wanglab/gogpt-training-data huggingface dataset:
Protein: Guanine nucleotide exchange factor SopE (Effector protein SopE) (Toxin SopE) (O52623)
Organism: Salmonella typhimurium
Function: Activator for both CDC42 and RAC1 by directly engaging these Rho GTPases and acting as potent guanine nucleotide exchange factor (GEF). This activation results in actin cytoskeleton rearrangements and stimulates membrane ruffling, promoting bacterial entry into non-phagocytic cells. Also activates MAPK8, indicating that it is capable of stimulating signaling pathways that can lead to nuclear responses. Chaperone InvB is required for secretion and translocation of SopE.
Subcellular location: Secreted {ECO:0000269|PubMed:9482928}. Note=Secreted via the type III secretion system 1 (SPI-1 T3SS).
Interaction partners:
Sequence:
MTKITLSPQNFRIQKQETTLLKEKSTEKNSLAKSILAVKNHFIELRSKLSERFISHKNTESSATHFHRGSASEGRAVLTNKVVKDFMLQTLNDIDIRGSASKDPAYASQTREAILSAVYSKNKDQCCNLLISKGINIAPFLQEIGEAAKNAGLPGTTKNDVFTPSGAGANPFITPLISSANSKYPRMFINQHQQASFKIYAEKIIMTEVAPLFNECAMPTPQQFQLILENIANKYIQNTP
Protein: General transcription factor IIH subunit 4 (A0A1U9X7S4)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU364024}.
Interaction partners:
Sequence:
MESTPSRGLNRVHLQCRNLQEFLGGLSPGVLDRLYGHPATCLAVFRELPSLAKNWVMRMLFLEQPLPQAAVALWVKKEFSKAQEESTGLLSGLRIWHTQLLPGGLQGLILNPIFRQNLRIALLGGGKAWSDDTSQLGPDKHARDVPSLDKYAEERWEVVLHFMVGSPSAAVSQDLAQLLSQAGLMKSTEPGEPPCITSAGFQFLLLDTPAQLWYFMLQYLQTAQSRGMDLVEILSFLFQLSFSTLGKDYSVEGMSDSLLNFLQHLREFGLVFQRKRKSRRYYPTRLAINLSSGVSGAGGTVHQPGFIVVETNYRLYAYTESELQIALIALFSEMLYRFPNMVVAQVTRESVQQAIASGITAQQIIHFLRTRAHPVMLKQTPVLPPTITDQIRLWELERDRLRFTEGVLYNQFLSQVDFELLLAHARELGVLVFENSAKRLMVVTPAGHSDVKRFWKRQKHSS
Protein: Sodium/hydrogen exchanger (B6VDZ5)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Subcellular location: Apical cell membrane {ECO:0000256|ARBA:ARBA00004424}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004424}. Early endosome membrane {ECO:0000256|ARBA:ARBA00004520}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004520}. Recycling endosome membrane {ECO:0000256|ARBA:ARBA00004195}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004195}.
Interaction partners:
Sequence:
MPALWRSTFVLVMVLLAISRPSLASEATGNGTEHTITTLPIVIWKWEEIHFPYLVALWVLVSWLCKLVFQLNPCLTRVIPESGLLICIGWVLGGIIYGADKVQTFRLQPFTFFFYLLPQIVLDAGYSMPNKLFFGNLGAILVYAVIGTCWNAATLGLALWGCWLGGAMGNIDTGLLQLLLFGSLIAAVDPVAVIAVFEEVHVNEVLYILVFGESLLNDGVTVVLFNVFDAFVSLGGAQIDAVEIIKGIISFFVVAVGGSLVGVVFALLISLLTRCTKNIQIIEPGFIFVLGYLSYLTAEMLSLSAILSCTFCGVCCQKYINANMDERSVSTVRSTMKVFANGSETIIFVFLGISAIDPSIWVWNTAFILLTLLFIFVFRFIGVFLLTWILNQYRLVPLDFIDQLVMGYGGLRGAVAYGLVLLLDENKYKEKKLMISTTLIVVYFTVMLQGITMKPLVTWLKVKRAAVSERTLAEKIQNRTFDHMLVAIEDISGQIGDNYMRDKWNNFEEKWLYWLLMTPIARKSCDPIFNIFHKLNIKDATSYVKEGERRGSLAFVRNENKADVDFNKKFGADFSEMMPYIMTENMGPDHVPVSSILRDSVPSVCLDMHEQDLKMRESEDFDAHHLLQQHLYKGRKQHRHRYSRKQLEVNKDEHEVQEIFQRTMRSRLESFKSAKMGVAPPKKISKHLKKDQPQKMPNGKSTDNSKSHAYGDEDFEFSEGDSASGYEAAGGSFPMRAYRGAGIVNPAFMAEMDTMDPMPPMQQIPSWLAETEVDSSNMVPSQRAQLRLPWTPSNLRRLAPLCLSTHSNDSFLLADSPATQEGISELPPPPPPQDGQGQGTHK
