wanglab/gogpt-training-data huggingface dataset:
Protein: ADP-ribosylation factor-like protein 2-binding protein (ARF-like 2-binding protein) (Binder of ARF2 protein 1) (Q32PC9)
Organism: Bos taurus (Bovine)
Function: Together with ARL2, plays a role in the nuclear translocation, retention and transcriptional activity of STAT3. May play a role as an effector of ARL2 (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Mitochondrion intermembrane space {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Nucleus {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250}. Note=Detected in the midbody matrix. Not detected in the Golgi, nucleus and on the mitotic spindle. Centrosome-associated throughout the cell cycle. Not detected to interphase microtubules (By similarity). In retina photoreceptor cells, localized in the distal connecting cilia, basal body, ciliary-associated centriole, and ciliary rootlet. Interaction with ARL2 may be required for cilia basal body localization (By similarity). The complex formed with ARL2BP, ARL2 and SLC25A4 is expressed in mitochondria. {ECO:0000250}.
Interaction partners:
- ADP-ribosylation factor-like protein 2
- Cilia- and flagella-associated protein 20
- Protein FAM76B
- RSPRY1 protein
Sequence:
MDALEEESFALSFSSASDAEFDAVVGYLEDIIMDDEFQLLQRNFMDKYYQEFEDTEENKLTYTPIFNEYISLVEKYIEEQLLERIPGFNMAAFTTTLQHHKDEVAGDIFDMLLTFTDFLAFKEMFLDYRAEKEGRGLDLSSGLVVTSLCKSSSVPASQNNLRP
Protein: Splicing factor Cactin (zCactin) (F1Q8W0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Plays a role in pre-mRNA splicing by facilitating excision of a subset of introns (By similarity). May be involved in the regulation of innate immune response (By similarity). Plays a role during early embryonic development. Involved in the formation of the anteroposterior axis with important roles also in neural development.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q8WUQ7}. Cytoplasm {ECO:0000250|UniProtKB:Q8WUQ7}.
Interaction partners:
- PRKR-interacting protein 1 homolog
- Protein FAM32A-like
- Splicing regulator SDE2
- Pre-mRNA-splicing factor SLU7
- Pre-mRNA-splicing factor CWC22 homolog
- FLJ22626-like
- Crooked neck-like protein 1
- Pre-mRNA-splicing factor syf2
- Cell division cycle 40 homolog
- Cell division cycle 5-like protein
Sequence:
MGSKKHRRSRSRSRSRERARVVRHDRSPGDRHSRNRSPVKSSRRRARSDSGGSRSSGGSAGPSRQRGRESGHSSDSDRQHRNTHGRNRDSSSDDDYHDKKKQALKKKHNDEKDSRSRRRKSRSSSGSSTNSSRERNRSKTSRSRERERRRRQSRSSSRERHRDQRRRRNSPERDRDRRRRSQSRSSSSSSSDSDHGGKSTQGGSSSKEEKKKQRDLMKALETPEEKRARRLAKKEAKERKKREKMGWSEEYMGYTNADNPFGDNNLLGTFIWQKALEKKGIGHLSEKNLKDRNKHIQEENRRELQKVKQLRLEREREKAMREQELEMLQREKEAEHFKTWAEQEDNFHLHQAKLRSKIRIRDGRAKPIDLLAKYISAEDDDLSVEMHEPYTFLNGLTVTDMEDLLEDIKVYMELECGKNVDFWRDMTTITEDEISKLRKLEASGKGPGDRREGINTSVSTDVQSVFKGKTYSQLQALYMNIESKIQAGGSNLDIGYWESLLQQVRVYMARARLRERHQDVLRQKLYKLKQEQGVESEPLFPIIKEEPEKEQPISREAGSGEEEAGSSSQQADREEDEDRRSRRTGGEEAERSGRSSPEEEKKGEEEEGEKDEAPEAVLTEEDLIQQSQAEYDSGRYSPTLLQNSELPLDTHIIAEEEDLQRLLLARRQMQVTGDASESAEDLFVRRAKEGMGGDEAQFSVEMPLTGKMYLWADKYRPRKPRFFNRVHTGFEWNKYNQTHYDFDNPPPKIVQGYKFNIFYPDLIDKRSTPQYFLEPCPDNKDFGILRFHAGPPYEDIAFKIVNREWEYSHRHGFRCQFANGIFQLWFHFKRYRYRR
Protein: D-galactonate dehydratase family member PC1_0802 (EC 4.2.1.-) (D-mannonate dehydratase) (EC 4.2.1.8) (C6D9S0)
Organism: Pectobacterium carotovorum subsp. carotovorum (strain PC1)
Function: Has low D-mannonate dehydratase activity (in vitro), suggesting that this is not a physiological substrate and that it has no significant role in D-mannonate degradation in vivo. Has no detectable activity with a panel of 70 other acid sugars (in vitro).
