wanglab/gogpt-training-data huggingface dataset:
Protein: C-X-C motif chemokine 3 (Dendritic cell inflammatory protein 1) (Q6W5C0)
Organism: Mus musculus (Mouse)
Function: Ligand for CXCR2. Has chemotactic activity for neutrophils. May play a role in inflammation and exert its effects on endothelial cells in an autocrine fashion.
Subcellular location: Secreted {ECO:0000250|UniProtKB:Q10746}.
Interaction partners:
- C-X-C chemokine receptor type 2
- C-X-C chemokine receptor type 1
- C-X-C motif chemokine 2
- Growth-regulated alpha protein
- Transcription factor Jun
- Nuclear factor NF-kappa-B p105 subunit
- Transcription factor p65
- C-X-C motif chemokine 5
- C-X-C motif chemokine 16
- Interleukin-1 beta
Sequence:
MAPPTCRLLSAALVLLLLLATNHQATGAVVASELRCQCLNTLPRVDFETIQSLTVTPPGPHCTQTEVIATLKDGQEVCLNPQGPRLQIIIKKILKSGKSS
Protein: Putative WAS protein family homolog 3 (Protein FAM39DP) (C4AMC7)
Organism: Homo sapiens (Human)
Function: Acts as a nucleation-promoting factor 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. Involved in endocytic trafficking of EGF. Involved in transferrin receptor recycling. Regulates the trafficking of endosomal alpha5beta1 integrin to the plasma membrane and involved in invasive cell migration (By similarity). In T-cells involved in endosome-to-membrane recycling of receptors including T-cell receptor (TCR), CD28 and ITGAL; proposed to be implicated in T cell proliferation and effector function. In dendritic cells involved in endosome-to-membrane recycling of major histocompatibility complex (MHC) class II probably involving retromer and subsequently allowing antigen sampling, loading and presentation during T-cell activation. Involved in Arp2/3 complex-dependent actin assembly driving Salmonella typhimurium invasion independent of ruffling (By similarity). Involved in the exocytosis of MMP14 leading to matrix remodeling during invasive migration and implicating late endosome-to-plasma membrane tubular connections and cooperation with the exocyst complex (By similarity). Involved in negative regulation of autophagy independently from its role in endosomal sorting by inhibiting BECN1 ubiquitination to inactivate PIK3C3/Vps34 activity (By similarity).
Subcellular location: Early endosome {ECO:0000269|PubMed:20175130, ECO:0000269|PubMed:20498093}. Early endosome membrane {ECO:0000250|UniProtKB:A8K0Z3}. Recycling endosome membrane {ECO:0000250|UniProtKB:Q8VDD8}. Cell projection, lamellipodium {ECO:0000269|PubMed:18159949}. Cell projection, filopodium {ECO:0000269|PubMed:18159949}. Cytoplasmic vesicle, autophagosome {ECO:0000250|UniProtKB:Q8VDD8}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250|UniProtKB:Q8VDD8}. Note=Localization to the endosome membrane is mediated via its interaction with WASHC2. Localizes to MMP14-positive late endosomes and transiently to invadipodia (By similarity). Localized to Salmonella typhimurium entry sites (By similarity). {ECO:0000250|UniProtKB:A8K0Z3, ECO:0000250|UniProtKB:Q8VDD8}.
Interaction partners:
Sequence:
MTPVRMQHSLAGQTYAVPLIQPDLRREEAVQQMADALQYLQKVSGDIFSRISQQVEQSRSQVQAIGEKVSLAQAKIEKIKGSKKAIKVFSSAKYPAPERLQEYGSIFTGAQDPGLQRRPRHRIQSKHRPLDERALQEKDFPVCVSTKPEPEDDAEEGLGGLPSNISSVSSLLLFNTTENLGKKYVFLDPLAGAVTKTHVMLGAETEEKLFDAPLSISKREQLEQQVPENYFYVPDLGQVPEIDVPSYLPDLPGITNDLMYIADLGPGIAPSAPGTIPELPTFHTEVAEPLKVDLQDGVLTPPPPPPPPPPAPEVLASAPPLPPSTAAPVGQGARQDDSSSSASPSVQGAPREVVDPSGGRATLLESIRQAGGIGKAKLRSMKERKLEKKQQKEQEQVRATSQGGHLMSDLFNKLVMRRKGISGKGPGAGEGPGGAFARVSDSIPPLPPPQQPQAEEDEDDWES
Protein: ESX-3 secretion system ATPase EccB3 (EC 3.6.-.-) (ESX conserved component B3) (Type VII secretion system protein EccB3) (T7SS protein EccB3) (P9WNR3)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: An ATPase (By similarity). Part of the ESX-3 specialized secretion system, which is important for iron and zinc uptake or homeostasis.