Protein: CHK kinase-like domain-containing protein (Q8IMT4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Uncharacterized protein, isoform A
- LP18071p
Sequence:
MSDNDDIVNPNEHLIIPDWINEKYFESVLAKDEPDHVKVLKFTVVAAIPPGENFTSTMLRVYIKLEMKDGSVKTKTYIFKTMLPEERGGSDINEFGLFPKEAMMYKTYLPAFEALYKDVGWDIQLAPKCLHTEEREGDIHFIFEDLCVKRFKNMDRTKGLDMEHMTKCLQKLAEYHAASAVYEELHGPYPSEFSEGFVKKDVKKFHVDGFQLKEKAYKKAMLSWGLKDADKYIKAFPTVKQYWAQCLSTLELNPDEFHVLNHGDFWSSNLMSSYLPDGTLEKLILIDFQIVMWGSPAMDLLFFLTLSPTNDLRIKEFDHFVRIYWERLVECLKVLKLKKPLPKLRDLQNSMNNKNHSFYAFFSILNHLPIILFPTDKDSNIHNLSANTEEGENYRLRLLSNPAFGNVMKDLYPFLYNRGILNFEDYDV
Protein: Flagellar Member 4 (Q57Y44)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
FHQMTYQQLEEVRKGMRTSLEHPVLSVGPGALMICRDYLSQVVTEKVEAALKNLKNESEGTDALGGETITAARMKALREKTDMDPSSYFHNVLMEAFCRRRKDPGKYDGVPDPWASVSRFIDDQRQDENRVRSELTVLQKRQRLTTRDFTDKAAAVAPLSEPTAGPVAMPHIVNAESEQIVAEAVTSLRDSNSLQCVVRLSIDLEEAKLRNKELPPPHSATVCAHGVKQRQPSDGKRRSICEEGTSSALPQELTERRERITSEQQCDKQVAVAVGVADGTPAAVGSSGGNNTAEGVVDTSIGHRRVPCPTSSIDCTLSSHRSNATARPVSSGETFCSLINKQKIAVSRKSDSNAMSSTLVKPFWNKGHALTDTDVGKQTTRYVGTISNEAGSGVFEELPSAVNEVSICAAQMGRKVPEVGVHISSDATYGELKCEQELHPFNLSAIKTSEDRVQAFKKLMPSLHDMPCEGVFIEDIDVSDPRLETLISRLQAVRENAAVGDRREVAVVEESVSSVVKLLAEELAAMTLGMLSRFPFLESRVCGVLLGNLQVLNVDNEFQWLEALYRSSQRERGFVRSIEQCLRARAEMLAKSSPYVVPVERHKGYMLGLPQKIGCGAPRNELAGDWDQQETSQGSETPSGDRYRRSGTPTPCLDTSKLTERVGMPNLPPPLPPSSLNGKSGETAPPGRFVRNVHVQEHPPTPCTPGICVNRDKASSNTTSIAQGRELLPPWHSTPSPGIPCSSSTQLCTELNKLTEGNASQKHFTCAGETVLLERRALEGKRLICEEVHRSHLHPPSSVKSGTAAPAAVNNKRQPSSAPLPIVRQESLIFSVDSLACEASHDPGELKGGEQLKTAKTAHFDATTGNSMDKSMRLGETTAARRPVANGCDSALSDSKQKTSEFGAPNTLSTSPGAPPTLSTGECRSQSPKISSSVEKTPTPSRRTQESTQLGQPLNHKVLSQVSLAGRFASGVPTTSSCAGLRLNTSATSDTLHNTTRFCGQRGQDTVVTKWGKGSEDRGTCVESAVGVGGAEKREQKQWGESSKVTSGSDKKRSCDLGIIQPSLKKVSGTSGTLCFKDTDVIPKYSRASVSSEEEPEEAKGLLPAVSVAASRGTSIDPIYKPKTPQNKQIPWGNSVDLSGPQSDPAPLNSFSFSCSAGASRGEHNNSFLPRLIPAAKFDSPICRGQEEELDAVEMNLLGLRQQYVAYCRRACVKPNSVLMRYFPDKPGIFVSRVDTSMNYIGPKGILPVVQVLRLNSGLEYLNLSHNNMENNEVVELVQVLLTECGASLGHLDLSNNPISTVGGAALLRLVQMRPHLLTVRVEGTLIPQKMCKSIQQVCEANAVARE
Protein: Zn(2)-C6 fungal-type domain-containing protein (G5EB36)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
Sequence:
MPGILPMKVIKVGNNTQSRIAQACDRCRSKKIRCDGIRPCCTQCANVGFECKTSDKLSRRAFPRGYTESLEERVRTLEAEVRELKSLLDEKDEKIDVLSRIHSFSSPSQQKTPAAVHSPTQPPPAAPTSVPTPSEGAVHVPDPVALSSTEESGVSNTRGFAAVFTNMLADQGRLAPETSTKALSASPTPITPSRLDQPLKTTPRLVSDQLINIFFQEWAPLYPVVHRPTILKAYEQYLSNSEHIQGNKHEMAQLNLIFAVAALGAISRTNQDPTLFEENWSSILESLHADISIPTLQCYVLAQMYCLTKGDYTNVLRYRGVAVGVCHQLKLQKSQKAFSSNALLAETRKKVFWCQYVLDRLCASLTGLPVLLREEHIQTEYPEDIDDENVTETGFLPTLPGESTRISSALALFSASRVLNSTLENIYPSDGAYEIPLSKMRFVTEQLDKWVKSLPAHLHLEFTQDKPSTNVISSRSPLLSVMYYFIRSLIHRPAVCFGDDHVRSPSVLAIADSGKHIIQILQLLDERRLCLSLSINRRELISSAGLGLLWQNVGLKRDSKLVKESQKVLTGVIDQLESESSVAATEFSALAGALVSLDTKRPTTTNPQQMSPPAQKPLKSPRRQLEAWKARLIGSTSPGQSQPKPEPLSRRNTFSGSSPGLAERQLRSPSWASLPPNDFPHHAPMSKNVYNHPMGYEGNPSMSCSVPTDHPAPPSGNLTVSDWEFVVSDMDQGYSNIFTGIYGGKECGEDHGPFASLTAEYMHKQGPGLPPSLTSSDELQGLSPEAWSATSSSDMAQPPELAAQSVYSDGSLGSRDHSLSLPSTMPFPMEDRPGSLLDPLQGVIIPAGDDDIEEFGLVNGWDRRLAV
Protein: Parathyroid hormone-like hormone (Parathyroid hormone-like hormone a isoform X2) (Q5SPK3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
- Parathyroid hormone/parathyroid hormone-related peptide receptor
- Tuberoinfundibular peptide of 39 residues
- Parathyroid hormone 1 receptor b
- Parathyroid hormone 2 receptor
- Parathyroid hormone 1a.
- Indian hedgehog B protein
- Importin subunit beta-1
- Parathyroid hormone
Sequence:
MRMLCCRRVLQQWVFALFLLCSPVPHHGRPVDALSSRMKRSVTHAQLMHDKGRTLQDFKRRMWLQELLHEVHTAEIREAQQPRGGVSISSGAGGGVGTGVSITLPAGVGVSTGAGTAHPKPAGGTKNLPIGFGLEDEEGTNLPQETHKSQNYKDNMMKGIRRKKKSRTGKRREGEKRKRRARSLQEFSSGVHLQPYSC
Protein: Serine/threonine-protein kinase haspin homolog hrk1 (EC 2.7.11.1) (O13924)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Serine/threonine haspin-like protein kinase involved in cell cycle regulation. Acts in chromosomal passenger complex (CPC) targeting to centromeres by phosphorylating histone H3 at 'Thr3' (H3T3ph).
Subcellular location: Cytoplasm. Chromosome.
Interaction partners:
- Serine/threonine-protein kinase srk1
Sequence:
MESRSKVKTYGKNRRYINKDIEIWASLDERPCALKPRNIENFNNQERSDLEHIHSKPKKDSLLSWNILLKKGSYKENELLAKRNQNLVPTVIIPASPRDNASKSVVSKKEVVNLSSSVALSGKPANNSKLDPLHRLLQIVAQEDALPFSQFVKSQTFEIQKIGEASYSEVYQASNADDVPVVWKVIPFGEDGQAQYADVLNEVQISQWIKVDGFANLHQVVVVKGTYPSLLLEEWDRYLMQNGSENDRPDSYSSTQLYCVLCLDHSGTDLEHFELRSWRECWSVFYETLKILSLVETRYEFEHRDLHWGNILIRKADRSEEEVSFLLNEISLDDIESVDFPGSQDKADDFDNILQVTLIDFTLARASYSQGIISYNEFNDPDLFNGVDDYQFDIYRLMSRVTKGRWAQFFPITNVLWLHYLIHQLLHKKNLSSPLTETETLMRSRLKQIFRLIDPVKTMQFQQAEDSIRSKSTVTSATSLLNWVRQKY
Protein: Fat storage-inducing transmembrane protein 1 (Fat-inducing protein 1) (A5D6W6)
Organism: Homo sapiens (Human)
Function: Plays an important role in the formation of lipid droplets (LDs) which are storage organelles at the center of lipid and energy homeostasis (By similarity). Directly binds to diacylglycerol (DAGs) and triacylglycerol (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000255|HAMAP-Rule:MF_03229, ECO:0000269|PubMed:18160536}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03229}.