Interaction partners:
- Mannitol dehydrogenase domain protein
- Mannonate dehydratase
- Mannitol dehydrogenase domain protein
- D-galactonate dehydratase family member PC1_4063
- Altronate dehydratase
- 2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase
- 2-dehydro-3-deoxygluconokinase
- Ribose-5-phosphate isomerase A
- Ribulose-phosphate 3-epimerase
- Sugar-phosphate isomerase, RpiB/LacA/LacB family
Sequence:
MKIVSAEVFVTCPGRNFVTLKITTDSGLTGLGDATLNGRELPVASYLNDHVCPQLIGRDAHQIEDIWQYFYKGAYWRRGPVTMSAISAVDMALWDIKAKAANMPLYQLLGGASRTGVMVYCHTTGHSIDEVLDDYAKHRDQGFKAIRVQCGVPGMETTYGMAKGKGLAYEPATKGSLPEEQLWSTEKYLDFTPKLFEAVRDKFGFNEHLLHDMHHRLTPIEAARFGKSVEDYRLFWMEDPTPAENQACFRLIRQHTVTPIAVGEVFNSIWDCKQLIEEQLIDYIRTTITHAGGITGMRRIADFASLYQVRTGSHGPSDLSPICMAAALHFDLWVPNFGVQEYMGYSEQMLEVFPHSWTFDNGYMHPGEKPGLGIEFDEKLAAKYPYDPAYLPVARLEDGTLWNW
Protein: Tropomyosin alpha-4 chain (Tropomyosin-4) (Q6IRU2)
Organism: Mus musculus (Mouse)
Function: Binds to actin filaments in muscle and non-muscle cells. Plays a central role, in association with the troponin complex, in the calcium dependent regulation of vertebrate striated muscle contraction. Smooth muscle contraction is regulated by interaction with caldesmon. In non-muscle cells is implicated in stabilizing cytoskeleton actin filaments. Binds calcium.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P09495}. Note=Associates with F-actin stress fibers. {ECO:0000250|UniProtKB:P09495}.
Interaction partners:
- Troponin I, cardiac muscle
- Actin, alpha cardiac muscle 1
- Tropomyosin alpha-1 chain
- Myosin-9
- Troponin T, cardiac muscle
- Troponin T, slow skeletal muscle
- Troponin T, fast skeletal muscle
- Tropomyosin beta chain
- Troponin I, slow skeletal muscle
- Myosin light polypeptide 6
Sequence:
MAGLNSLEAVKRKIQALQQQADDAEDRAQGLQRELDGERERREKAEGDAAALNRRIQLLEEELDRAQEQLATALQNLEEAEKAADESERGMKVIENRAMKDEEKMEILEMQLKEAKHITDEADRKYEEVARKLVILEGELKRAEERAEVSELKCGDLEEELKNVTNNLKSLEAASEKYSEKEDKYEEEIKLLSDKLKEAETRAEFAERTVSKLEKTIDDLEEKLAQAKEENVGLHQTLDQTLNELNCI
Protein: Regulatory solute carrier protein family 1 member 1 (Transporter regulator RS1) (hRS1) (Q92681)
Organism: Homo sapiens (Human)
Function: Mediates transcriptional and post-transcriptional regulation of SLC5A1. Inhibits a dynamin and PKC-dependent exocytotic pathway of SLC5A1. Also involved in transcriptional regulation of SLC22A2. Exhibits glucose-dependent, short-term inhibition of SLC5A1 and SLC22A2 by inhibiting the release of vesicles from the trans-Golgi network.
Subcellular location: Cell membrane {ECO:0000269|PubMed:16788147}. Nucleus {ECO:0000269|PubMed:16788147}. Golgi apparatus, trans-Golgi network {ECO:0000269|PubMed:16788147}. Note=Localizes at the inner side of the plasma membrane.
