wanglab/gogpt-training-data huggingface dataset:
Protein: GPI mannosyltransferase 2 (EC 2.4.1.-) (GPI mannosyltransferase II) (GPI-MT-II) (Phosphatidylinositol-glycan biosynthesis class V protein) (PIG-V) (Q9NUD9)
Organism: Homo sapiens (Human)
Function: Alpha-1,6-mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers the second mannose to the glycosylphosphatidylinositol during GPI precursor assembly.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:15623507}; Multi-pass membrane protein {ECO:0000269|PubMed:15623507}.
Interaction partners:
- GPI alpha-1,4-mannosyltransferase I, catalytic subunit
- GPI alpha-1,2-mannosyltransferase 3
- GPI ethanolamine phosphate transferase 1
- Dolichol phosphate-mannose biosynthesis regulatory protein
- GPI ethanolamine phosphate transferase 3, catalytic subunit
- Dolichol-phosphate mannosyltransferase subunit 3
- Acyltransferase PGAP2
- Glucosaminyl-phosphatidylinositol-acyltransferase PIGW
- Dol-P-Man:Man
- N-acetylglucosaminyl-phosphatidylinositol de-N-acetylase
Sequence:
MWPQDPSRKEVLRFAVSCRILTLMLQALFNAIIPDHHAEAFSPPRLAPSGFVDQLVEGLLGGLSHWDAEHFLFIAEHGYLYEHNFAFFPGFPLALLVGTELLRPLRGLLSLRSCLLISVASLNFLFFMLAAVALHDLGCLVLHCPHQSFYAALLFCLSPANVFLAAGYSEALFALLTFSAMGQLERGRVWTSVLLFAFATGVRSNGLVSVGFLMHSQCQGFFSSLTMLNPLRQLFKLMASLFLSVFTLGLPFALFQYYAYTQFCLPGSARPIPEPLVQLAVDKGYRIAEGNEPPWCFWDVPLIYSYIQDVYWNVGFLKYYELKQVPNFLLAAPVAILVAWATWTYVTTHPWLCLTLGLQRSKNNKTLEKPDLGFLSPQVFVYVVHAAVLLLFGGLCMHVQVLTRFLGSSTPIMYWFPAHLLQDQEPLLRSLKTVPWKPLAEDSPPGQKVPRNPIMGLLYHWKTCSPVTRYILGYFLTYWLLGLLLHCNFLPWT
Protein: Uncharacterized protein (O51254)
Organism: Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31) (Borrelia burgdorferi)
Interaction partners:
- LysM domain protein
- C4-type zinc ribbon domain-containing protein
- TPR domain protein
- Tetratricopeptide repeat domain protein
- Tetratricopeptide repeat domain protein
Sequence:
MRRLFLLYILCSFVFLNLFAQGSSSYIDKQKELAIFYYEVGQRYINVGKIKKGKLFQAKALKIYPDLKKGFDIKLAVKELDARIKDDNPKVVMLEDIKLEEIPGIVHEKIEINDFTNAPKIEYIAQRERSKNQDKIIKFQFGKFARALISRNFDLFDSVIADKVNVMGQFESKNDFISTLSSASSKADADELEYLSVDDYYDLKSLKISKSNDTSFAVNVNAKKNDVTKNFPFWKERQTLIFTTEDDNNWFLSSIN
Protein: DNA topoisomerase 2, mitochondrial (DNA topoisomerase II) (EC 5.6.2.2) (P90520)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Control of topological states of DNA by transient breakage and subsequent rejoining of DNA strands. Topoisomerase II makes double-strand breaks (By similarity).
Subcellular location: Mitochondrion {ECO:0000269|PubMed:9177484}.
