interaction partners:
- Protein PML
- Sigma non-opioid intracellular receptor 1
- Antiviral innate immune response receptor RIG-I
- Sigma intracellular receptor 2
- Inositol 1,4,5-trisphosphate-gated calcium channel ITPR3
- Eukaryotic translation initiation factor 4E
- Interferon-induced helicase C domain-containing protein 1
- Proteasome subunit beta type-2
- Alpha-1-antitrypsin
Sequence:
MADPDPRYPRSSIEDDFNYGSSVASATVHIRMAFLRKVYSILSLQVLLTTVTSTVFLYFESVRTFVHESPALILLFALGSLGLIFALILNRHKYPLNLYLLFGFTLLEALTVAVVVTFYDVYIILQAFILTTTVFFGLTVYTLQSKKDFSKFGAGLFALLWILCLSGFLKFFFYSEIMELVLAAAGALLFCGFIIYDTHSLMHKLSPEEYVLAAISLYLDIINLFLHLLRFLEAVNKK
Protein: Receptor-like protein 18 (AtRLP18) (Q9ZUK7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
- Pentatricopeptide repeat-containing protein At2g01360
- Cysteine/Histidine-rich C1 domain family protein
- ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase
- Quinoprotein amine dehydrogenase, beta chain-like RIC1-like guanyl-nucleotide exchange factor
- Disease resistance protein
- ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase
- Probable disease resistance protein RDL6
- Ubiquinone biosynthesis O-methyltransferase, mitochondrial
- Disease resistance protein
- At5g07590
Sequence:
MRCQVWNVIELNLSSSCLHGLLNSKSNIFSLQNLRFLDLSNNHFSGQILSSLGNFSSLTTLDLSENHFSGQIPSSLGNLLHLTSLDLTDNNFVGDIPTSLGNLSHLTLLLLGANNLVGEIPFSLGNLSHLTDLTLCENDLAGEIPSSFENLSHLTNLDLSQNNLVGEIPSFFGSFNQLVSLAVEENEFTGNFLLILLNLTNLSDLSLSRNQFTGTLPPNMSSLSNLVLFYADANAFTGTIPSSLLNIPSLSCFDLSDNQLNGNIEFGNISSSLSDLLLGNNNFRGSIHKSISKLVNLYTLDLSHFNTQGSINFSIFSDLKLLVDLHLSHLNTTTTIDLNTFLSSFKSLDTLDLSGNHISAINKSSVSNPVTTARPGLGLTNPLLLSRFNLSGCGVTEFPEFLRTQQTMEILDISNNKINGQVPGWLWTLPTLDYVNLSNNTFTGFQRLMVPSSWQPSMNYFSGANNNFTGNLPAFICAFTLQALHLRKNHLSGVFPENISESLKSLDVGHNQLVGKLPRSLVRISSLEVLNVENNKINDTFPFWLSSLEELQVLVLRSNAFHGPMQQTRFPNLRIIDVSHNHFNGTLPSDFFVNWTVMFLLGENEDQFNGEYMGTSYYSDSIVVMNKGLEMEMVRILKIFTSVDFSRNKFEGEIPKSIGLLKELHVLNLSSNTFTGHIPSSMGKLRELESLDVAQNKLSGDIPQDLGDLSYLAYMNFSHNQLVGPLPGGTQFLTQNCSSFEENAGHFGPSLEKVCDIHGKTMQESEMPGSEEDEEEVISWIAATIGFIPGIAFGLMMGYILVCYKPEWFMNVFGKNKSRSTSSTTR
Protein: DnaJ protein P58IPK homolog A (OsP58A) (Chaperone protein dnaJ C16) (OsDjC16) (A0A0P0VG31)
Organism: Oryza sativa subsp. japonica (Rice)
Function: May play a role in protein folding in the endoplasmic reticulum.
Subcellular location: Endoplasmic reticulum lumen {ECO:0000269|PubMed:24153418}. Note=Localizes to the endoplasmic reticulum (ER) and to punctae around the ER. {ECO:0000269|PubMed:24153418}.