Interaction partners:
- Protein DDI1 homolog 1
- Probable glucose sensor protein SLC5A4
- Protein DDI1 homolog 2
- Threonylcarbamoyl-AMP synthase
- Sodium/glucose cotransporter 1
- Sodium-dependent noradrenaline transporter
- Beta-alanine-activating enzyme
- Solute carrier family 22 member 6
- Serine hydrolase RBBP9
Sequence:
MSSLPTSDGFNHPARSSGQSPDVGNPMSLARSVSASVCPIKPSDSDRIEPKAVKALKASAEFQLNSEKKEHLSLQDLSDHASSADHAPTDQSPAMPMQNSSEEITVAGNLEKSAERSTQGLKFHLHTRQEASLSVTSTRMHEPQMFLGEKDWHPENQNLSQVSDPQQHEEPGNEQYEVAQQKASHDQEYLCNIGDLELPEERQQNQHKIVDLEATMKGNGLPQNVDPPSAKKSIPSSECSGCSNSETFMEIDTAQQSLVTLLNSTGRQNANVKNIGALDLTLDNPLMEVETSKCNPSSEILNDSISTQDLQPPETNVEIPGTNKEYGHYSSPSLCGSCQPSVESAEESCPSITAALKELHELLVVSSKPASENTSEEVICQSETIAEGQTSIKDLSERWTQNEHLTQNEQCPQVSFHQAISVSVETEKLTGTSSDTGREAVENVNFRSLGDGLSTDKEGVPKSRESINKNRSVTVTSAKTSNQLHCTLGVEISPKLLAGEEDALNQTSEQTKSLSSNFILVKDLGQGIQNSVTDRPETRENVCPDASRPLLEYEPPTSHPSSSPAILPPLIFPATDIDRILRAGFTLQEALGALHRVGGNADLALLVLLAKNIVVPT
Protein: serine O-acetyltransferase (EC 2.3.1.30) (Q4Q2Q9)
Organism: Leishmania major
Interaction partners:
- cysteine synthase
- cystathionine beta-synthase
- Putative serine-threonine dehydratase
- Homoserine kinase
- Cysteine desulfhydrase
- Serine hydroxymethyltransferase
- Serine hydroxymethyltransferase
- Homoserine dehydrogenase
Sequence:
MKRLDRIREALEQLNPQRADSTLPTFHPRISLHKLKELVECLFYVFFPECTNPPSEVTPTFAEADSLMEWVIGHIADILVTQIYVAFVLHGDAHAVEDTKPFKPLNTSQRTQLEWNGQRCATLSLLAMESRSTKGGFAVAAAAEQDALKASLEELSCTGNRARLPSTEVSSKSAASKANAMRVTADINSSANQDFLTNCKRRADAIVTKFVVERLAHVHWLLHTDVEAIFKGDVAASSPSEVVLCYPGLRCMVHQRVAHQLHLLGVPQNFTRMLTELAHSETGIDIHPNTAIGHHFFIDHGTGVVIGATAVIGNDVSIYQGVTLGARSFPTDEKTGERIRDLPRHPIIEDGVTLYANAVVLGRVTIGERSTIGGNCWVVRDVPPFSAIVQRSHHVLQPHERMFLEGDGSGI
Protein: Acetyl-CoA--deacetylcephalosporin C acetyltransferase (DAC acetyltransferase) (DAC-AT) (DCPC-ATF) (EC 2.3.1.175) [Cleaved into: Acetyl-CoA--deacetylcephalosporin C O-acetyltransferase chain 1; Acetyl-CoA--deacetylcephalosporin C O-acetyltransferase chain 2] (P39058)
Organism: Hapsidospora chrysogena (Acremonium chrysogenum)
Function: Catalyzes the conversion of deacetylcephalosporin C to cephalosporin C.
Interaction partners:
Sequence:
MLPSAQVARLKPDPFPPSLSPIPHGAVTFAALAPCHNLPIFSSRQMLRDSLTYSHTSPTMSPQIANRFEASLDAQDIARISLFTLESGVILRDVPVAYKSWGRMNVSRDNCVIVCHTLTSSAHVTSWWPTLFGQGRAFDTSRYFIICLNYLGSPFGSAGPCSPDPDAEGQRPYGAKFPRTTIRDDVRIHRQVLDRLGVRQIAAVVGASMGGMHTLEWAFFGPEYVRKIVPIATSCRQSGWCAAWFETQRQCIYDDPKYLDGEYDVDDQPVRGLETARKIANLTYKSKPAMDERFHMAPGVQAGRNISSQDAKKEINGTDSGNSHRAGQPIEAVSSYLRYQAQKFAASFDANCYIAMTLKFDTHDISRGRAGSIPEALAMITQPALIICARSDGLYSFDEHVEMGRSIPNSRLCVVDTNEGHDFFVMEADKVNDAVRGFLDQSLM
Protein: Uridine kinase-like protein 3 [Includes: Uridine kinase (UK) (EC 2.7.1.48); Putative uracil phosphoribosyltransferase (UPRTase) (EC 2.4.2.9) (UMP pyrophosphorylase)] (Q8VYB2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in the pyrimidine salvage pathway. The uracil phosphoribosyltransferase (UPRT) activity, that catalyzes the conversion of uracil and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to UMP and diphosphate, is unsure.