Interaction partners:
- DNA topoisomerase 1
- Structural maintenance of chromosomes protein 2
- ATPase subunit 8
- ATPase subunit 4
- Probable tRNA
- Proliferating cell nuclear antigen
- Bifunctional protein argC
- Cytochrome b5 reductase
- Cytochrome b5 heme-binding domain-containing protein
- DNA helicase
Sequence:
MSKLLNNNNHKNLTNYLKFGKGIINNLNNKSKQVGIISFISQSSIQSQSSIQSQSFLSINNNSNNKYFSTKLNKNEKISEKTTTRKIEDIYQKKTPTEHVLLRPDSYIGTIEKIEDDMWVLSNSMFNKEKKTIELNNDNNEKNVESTTTTTTKTNKKPLTYIHPIKATYIPGLLKIYDEILVNAADNKKRDSKMSFIKVEINPNENSISIMNDGKGIPVVMHQTENCYVVEMVMGNLMSGSNFNDSELKVVGGRNGFGAKLTNIFSKEFTVETVDKSSGKKYFQRWSNNMGDRSEPIITPIGEGESDYTKITFKPDLEKFKIKSLWDDNILQLMERRLYDIAGCNTELMVTLNGKRLNYNFQSYVKLYEHHLNNSTKREDNEEQYREESFEFGEISPRWKIGIGLSETGQFTQVSFVNSINTVKGGTHVNFLADQIVRYVGEKLKKKHSDLEIRPMNIKHHLALFVNCLVDNPSFDSQSKETLTTKPMLFGSTPEIPESLLAQFVKNSKIIERVAGWALMKQKADLIHSTSGRQSKTTLIKSISKLDDANWAGGLKSKECTLIITEGDSAKSLALAGLSVVGRNSYGVFPLRGKLLNVRDVASKQLLSNEEINNLTTILGLSHKNSYDTDESMEDLRYGRVMIMADQDHDGSHIKGLVMNFIHYFWPNLLKRGFLVEFVTPIIKATKSSTQKKSFFTIKDYEKWRETISSDQLKQYTIKYYKGLGTSTSAEAKEYFSNLDKHVIKFIWGDEADDLIKMAFAKDLSSLRQRWIKETDMSQGIDHSIKEITYPDFINKELIHYSWAANLRSIPSLIDGLKPGQRKILFASFKRRLTNEIKVSQLSGYVAEQTSYHHGEQSLNSTIVKMAHNFVGSNNLPLLTPSGQFGTRLQGGSDSASARYIFTKLEPVARYLFNELDDPLLNYLEEEGESIQPDYYIPIIPMLLVNGSEGIGVGMSTSIPLFSPIDIIDQLMLRLNNQVALKKLIPWYRGFKGTISPDRHTYRTNGVIKLVGRNLEITELPIGRWTSDYKEVLNDLIDKDVIKSFQESNTENSVHFTILLNNNQLEQMEDLTENELIKLFKLSASLNFHLTCFDENSKIQKLESVEEIIDQFYKVRLQFYGKRREYLLKSLDNQIKRLTTTIQFLEVIASGKLKIQGRSKQDLIKELESGEIVGFENFGTHPPEVYQHLFSLSILDITKERIDNLTNQLTKRKSEHQSISSSDPKSLWTADLQQLKEYLEKSDKEFQKKPLKTSSSSSFDVSSSSESAKLSSTRKSKTDKIKSK
Protein: FI18374p1 (Spinophilin, isoform D) (H5V864)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}. Synapse {ECO:0000256|ARBA:ARBA00034103}.
Interaction partners:
Sequence:
MEKPMHHAPAPVGKVSQIANIFQRKPIEIQPVEQLSAVAAAHAAAAAAAAAAHHAHVQGAPAVRTESHSARFNNARALFEKLGVESNSNVSSRLLRSGSREDNLCDGSDRSSSRSSDRSQSPPKRRTPFPSGVSLVHNNNNAAIVAQNGVPPEQRLSNSKFIVEPAAQVVPTSVVKYPQHNISRLKSEEPSPVPPPASGSVSALFASSGGDKPEKPERKFNSRELIEKQKKWTSHFTKTKTTRTHSDLNRCDIIRTVPGTGLIMDSEKVAKPAMEPPQPPPNASPNPPMRAQAPPEIKPRSGKIGSPVKSPPLPPIPAVKPKNVSPVKFNPDRLRQSPTKTADNSPPPPPAKSAAVLQRSLMQEQQELLRNSCDQGVAPIPPEKPRKKSVDLIEDTLPLTNCSTPSSCASPTSSYLMQPAKRGSLDGGSGNGQYPGNGLSGSTNSATSGSPVASASSGPSSPVHTEDEKQENESTEKSEMEYYHGGNYNSVPRRRRSENEGRKSVDESSPSANNSQQQQQHSIPGSAAGSPQRVANKRSSITVNMPAAGLGQRPPSIISTTSQDEGGFNESAPELKAKLQPAYDQTEEQPHSLNYVDVGYRLNPDGSESREVYGSEAELYDTAKVTDMQRKFHGANGFGQESSTVYAIIKPDVQESQPVAPSRSVLIQSPNSSSVEGSPLHRGSYSSPPVGVVSPIRRRNSSNQDQSVGGGGSAKTTPQCSPARSALVKGIAPIASIDAHEEEELDLVEEDEHLAVEYVEVLELQQDEEEEEAPVLPERRAPAQGSLELQDLEYADTSAGEDEEDIINHLKDGDVLDVELIDDVVDEVIKVHVNHSVATAPSIQAATPAAAIPREDSLPDDMTAAEAERLLSSSILENKIRQQSLLSDEQAKEVEQILNAAPSVGVAVATVVATATSPTSIKNLIEDLPGQSAVAASAANGEQDIQIAAVPAIVEEDEDEEEDFPEDDEEDHARADFDANGGDADGDSDDVEAVDIVGYGHASTALNATFVKADSTETETTTTTPSTATTATTRHDDDEPEWLRDVLEAPKRSLENLLITSATSSRAPGQREELENGYDLHEKHSDLNQTYITGGESLHESIVSVESTQSDATLNQTTTIDDSIISSKHNSTYSLADAEQATSSTVLSTGVTELDDSQYYIPEYPPVRSKEVLVEAGVHYFEDGNFWMEVPGLLDFDDDDCSYPPITVRKNPKVRFSSGPIHVYSTFSVNDYDRRNEDVDPVAASAEYELEKRVEKMHVFPVELMKGPEGLGLSIIGMGVGADAGLEKLGIFVKTITDNGAAARDGRIQVNDQIIEVDGKSLVGVTQAYAASVLRNTSGLVKFQIGRERDPENSEVAQLIRLSLQADREKEERLKRYFSQQEEYLRRTLDYSEDSTQPVSANSSVCEGPSSPVQVEHPMEVEATHSQEVESLKRLLQESEMGCLVKEEIIQNLKRKLVKLETTGNENELLSERLRQSERELGNIRKEAANLQNMLQQSQGQYMALDKKYNKAKRLVREYQQRELDMCHREEFYQQLLQEKDTEYNALVKKLKDRVINLEHELQETQRKAGFPVGLPYDSATLKLTPQMMRKTPPKPLFHKLETELSDTEISDLSPDGDGVKTATVERKVPVKDELDAAVPQHELLDNSINKTKIDLASRGGLANRQLPSANGNSSTSNGAAVDLGQLSNGNLLKRSRSNSRSSDCTLDDTDEEEEREGSALNLAGAPVAHETISLSNGNSHLLANVNNLLQHHPPAMATVIATPSNGHLGTTTPILLNSTSSASSSSSNQSTAREAQINQLYAQVHKDPSKQQHQQQQQQQQQAQAVTTSIPSIFKNALGSPADNGLNDFHRGSMTTFGTGPATSSNRDLNSSYDSILGSNDKLAENDPAESWMYPSRRRVAPNGSKVPLPGSSFTDQLNQALSDRERRLGDGSSRHSSDDYTEINKSQSAAAINCKTLINEIRQAVNEAQPKVPWQQQHHQQIQQQPSAHTTGPPSPTSMSSGCSSPGYSPSRTLDLSGSSSSFSDRKAMAAGYTYKGGPVHEWTKDQVGHWLMGIELERYIPVFKENNVEGGALLTLDSKDFKTLGICGDDKHRLKKRLKDLKANIEKERKDMERERREREKAIRKAEKKAAKKK
Protein: Terpineol synthase, chloroplastic (EC 4.2.3.111) (1,8-cineol synthase, chloroplastic) (EC 4.2.3.108) (Beta-myrcene synthase) (EC 4.2.3.15) (Limonene synthase) (EC 4.2.3.-) (Sabinene synthase) (EC 4.2.3.-) (H6WZF2)
Organism: Nicotiana alata (Winged tobacco) (Persian tobacco)
Function: Monoterpene synthase (TPS) involved in the biosynthesis of monoterpene natural products of the 'cineole cassette', volatile compounds present in floral scent. Catalyzes the conversion of (2E)-geranyl diphosphate (GPP) into alpha-terpineol and, as minor products, sabinene, beta-myrcene, limonene and 1,8-cineole.
Subcellular location: Plastid, chloroplast {ECO:0000255}.
Interaction partners:
Sequence:
MNTEPSPNHYSAISSSDQNLTRRSGNYQPTMWDFEYIQSIHNDYAGDKYMKRFNELKEEMKKMIMAEGSQELEKLELIDNLQRLGVSYHFKHEIMQILSSIKQHSTPADSLYATALKFRLLREHGFHISQEIFDGLSETHTKDTKGMLYLYEASFLATEGESELEQAWTEKHLREYLKNKNIDQNVAKLVHRALELPLHWRMLRLEARWFISFYKKRQDMIPLLLELAILDFNIVQAAHIQDLKYVARWWKETGLAENLPFARDRLVENFFWTIGVNFLPQYGYFRRIETKVNALVTTIDDVYDVFGTLDELQCFTDAIQRWNTDELDNLPDNMKMCYFALDDFINEVACDALIVPYLRNAWTDLCKSYLIEAKWYFSKYIPTMEEYMDNAWISISAPVILVHAYFLIANPVNKEALHYLRNYHDIIRWSALILRLANDLGTSSDELKRGDVPKSIQCYMNEKKVSEEEARQHIRLLISETWKKLNEAHNVAAHPFPKMFVKSAMNLARMAQCMYQHGDGHGGQNSETQNRIMALLFESIPPA
Protein: IP20259p (A1ZAZ6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Uncharacterized protein
- GEO12017p1
- AT24116p
- GEO12122p1
- AT14585p
- Testis-enriched HMG-box-containing protein 2, isoform B
Sequence:
MVDRGNNLVLPVGPCSTELTESQASFAPPKIKKVLPTRANRMEQFLWQELFAEYNRQASAQVDLGEDRTEYYDQFCKDVPPKNEETEEVLVNKYPLYCTTAVTVWNHEGDFTKTFKRKYSITRPIDLCPDKFAL
Protein: Activating signal cointegrator 1 (Thyroid hormone receptor interactor 4) (A0A0R4IR18)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Activating signal cointegrator 1 complex subunit 2
- Activating signal cointegrator 1 complex subunit 3
- Activating signal cointegrator 1 complex subunit 1.