Subcellular location: Cell inner membrane {ECO:0000250|UniProtKB:B2HST3}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- ESX-3 secretion system protein EccD3
- ESX-3 secretion system protein EccC3
- ESX-3 secretion system protein EccE3
- ESX-3 secretion system protein EccA3
- Mycosin-3
- ESX-3 secretion-associated protein EspG3
- PPE family protein PPE4
- ESX-5 secretion system protein EccD5
- ESX-5 secretion system protein EccC5
- ESX-4 secretion system protein EccC4
Sequence:
MTNQQHDHDFDHDRRSFASRTPVNNNPDKVVYRRGFVTRHQVTGWRFVMRRIAAGIALHDTRMLVDPLRTQSRAVLMGVLIVITGLIGSFVFSLIRPNGQAGSNAVLADRSTAALYVRVGEQLHPVLNLTSARLIVGRPVSPTTVKSTELDQFPRGNLIGIPGAPERMVQNTSTDANWTVCDGLNAPSRGGADGVGVTVIAGPLEDTGARAAALGPGQAVLVDSGAGTWLLWDGKRSPIDLADHAVTSGLGLGADVPAPRIIASGLFNAIPEAPPLTAPIIPDAGNPASFGVPAPIGAVVSSYALKDSGKTISDTVQYYAVLPDGLQQISPVLAAILRNNNSYGLQQPPRLGADEVAKLPVSRVLDTRRYPSEPVSLVDVTRDPVTCAYWSKPVGAATSSLTLLAGSALPVPDAVHTVELVGAGNGGVATRVALAAGTGYFTQTVGGGPDAPGAGSLFWVSDTGVRYGIDNEPQGVAGGGKAVEALGLNPPPVPIPWSVLSLFVPGPTLSRADALLAHDTLVPDSRPARPVSAEGGYR
Protein: AN1-type zinc finger protein 3 (Testis-expressed protein 27) (Q9H8U3)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MGDAGSERSKAPSLPPRCPCGFWGSSKTMNLCSKCFADFQKKQPDDDSAPSTSNSQSDLFSEETTSDNNNTSITTPTLSPSQQPLPTELNVTSPSKEECGPCTDTAHVSLITPTKRSCGTDSQSENEASPVKRPRLLENTERSEETSRSKQKSRRRCFQCQTKLELVQQELGSCRCGYVFCMLHRLPEQHDCTFDHMGRGREEAIMKMVKLDRKVGRSCQRIGEGCS
Protein: UDP-galactose transporter 1 (At-UDP-GalT1) (Q9C521)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Nucleotide sugar transporter that specifically transports UDP-galactose.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- WAT1-related protein At3g18200
- Maternal effect embryo arrest 9
- AT4g32140/F10N7_50
Sequence:
MEEGSMFRSLLAILQWWGFNVTVIIMNKWIFQKLDFKFPLSVSCVHFICSSIGAYIVIKVLKLKPLIVVDPEDRWRRIFPMSFVFCINIVLGNVSLRYIPVSFMQTIKSFTPATTVVLQWLVWRKYFDWRIWASLVPIVGGILLTSVTELSFNMFGFCAALFGCLATSTKTILAESLLHGYKFDSINTVYYMAPFATMILGIPALLLEGSGILSWFEAHPAPWSALIIILSSGVLAFCLNFSIFYVIHSTTAVTFNVAGNLKVAVAVMVSWLIFRNPISYMNAVGCGITLVGCTFYGYVRHMLSQQTPGTPRTPRTPRSKMELLPLVNNDKLEGKV
Protein: C2 domain-containing protein (Q386A0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MATLTVTVHEARDLPVMDRTTGLADTYVVVKLDDLEYTTDISRMSCHPVWNRVFRFDTPDLLVLQEDPLEVRVYDHDIFSRDDIVGHTFVDLNSMVLKSNASMSGWFPLFDTSTEGIRGEIRLTLKIKFHTAENPLAPRLPKRYVCKLPSPQNTRSPHTRGETSQQPQAVPSAAFMQMSSDLEPLRAARAQHPSFTMGDEGVLIFSAWRLDPSVYRVETMLTMVEELIVKADPEHSKLTNLRSTRSTNEARIIQLYKLSGKVRRQLARKVVEMQCNAVLGYVEEFDMEANGIIVRAYGTPCVLSAVKFVDPGGADTVPAAQIQVVKRLTPPMSDSPVAMHCSMPTPLQMPPAVGHGDLAGNNVVAMNIRCLEQEAVQAAQQPQQQRLGISTAAQQTSSFHGTSALIPFVHESNSPGATRGDNPSMESLPPAPTGMRTNVLLLTVKDLPCGTVEHVGGHISAMSVKIVAKMKSRHLISQERDAWWMELREELRANARAFHCNVVIGYEEAVLYHEDVVVLSLFGTAVMLNLTLHPLRCGPELLYQSVRKRFAARKACSLLHLYAPVVRYKDATEEDANQFMCNVCHSRLVPEVLLTSCAMPQELIYRERPRLVQAVVTKEKSAIRGVGLALAVSQALPYIEYSLHKQLLFNLKFQKLNAVFGIRITLSISHDTIIGTLTGTGCCLVGLPVPSPPRVEVLDPAIRNKESVIRLEAVAEQLGRSRHHRLGGLAMNIGARFANSNLRGSDSSCDPFEVCADDFMSDHWDDNESFGGSCSNHEPGGAGKADKTTDYIVKIDDEEEAEMMLGMIGDLSFEDSLMVTIPYVPESANMYGSQERVVLNTRFALPRTYHGATAVATVSECVANAKRSYVQTVCRAALRRCGRSSLSRLCVTSYACDFFFEPNSGELHLRMEGCLMTCTTEQQIRLMELEKRSFSECMRYLDADTKPVDHGSNSHGETHMVDGLRSPPLGSSSCGAGPAPQDAEPRVFTMSNAPYTLPYVFKVDAVNPAQWWNERIVAPVSAPSDAFEFYSDNRRRHGVIGRKLRTFASKVTAFVGNILKPTGSQTNRRPRSNAQQCETTPISSEVAGGGYLLHEPMRRIPSDPGELEAGDPVVIFTSQDFVAGQAIKRYVGRLSQHFIREAYEVDNSTDLGIFFQQTEIEMQCMVQAMVILMGGNALLKHRVTYHEVWDSDGSGCASLFATVTGDVVETCATPLVPLPCGGTGDNSGEPLICGY
Protein: Histone demethylase UTY (EC 1.14.11.68) (Male-specific histocompatibility antigen H-YDB) (Ubiquitously transcribed TPR protein on the Y chromosome) (Ubiquitously transcribed Y chromosome tetratricopeptide repeat protein) ([histone H3]-trimethyl-L-lysine(27) demethylase UTY) (P79457)
Organism: Mus musculus (Mouse)
Function: Male-specific histone demethylase that catalyzes trimethylated 'Lys-27' (H3K27me3) demethylation in histone H3. Has relatively low KDM activity.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Lysine-specific demethylase 5D
- ATP-dependent RNA helicase DDX3Y
- Eukaryotic translation initiation factor 2 subunit 3, Y-linked
- Lysine-specific demethylase 6A
- Ubiquitin carboxyl-terminal hydrolase 9Y
- Set1/Ash2 histone methyltransferase complex subunit ASH2
- ATP synthase F
- Histone H3.1
- Histone H3.2
- ATP synthase F
Sequence:
MKSYGLSLTTAALGNEEKKMAAEKARGEGEEGSFSLTVEEKKALCGLDSSFFGFLTRCKDGAKMKTLLNKAIHFYESLIVKAEGKVESDFFCQLGHFNLLLEDYSKALSSYQRYYSLQTDYWKNAAFLYGLGLVYFYYNAFQWAIRAFQEVLYVDPNFCRAKEIHLRLGFMFKMNTDYESSLKHFQLALIDCNVCTLSSVEIQFHIAHLYETQRKYHSAKAAYEQLLQIESLPSQVKATVLQQLGWMHHNMDLIGDNTTKERYAIQYLQKSLEEDPNSGQSWYFLGRCYSCIGKVQDAFVSYRQSIDKSEASADTWCSIGVLYQQQNQPMDALQAYICAVQLDHGHAAAWMDLGILYESCNQPQDAIKCYLNAARSKSCNNTSALTSRIKFLQAQLCNLPQSSLQNKTKLLPSIEEAWSLPIPAELTSRQGAMNTAQQSVSDTWNSVQTASHHSVQQKVYTQCFTAQKLQSFGKDQQPPFQTGSTRYLQAASTNDQNQNGNHTLPQNSKGDAQNHFLRIPTSEEQKIINFTKESKDSRSKSLTSKTSRKDRDTSNICVNAKKHSNHIYQISSVPISSLNNKESVSPDLIIVDNPQLSVLVGETIDNVDHDIGTCNKVNNVHLAIHKKPDNLSASSPSSAISTETLSLKLTEQTHIVTSFISPHSGLHTINGEGHENLESSASVNVGLRPRSQIIPSMSVSIYSSSTEVLKACRSLGKNGLSNGHILLDICPPPRPPTSPYPPLPKEKLNPPTPSIYLENKRDAFFPPLHQFCINPKNPVTVIRGLAGALKLDLGLFSTKTLVEANNEHIVEVRTQLLQPADENWDPSGTKKIWRYENKSSHTTIAKYAQYQACSFQESLREENERRTQVKDYSDNESTCSDNSGRRQKAPFKTIKCGINIDLSDNKKWKLQLHELTKLPAFVRVVSAGNLLSHVGYTILGMNSVQLCMKVPGSRIPGHQENNNFCSVNINIGPGDCEWFVVPEDYWGVLNDFCEKNNLNFLMSSWWPNLEDLYEANVPVYRFIQRPGDLVWINAGTVHWVQAIGWCNNITWNVGPLTAFQYKLAVERYEWNKLQSVKSVVPMVHLSWNMARNIKVSDPKLFEMIKYCLLKILKHCQTLREALVAAGKEVLWHGRINDEPAPYCSICEVEVFNLLFVTNESNSQKTYIVHCQNCARKTSGNLENFVVLEQYKMEDLIQVYDQFTLAPSLSSAS
Protein: Three-finger hemachatoxin (B3EWH9)
Organism: Hemachatus haemachatus (Rinkhals) (Sepedon haemachatus)
Function: This protein lyses red blood cells and has cardiotoxic and hypotensive activities.