Interaction partners:
- Uridine nucleosidase 1
- Uridine 5'-monophosphate synthase
- UMP kinase
- Uracil phosphoribosyltransferase, chloroplastic
- dCMP deaminase
- Alkaline-phosphatase-like family protein
- Dihydroorotate dehydrogenase
- Aspartate carbamoyltransferase, chloroplastic
- Cytidine deaminase 5
- Cytidine deaminase 6
Sequence:
MASKSDVNIIETSSKVHFSGFHQMDGLASNRPEQMAEEEEHGQPFVIGVAGGAASGKTTVCDMIMQQLHDQRAVVVNQDSFYHNVNEVELVRVHDYNFDHPDAFDTEQLLSSMEKLRKGQAVDIPNYDFKSYKNNVFPPRRVNPSDVIILEGILIFHDPRVRDLMNMKIFVDADADVRLARRIKRDTVEKGRDIATVLDQYSKFVKPAFEDFILPTKKYADIIIPRGGDNHVAIDLIVQHIHTKLGQHDLCKIYPNLYVIQSTFQIRGMHTLIRDSKTTKHDFIFYSDRLIRLVVEHGLGHLPFTEKQVVTPTGSVYSGVDFCKKLCGVSVIRSGESMENALRACCKGIKIGKILIHREGDNGQQLIYEKLPSDISERHVLLLDPILGTGNSAVQAIRLLISKGVPESNIIFLNLISAPEGVNVVCKKFPRIKIVTSEIELGLNDEFRVVPGMGEFGDRYFGTDDE
Protein: Inner membrane protein YqiJ (P76657)
Organism: Escherichia coli (strain K12)
Subcellular location: Cell inner membrane; Multi-pass membrane protein.
Interaction partners:
- Flotillin family inner membrane protein YqiK
- Uncharacterized protein YjbS
- Uncharacterized protein YjfJ
Sequence:
MILFADYNTPYLFAISFVLLIGLLEIFALICGHMLSGALDAHLDHYDSITTGHISQALHYLNIGRLPALVVLCLLAGFFGLIGILLQHACIMVWQSPLSNLFVVPVSLLFTIIAVHYTGKIVAPWIPRDHSSAITEEEYIGSMALITGHQATSGNPCEGKLTDQFGQIHYLLLEPEEGKIFTKGDKVLIICRLSATRYLAENNPWPQIL
Protein: Auxin-responsive protein IAA11 (Indoleacetic acid-induced protein 11) (Q75GK0)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Aux/IAA proteins are short-lived transcriptional factors that function as repressors of early auxin response genes at low auxin concentrations.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Auxin response factor 11
- Transport inhibitor response 1-like protein Os05g0150500
- Auxin response factor 7
- Auxin response factor 9
- Auxin response factor 2
- Auxin response factor 15
- Auxin response factor 3
- Auxin response factor 14
- Auxin response factor 1
- Auxin response factor 16
Sequence:
MAGLGFDETELRLGLPGAGELAARSSGKRGFAETIDLKLKLQPAAPAAVSGEEGAQEDKEDADAAAAAADEKMSMKRSASQSSVVTAEPDPDKPRAPKAQVVGWPPVRSFRKNVLAEKCKAAALVKVSMDGAPYLRKIDVAMYKSYPELSMAFQNMFTSFTIGKCGSHQQLKESNKLRDDLEYVPTYEDKDGDWMLVGDVPWEMFVESCKRLRIMKGSEAIGLAPRAVEKCKS
Protein: Tubulin delta chain (Delta-tubulin) (Q9NI45)
Organism: Trypanosoma brucei
Subcellular location: Cell projection, cilium {ECO:0000256|ARBA:ARBA00004138}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000256|ARBA:ARBA00004114}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MACVHVLVGQCGNQLGAHFLTALTDEARRCSDEDYASQISADHFRPAPTQKGIRRGGVSNGNSGHHDEPPLPRSVMIDMEPKVVESVVTGVNDGGAFQVRAEQCVTRDEGSGNNWAFGYYEQGSRCDEIVESLRRQSEARGAAHSFHIVHSVAGGTGSGVGCLVSDAIRVEFPRALLLHTAVWPFATGEVVTQWYNCVLAMSALRESADAVFVAHNDDFDVSARPLQKAVNGRTSEVSFDTINHEIGRLLLDLHLPKKLYPVPSTAPEKKPHPQSTFPASRTTSSTGAMASLRCGGLTDVVEAVALDPALKFFSGLALPVTPPDNRVVAPEATSWYPLLCEASRRTGELFVPAPSGDNNTSNNLSTAFIEQRPLLWSLRGPAACSEGLAHLREVLSRSTPTHDGRELYVPPSALLLHEERLLGRRAHVSVFGPTHNIGLRLASALERAEDLLRVSAYVHHFSRYGVGEEELRDAVVRMWDTAAAYGAA
Protein: Coagulation factor VIII (Antihemophilic factor) (AHF) (Procoagulant component) [Cleaved into: Factor VIIIa heavy chain, 200 kDa isoform; Factor VIIIa heavy chain, 92 kDa isoform; Factor VIII B chain; Factor VIIIa light chain] (P00451)
Organism: Homo sapiens (Human)
Function: Factor VIII, along with calcium and phospholipid, acts as a cofactor for F9/factor IXa when it converts F10/factor X to the activated form, factor Xa.