- Mediator of RNA polymerase II transcription subunit 24
- Mediator of RNA polymerase II transcription subunit 27
- Mediator of RNA polymerase II transcription subunit 23
- Mediator of RNA polymerase II transcription subunit 17
- Mediator of RNA polymerase II transcription subunit 10
- Mediator of RNA polymerase II transcription subunit 25
- Mediator of RNA polymerase II transcription subunit 4
Sequence:
MSDSLLRWTVDKLKHGFGLDASDDIVQYILSIDNADEIVEYVGDLLQGTEGNKQEFVDELVQRWQRCQTQTSDGLGGVLRKEVVMEELDTAPKDTQKKSKRKGRNKQEIVTVSQAEPEPVRTPIDLMKAQESSNSSSVKKKSKFVNLYAKEGKDKLAVLLPGRQACECLAQKHRLINNCLSCGRIVCEQEGSGPCLFCGSLVCTNEEQEILQRDSNKSQKLRKKLMGEGTEREYLPHQESKMKAGLEKAVKHKDKLLEFDKNSVKRTQVLDDESDYFATDSNQWLSPGEREALRKREEELRELRHASRKDRKITLDFAGRRVLDEGENLSPYYQKFDETVKAINTGSFGQKAKHSAPADRQHFRELVNPNILQSAPEWVDVASSNPSRKSSSKAASGKETSERSRLRLQDKELQEIADGGWCLSMHQPWASLLVKGIKRVEGRTWYTSHRGRLWIAAAANRPTPQEIAEVEAMYRHLYKHEPQFPAEYPTGCLLGCVNVSDCLSQEQFREQYPQISEESTSPFVFICSNPQELVVKFPMKGKHKIWKLESQSHQSAKKCLMQPA
Protein: Transcription factor bHLH109 (Basic helix-loop-helix protein 109) (AtbHLH109) (bHLH 109) (bHLH transcription factor bHLH109) (Q5XVH0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription factor involved in somatic embryogenesis. Acts as positive regulator of somatic embryo formation. Acts as positive regulator of ECP63 by targeting its promoter and inducing its expression.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}.
Interaction partners:
- Late embryogenesis abundant
- Late embryogenesis abundant protein ECP63
- Basic leucine zipper 43
- Probable transcription factor At5g61620
- TRF-like 10
- Basic leucine zipper 4
- Late embryogenesis abundant
Sequence:
MERNNRNEGTHEEEQCSLSDIIYSFCSENHSELNPLQEIFGVTKNNDHEKHDEEPDEESYRMAKRQRSMEYRMMMEKKRRKEIKDKVDILQGLMPNHCTKPDLASKLENIIEYIKSLKYQVDVMSMAYTTTPVYTPPFYAAAQAPCMSPWGYYTPGVPMMPQQNMTYIPQYPQVYGTVPPNQTQP
Protein: Kinesin like protein at 38B (Q7KQ58)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSNKSTPVRQRIQQFQTRGVHKSTPASEMRKKVLMTRAEDREHRDRPEQLLNTAFSGSTPQPKPKPTALNACYTPSSLYRNSNSTPGRAKTPGTGKSSCSRTKKRDSLMESCLSVSEESNMIVAVRVRPLNALECTRGQVTNVVQVHGNSNELTVQAGSSADASAGVTHFFSYDQVYYSCDPERKNFACQAKVFEGTARPLIDTAFEGYNACLFAYGQTGSGKSYSMMGIEALDDAALDGGPPHDEAGIIPRFCHELFRRIEAVKSQQQLQVEVEVSYFEIYNEKIHDLLSVQHAAAATGESTPIQQQQQQQRPALKVREHPIFGPYVVDLSAHSVDSYSALRNWLAVGNSQRATASTAMNDKSSRSHSIFNIVLNLTDLSSDDGLSSDTDSSTASSLRQTRRSKISLVDLAGSERISVSGSNGERIREGVSINKSLLTLGKVIAALADSRKAIANGPLGSGTPSTFVPYRESVLTWLLRENLGGNSKTVMLATISPASIHADETLATLRYACKARSIVNRVKVNESPHDKIIRDLRAEVDRLKSLRNEYERQRRLSGNSNNPVPRKIIIETSVDETEVEALRQQLAERERELSRAQKSWMEKLKEAEDQRKSELRVLKRRGLALELTAEQKQACLVNLTADPILSGTLFYLLPQGLVRIGRGRLPGGSSSSQPDIVLDGPLVALQHCSIEHERGGKLYVIPGSEDFETYVNGELLKDRRQLFHGDRLVIGGSHYFRISNPFCSQRGKADHPVDFQLAHQEILQKQEQQLRSELEAEKRAALTKIEQERAQHARDFEERLQCLELEQFKYKCNSEMLETERQALALAQQQEHTPLRHEDGVSTPAQKSTILEDIQRIMLNPSEESLHKTQLMVKEATQRCRQLDLPLEFRQTQTPDEFGLLRTVILILDKQRGLKAEWPTARLGVWLDLVRDNAEQQEKLNATTIFQSVEVNWEPLDADLNETLSDTHNSSRIALNLSAMKDVLLNKPLKRLLNASSSKSNTPRQTSTPSPGSQLVHFTKRLLTYDPEEIPESQSSYTTLVQQELQIMQRSAQRLRRHCEAALLERENHQDNGVLAVSLQEALARMDTVLNGMHTSLARAEATACVTSPTKTQKAVRFLID
Protein: Glycolipid 2-alpha-mannosyltransferase (EC 2.4.1.-) (Alpha-1,2-mannosyltransferase) (P27809)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Mannosyltransferase that transfers an alpha-D-mannosyl residue from GDP-mannose into lipid-linked oligosaccharide, forming an alpha-(1->2)-D-mannosyl-D-mannose linkage. Required for the attachment of the third mannose residue of O-linked saccharides.