Subcellular location: Secreted {ECO:0000269|PubMed:23144733}.
Interaction partners:
Sequence:
LKCHNKLVPFLSKTCPEGKNLCYKMTLMKMPKIPIKRGCTDACPKSSLLVKVVCCNKDKCN
Protein: V-type proton ATPase subunit G (D3ZTZ4)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- V-type proton ATPase subunit D
- Vacuolar proton pump subunit B
- V-type proton ATPase subunit a
- V-type proton ATPase subunit F
- V-type proton ATPase subunit C 2
- ATPase H+ transporting V1 subunit E2
- V-type proton ATPase subunit d 2
- V-type proton ATPase subunit H
- V-type proton ATPase subunit S1
- V-type proton ATPase catalytic subunit A
Sequence:
MCSLLTKQAEFGGDPLGNKRACASQLPQTSPSLEQDTMTSQSQGIQQLLQAEKRAKDKLDEAKKRKGKRLRQAKEEAVAETDQYRMQREKEFRLKQSKIMGSQSHLSDELEEQTLEKIKELSGSYHKCMDSVIKQLLSMVCEMKPEVHVNYRATS
Protein: Sodium/proline symporter (Proline permease) (P10502)
Organism: Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Function: Catalyzes the sodium-dependent uptake of extracellular L-proline.
Subcellular location: Cell inner membrane {ECO:0000250|UniProtKB:P07117}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Bifunctional protein PutA
- Aminodeoxychorismate synthase component 1
- Tryptophan synthase beta chain
- Proline/betaine transporter
- Tryptophan synthase alpha chain
- Alanine/glycine transport protein
- Transcriptional regulator, Lrp family
- DNA polymerase IV
Sequence:
MAISTPMLVTFCVYIFGMILIGFIAWRSTKNFDDYILGGRSLGPFVTALSAGASDMSGWLLMGLPGAIFLSGISESWIAIGLTLGAWINWKLVAGRLRVHTEFNNNALTLPDYFTGRFEDKSRVLRIISALVILLFFTIYCASGIVAGARLFESTFGMSYETALWAGAAATIIYTFIGGFLAVSWTDTVQASLMIFALILTPVMVIVGVGGFSESLEVIKQKSIENVDMLKGLNFVAIISLMGWGLGYFGQPHILARFMAADSHHSIVHARRISMTWMILCLAGAVAVGFFGIAYFNNNPALAGAVNQNSERVFIELAQILFNPWIAGVLLSAILAAVMSTLSCQLLVCSSAITEDLYKAFLRKSASQQELVWVGRVMVLVVALIAIALAANPDNRVLGLVSYAWAGFGAAFGPVVLFSVMWSRMTRNGALAGMIIGAVTVIVWKQYGWLDLYEIIPGFIFGSLGIVIFSLLGKAPTAAMQERFAKADAHYHSAPPSKLQAE
Protein: Phosphate-specific transport system accessory protein PhoU (A0A0H2UQU1)
Organism: Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Subcellular location: Cytoplasm {ECO:0000256|PIRNR:PIRNR003107}.
Interaction partners:
Sequence:
MLRSQFEEDLEKLHNQFYAMGQEVLSQINRTVRAFVTHDRDLAKEVIEDDAEVNEYEVKLEKKSFEMIALQQPVSQDLRTVLTVLKAVSDVERMGDHAVAIAQATIRMKGEERIPAVEEEIKKMGREVKSVVEAALDLYLNGSVDDAYRVASMDEQINHYFETIRDLATEEIKKNPEAIVTGRDYFQVISYLERIGDYAKNICEWVVYFETGKIVEL
Protein: Zinc finger protein-like 1 (E9PQA5)
Organism: Homo sapiens (Human)
Subcellular location: Golgi apparatus, cis-Golgi network membrane {ECO:0000256|ARBA:ARBA00004612, ECO:0000256|RuleBase:RU369078}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004612, ECO:0000256|RuleBase:RU369078}.