Subcellular location: Secreted, extracellular space.
Interaction partners:
- von Willebrand factor
- Coagulation factor X
- Coagulation factor IX
- Prothrombin
- Fibronectin
- Multiple coagulation factor deficiency protein 2
- Coagulation factor VII
- Coagulation factor XI
- Vitamin K-dependent protein C
- A disintegrin and metalloproteinase with thrombospondin motifs 13
Sequence:
MQIELSTCFFLCLLRFCFSATRRYYLGAVELSWDYMQSDLGELPVDARFPPRVPKSFPFNTSVVYKKTLFVEFTDHLFNIAKPRPPWMGLLGPTIQAEVYDTVVITLKNMASHPVSLHAVGVSYWKASEGAEYDDQTSQREKEDDKVFPGGSHTYVWQVLKENGPMASDPLCLTYSYLSHVDLVKDLNSGLIGALLVCREGSLAKEKTQTLHKFILLFAVFDEGKSWHSETKNSLMQDRDAASARAWPKMHTVNGYVNRSLPGLIGCHRKSVYWHVIGMGTTPEVHSIFLEGHTFLVRNHRQASLEISPITFLTAQTLLMDLGQFLLFCHISSHQHDGMEAYVKVDSCPEEPQLRMKNNEEAEDYDDDLTDSEMDVVRFDDDNSPSFIQIRSVAKKHPKTWVHYIAAEEEDWDYAPLVLAPDDRSYKSQYLNNGPQRIGRKYKKVRFMAYTDETFKTREAIQHESGILGPLLYGEVGDTLLIIFKNQASRPYNIYPHGITDVRPLYSRRLPKGVKHLKDFPILPGEIFKYKWTVTVEDGPTKSDPRCLTRYYSSFVNMERDLASGLIGPLLICYKESVDQRGNQIMSDKRNVILFSVFDENRSWYLTENIQRFLPNPAGVQLEDPEFQASNIMHSINGYVFDSLQLSVCLHEVAYWYILSIGAQTDFLSVFFSGYTFKHKMVYEDTLTLFPFSGETVFMSMENPGLWILGCHNSDFRNRGMTALLKVSSCDKNTGDYYEDSYEDISAYLLSKNNAIEPRSFSQNSRHPSTRQKQFNATTIPENDIEKTDPWFAHRTPMPKIQNVSSSDLLMLLRQSPTPHGLSLSDLQEAKYETFSDDPSPGAIDSNNSLSEMTHFRPQLHHSGDMVFTPESGLQLRLNEKLGTTAATELKKLDFKVSSTSNNLISTIPSDNLAAGTDNTSSLGPPSMPVHYDSQLDTTLFGKKSSPLTESGGPLSLSEENNDSKLLESGLMNSQESSWGKNVSSTESGRLFKGKRAHGPALLTKDNALFKVSISLLKTNKTSNNSATNRKTHIDGPSLLIENSPSVWQNILESDTEFKKVTPLIHDRMLMDKNATALRLNHMSNKTTSSKNMEMVQQKKEGPIPPDAQNPDMSFFKMLFLPESARWIQRTHGKNSLNSGQGPSPKQLVSLGPEKSVEGQNFLSEKNKVVVGKGEFTKDVGLKEMVFPSSRNLFLTNLDNLHENNTHNQEKKIQEEIEKKETLIQENVVLPQIHTVTGTKNFMKNLFLLSTRQNVEGSYDGAYAPVLQDFRSLNDSTNRTKKHTAHFSKKGEEENLEGLGNQTKQIVEKYACTTRISPNTSQQNFVTQRSKRALKQFRLPLEETELEKRIIVDDTSTQWSKNMKHLTPSTLTQIDYNEKEKGAITQSPLSDCLTRSHSIPQANRSPLPIAKVSSFPSIRPIYLTRVLFQDNSSHLPAASYRKKDSGVQESSHFLQGAKKNNLSLAILTLEMTGDQREVGSLGTSATNSVTYKKVENTVLPKPDLPKTSGKVELLPKVHIYQKDLFPTETSNGSPGHLDLVEGSLLQGTEGAIKWNEANRPGKVPFLRVATESSAKTPSKLLDPLAWDNHYGTQIPKEEWKSQEKSPEKTAFKKKDTILSLNACESNHAIAAINEGQNKPEIEVTWAKQGRTERLCSQNPPVLKRHQREITRTTLQSDQEEIDYDDTISVEMKKEDFDIYDEDENQSPRSFQKKTRHYFIAAVERLWDYGMSSSPHVLRNRAQSGSVPQFKKVVFQEFTDGSFTQPLYRGELNEHLGLLGPYIRAEVEDNIMVTFRNQASRPYSFYSSLISYEEDQRQGAEPRKNFVKPNETKTYFWKVQHHMAPTKDEFDCKAWAYFSDVDLEKDVHSGLIGPLLVCHTNTLNPAHGRQVTVQEFALFFTIFDETKSWYFTENMERNCRAPCNIQMEDPTFKENYRFHAINGYIMDTLPGLVMAQDQRIRWYLLSMGSNENIHSIHFSGHVFTVRKKEEYKMALYNLYPGVFETVEMLPSKAGIWRVECLIGEHLHAGMSTLFLVYSNKCQTPLGMASGHIRDFQITASGQYGQWAPKLARLHYSGSINAWSTKEPFSWIKVDLLAPMIIHGIKTQGARQKFSSLYISQFIIMYSLDGKKWQTYRGNSTGTLMVFFGNVDSSGIKHNIFNPPIIARYIRLHPTHYSIRSTLRMELMGCDLNSCSMPLGMESKAISDAQITASSYFTNMFATWSPSKARLHLQGRSNAWRPQVNNPKEWLQVDFQKTMKVTGVTTQGVKSLLTSMYVKEFLISSSQDGHQWTLFFQNGKVKVFQGNQDSFTPVVNSLDPPLLTRYLRIHPQSWVHQIALRMEVLGCEAQDLY
Protein: WASH complex subunit 5 (Strumpellin) (WASH complex subunit strumpellin) (Q12768)
Organism: Homo sapiens (Human)