Subcellular location: Golgi apparatus membrane; Single-pass type II membrane protein.
Interaction partners:
- Vacuolar protein sorting-associated protein 74
- Probable mannosyltransferase KTR3
- Alpha-1,2 mannosyltransferase KTR1
- Mannan polymerase complexes subunit MNN9
- Alpha-1,2-mannosyltransferase MNN2
- Initiation-specific alpha-1,6-mannosyltransferase
- Alpha-1,3-mannosyltransferase MNN1
- Alpha-1,2-mannosyltransferase MNN5
- Mannan polymerase I complex VAN1 subunit
- Mannosyltransferase KTR6
Sequence:
MALFLSKRLLRFTVIAGAVIVLLLTLNSNSRTQQYIPSSISAAFDFTSGSISPEQQVISEENDAKKLEQSALNSEASEDSEAMDEESKALKAAAEKADAPIDTKTTMDYITPSFANKAGKPKACYVTLVRNKELKGLLSSIKYVENKINKKFPYPWVFLNDEPFTEEFKEAVTKAVSSEVKFGILPKEHWSYPEWINQTKAAEIRADAATKYIYGGSESYRHMCRYQSGFFWRHELLEEYDWYWRVEPDIKLYCDINYDVFKWMQENEKVYGFTVSIHEYEVTIPTLWQTSMDFIKKNPEYLDENNLMSFLSNDNGKTYNLCHFWSNFEIANLNLWRSPAYREYFDTLDHQGGFFYERWGDAPVHSIAAALFLPKDKIHYFSDIGYHHPPYDNCPLDKEVYNSNNCECDQGNDFTFQGYSCGKEYYDAQGLVKPKNWKKFRE
Protein: Ensconsin, isoform C (Q8IRC1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MASLGGQHGNISTNPEASKDREEKLKYARDRQNEERHRKIEELRAQAEAAQRYREQKEEERRRRIEEIRTRDTEKRHQVEERKKAIFEAEKERREYILKKNQERESRIEVKKRDRNSIGFAFGSSTPRLLDVPADYGLVSPSAFWGQRRSTSISNVAGASLTRRSSERELADSGAKKRASSSTDRQDGSRSGNATPGGHFNNSRPGSAMSTSTNMSTSGLVPRRPATAPRKPRPASIAGTGMSLEEINKLKRDQKPPVKTTAASPSAQTTPKRTANLMSTSLIVTSSSSRLSSAEKKTPSKREPPVPKAASASKALPSRTASSERISRLTKEPKTKDTSAMTRSMIVTSSSTSTITKPAPAPVAPTSAPVPEQNGVAKEVEKTTADEPVPEAEVPTEAPVVVPSVSKAEKEALNTEKTEEGARQEEEQILAVESVPEALVTSINVEEKSDEGNEKEVPKPQEQAAPKKPSRSKENSEVRELTPPEGADLMTASMMAKKITTEEEAKAALAERRRLAREEAERQAELERQRLEAERLAEIKAQEEEAERQRLFEEESTRLAEEQRRGEEERLRKAIEEAQQREEEEKRRREEEEKQRVEREEAEKKAKEEAEKQRVEVAERLKREEKEREERRKRVEAIMLRTRKGGAATTPSKDANDKAAPAATAPENNSSSNSSVTGSSNNSAEGSPSAADSTPAPTATETVQEAPNSQAMYEQSVLDKENSLINSFSTMIIDENAKNLQQVSNGKLLVDFESTNTVPAVANGNGHIENVNNKNDINLLQDVVAPVATQLIDLSIESQDLHLNNNNSLLTSTAATTTLVTADSHENKDISLL
Protein: CD63 antigen (Granulophysin) (Lysosomal-associated membrane protein 3) (LAMP-3) (Lysosome integral membrane protein 1) (Limp1) (Melanoma-associated antigen ME491) (OMA81H) (Ocular melanoma-associated antigen) (Tetraspanin-30) (Tspan-30) (CD antigen CD63) (P08962)
Organism: Homo sapiens (Human)
Function: Functions as cell surface receptor for TIMP1 and plays a role in the activation of cellular signaling cascades. Plays a role in the activation of ITGB1 and integrin signaling, leading to the activation of AKT, FAK/PTK2 and MAP kinases. Promotes cell survival, reorganization of the actin cytoskeleton, cell adhesion, spreading and migration, via its role in the activation of AKT and FAK/PTK2. Plays a role in VEGFA signaling via its role in regulating the internalization of KDR/VEGFR2. Plays a role in intracellular vesicular transport processes, and is required for normal trafficking of the PMEL luminal domain that is essential for the development and maturation of melanocytes. Plays a role in the adhesion of leukocytes onto endothelial cells via its role in the regulation of SELP trafficking. May play a role in mast cell degranulation in response to Ms4a2/FceRI stimulation, but not in mast cell degranulation in response to other stimuli.