Interaction partners:
Sequence:
MGLCKCPKRKVTNLFCFEHRVNVCEHCLCIVQSYLQWLQDSDYNPNCRLCNIPLASRETTRLVCYDLFHWACLNERAAQLPRNTAPAGYQCPSCNGPIFPPTNLAGPVASALREKLATVNWARAGLGLPLIDEVVSPEPEPLNTSDFSDWSSFNASSTPGPEEVDSASAAPA
Protein: Programmed cell death protein 7 (ES18) (hES18) (Q8N8D1)
Organism: Homo sapiens (Human)
Function: Promotes apoptosis when overexpressed.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- U11/U12 small nuclear ribonucleoprotein 35 kDa protein
- Zinc finger matrin-type protein 5
- U2 small nuclear ribonucleoprotein auxiliary factor 35 kDa subunit-related protein 2
- U11/U12 small nuclear ribonucleoprotein 48 kDa protein
- U11/U12 small nuclear ribonucleoprotein 25 kDa protein
- Zinc finger CCHC-type and RNA-binding motif-containing protein 1
- Small nuclear ribonucleoprotein E
- Small nuclear ribonucleoprotein F
- Small nuclear ribonucleoprotein G
- PHD finger-like domain-containing protein 5A
Sequence:
MALPPFFGQGRPGPPPPQPPPPAPFGCPPPPLPSPAFPPPLPQRPGPFPGASAPFLQPPLALQPRASAEASRGGGGAGAFYPVPPPPLPPPPPQCRPFPGTDAGERPRPPPPGPGPPWSPRWPEAPPPPADVLGDAALQRLRDRQWLEAVFGTPRRAGCPVPQRTHAGPSLGEVRARLLRALRLVRRLRGLSQALREAEADGAAWVLLYSQTAPLRAELAERLQPLTQAAYVGEARRRLERVRRRRLRLRERAREREAEREAEAARAVEREQEIDRWRVKCVQEVEEKKREQELKAAADGVLSEVRKKQADTKRMVDILRALEKLRKLRKEAAARKGVCPPASADETFTHHLQRLRKLIKKRSELYEAEERALRVMLEGEQEEERKRELEKKQRKEKEKILLQKREIESKLFGDPDEFPLAHLLEPFRQYYLQAEHSLPALIQIRHDWDQYLVPSDHPKGNFVPQGWVLPPLPSNDIWATAVKLH
Protein: Protein RecA (Recombinase A) (Q9PH23)
Organism: Xylella fastidiosa (strain 9a5c)
Function: Can catalyze the hydrolysis of ATP in the presence of single-stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. It interacts with LexA causing its activation and leading to its autocatalytic cleavage.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00268}.
Interaction partners:
- LexA repressor
- DNA polymerase I
- Helix-turn-helix domain-containing protein
- DNA helicase RecQ
- Beta sliding clamp
- DNA repair protein RecN
- Chaperone protein DnaK
- DNA repair protein RadA
- DNA gyrase subunit B
- Chaperonin GroEL
Sequence:
MDENKKRALSVALSQIEKQFGKGSVMRMGDRVIEAVEAIPTGSLMLDLALGIGGLPKGRVVEIYGPESSGKTTLTLQAIAQCQKKGGTAAFIDAEHALDPIYAGKLGVNVDDLLLSQPDTGEQALEIADMLVRSGSIDIMVIDSVAALTPRAEIEGEMGDQLPGLQARLMSQALRKLTGNIKRSNTLVIFINQLRMKIGVMMPGQSPETTTGGNALKFYASVRLDIRRIGAIKKGDEIIGNQTKIKVVKNKLAPPFKQVVTEILYGEGISREGELIEMGVEAKLVEKAGAWYSYGGERIGQGKDNARGYLRENPHLAAKLEADLREKFEPTELSREEGDEDTLEDTM
Protein: 17.9 kDa class I heat shock protein (17.9 kDa heat shock protein 1) (OsHsp17.9A) (Q84Q77)
Organism: Oryza sativa subsp. japonica (Rice)
Subcellular location: Nucleus {ECO:0000269|PubMed:15659629}.