Function: Acts as a component of the WASH core complex that functions as a nucleation-promoting factor (NPF) at the surface of endosomes, where it recruits and activates the Arp2/3 complex to induce actin polymerization, playing a key role in the fission of tubules that serve as transport intermediates during endosome sorting. May be involved in axonal outgrowth. Involved in cellular localization of ADRB2. Involved in cellular trafficking of BLOC-1 complex cargos such as ATP7A and VAMP7.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:20833645}. Endoplasmic reticulum {ECO:0000269|PubMed:20833645}. Early endosome {ECO:0000269|PubMed:23085491, ECO:0000269|PubMed:23676666}. Note=Colocalizes with SYP/synaptophysin in the external molecular layer of the dentate gyrus and in motoneurons of the ventral horn of spinal cord. {ECO:0000269|PubMed:20833645}.
Interaction partners:
- WASH complex subunit 3
- WASH complex subunit 4
- WASH complex subunit 1
- WASH complex subunit 2C
- WASH complex subunit 2A
- F-actin-capping protein subunit alpha-1
- F-actin-capping protein subunit beta
- Receptor expression-enhancing protein 1
- Vacuolar protein sorting-associated protein 35
- Spastin
Sequence:
MLDFLAENNLCGQAILRIVSCGNAIIAELLRLSEFIPAVFRLKDRADQQKYGDIIFDFSYFKGPELWESKLDAKPELQDLDEEFRENNIEIVTRFYLAFQSVHKYIVDLNRYLDDLNEGVYIQQTLETVLLNEDGKQLLCEALYLYGVMLLVIDQKIEGEVRERMLVSYYRYSAARSSADSNMDDICKLLRSTGYSSQPGAKRPSNYPESYFQRVPINESFISMVIGRLRSDDIYNQVSAYPLPEHRSTALANQAAMLYVILYFEPSILHTHQAKMREIVDKYFPDNWVISIYMGITVNLVDAWEPYKAAKTALNNTLDLSNVREQASRYATVSERVHAQVQQFLKEGYLREEMVLDNIPKLLNCLRDCNVAIRWLMLHTADSACDPNNKRLRQIKDQILTDSRYNPRILFQLLLDTAQFEFILKEMFKQMLSEKQTKWEHYKKEGSERMTELADVFSGVKPLTRVEKNENLQAWFREISKQILSLNYDDSTAAGRKTVQLIQALEEVQEFHQLESNLQVCQFLADTRKFLHQMIRTINIKEEVLITMQIVGDLSFAWQLIDSFTSIMQESIRVNPSMVTKLRATFLKLASALDLPLLRINQANSPDLLSVSQYYSGELVSYVRKVLQIIPESMFTSLLKIIKLQTHDIIEVPTRLDKDKLRDYAQLGPRYEVAKLTHAISIFTEGILMMKTTLVGIIKVDPKQLLEDGIRKELVKRVAFALHRGLIFNPRAKPSELMPKLKELGATMDGFHRSFEYIQDYVNIYGLKIWQEEVSRIINYNVEQECNNFLRTKIQDWQSMYQSTHIPIPKFTPVDESVTFIGRLCREILRITDPKMTCHIDQLNTWYDMKTHQEVTSSRLFSEIQTTLGTFGLNGLDRLLCFMIVKELQNFLSMFQKIILRDRTVQDTLKTLMNAVSPLKSIVANSNKIYFSAIAKTQKIWTAYLEAIMKVGQMQILRQQIANELNYSCRFDSKHLAAALENLNKALLADIEAHYQDPSLPYPKEDNTLLYEITAYLEAAGIHNPLNKIYITTKRLPYFPIVNFLFLIAQLPKLQYNKNLGMVCRKPTDPVDWPPLVLGLLTLLKQFHSRYTEQFLALIGQFICSTVEQCTSQKIPEIPADVVGALLFLEDYVRYTKLPRRVAEAHVPNFIFDEFRTVL
Protein: Neuregulin 1 (A0A494C114)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}. Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MSERKEGRGKGKGKKKERGSGKKPESAAGSQSPALPPRLKEMKSQESAAGSKLVLRCETSSEYSSLRFKWFKNGNELNRKNKPQNIKIQKKPGKSELRINKASLADSGEYMCKVISKLGNDSASANITIVESNATSTSTTGTSHLVKCAEKEKTFCVNGGECFMVKDLSNPSRYLCKCPNEFTGDRCQNYVMASFYSTSTPFLSLPE
Protein: Diabetes and obesity regulated, isoform F (A8JNK7)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm, cytosol {ECO:0000256|ARBA:ARBA00004514}. Cytoplasmic vesicle, autophagosome {ECO:0000256|ARBA:ARBA00004419}. Nucleus, nuclear body {ECO:0000256|ARBA:ARBA00034306}.