Subcellular location: Cell membrane {ECO:0000269|PubMed:15351990, ECO:0000269|PubMed:19640571, ECO:0000269|PubMed:23632027}; Multi-pass membrane protein {ECO:0000255}. Lysosome membrane {ECO:0000269|PubMed:17897319, ECO:0000269|PubMed:19640571, ECO:0000269|PubMed:1993697, ECO:0000269|PubMed:22431521, ECO:0000269|PubMed:23632027}; Multi-pass membrane protein {ECO:0000255}. Late endosome membrane {ECO:0000269|PubMed:10793155, ECO:0000269|PubMed:23632027}; Multi-pass membrane protein {ECO:0000255}. Endosome, multivesicular body {ECO:0000269|PubMed:21962903, ECO:0000269|PubMed:38682696}. Melanosome {ECO:0000269|PubMed:21962903}. Secreted, extracellular exosome {ECO:0000269|PubMed:22660413}. Cell surface {ECO:0000269|PubMed:16917503, ECO:0000269|PubMed:23632027, ECO:0000269|PubMed:24635319}. Note=Also found in Weibel-Palade bodies of endothelial cells (PubMed:10793155). Located in platelet dense granules (PubMed:7682577). Detected in a subset of pre-melanosomes. Detected on intralumenal vesicles (ILVs) within multivesicular bodies (PubMed:21962903). {ECO:0000269|PubMed:10793155, ECO:0000269|PubMed:21962903, ECO:0000269|PubMed:7682577}.
Interaction partners:
- Tumor susceptibility gene 101 protein
- Metalloproteinase inhibitor 1
- Integrin beta-1
- Syntenin-1
- CD9 antigen
- CD81 antigen
- Lysosome-associated membrane glycoprotein 2
- Syntenin-2
- CD82 antigen
- Lysosome-associated membrane glycoprotein 1
Sequence:
MAVEGGMKCVKFLLYVLLLAFCACAVGLIAVGVGAQLVLSQTIIQGATPGSLLPVVIIAVGVFLFLVAFVGCCGACKENYCLMITFAIFLSLIMLVEVAAAIAGYVFRDKVMSEFNNNFRQQMENYPKNNHTASILDRMQADFKCCGAANYTDWEKIPSMSKNRVPDSCCINVTVGCGINFNEKAIHKEGCVEKIGGWLRKNVLVVAAAALGIAFVEVLGIVFACCLVKSIRSGYEVM
Protein: ADP-ribosylation factor 6 (Q6P2U5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell projection, filopodium membrane {ECO:0000256|ARBA:ARBA00004527}; Lipid-anchor {ECO:0000256|ARBA:ARBA00004527}. Cell projection, ruffle {ECO:0000256|ARBA:ARBA00004466}. Cleavage furrow {ECO:0000256|ARBA:ARBA00004626}. Midbody, Midbody ring {ECO:0000256|ARBA:ARBA00004476}. Recycling endosome membrane {ECO:0000256|ARBA:ARBA00004139}; Lipid-anchor {ECO:0000256|ARBA:ARBA00004139}.
Interaction partners:
- Cytohesin 4b
- Cytohesin 1a
- Cytohesin 3a
- Si:dkey-283b15.4.
- Cytohesin 1-like protein
- Cytohesin 1b.
- Cytohesin 4a
- ADP-ribosylation factor
- Golgi-associated, gamma adaptin ear-containing, ARF-binding protein 3a.
- ADP-ribosylation factor 2a
Sequence:
MGKMLSKIFGNKEMRILMLGLDAAGKTTILYKLKLGQSVTTIPTVGFNVETVTYKNVKFNVWDVGGQDKIRPLWRHYYTGTQGLIFVVDCADRDRIDEARQELHRIINDREMRDAIILIFANKQDLPDAMKPHEIQEKLGLTRIRDRNWYVQPSCATTGDGLYEGLTWLTSNYKS
Protein: Nucleotide sugar transporter (UDP-galactose/UDP-N-acetylglucosamine transporter srf-3) (G5EFD3)
Organism: Caenorhabditis elegans
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MKTAILIWLTLQNSIHTLLIRYSRAREVDAMFVSTVAVWLTEVIKCFICLFLVAQEETPRRFIHALRTQILEQPYDTLKVCIPAMIYIVQNNLFYVAASHLDAATFMITSQLKIFTAAIFTVIILRRSLNRTQWFALAVLFVGVSLVQLQGTKAKESSGESPFVGFVAVVVACCLSGFAGIYFEKILKGSAPVSLWMRNVQMAVFSIPASFSAIYMQDSKTVNEYGLLYGFDSIVWLTVLWYGVGGLSVAVCIKYADNIAKNFATSVAIILSTIGSIFLFDFIPSFTFLLGASLVIFSIFLYSSHQSMVAALGRLRGEIPSTKEAFCL
Protein: Cadherin-18 (Cadherin-14) (Q13634)
Organism: Homo sapiens (Human)
Function: Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types.
Subcellular location: Cell membrane; Single-pass type I membrane protein.