Interaction partners:
Sequence:
MERGPVVGAGLGAGARIQALLGCLLKVLLWVASALLYFGSEQAARLLGSPCLRRLYHAWLAAVVIFGPLLQFHVNPRTIFASHGNFFNIKFVNSAWGWTCTFLGGFVLLVVFLATRRVAVTARHLSRLVVGAAVWRGAGRAFLLIEDLTGSCFEPLPQGLLLHELPDRRSCLAAGHQWRGYTVSSHTFLLTFCCLLMAEEAAVFAKYLAHGLPAGAPLRLVFLLNVLLLGLWNFLLLCTVIYFHQYTHKVVGAAVGTFAWYLTYGSWYHQPWSPGSPGHGLFPRPHSSRKHN
Protein: Protein-glutamine deamidase Cif (EC 3.5.1.44) (Cycle-inhibiting factor homolog) (CHBP) (Q63KH5)
Organism: Burkholderia pseudomallei (strain K96243)
Function: Protein-glutamine deamidase effector that inhibits the host cell cycle and other key cellular processes such as the actin network and programmed-cell death. Acts by mediating the side chain deamidation of 'Gln-40' of host NEDD8, converting it to glutamate, thereby abolishing the activity of cullin-RING-based E3 ubiquitin-protein ligase complexes (CRL complexes). Inactivation of CRL complexes prevents ubiquitination and subsequent degradation of the cyclin-dependent kinase inhibitors CDKN1A/p21 and CDKN1B/p27, leading to G1 and G2 cell cycle arrests in host cells. Deamidation of 'Gln-40' of host NEDD8 also triggers macrophage-specific programmed cell death. Also able to catalyze deamidation of 'Gln-40' of host ubiquitin in vitro; however, NEDD8 constitutes the preferred substrate in vivo. Also regulates the host NF-kappa-B signaling via activation of MAPK/ERK cascade: activation of host MAPK/ERK cascade is independent of CRL complexes inhibition, suggesting that Cif has other host protein targets than NEDD8.
Subcellular location: Secreted {ECO:0000269|PubMed:19308257, ECO:0000269|PubMed:20688984}. Host nucleus {ECO:0000250|UniProtKB:P0DUW5}. Note=Secreted via the type III secretion system (T3SS). {ECO:0000269|PubMed:19308257, ECO:0000269|PubMed:20688984}.
Interaction partners:
Sequence:
MLEHGVMKIPGINNVGKTGQAGGETERIPSTEPLGSSAATSPAGPLGGLPARSSSISNTNRTGENPMITPIISSNLGLKHRVTLRKATLASLMQSLSGESSNRVMWNDRYDTLLIARDPREIKNAIEKSVTDFGGLENYKELTGGADPFALMTPVCGLSANNIFKLMTEKDVPIDPTSIEYLENTSFAEHVNTLDSHKNYVVIVNDGRLGHKFLIDLPALTQGPRTAYIIQSDLGGGALPAVRVEDWISRRGSDPVSLDELNQLLSKDFSKMPDDVQTRLLASILQIDKDPHKVDIKKLHLDGKLRFASHEYDFRQFQRNAQYVAGLG
Protein: Polyribonucleotide nucleotidyltransferase (EC 2.7.7.8) (Polynucleotide phosphorylase) (PNPase) (Q9RSR1)
Organism: Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / CCUG 27074 / LMG 4051 / NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1)
Function: Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01595}.
Interaction partners:
- RNA helicase
- RNA-binding protein RO60
- Translation initiation factor IF-2
- DNA-directed RNA polymerase subunit beta
- Transcription termination/antitermination protein NusA
- DNA-directed RNA polymerase subunit alpha
- Large ribosomal subunit protein uL3
- Transcription termination factor Rho
- Ribonuclease PH
- Small ribosomal subunit protein uS4
Sequence:
MIGKTFTTMLGGRELSIETGKLAKLVSGSVTVRYGDTLLLVTAQASDTQSKLDFLPLTVEFEERHYAVGKIPGSFQRREGRPGEKAILSARITDRQIRPLFPKGYRHETQVIITVLSADGQNAPDVLGPIGAAAALSISDIPWAGPTACVRVGQIDGQYVVNPTTEQLTRSRMDLVVAGTREAVMMVECGAQTVSEDDLVGAIEFAHAEMQGVIALIEQMRAEVGHEKFNFLAEEGPANDYVPELTEKAKAAGLRDALLTHGKKDRSARLKALRNGLIEGYVPDPTAEGSAELTQALKDAFGKVEKRELRRLILEENLRADGRDSKTVRPIWIEARPLPTAHGSAVFTRGETQVLGVTTLGTERDEILIDDLTAESGDKFLLHYNFPPYSTGEVKRMGGQSRREIGHGNLAKRAIRAVLPSFEEFPYVIRVVGDVLESNGSSSMGTVCAGTLSLMDAGVPLKAPVAGVAMGLVMEGDNYRVLTDILGLEDALGDMDFKVCGTAEGVTALQMDIKVGGITPQIMREALAQAKEGRLHILGKMAEVLAAPRAELSPTAPHILSLKINPELIGKVIGPGGKQVRELEAMGAQVTIEEDGTVRIFSASGESAEAVKARIEAVTKEAKVGEEFEGTVVKIAPFGAFVNLFPGQDGMLHISQLSEQRVENVEDVLTVGDKLKVKIANIDDRGKIDLIRPELEGKVPLREPRAPRGGDRGPRRDSDRGGDRGPRREFSDRGPRPEGARSERPEGQRTERPATAPATQESSQSSDAPAAPVFPRRED
Protein: Tubby-related protein 2 (Cancer/testis antigen 65) (CT65) (Tubby-like protein 2) (O00295)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000250}. Secreted {ECO:0000250}. Note=Does not have a cleavable signal peptide and is secreted by a non-conventional pathway. {ECO:0000250}.