Interaction partners:
- DnaJ protein ERDJ3B
- Os02g0710900 protein
- Os01g0757900 protein
- Endoplasmin homolog
- Heat shock 70 kDa protein BIP4
- Os11g0696600 protein
- Os05g0181000 protein.
- 70 kDa heat shock protein
- Os06g0679800 protein
- Heat shock 70 kDa protein BIP5
Sequence:
MVAMARWPWRVLLPLLLLHSSPVFFVFAQEGQDNDPSTLFKRALEMMNLRKYDGSLGLLNAVLEVEPNHSEAYRQRASVLRHKCRYKEAEGDYSKYLELKPGSSSVEKELSQLLQAQNALESAYGQFESHDFSKVLDYINKIVLVFSPDCLKAKLLKAKALLALKDYSTVISETGFILKEDEDNLDALLLRGRAYYYLADHDVASRHYQKGLRLDPEHSELKKAYFGLKNLVKKTKSAEDNAAKGKLRVSAEDYKASLAMDPDHTSYNVHLYLGLCKVLVKLGRGKEAISSCTEALNIDGELVDALTQRGEAKLLTEDWEGAVQDLKEAAQKSPQDMGIREALMRAEKQLKLSKRKDWYKILGISKTASAAEIKRAYKKLALQWHPDKNVDKREEAENMFREIAAAYEVLGDEDKRVRYDRGEDLDEMNMGGGGGGGFNPFGGGGQQYTFHYDGGFHGGGGFPGGGFPGGFQFNFG
Protein: GH10249p (Vesicular monoamine transporter, isoform D) (Q8IH57)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Aromatic-L-amino-acid decarboxylase
- Synaptotagmin 1
- Ras-related protein Rab-3
- MIP05841p)
- Sodium-dependent serotonin transporter
- Vesicular glutamate transporter, isoform A
- Portabella
- Tyramine beta-hydroxylase
- Tyrosine 3-monooxygenase
- Neuronal synaptobrevin, isoform J
Sequence:
MQSSTDAGNGGPRKHTQSTAPQKQSEISETTSFTVNANTTTNSQQQQIPGGPASNTPSKNPFKQQLDSNQQNGNMEPDCGIMGVGKEPPVPPPPTYQSQTYAGRQAPPPADQYREEDPRAAGSWAAAKSWMVSWRGSNRLVLVIVAIALLLDNMLLTTVVPIIPEFLYDIRHPDAPLDSFPRTPLTSNVPPPPTPCPCNKDGSEAAPLEISTISPEENETYYRELEERHNELVGETVEVGLLFASKAFVQLLVNPIVGPLTHRIGYSIPMFAGFVIMFLSTIIFAFGRSYLVLFVARALQGIGSSCSSVSGMGMLADRFTDDKERGNAMGIALGGLALGVLIGPPFGGVMYEFVGKSAPFLILAALALGDGLLQLFMLQPSIQKAETEPPSLKSLISDPYILIAAGAITFANMGIAMLEPSLPLWMVDNMGATRWEQGVAFLPASISYLIGTNLFGPLGHKIGRWFAACLGLIIIGGCLIFIPMATSITHLIIPNAGLGFAIGMVDSSMMPELGYLVDIRHSAVYGSVYALGDVAFCVGFAVGPALSGSLVKSIGFEWMLFGIAILCFMYAPLLTLLKNPPTSDEKKVRMAREAAEAAAAAAAASGEFSGIPQMTASCPAIMHGASVPDSDAEAGRTNEAYESERL
Protein: Integrin linked kinase, isoform A (LD24671p) (Putative integrin-linked kinase) (Q9V400)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004202}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004202}. Cytoplasm, myofibril, sarcomere {ECO:0000256|ARBA:ARBA00004204}.