Interaction partners:
Sequence:
MVTVATGTAFNCRRRQGVNSCSLYSGPRPQQQRNYLQRSRVSRPLSISTLSPPRSVPALGAGDHDTLTQSLYVASPSGSDQGQDHGQGANVLMEESCMSVYHSIRSTQEGTDSFVNLDLGVSTEVPQQREEPEPEAEPQDQRQALQEQQRAPNARFDSHAAVQLKQQTLARQSQKSKNKKEHQQLCRSAIKRANKVRDFQAKANRPRRSEMQHCKLVSGANNNRSKCCY
Protein: Tyrosine aminotransferase (TAT) (EC 2.6.1.5) (L-tyrosine:2-oxoglutarate aminotransferase) (Q93703)
Organism: Caenorhabditis elegans
Function: Transaminase involved in tyrosine breakdown. Converts tyrosine to p-hydroxyphenylpyruvate. Has no transaminase activity towards phenylalanine. Plays protective role against oxidative stress, metabolizing meta-tyrosine and negatively regulating its accumulation. Plays a role in modulating the daf-2/insulin receptor-like transduction pathway through regulating tyrosine levels. Negatively regulates dauer formation. Plays a role in longevity.
Interaction partners:
- 4-hydroxyphenylpyruvate dioxygenase
- Putative protein C31H2.4
- Aspartate aminotransferase
- Aspartate aminotransferase
- Aspartate aminotransferase, cytoplasmic
- Probable S-adenosylmethionine synthase 1
- Phenylalanine-4-hydroxylase
- Probable S-adenosylmethionine synthase 3
- Probable S-adenosylmethionine synthase 4
- Probable S-adenosylmethionine synthase 5
Sequence:
MQTLMSHSRITPLPGAITKEEIKNQLLVHERRFLSKPNRKDQWNVLPQSAHSKNTVNPVRKIADACAVPPHPEKKVIKLHLGDPSVGGKLPPSEIAVQAMHESVSSHMFDGYGPAVGALAAREAIVERYSSADNVFTADDVVLASGCSHALQMAIEAVANAGENILVPHPGFPLYSTLCRPHNIVDKPYKIDMTGEDVRIDLSYMATIIDDNTKAIIVNNPGNPTGGVFTKEHLEEILAFAHQYKLIIIADEIYGDLVYNGATFYPLASLSPKVPIITCDGIAKRWMVPGWRLGWLIIHNHFGVLTDVKNGIVALSQKIVGPCSLVQGALPKILRETPEDYFVYTRNVIETNANIVDSILADVPGMRVVKPKGAMYMMVNISRTAYGSDVSFCQNLIREESVFCLPGQAFSAPGYFRVVLTCGSEDMEEAALRIREFCYRNFNQHSDSEDSSDEGLDLSAMESD
Protein: C-X-C chemokine receptor type 6 (CXC-R6) (CXCR-6) (CDw186) (G-protein coupled receptor STRL33) (G-protein coupled receptor bonzo) (CD antigen CD186) (O00574)
Organism: Homo sapiens (Human)
Function: Receptor for the C-X-C chemokine CXCL16. Used as a coreceptor by SIVs and by strains of HIV-2 and m-tropic HIV-1.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- C-X-C motif chemokine 16
- C-X-C motif chemokine 9
- Stromal cell-derived factor 1
- C-X-C motif chemokine 10
- C-C motif chemokine 20
- C-C motif chemokine 5
- Fractalkine
- C-C motif chemokine 3
- C-C chemokine receptor type 5
- FYVE and coiled-coil domain-containing protein 1
Sequence:
MAEHDYHEDYGFSSFNDSSQEEHQDFLQFSKVFLPCMYLVVFVCGLVGNSLVLVISIFYHKLQSLTDVFLVNLPLADLVFVCTLPFWAYAGIHEWVFGQVMCKSLLGIYTINFYTSMLILTCITVDRFIVVVKATKAYNQQAKRMTWGKVTSLLIWVISLLVSLPQIIYGNVFNLDKLICGYHDEAISTVVLATQMTLGFFLPLLTMIVCYSVIIKTLLHAGGFQKHRSLKIIFLVMAVFLLTQMPFNLMKFIRSTHWEYYAMTSFHYTIMVTEAIAYLRACLNPVLYAFVSLKFRKNFWKLVKDIGCLPYLGVSHQWKSSEDNSKTFSASHNVEATSMFQL