Interaction partners:
- Parafibromin
Sequence:
MSQDNDTLMRDILGHELAAMRLQKLEQQRRLFEKKQRQKRQELLMVQANPDASPWLWRSCLREERLLGDRGLGNPFLRKKVSEAHLPSGIHSALGTVSCGGDGRGERGLPTPRTEAVFRNLGLQSPFLSWLPDNSDAELEEVSVENGSVSPPPFKQSPRIRRKGWQAHQRPGTRAEGESDSQDMGDAHKSPNMGPNPGMDGDCVYENLAFQKEEDLEKKREASESTGTNSSAAHNEELSKALKGEGGTDSDHMRHEASLAIRSPCPGLEEDMEAYVLRPALPGTMMQCYLTRDKHGVDKGLFPLYYLYLETSDSLQRFLLAGRKRRRSKTSNYLISLDPTHLSRDGDNFVGKVRSNVFSTKFTIFDNGVNPDREHLTRNTARIRQELGAVCYEPNVLGYLGPRKMTVILPGTNSQNQRINVQPLNEQESLLSRYQRGDKQGLLLLHNKTPSWDKENGVYTLNFHGRVTRASVKNFQIVDPKHQEHLVLQFGRVGPDTFTMDFCFPFSPLQAFSICLSSFN
Protein: Methionine gamma-lyase (AtMGL) (EC 4.4.1.11) (L-methioninase) (Q9SGU9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the degradation of L-methionine to alpha-ketobutyrate, methanethiol and ammonia. Exhibits a high activity toward L-methionine, L-ethionine, L-homocysteine and seleno-L-methionine, but not L-cysteine. Involved in an alternative cysteine biosynthesis pathway to the reverse trans-sulfuration pathway (methionine->homocysteine->cystathionine->cysteine) in which methanethiol is an intermediate. Mediates also an alternative isoleucine biosynthesis pathway in which 2-ketobutyrate is an intermediate.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:17030798}.
Interaction partners:
- Homocysteine S-methyltransferase 2
- Homocysteine S-methyltransferase 1
- Homocysteine S-methyltransferase 3
- 5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase 1
- 5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase 3, chloroplastic
- 5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase 2
- cysteine synthase
- Bifunctional L-3-cyanoalanine synthase/cysteine synthase D1
- Bifunctional L-3-cyanoalanine synthase/cysteine synthase D2
- Cysteine synthase 1
Sequence:
MAHFLETQEPLVFSGKKRNDRDDEDGDALVAKKSALAVCDADPAAAIANIRHEFGEHGGVNMSIEASATFTVMEPDTMRRMFTGELGPDNDFYVYSRHFNPTVLNLSRQMAALEGTQAAYCTSSGMSAISSVMLQLCSSGGHVVAASTLYGGTHALLSHFLPRTCNITTSFVDITDHGAVANAIVEGRTQVLYFESVANPTLTVADIPELSRMAHEKGVTVVVDNTFAPMVLSPAKLGADVVVHSISKFISGGADIIAGAVCGSENLVKEMMDLRGGSLMLLGPTMNAKVAFELSERIPHLGLRMREHSHRAQVYAERMRDLGMKVIYPGLETHPQHKLFKGMVNRDYGYGGLLSIDMETEEKANKLMAYLQNATQFGFMAVSLGYYETLMSCSGSSTSSELDPSQKEAAGISPGLVRMSVGYVGTLEQKWTQFEKAFLRM
Protein: Protein phosphatase Slingshot homolog 2 (EC 3.1.3.16) (EC 3.1.3.48) (SSH-like protein 2) (SSH-2L) (hSSH-2L) (Q76I76)
Organism: Homo sapiens (Human)
Function: Protein phosphatase which regulates actin filament dynamics. Dephosphorylates and activates the actin binding/depolymerizing factor cofilin, which subsequently binds to actin filaments and stimulates their disassembly. Inhibitory phosphorylation of cofilin is mediated by LIMK1, which may also be dephosphorylated and inactivated by this protein.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q5SW75}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q5SW75}. Cell junction, focal adhesion {ECO:0000250|UniProtKB:Q5SW75}. Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000250|UniProtKB:Q5SW75}. Note=Colocalizes with filamentous actin in the cytoplasm and the cell periphery. {ECO:0000250|UniProtKB:Q5SW75}.