Interaction partners:
- LIM domain-containing protein
- GH23568p
- Rhea, isoform B
- Integrin beta-PS
- Ras suppressor protein 1
- Paxillin, isoform F
- Vinculin
- Unc-112-related protein
- Fermitin 2
- Integrin beta-nu
Sequence:
MEDIFHWCREGNSIQVRLWLDETEHDNNLGDDHGFSPLHWVAKEGHAKLVETLLQRGSRVNATNMGDDIPLHLAAAHGHRDVVQMLIKERSDVNAVNEHGNTPLHYACFWGYDMICEDLLNAGAQVGIANKDGHTPLEKAKPSLAKRLQDLVEKSGREVKVISFKEQSWQGLKTRSRDATLSRFKGISMGDLDLHTKLSVTPSGETWRGRWQKNDVVAKILAVRQCTPRISRDFNEEFPKLRIFSHPNILPIIGACNSPPNLVTISQFMPRSSLFSLLHGATGVVVDTSQAVSFALDVARGMAFLHSLERIIPTYHLNSHHVMIDDDLTARINMGDAKFSFQEKGRIYQPAWMSPETLQRKQADRNWEACDMWSFAILIWELTTREVPFAEWSPMECGMKIALEGLRVKIPPGTSTHMAKLISICMNEDPGKRPKFDMVVPILEKMRR
Protein: Outer dense fiber protein 4 (Outer dense fiber of sperm tails protein 4) (Testis-specific protein oppo 1) (Q8VI88)
Organism: Mus musculus (Mouse)
Function: Component of the outer dense fibers (ODF) of spermatozoa which could be involved in sperm tail structure, sperm movement and general organization of cellular cytoskeleton.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Ciliary microtubule associated protein 1A
Sequence:
MEPDLNEEESERIRTSRNRRSLEHRRNSLLPFQWKATNNSRWMAQVVASEFSLVAFLLLLVMVFSKKWLYPSKSRFHQRYPQNVTKRVYTSIHSMSTGLLYICVSKSCPSSDNGEDNFKMWTIHPVFGVAKISFTLAIGLGFVLTTWLHLPYLPCLQRMPFFGLIGIILSFCEVTLIFLTLLLFPVNLWIYELRKNISVPIGWSYFIGWLVLILYFTCGILCYLNHKNYWSLIMSSTTINTACSSLGPESLVSPSQTPSSQENSQESPKDDQKPSSPDKVVSPPQPDTTG
Protein: Hemomucin (Q58SN4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
VTPPKDLKGALESNFHLEGAERLLEWRVYGPECLIARNNEIYTGIHGGEVIKLTSNHVTHVTKIGQPCEDIYEESRCGRPLGLAFDTQGNNLIIADAYYGLWQVDLGTNKKTLLVSPAQELAGKSINRPAKIFNGVTVSKEGDVYWTDSSSDFTIEDLVFASFANPSGRLFKYNRSKNVSEVLLDELAFANGLALSPNEDFIVVAETGAMRLTKYHLKGAKAGQSEVFVDGLPGLPDNLTPDAEGIWVPLVQSADSEHPNGFTLFTRFPSVRLFLARMLALFELPFRYLNSVYPNKFSQRFIHFVGHMESITVLAPKRTTVVRVDWNGNIVGSLHGFDKSAATVSHVLEFQDFLFLGSPTNQYLARVKSPKAKQPTLKVRNVRVEGEGLQASIGVPPSKATPKPKAAPSTTTPKPTATTTTTTPKPTTKTTTTTTTPKPTTTTTTKKPTTTTTTTTTTPKPTTTKPPTAKPSTTTTTTTTPKPTTTTTPTTPTTPTPEPSKPKVKRTVPEKPAPVEEEIPSD
Protein: Exostosin-1 (EC 2.4.1.225) (Exostosin glycosyltransferase 1) (Multiple exostoses protein 1 homolog) (N-acetylglucosaminyl-proteoglycan 4-beta-glucuronosyltransferase) (P97464)
Organism: Mus musculus (Mouse)
Function: Glycosyltransferase required for the biosynthesis of heparan-sulfate. The EXT1/EXT2 complex possesses substantially higher glycosyltransferase activity than EXT1 or EXT2 alone. Required for the exosomal release of SDCBP, CD63 and syndecan (By similarity).
Subcellular location: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q16394}; Single-pass type II membrane protein {ECO:0000255}. Golgi apparatus, cis-Golgi network membrane {ECO:0000250|UniProtKB:Q16394}; Single-pass type II membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:9703997}; Single-pass type II membrane protein {ECO:0000255}. Note=The active heparan sulfate polymerase complex composed of EXT1 and EXT2 is localized to the Golgi apparatus. If both proteins are individually detected in the endoplasmic reticulum, the formation of the complex promotes their transport to the Golgi. {ECO:0000250|UniProtKB:Q16394}.