Protein: Probable citrate synthase, mitochondrial (EC 2.3.3.16) (Q10306)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Mitochondrion matrix {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Malate dehydrogenase, mitochondrial
- Aconitate hydratase, mitochondrial
- Probable acetyl-coenzyme A synthetase
- Probable ATP-citrate synthase subunit 1
- Probable ATP-citrate synthase subunit 2
- Acetyl-CoA acetyltransferase
- Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial
- Probable isocitrate dehydrogenase, mitochondrial
- Pyruvate carboxylase
- Succinate--CoA ligase subunit beta, mitochondrial
Sequence:
MMIILNAPRFMTNTRLASTRRLASSLLSQASLRSRQLNPLFTSSYSTRSSSLKDRLAELIPEKQAEIKKFRAEHGQDVIGEVTINQMYGGARGVRSLIWEGSVLDPNEGIRFRGYTIPECQKLLPSSPNGKQPLPESLFWLLVTGEIPTLSQVQALSADWAARSQLPKFVEELIDRCPPTLHPMAQFSLAVTALEHDSAFAKAYERGMNKHDYWKYEYEDCMDLIAKTVPIAGRIYRNLYRDGVVAPIQMDKDHSYNFANVLGFANNEEFVELMRLYLTIHADHEGGNVSAHTGHLVGSALSSPFLSMAASLNGLAGPLHGLANQEVLNFLITMKKEIGDDLSEETIKSYLWKLLNSGRVVPGYGHAVLRKTDPRYTAQREFALEHLPKDPMFQLVSRLYEIVPGVLTEHGKTKNPYPNVDSHSGVLLQYYGLKEQSFYTVLFGVSRTLGVASQLIWDRALGLPIERPKSFSTEALKKMVETK
Protein: O-phosphoseryl-tRNA(Sec) selenium transferase (EC 2.9.1.2) (Selenocysteine synthase) (Sec synthase) (Selenocysteinyl-tRNA(Sec) synthase) (Sep-tRNA:Sec-tRNA synthase) (SepSecS) (UGA suppressor tRNA-associated protein) (Q6P6M7)
Organism: Mus musculus (Mouse)
Function: Converts O-phosphoseryl-tRNA(Sec) to selenocysteinyl-tRNA(Sec) required for selenoprotein biosynthesis.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9HD40}.
Interaction partners:
- L-seryl-tRNA
- Selenide, water dikinase 2
- Selenide, water dikinase 1
- tRNA selenocysteine 1-associated protein 1
- Selenocysteine-specific elongation factor
- Serine--tRNA ligase, cytoplasmic
- Serine--tRNA ligase, mitochondrial
- Selenocysteine insertion sequence-binding protein 2
- Selenocysteine lyase
- tRNA-splicing endonuclease subunit Sen2
Sequence:
MNPESFAAGERRVSPAYVRQGCEARRAHEHLIRLLLEQGKCPEDGWDESTLELFLHELAVMDSNNFLGNCGVGEREGRVASALVARRHYRFIHGIGRSGDISAVQPKAAGSSLLNKITNSLVLNVIKLAGVHSVASCFVVPMATGMSLTLCFLTLRHKRPKAKYIIWPRIDQKSCFKSMVTAGFEPVVIENVLEGDELRTDLKAVEAKIQELGPEHILCLHSTTACFAPRVPDRLEELAVICANYDIPHVVNNAYGLQSSKCMHLIQQGARVGRIDAFVQSLDKNFMVPVGGAIIAGFNEPFIQDISKMYPGRASASPSLDVLITLLSLGCSGYRKLLKERKEMFVYLSTQLKKLAEAHNERLLQTPHNPISLAMTLKTIDGHHDKAVTQLGSMLFTRQVSGARAVPLGNVQTVSGHTFRGFMSHADNYPCAYLNAAAAIGMKMQDVDLFIKRLDKCLNIVRKEQTRASVVSGADRNKAEDADIEEMALKLDDVLGDVGQGPAL