Interaction partners:
- Cofilin-1
- Cofilin-2
- Protein phosphatase 3 catalytic subunit alpha
- Serine/threonine-protein phosphatase 2B catalytic subunit beta isoform
- LIM domain kinase 1
- Serine/threonine-protein phosphatase 2B catalytic subunit gamma isoform
- Protein phosphatase Slingshot homolog 1
- Protein phosphatase Slingshot homolog 3
- Calcineurin subunit B type 1
- Calcineurin subunit B type 2
Sequence:
MALVTVQRSPTPSTTSSPCASEADSGEEECRSQPRSISESFLTVKGAALFLPRGNGSSTPRISHRRNKHAGDLQQHLQAMFILLRPEDNIRLAVRLESTYQNRTRYMVVVSTNGRQDTEESIVLGMDFSSNDSSTCTMGLVLPLWSDTLIHLDGDGGFSVSTDNRVHIFKPVSVQAMWSALQSLHKACEVARAHNYYPGSLFLTWVSYYESHINSDQSSVNEWNAMQDVQSHRPDSPALFTDIPTERERTERLIKTKLREIMMQKDLENITSKEIRTELEMQMVCNLREFKEFIDNEMIVILGQMDSPTQIFEHVFLGSEWNASNLEDLQNRGVRYILNVTREIDNFFPGVFEYHNIRVYDEEATDLLAYWNDTYKFISKAKKHGSKCLVHCKMGVSRSASTVIAYAMKEYGWNLDRAYDYVKERRTVTKPNPSFMRQLEEYQGILLASKQRHNKLWRSHSDSDLSDHHEPICKPGLELNKKDITTSADQIAEVKTMESHPPIPPVFVEHMVPQDANQKGLCTKERMICLEFTSREFHAGQIEDELNLNDINGCSSGCCLNESKFPLDNCHASKALIQPGHVPEMANKFPDLTVEDLETDALKADMNVHLLPMEELTSPLKDPPMSPDPESPSPQPSCQTEISDFSTDRIDFFSALEKFVELSQETRSRSFSHSRMEELGGGRNESCRLSVVEVAPSKVTADDQRSSSLSNTPHASEESSMDEEQSKAISELVSPDIFMQSHSENAISVKEIVTEIESISQGVGQIQLKGDILPNPCHTPKKNSIHELLLERAQTPENKPGHMEQDEDSCTAQPELAKDSGMCNPEGCLTTHSSIADLEEGEPAEGEQELQGSGMHPGAKWYPGSVRRATLEFEERLRQEQEHHGAAPTCTSLSTRKNSKNDSSVADLAPKGKSDEAPPEHSFVLKEPEMSKGKGKYSGSEAGSLSHSEQNATVPAPRVLEFDHLPDPQEGPGSDTGTQQEGVLKDLRTVIPYQESETQAVPLPLPKRVEIIEYTHIVTSPNHTGPGSEIATSEKSGEQGLRKVNMEKSVTVLCTLDENLNRTLDPNQVSLHPQVLPLPHSSSPEHNRPTDHPTSILSSPEDRGSSLSTALETAAPFVSHTTHLLSASLDYLHPQTMVHLEGFTEQSSTTDEPSAEQVSWEESQESPLSSGSEVPYKDSQLSSADLSLISKLGDNTGELQEKMDPLPVACRLPHSSSSENIKSLSHSPGVVKERAKEIESRVVFQAGLTKPSQMRRSASLAKLGYLDLCKDCLPEREPASCESPHLKLLQPFLRTDSGMHAMEDQESLENPGAPHNPEPTKSFVEQLTTTECIVQSKPVERPLVQYAKEFGSSQQYLLPRAGLELTSSEGGLPVLQTQGLQCACPAPGLAVAPRQQHGRTHPLRRLKKANDKKRTTNPFYNTM
Protein: 14 kDa phosphohistidine phosphatase (EC 3.9.1.3) (Phosphohistidine phosphatase 1) (Protein histidine phosphatase) (V9HWC4)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MAVADLALIPDVDIDSDGVFKYVLIRVHSAPRSGAPAAESKEIVRGYKWAEYHADIYDKVSGDMQKQGCDCECLGGGRISHQSQDKKIHVYGYSMAYGPAQHAISTEKIKAKYPDYEVTWANDGY
Protein: CX chemokine ligand 34b, duplicate 11 precursor (Chemokine CXL-C24a) (A9ZPE1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MHLSSVSHQMIISSRLLLLLYAFTSVVFISVSEGWSSTDKNFDNRPGVCFKVLTTKEPKANIKRCYNLPKTNNCLKCVLFVDASNRMKCIDPNASWLAERLYRLKEKGVTCRGEA
Protein: Glutathione S-transferase F13 (AtGSTF13) (EC 2.5.1.18) (GST class-phi member 13) (Q9LZI9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May be involved in the conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles and have a detoxification role against certain herbicides.