Interaction partners:
- Catenin beta-1
- Cadherin-6
- Cadherin-10
- Cadherin-12
- Cadherin-2
- Cadherin-9
- Cadherin-7
- Cadherin-15
- Cadherin-19
- Catenin alpha-2
Sequence:
MKITSTSCICPVLVCLCFVQRCYGTAHHSSIKVMRNQTKHIEGETEVHHRPKRGWVWNQFFVLEEHMGPDPQYVGKLHSNSDKGDGSVKYILTGEGAGTIFIIDDTTGDIHSTKSLDREQKTHYVLHAQAIDRRTNKPLEPESEFIIKVQDINDNAPKFTDGPYIVTVPEMSDMGTSVLQVTATDADDPTYGNSARVVYSILQGQPYFSVDPKTGVIRTALHNMDREAREHYSVVIQAKDMAGQVGGLSGSTTVNITLTDVNDNPPRFPQKHYQLYVPESAQVGSAVGKIKANDADTGSNADMTYSIINGDGMGIFSISTDKETREGILSLKKPLNYEKKKSYTLNIEGANTHLDFRFSHLGPFKDATMLKIIVGDVDEPPLFSMPSYLMEVYENAKIGTVVGTVLAQDPDSTNSLVRYFINYNVEDDRFFNIDANTGTIRTTKVLDREETPWYNITVTASEIDNPDLLSHVTVGIRVLDVNDNPPELAREYDIIVCENSKPGQVIHTISATDKDDFANGPRFNFFLDERLPVNPNFTLKDNEDNTASILTRRRRFSRTVQDVYYLPIMISDGGIPSLSSSSTLTIRVCACERDGRVRTCHAEAFLSSAGLSTGALIAILLCVLILLAIVVLFITLRRSKKEPLIISEEDVRENVVTYDDEGGGEEDTEAFDITALRNPSAAEELKYRRDIRPEVKLTPRHQTSSTLESIDVQEFIKQRLAEADLDPSVPPYDSLQTYAYEGQRSEAGSISSLDSATTQSDQDYHYLGDWGPEFKKLAELYGEIESERTT
Protein: Candida glabrata strain CBS138 chromosome K complete sequence (Q6FMJ4)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
Sequence:
MILHKLLLLLNLDWNPDNTAQDLDFRALPGYFKGYTVQDTPDTKINATIFDFLALDDRFSNWQQMYQAIPNDTETHSYKLVILARHGQGYHNIGYDRYGEKAWYDYWARLDGDQYGNWFDSELTPLGKKQALEAGQTYLTNLTDGLQRLPDKFFVSPLRRCLDTCIREWEPIFAKHKPANSTVHVKVIEYLRETLGIDKSNERVDHSQALAEYQDHKYNTSDVTVHFDYPDDYAEKDQLWQPEHLETYPELDRRIKVGLREVFSSVNATDRVLSLTVHSDVIESILRNIKHPALVGLQTGKVIYTVVETTKKPADDQSILVVS
Protein: Ribosome-binding protein 1 (Q9GRZ9)
Organism: Caenorhabditis elegans
Interaction partners:
- TPR_MLP1_2 domain-containing protein
- PERMeable eggshell
- Probable dynactin subunit 2
Sequence:
MDSSFVDPSTALGILGGVGVFVFAIYYMIFMNRQEDNFDKAYNRDALALLTDNNEKKKQPKNKTKKQQQTGKKAQDAAPAPASAAPAAPNAPTPTAQQQPSPKASAAPIPEKPEIQVQKVESTQASAPIPAPAAPTTQKSSPKERKSVNLKDLDQKKVLNKLSGLPELDEAYIQFLAGAFRDSDAQKNNLSLEVKALNKKMTESAVKIEKLNKEKMAVEQREKHEQAQRQQLLQKVAQNQAHESELARQIQGIEGKLRVKEQELVAAGKAVKNNEEHEKELKLLRSTNSSFSTELKTIRKEHEAQLQKKQEEWKKLHEQLEQEKEKLISEKEHAKQTHLKLAAAVENVEAELEKQGKEWIQLSTHNQTLKQHNLELEAALSVAKARDQDGEAQKWTMEKAQMIENYTRLEALIGELNRDISEFHEYKKQQEVIVNELNHREKAHLDTIEQLREQISIEKSKLAELQVVLDAEKSKIVEIPLNQPLVVEEVIELKKTNANLAAAAPSTSSGASKEDEETEKLKAENAQLHEKNEELRRRNMTILEKTEAEPGLVICERKRVAEEMGKLVKKQFKTFDDQSRYYEWLNESVSGIKKDLDSKASAPAASVVAPTKAQKAPKCTAAAPAASTAAARSTNEGECWKALKAMKDHLELIDQLNDEQERRHQEELDALRAQLA
Protein: HEAT repeat-containing protein 5B (Q9P2D3)
Organism: Homo sapiens (Human)
Function: Component of clathrin-coated vesicles. Component of the aftiphilin/p200/gamma-synergin complex, which plays roles in AP1G1/AP-1-mediated protein trafficking including the trafficking of transferrin from early to recycling endosomes, and the membrane trafficking of furin and the lysosomal enzyme cathepsin D between the trans-Golgi network (TGN) and endosomes.
Subcellular location: Cytoplasm, perinuclear region {ECO:0000269|PubMed:15758025}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000269|PubMed:15758025}. Note=Localization at clathrin-coated vesicles depends on AFTPH/aftiphilin. {ECO:0000269|PubMed:15758025}.
Interaction partners:
- AP-1 complex subunit mu-2
Sequence:
MELAHSLLLNEEALAQITEAKRPVFIFEWLRFLDKVLVAANKTDVKEKQKKLVEQLTGLISSSPGPPTRKLLAKNLAALYSIGDTFTVFQTLDKCNDIIRNKDDTAAYLPTKLAAVACVGAFYEKMGRMLGSAFPETVNNLLKSLKSAESQGRSEILMSLQKVLSGLGGAAASSHRDIYKNARSLLTDRSMAVRCAVAKCLLELQNEAVFMWTAELENIATLCFKALENSNYGVRVAVSKLLGTVMATALMPKQATVMRQNVKRATFDEVLELMATGFLRGGSGFLKSGGEMLKVGGSVNREVRVGVTQAYVVFVTTLGGQWLERSFATFLSHVLDLVSHPRATQTHVEAVYSRRCVSFILRATVGSLLGEKAQIAAAKEICQAIGKQMKAVEAVVNDTSGENKSGAADIAASQHVMVCALQELGSLVQSLNATASPLIQEASIGLLEIVTSVLLHPSMAARLAAAWCLRCVAVALPFQLTPFLDRCAERLNNLKTSPEAVSGYSFAMAALLGGVHQCPLGIPHAKGKMVVSIAEDLLRTAAQNSRLSLQRTQAGWLLLGALMTLGPSVVRYHLPKMLLLWRNVFPRSLKELEAEKARGDSFTWQVTLEGRAGALCAMRSFVAHCPELLTEDVIRKLMTPIECAMTMMSHIPSVMKAHGAHLKASAAMVRLRLYDILALLPPKTYEGSFNALLRELVAEFTLTDNSANTTTSLLRSLCHYDDSVLLGSWLQETDHKSIEDQLQPNSASGSGALEHDPSSIYLRIPAGEAVPGPLPLGVSVIDASVALFGVVFPHVSYKHRLQMLDHFAECVKQAKGVRQQAVQLNIFTAVLSALKGLAENKSTLGPEEVRKSALTLVMGPLDNPNPILRCAAGEALGRMAQVVGEATFIARMAQYSFDKLKSARDVVSRTGHSLALGCLHRYVGGIGSGQHLKTSVSILLALAQDGTSPEVQTWSLHSLALIVDSSGPMYRGYVEPTLSLVLTLLLTVPPSHTEVHQCLGRCLGAIITTVGPELQGNGATTSTIRSSCLVGCAITQDHSDSLVQAAAISCLQQLHMFAPRHVNLSSLVPSLCVHLCSSHLLLRRAAVACLRQLAQREAAEVCEYAMSLAKNTGDKESSSANVSPFAPGVSSRTDIHCRHQGVNITETGLEGLLFGMLDRETDRKLCSDIHDTLGHMLSSLAVEKLSHWLMLCKDVLAASSDMSTATLLSSGKDEEAEKKDEMDDDTMFTTLGEEDKSKPFVAPRWATRVFAADCLCRIINLCENADQAHFDLALARSAKLRNPTNDLLVLHLSDLIRMAFMAATDHSNQLRMAGLQALEDIIKKFASVPEPEFPGHVILEQYQANVGAALRPAFSQDTPSDIIAKACQVCSTWIGSGVVSDLNDLRRVHNLLVSSLDKVQAGKGSSSQLYRESATTMEKLAVLKAWAEVYVVAMNIKKEAESKPKRAIKNTDDDDDDCGTIDELPPDSLITLVQPELPTLSRLWLAALKDYALLTLPAEFSSQLPPDGGAFYTPETIDTARLHYRNSWAPILHAVALWLNSTGFTCSESTEAAAISGLQKRSTSVNLNQASGAVGSAKSLPEINKDRMHLILGVSIQFLCSPRPEEPIEHVTACLQALHTLLDSPYARVHIAEDQLIGVELLSVLHRLLLTWNPSSVQLLVTGVVQQIVRAAQDYLQEKRNTLNEDDMEKEACTVLGEGGDSGGLIPGKSLVFATMELLMFILVRHMPHLSTKVSDSPSHIATKTRLSEESARLVAATVTILSDLPSLCSPAGCMTILPTILFLIARILKDTAIKSADNQVPPPVSAALQGIKSIVTLSMAKTEAGVQKQWTALIRSTLACILEYSQPEDSVPTPDEVSMLTAIALFLWSASNEIIGVQSLQNGCMNRFKNALNSCDPWVQAKCYQLLLSVFQHSNRALSTPYIHSLAPIVVEKLKAVERNRPASNIELLAVQEGIKVLETLVALGEEQNRVQLLALLVPTLISYLLDENSFASASSASKDLHEFALQNLMHIGPLYPHAFKTVMGAAPELKVRLETAVRASQASKAKAAARQPAPAIHSAPTIKLKTSFF