Interaction partners:
Sequence:
MSLIRRSNVFDPFSLDLWDPFDGFPFGSGGSSSGSIFPSFPRGASSETAAFAGARIDWKETPEAHVFKADVPGLKKEEVKVEVDDGNILQISGERNKEQEEKTDQWHRVERSSGKFLRRFRLPDNAKPEQIKASMENGVLTVTVPKEEAKKPDVKSIQISG
Protein: Septin-10 (Q8C650)
Organism: Mus musculus (Mouse)
Function: Filament-forming cytoskeletal GTPase (By similarity). May play a role in cytokinesis (Potential).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9P0V9}. Cytoplasm, cytoskeleton {ECO:0000250}. Cell projection, cilium, flagellum {ECO:0000269|PubMed:35700329}. Note=Detected in the annulus of the sperm flagellum and in the neck region in spermatids and mature sperm. {ECO:0000269|PubMed:35700329}.
Interaction partners:
- Septin-11
- Septin-7
- Septin-1
- Septin-9
- Septin-8
- Septin-2
- Septin-5
- Septin-14
- Septin-4
- Septin
Sequence:
MASCDEIKEHPRSLSMCGHVGFESLPDQLVDRSIEQGFCFNILCVGETGIGKSTLINTLFNTNFEELESSHFCPCVRLRAQTYELQESNVRLKLTIVNTVGFGDQINKEDSYQPIVDYIDDQFEAYLQEEVKIKRALFNYHDSRIHVCLYFIAPTGHSLRTLDLLTMKSLDNKVNIIPLIAKADTISKSELQKFKMKLMNELVINGVQIYQFPTDDDTTSKINGAMNGHLPFAVVGSMDEIKVGNKMVKGRQYPWGIVQVENENHCDFVKLREMLICTNMEDLREQTHMRHYELYRRCKLQEMGFVDMGPENKPLSLQETYEAKRHEFYGERQRKEEQMKQMFVQRVKEKEAILKEAERELQAKFEHLKRIHQEERMKLEEKRRMLEEESVAFAKKKATCELFPNQSFLASGSSIRKDKDRKKADGASAFCDCLTAQESVRLCISSPRKDMD
Protein: DNA helicase (EC 3.6.4.12) (H3BTW3)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSSVKRPRGRPPSSKKSDGSGTYTKLQNTQVRVMSEKKQRKKVESESKQEKANRIISEAIAKAKERGERNIPRVMSPENFPTASVEGKEEKKGRRMKSKPKDKDSKKTKTCSKLKEKTKIGKLIITLGKKQKRKNESSDEISDAEQMPQHTLKDQDSQKRRSNRQIKRKKYAEDIEGKQSEEEVKGSMKIKKNSAPLPGEQPLQLFVENPSEEDAAIVDKILSSRTVKKEISPGVMIDTEEFFVKYKNYSYLHCEWATEEQLLKDKRIQQKIKRFKLRQAQRAHFFADMEEEPFNPDYVEVDRVLEVSFCEDKDTGEPVIYYLVKWCSLPYEDSTWELKEDVDLAKIEEFEQLQASRPDTRRLDRPPSNIWKKIDQSRDYKNGNQLREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFLYEILLTGIRGPFLIIAPLSTIANWEREFRTWTDINVVVYHGSLISRQMIQQYEMYFRDSQGRIIRGAYRFQAIITTFEMILGGCGELNAIEWRCVIIDEAHRLKNKNCKLLEGLKLMNLEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFGDLKTEEQVQKLQAILKPMMLRRLKEDVEKKLAPKEETIIEVELTNIQKKYYRAILEKNFSFLSKGAGQTNVPNLVNTMMELRKCCNHPYLIKGAEEKILGEFRDTYNPAASDFHLQAMIQSAGKLVLIDKLLPKMKAGGHKVLIFSQMVRCLDILEDYLIHKRYLYERIDGRVRGNLRQAAIDRFSKPDSDRFVFLLCTRAGGLGINLTAADTCIIFDSDWNPQNDLQAQARCHRIGQNKAVKVYRLVTRNSYEREMFDRASLKLGLDKAVLQSMSGRESNVGGIQQLSKKEIEDLLRRGAYGAIMEEEDEGSKFCEEDIDQILLRRTKTITIESEGRGSTFAKASFVASGNRTDISLDDPNFWQKWAKKAEIDIEAISGRNSLVIDTPRIRKQTRPFSATKDELAELSEAESEGDEKPKLRRPCDRSNGYGRTECFRVEKNLLVYGWGRWREILSHGRFKRQLNEHDVEIICRALLAYCLVHYRGDEKIKGFIWDLITPTEDGQTRELQNHLGLSAPVPRGRKGKKVKTQTSSFDIQKAEWLRKYNPEQLLQDEGYKKHIKHHCNKVLLRVRMLYYLKQEVIGNECQKVFDGVDASDIDVWVPEPDHSEVPAEWWDFDADKSLLIGVFKHGYEKYNTIRADPALCFLERVGKPDEKAVAAEQRANDYMDGDVEDPEYKPAPAIFKDDIEDDVSSPGDLVIADGDGQLMEGDKVYWPTQSALTTRLRRLITAYQRTNKNRQIQQIQPTFSVPTSVMQPIYEEATLNPKMAAKIERQQRWTRREEADFYRVVSTFGVVFDPDRGQFDWTKFRAMARLHKKTDDSLEKYLYAFMSMCRRVCRLPSKEELVDPNIFIQPITEERASRTLYRIELLRKVREQALRHPQLFERLKLCHPNPDLPVWWECGPHDRDLLIGAAKHGVSRTDYHILRDPELSFMAAQRNYSQSKMAHSRTSTPLLQQYQVALSASPLTSLPRLLDAKGIILEEMKVKSENLKEEPQSSEEESMSSVETRTLIKSEPVSPKNGVLPQATGDQKSGGKCETDRRMVAARTEPLTPNPASKKPRVHKRGSESSSDSDSDSERSSCSSRSSSSSSSSSCSHSRSGSSSSSSSSCSSASSSSSSSTSSSSSSSSSSSEESDSDEEEAQKRAESTTHMKAYDEESVASLSTTQDETQDSFQMNNGTPESAYILQGGYMLAASYWPKDRVMINRLDSICQTVLKGKWPSARRSYDANTVASFYTTKLLDSPGAATEYSDPSVPTPPGAGVKEEHDQSTQMSKVKKHVREKEFTVKIKDEGGLKLTFQKQGLAQKRPFDGEDGALGQQQYLTRLRELQSASETSLVNFPKSIPVSGTSIQPTLGANGVILDNQPIVKKRRGRRKNVEGVDIFFFNRNKPPNHVSLGLTSSQISTGINPALSYTQPQGIPDTESPVPVINLKDGTRLAGDDAPKRKDLEKWLKEHPGYVEDLGAFIPRMQLHEGRPKQKRHRCRNPNKLDVNSLTGEERVQLINRRNARKVGGAFAPPLKDLCRFLKENSEYGVAPEWGDVVKQSGFLPESMYERILTGPVVREEVSRRGRRPKSGIAKATAAAAAASATSVSGNPLLANGLLPGVDLTTLQALQQNLQNLQSLQVTAGLMGMPTGLPSGGEAKNMAAMFPMLLSGMAGLPNLLGMGGLLTKPTESGTEDKKGSDSKESEGKTERTESQSSENGGENSVSSSPSTSSTAALNTAAAANPLALNPLLLSNILYPGMLLTPGLNLHIPTLSQSNTFDVQNKNSDLGSSKSVEVKEEDSRIKDQEDKGGTEPSPLNENSTDEGSEKADASSGSDSTSSSSEDSDSSNED
Protein: Activating signal cointegrator 1 complex subunit 2 (ASC-1 complex subunit p100) (Trip4 complex subunit p100) (Q9H1I8)
Organism: Homo sapiens (Human)
Function: Plays a role in DNA damage repair as component of the ASCC complex. Recruits ASCC3 and ALKBH3 to sites of DNA damage by binding to polyubiquitinated proteins that have 'Lys-63'-linked polyubiquitin chains. Part of the ASC-1 complex that enhances NF-kappa-B, SRF and AP1 transactivation. Involved in activation of the ribosome quality control (RQC) pathway, a pathway that degrades nascent peptide chains during problematic translation. As part of the ribosome quality control trigger (RQT) complex, recognizes ZNF598-dependent ubiquitination of stalled ribosomes (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:12077347, ECO:0000269|PubMed:26924529, ECO:0000269|PubMed:29144457}. Nucleus speckle {ECO:0000269|PubMed:29144457, ECO:0000269|PubMed:29997253}. Note=Colocalizes with the spliceosomal components PRPF8 and SNRNP200/BRR2 in nuclear foci when cells have been exposed to alkylating agents that cause DNA damage. Colocalizes with RNF113A and 'Lys-63'-linked polyubiquitinated proteins, ALKBH3 and ASCC3 in nuclear foci when cells have been exposed to alkylating agents that cause DNA damage. {ECO:0000269|PubMed:29144457}.