Subcellular location: Cytoplasm, cytosol {ECO:0000305}.
Interaction partners:
- Methionine--tRNA ligase, cytoplasmic
- Glutathione S-transferase L2, chloroplastic
- Glutathione S-transferase U15
- Glutathione synthetase, chloroplastic
- Glutathione S-transferase U17
- 1-Cys peroxiredoxin PER1
- Glutathione S-transferase U21
Sequence:
MAMKLYGDEMSACVARVLLCLHEKNTEFELVPVNLFACHHKLPSFLSMNPFGKVPALQDDDLTLFESRAITAYIAEKHRDKGTDLTRHEDPKEAAIVKLWSEVEAHHFNPAISAVIHQLIVVPLQGESPNAAIVEENLENLGKILDVYEERLGKTKYLAGDTYTLADLHHVPYTYYFMKTIHAGLINDRPNVKAWWEDLCSRPAFLKVSPGLTVAPTTN
Protein: Syntaxin-binding protein 3 (Platelet Sec1 protein) (PSP) (Protein unc-18 homolog 3) (Unc18-3) (Protein unc-18 homolog C) (Unc-18C) (O00186)
Organism: Homo sapiens (Human)
Function: Together with STX4 and VAMP2, may play a role in insulin-dependent movement of GLUT4 and in docking/fusion of intracellular GLUT4-containing vesicles with the cell surface in adipocytes.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:10194441}. Cell membrane {ECO:0000269|PubMed:10194441}. Note=In platelets, predominantly cytosolic. Low amounts membrane-associated.
Interaction partners:
- Syntaxin-4
- Vesicle-associated membrane protein 2
- Synaptosomal-associated protein 23
- Vesicle-associated membrane protein 8
- Syntaxin-3
- Syntaxin-2
- Solute carrier family 2, facilitated glucose transporter member 4
- Syntaxin-1A
- Vesicle-associated membrane protein 3
- Syntaxin-1B
Sequence:
MAPPVAERGLKSVVWQKIKATVFDDCKKEGEWKIMLLDEFTTKLLASCCKMTDLLEEGITVVENIYKNREPVRQMKALYFITPTSKSVDCFLHDFASKSENKYKAAYIYFTDFCPDNLFNKIKASCSKSIRRCKEINISFIPHESQVYTLDVPDAFYYCYSPDPGNAKGKDAIMETMADQIVTVCATLDENPGVRYKSKPLDNASKLAQLVEKKLEDYYKIDEKSLIKGKTHSQLLIIDRGFDPVSTVLHELTFQAMAYDLLPIENDTYKYKTDGKEKEAILEEEDDLWVRIRHRHIAVVLEEIPKLMKEISSTKKATEGKTSLSALTQLMKKMPHFRKQITKQVVHLNLAEDCMNKFKLNIEKLCKTEQDLALGTDAEGQKVKDSMRVLLPVLLNKNHDNCDKIRAILLYIFSINGTTEENLDRLIQNVKIENESDMIRNWSYLGVPIVPQSQQGKPLRKDRSAEETFQLSRWTPFIKDIMEDAIDNRLDSKEWPYCSQCPAVWNGSGAVSARQKPRANYLEDRKNGSKLIVFVIGGITYSEVRCAYEVSQAHKSCEVIIGSTHVLTPKKLLDDIKMLNKPKDKVSLIKDE
Protein: Dorsocross3 (Q8T6Q0)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00201}.