Interaction partners:
- Exostosin-2
- Bifunctional heparan sulfate N-deacetylase/N-sulfotransferase 1
- Heparan sulfate 2-O-sulfotransferase 1
- Bifunctional heparan sulfate N-deacetylase/N-sulfotransferase 2
- D-glucuronyl C5-epimerase
- Heparan-sulfate 6-O-sulfotransferase 1
- Heparan sulfate glucosamine 3-O-sulfotransferase 1
- Syndecan-4
- Glypican-4
- Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 3
Sequence:
MQAKKRYFILLSAGSCLALLFYFGGVQFRASRSHSRREEHSGRNGLHQPSPDHFWPRFPDALRPFFPWDQLENEDSSVHISPRQKRDANSSIYKGKKCRMESCFDFTLCKKNGFKVYVYPQQKGEKIAESYQNILAAIEGSRFYTSDPSQACLFVLSLDTLDRDQLSPQYVHNLRSKVQSLHLWNNGRNHLIFNLYSGTWPDYTEDVGFDIGQAMLAKASISTENFRPNFDVSIPLFSKDHPRTGGERGFLKFNTIPPLRKYMLVFKGKRYLTGIGSDTRNALYHVHNGEDVLLLTTCKHGKDWQKHKDSRCDRDNTEYEKYDYREMLHNATFCLVPRGRRLGSFRFLEALQAACVPVMLSNGWELPFSEVINWNQAAVIGDERLLLQIPSTIRSIHQDKILALRQQTQFLWEAYFSSVEKIVLTTLEIIQDRIFKHISRNSLIWNKHPGGLFVLPQYSSYLGDFPYYYANLGLKPPSKFTAVIHAVTPLVSQSQPVLKLLVAAAKSQYCAQIIVLWNCDKPLPAKHRWPATAVPVIVIEGESKVMSSRFLPYDNIITDAVLSLDEDTVLSTTEVDFAFTVWQSFPERIVGYPARSHFWDNSKERWGYTSKWTNDYSMVLTGAAIYHKYYHYLYSHYLPASLKNMVDQLANCEDILMNFLVSAVTKLPPIKVTQKKQYKETMMGQTSRASRWADPDHFAQRQSCMNTFASWFGYMPLIHSQMRLDPVLFKDQVSILRKKYRDIERL
Protein: Class E basic helix-loop-helix protein 40 (bHLHe40) (Class B basic helix-loop-helix protein 2) (bHLHb2) (Enhancer-of-split and hairy-related protein 2) (SHARP-2) (O35780)
Organism: Rattus norvegicus (Rat)
Function: Transcriptional repressor involved in the regulation of the circadian rhythm by negatively regulating the activity of the clock genes and clock-controlled genes. Acts as the negative limb of a novel autoregulatory feedback loop (DEC loop) which differs from the one formed by the PER and CRY transcriptional repressors (PER/CRY loop). Both these loops are interlocked as it represses the expression of PER1/2 and in turn is repressed by PER1/2 and CRY1/2. Represses the activity of the circadian transcriptional activator: CLOCK-BMAL1|BMAL2 heterodimer by competing for the binding to E-box elements (5'-CACGTG-3') found within the promoters of its target genes. Negatively regulates its own expression and the expression of DBP and BHLHE41/DEC2. Acts as a corepressor of RXR and the RXR-LXR heterodimers and represses the ligand-induced RXRA and NR1H3/LXRA transactivation activity. May be involved in the regulation of chondrocyte differentiation via the cAMP pathway (By similarity). Represses the transcription of NR0B2 and attentuates the transactivation of NR0B2 by the CLOCK-BMAL1 complex (By similarity). Drives the circadian rhythm of blood pressure through transcriptional repression of ATP1B1 in the cardiovascular system (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:O14503}. Nucleus {ECO:0000250|UniProtKB:O14503}. Note=Predominantly localized in the nucleus (By similarity). {ECO:0000250|UniProtKB:O14503}.