Interaction partners:
- Activating signal cointegrator 1 complex subunit 1
- Activating signal cointegrator 1 complex subunit 3
- Activating signal cointegrator 1
- Alpha-ketoglutarate-dependent dioxygenase alkB homolog 3
- E3 ubiquitin-protein ligase ZNF598
- RING-type E3 ubiquitin-protein ligase PPIL2
Sequence:
MPALPLDQLQITHKDPKTGKLRTSPALHPEQKADRYFVLYKPPPKDNIPALVEEYLERATFVANDLDWLLALPHDKFWCQVIFDETLQKCLDSYLRYVPRKFDEGVASAPEVVDMQKRLHRSVFLTFLRMSTHKESKDHFISPSAFGEILYNNFLFDIPKILDLCVLFGKGNSPLLQKMIGNIFTQQPSYYSDLDETLPTILQVFSNILQHCGLQGDGANTTPQKLEERGRLTPSDMPLLELKDIVLYLCDTCTTLWAFLDIFPLACQTFQKHDFCYRLASFYEAAIPEMESAIKKRRLEDSKLLGDLWQRLSHSRKKLMEIFHIILNQICLLPILESSCDNIQGFIEEFLQIFSSLLQEKRFLRDYDALFPVAEDISLLQQASSVLDETRTAYILQAVESAWEGVDRRKATDAKDPSVIEEPNGEPNGVTVTAEAVSQASSHPENSEEEECMGAAAAVGPAMCGVELDSLISQVKDLLPDLGEGFILACLEYYHYDPEQVINNILEERLAPTLSQLDRNLDREMKPDPTPLLTSRHNVFQNDEFDVFSRDSVDLSRVHKGKSTRKEENTRSLLNDKRAVAAQRQRYEQYSVVVEEVPLQPGESLPYHSVYYEDEYDDTYDGNQVGANDADSDDELISRRPFTIPQVLRTKVPREGQEEDDDDEEDDADEEAPKPDHFVQDPAVLREKAEARRMAFLAKKGYRHDSSTAVAGSPRGHGQSRETTQERRKKEANKATRANHNRRTMADRKRSKGMIPS
Protein: Exocyst complex component SEC5B (AtSec5b) (F4HWE6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane during regulated or polarized secretion. Involved in polarized cell growth and organ morphogenesis. During cytokinesis, involved in cell plate initiation, cell plate maturation and formation of new primary cell wall.
Interaction partners:
- Exocyst complex component SEC3A
- Exocyst complex component SEC8
- Exocyst complex component SEC3B
- Exocyst complex component SEC6
- Exocyst complex component EXO84B
- Exocyst complex component EXO84A
- Exocyst complex component EXO84C
- Exocyst complex component SEC15B
- Exocyst complex component SEC10b
- Exocyst complex component SEC10a
Sequence:
MSSSDDLDEDELLQMALKEQSQRDVTYQKPPSANSRKPVTNLVQQPRRQKRAAAPPSKGGAKASRKPSMDEDDESEVELLSISSGDEDEGNDRGRGGGGDGGGGRGRGGSGKERGRARKEDDRAWDGVEPDCWKRVNEAELARKVRDMRESRTAPSVTQNLDRKVSGADKKVVLTSLQSFPRGMECIDPLKLGIIDNKTLRLITESSESLSKAEKVDNALREKLVYTSDHFDPKLFISRIHQETSAADLESGALALKSDLKGRNLQRKQLVKDNFDCFVSCKTTIDDIESKLKRIEDDPDGSGTTHLFNCMKSVTSRANRAFEPLFERQAQAEKIRSVQGMLQRFRTLFNLPSIIRSSISKGEYDLAVREYKKAKSIALPSHVNLLKRVLEEVEKVMQEFKGTLYRSMEDPKIDFTSLENTVRLLLELEPESDPVWHYLNVQNHRIHGMLEKCTFDHEARMEILRNQVHERALSDAKWRQIQQNGVQLSDDTSSMEDNQVQVDQPLEESARREKDALRGRYIKILTAVIVYHLPTFWKTALSVFTGKFAKSSQVNDTSASKAEEKAEEARYSSHSLEEIAGMIRNTISVYEAKVQSTFHDFDESYILHPYMSDTIKEVSKACQAFEAKESAPHSAVMALRKVKVEITKIYIQRLCSWMRASTEEISKEETWIPVSILERNRSPYSISYLPLAFRSIIVSGMEQINMMILSLKGEAARSEDMFAHIEEILISVRLAFLNCFLDFAAHLEQIGADLSQRTTKRESWQNGYSNDHQEEQSINAPESVVDPHRQLLMILSNIGYCKDELASELYNKYKYTWLQSRRNDEDISDLQDLMMSFSGLGEKVLEHYTFAKANLIRTAATNYLLDSGIQWGAAPPVKGIRDAAVELLHTLVAVHAEVFAGAKPLLDKILGTLVEGLIDTFLSLLDENRSDDLSSIDANGFCQLMLELEYFETILKPYLTVDATESLKSLQGAVLEKAIESISETVENNPGGHQRKPTRGSEDAISDDKQSSVSPDDLLALAQQCTSGMLQLELEKTRLNSACFIETIPLDPVPPVAKAAYSRTSTDSPSRNYRESQPMGSPVQARPRRR