Interaction partners:
Sequence:
MLTLPNIADLRLQQQIAQEIYRQQIMQRLPDPLCGLLPNFAGHFMPPPPPPQPTLPGDVEAKLENNELWQQFHSIGTEMIITKCGRRMFPSMRVSLSGLEEEASYCVLLEMVPIGDCRYKFSGSQWVPAGGAEPQSPQRMYLHPESPATGKHWQSQALLFSKVKLTNNTLDNNGHIVLASMHKYQPRLHVIRTSDLGQIPWAPQQAFVFPETEFIAVTAYQNDRITKLKIDNNPFAKGFRESGQSRCKRKINDSPPPTQPEANQVDRSPVTSPLAKRLRLVEEFPQHHHHQSHHSVPMQRHYLLDALEANFYVPAPPPPAIEYARHIGGAYPSWAYTPPSPASSVSSSSAGSTSGESAADREADADADTFVDVVGTAPAAPPSPSPPVPATATAPASSSSDPTMAKPKRSSFSISDILGTSSSI
Protein: Procyclin-associated gene 1 (PAG1) protein, putative (Q38AP7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MVELVRLKIVKVRGNEGGNSNWTSCTGIAKFLKRVGSKVNRVKRRELKRLRYLGYSAVGAAGIAAGRLDEMINVWRRAYSSGKGDFCVGNSEHHATRNQLLNCYLSDSEKDEFISLGGMHRMERVEEMNMTRESMNELLRLTGGGGNPLERYVHSANCHLTNTRPGAATSPKTAPPEEYSGEIELFPLNEVEEDSLGGQEKPVQRF
Protein: Mitochondrial brown fat uncoupling protein 1 (UCP 1) (Solute carrier family 25 member 7) (Thermogenin) (P04633)
Organism: Rattus norvegicus (Rat)
Function: Mitochondrial protein responsible for thermogenic respiration, a specialized capacity of brown adipose tissue and beige fat that participates in non-shivering adaptive thermogenesis to temperature and diet variations and more generally to the regulation of energy balance (By similarity). Functions as a long-chain fatty acid/LCFA and proton symporter, simultaneously transporting one LCFA and one proton through the inner mitochondrial membrane. However, LCFAs remaining associated with the transporter via their hydrophobic tails, it results in an apparent transport of protons activated by LCFAs. Thereby, dissipates the mitochondrial proton gradient and converts the energy of substrate oxydation into heat instead of ATP. Regulates the production of reactive oxygen species/ROS by mitochondria (By similarity).
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P12242}; Multi-pass membrane protein {ECO:0000269|PubMed:7691596}.
Interaction partners:
- Lipid transferase CIDEA
- Beta-3 adrenergic receptor
- Peroxisome proliferator-activated receptor gamma coactivator 1-alpha
- PR/SET domain 16.
- Peroxisome proliferator-activated receptor gamma
- Peroxisome proliferator-activated receptor alpha
- 30 kDa adipocyte complement-related protein
- Leptin
- Hormone-sensitive lipase
- Transmembrane protein 26
Sequence:
MVSSTTSEVQPTMGVKIFSAGVSACLADIITFPLDTAKVRLQIQGEGQASSTIRYKGVLGTITTLAKTEGLPKLYSGLPAGIQRQISFASLRIGLYDTVQEYFSSGRETPASLGSKISAGLMTGGVAVFIGQPTEVVKVRMQAQSHLHGIKPRYTGTYNAYRVIATTESLSTLWKGTTPNLMRNVIINCTELVTYDLMKGALVNHHILADDVPCHLLSALVAGFCTTLLASPVDVVKTRFINSLPGQYPSVPSCAMTMYTKEGPAAFFKGFAPSFLRLGSWNVIMFVCFEQLKKELMKSRQTVDCTT
Protein: C2 domain-containing protein (Q7Z1P9)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MLWVILSWGLVAVLCYFALNHLGSTGEAAHTSSTFGSSVSGNGVANGGTHTSSGEWSNEIVSWLYSNFHKVPAPMDAWIKSLNEAAKKVTSPTKCEVLFEGFGDHSDVLQPPKISNVRVEHGPRDHLTVRSNVHLPCVKLRLVSSQRTPERMIVSNYDVSIVDLRGEVECRMACIANQLYLMGCFSGRPEMDIELRNTDPNAQYQVSIPMVEESIRRCLLSAVTNINLSEEMPEERNTFADTFSRTIYNPPTHSPSGTMRNSYNNYDTNLHVDAYGTQSSHRSNSPSGDVPEMFKKLNESHLISPSYNTNSIPNKMRIKVIKASRLGREVSQPFVNVEMDEPAQKYSTTKGINANPFWEETFDFDLTPATEEILFEIYEGNDKLHMNDDEGFLGLAIVNFEEIRRSGETVHSLKLQGRPYRKDAISGEITVQFDFFYDPNLLTSGKLTDTVKVTNPNGSEFRETLTTHRRPIYDPHDNFDGHEPIVPSKTTTVTVKTVSQTLKEKPTIQSVHGSLENAVDPATQKILDRQFKNHNDPKTRELEAKLQSVAQSMSASSTLDRPSKNGNNGQYYRDQTAPPEFHEELDVRQSRDKSKKAPTEKRDRSFFGELKDRLSGRRGRSQKRSKSVDVENNQLLEEAVSLPPSRDPSRTRYAVSSNDKYRETHSVGGRSGESTKSLYQHSTLILELDQDKQAKYFLIPPAMLNEPAASRLMRKGKKLHIYNDHTFVAVKVKGCSGATCNVCQQRIRSSFSKQAYQCRDCKMVCHKTCHYKTDAFCTQSNVSKLQIAKDVDWAHFLSHYQLEEFISSEGL