Interaction partners:
- Basic helix-loop-helix ARNT-like protein 1
- Cryptochrome-1
- Period circadian protein homolog 2
- Nuclear receptor subfamily 1 group D member 1
- Period circadian protein homolog 3
- Nuclear factor interleukin-3-regulated protein
- Cryptochrome-2
- Circadian locomoter output cycles protein kaput
- Neuronal PAS domain protein 2
- Nuclear receptor subfamily 1 group D member 2
Sequence:
MERIPSAQPPPTCLPKTPGLEHGDLSGMDFAHMYQVYKSRRGIKRSEDSKETYKLPHRLIEKKRRDRINECIAQLKDLLPEHLKLTTLGHLEKAVVLELTLKHVKALTNLIDQQQQKIMALQSGLQAGDLSGKNIEAGQEMFCSGFQTCAREVLQYLAKHENTRDLKSSQLVTHLHRVVSELLQGSASRKPLDSAPKPVDFKEKPSFLAKGSEGPGKNCVPVIQRTFAPSGGEQSGSDTDTDSGYGGELEKGDLRSEQPYFKSDHGRRFTVGERVSTIKQESEEPPTKKSRMQLSDEEGHFVGSDLMGSPFLGPHPHQPPFCLPFYLIPPSATAYLPMLEKCWYPTSVPLLYPGLNTSAAALSSFMNPDKIPTPLLLPQRLPSPLAHSSLDSSALLQALKQIPPLNLETKD
Protein: PTI1-like tyrosine-protein kinase 2 (PTI1-2) (EC 2.7.10.2) (O49339)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable tyrosine-protein kinase involved in oxidative burst-mediated signaling leading to specific genes expression.
Interaction partners:
- Serine/threonine-protein kinase OXI1
Sequence:
MRRWICCGDKKGDSDLSNEEVHLKSPWQNSEANQKNQKPQAVVKPEAQKEALPIEVPPLSVDEVKEKTDNFGSKSLIGEGSYGRVYYATLNDGKAVALKKLDVAPEAETNTEFLNQVSMVSRLKHENLIQLVGYCVDENLRVLAYEFATMGSLHDILHGRKGVQGAQPGPTLDWLTRVKIAVEAARGLEYLHEKVQPPVIHRDIRSSNVLLFEDYQAKVADFNLSNQAPDNAARLHSTRVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKPVDHTMPRGQQSLVTWATPRLSEDKVKQCVDPKLKGEYPPKSVAKLAAVAALCVQYESEFRPNMSIVVKALQPLLKPPAPAPAPVPES
Protein: Taste receptor type 2 member 31 (T2R31) (Taste receptor type 2 member 44) (T2R44) (Taste receptor type 2 member 53) (T2R53) (P59538)
Organism: Homo sapiens (Human)
Function: Receptor that may play a role in the perception of bitterness and is gustducin-linked. May play a role in sensing the chemical composition of the gastrointestinal content. The activity of this receptor may stimulate alpha gustducin, mediate PLC-beta-2 activation and lead to the gating of TRPM5 (By similarity). Activated by the sulfonyl amide sweeteners saccharin and acesulfame K.
Subcellular location: Membrane; Multi-pass membrane protein.
Interaction partners:
- Guanine nucleotide-binding protein G
- Taste receptor type 1 member 2
- Taste receptor type 1 member 3
- Taste receptor type 1 member 1
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-2
Sequence:
MTTFIPIIFSSVVVVLFVIGNFANGFIALVNSIERVKRQKISFADQILTALAVSRVGLLWVLLLNWYSTVFNPAFYSVEVRTTAYNVWAVTGHFSNWLATSLSIFYLLKIANFSNLIFLHLKRRVKSVILVMLLGPLLFLACQLFVINMKEIVRTKEYEGNLTWKIKLRSAVYLSDATVTTLGNLVPFTLTLLCFLLLICSLCKHLKKMQLHGKGSQDPSTKVHIKALQTVIFFLLLCAVYFLSIMISVWSFGSLENKPVFMFCKAIRFSYPSIHPFILIWGNKKLKQTFLSVLRQVRYWVKGEKPSSP