wanglab/gogpt-training-data huggingface dataset:
Protein: TRAF3-interacting protein 1 (Intraflagellar transport protein 54 homolog) (Microtubule-interacting protein associated with TRAF3) (MIP-T3) (Q149C2)
Organism: Mus musculus (Mouse)
Function: Plays an inhibitory role on IL13 signaling by binding to IL13RA1. Involved in suppression of IL13-induced STAT6 phosphorylation, transcriptional activity and DNA-binding. Recruits TRAF3 and DISC1 to the microtubules (By similarity). Involved in epithelial morphogenesis and in the regulation of microtubule cytoskeleton organization. Is a negative regulator of microtubule stability, acting through the control of MAP4 levels. Involved in ciliogenesis.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q8TDR0}. Cell projection, cilium {ECO:0000269|PubMed:19253336}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:21945076}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:21945076}. Note=Microtubules. In the cilium, it is observed at the ciliary base, ciliary transition zone and ciliary tip. {ECO:0000250|UniProtKB:Q8TDR0}.
Interaction partners:
- Intraflagellar transport protein 57 homolog
- Intraflagellar transport protein 172 homolog
- Intraflagellar transport protein 20 homolog
- Intraflagellar transport protein 80 homolog
- Intraflagellar transport protein 52 homolog
- Intraflagellar transport protein 46 homolog
- Intraflagellar transport protein 81 homolog
- Intraflagellar transport protein 22 homolog
- Intraflagellar transport protein 27 homolog
- Intraflagellar transport protein 88 homolog
Sequence:
MNAAVVRRTQEALGKVIRRPPLTEKLLNKPPFRYLHDIITEVIRITGFMKGLYTDAEMKSENVKDKDAKISFLQKAIDVVMMVSGEPLAAKPARIVAGHEPERTNELLQLIGKCCLSKLSSDEAVKRVLAGDKGDSRGRAQRTSKAQEPNNKSGKEEESRIHKEDKRSSEAKERSASAEHKQKEELKEDSKPREKERDKEKAKEADRDRHRDPDRDRNRDGEREKARARAKDRDRNNRDRDREAERDRERDRRSEGGKEKERVKDRDRDRDKGRDRERRKSKNGEHTRDPDREKSRDADKPEKKSSSSGEISRKLSDGSFKDVKAEMEADISVGASRSSTLKPSKRRSKHSLEGDSPSDAEVEAGPAGQDKPEVMENAEVPSELPSSLRRIPRPGSARPAPPRVKRQESTETLVVDRSGSGKTVSSVIIDSQNSDNEDDEQFVVEAAPQLSEIADIDMVPSGELEDEEKHGGLVKKILETKKDYEKLQQSLKPGEKERSLIFESAWKKEKDIVSKEIEKLRVSIQTLCKSALPLGKIMDYIQEDVDAMQNELQLWHSENRQHAEALSQEQSITDSAVEPLKAELSELEQQIRDQQDKICAVKANILKNEEKIQKMVHSINLSSRR
Protein: Carbohydrate-responsive element-binding protein (ChREBP) (Class D basic helix-loop-helix protein 14) (bHLHd14) (MLX interactor) (MLX-interacting protein-like) (WS basic-helix-loop-helix leucine zipper protein) (WS-bHLH) (Williams-Beuren syndrome chromosomal region 14 protein) (Q8VIP2)
Organism: Rattus norvegicus (Rat)
Function: Transcriptional repressor. Binds to the canonical and non-canonical E box sequences 5'-CACGTG-3' (By similarity).
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}.
Interaction partners:
Sequence:
MARALADLSVNLQVPRVVPSPDSDSDTDLEDPSPRRSAGGLHRSQVIHSGHFMVSSPHSDSLTRRRDQEGPVGLADFGPRSIDPTLTRLFECLSLAYSGKLVSPKWKNFKGLKLLCRDKIRLNNAIWRAWYIQYVQRRKSPVCGFVTPLQGSEADEHRKPEAVVLEGNYWKRRIEVVMREYHKWRIYYKKRLRKSSREGDFLAPKQVEGGWPPPERWCEQLFSSVVPVLLGGSEEEPGGRQLLDLDCFLSDISDTLFTMTQPSPSSLQLPSEDAYVGNADMIQPDLTPLQPSLDDFMEISDFFTNYRPPQTPTSSNFPEPPSFGPMADSLFSGGILGPEMPSPASASSSSGMTPLSGNTRLQARNSCSGPLDPSTFPSSEFLLPEDPKTKMPPAPVPTPLLPYPGPVKVHGLEPCTPSPFPTMAPPPALLSEEPLFSARFPFTTVPPAPGVSTLPAPTTFVPTPQPGPGPGPVPFPVDHLPHGYLEPVFGPHFTVPQGVQPRCKPCSPPPGGRKASPPTLTSATASPTATATARDNNPCLTQLLRAAKPEQVLEPSTVPSTLLRPPESPDAVPEIPRVRAFYPPIPAPTPPRPPPGPATLAPPRSLVVPKAERLSPPASSGSERRPSGDLNSIQPPGALSVHLSPPQTVLSRGRVDNNKMENRRITHISAEQKRRFNIKLGFDTLHGLVSTLSAQPSLKVSKATTLQKTAEYILMLQQERAAMQEEAQQLRDEIEELNAAINLCQQQLPATGVPITHQRFDQMRDMFDDYVRTRTLHNWKFWVFSILIRPLFESFNGMVSTASLHSLRQTSLAWLDQYCSLPALRPTVLNSLRQLSTSTSILTDPSLVPEQATRAVTEGPLGRPL
Protein: Transcription factor MYB65 (Myb-related protein 65) (AtMYB65) (Q9FR97)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcriptional activator of alpha-amylase expression that binds to 5'-CAACTGTC-3' motif in target gene promoter. In vegetative tissues, inhibits growth by reducing cell proliferation. Promotes the expression of aleurone-related genes (e.g. CP1, CP, GASA1, BXL1 and BXL2) in seeds. Together with MYB33 and MYB101, promotes the programmed cell death (PCD) the vacuolation of protein storage vacuoles (PSVs) in the aleurone layers during seed germination. Together with MYB33, facilitates anther and tapetum development.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625}.
Interaction partners:
- Transcription factor TCP4
Sequence:
MSYTTATADSDDGMHSSIHNESPAPDSISNGCRSRGKRSVLKKGPWTSTEDGILIDYVKKHGEGNWNAVQKHTSLARCGKSCRLRWANHLRPNLKKGAFSQEEEQLIVEMHAKMGNKWAQMAEHLPGRTDNEIKNYWNTRIKRRQRAGLPLYPPEIYVDDLHWSEEYTKSNIIRVDRRRRHQDFLQLGNSKDNVLFDDLNFAASLLPAASDLSDLVACNMLGTGASSSRYESYMPPILPSPKQIWESGSRFPMCSSNIKHEFQSPEHFQNTAVQKNPRSCSISPCDVDHHPYENQHSSHMMMVPDSHTVTYGMHPTSKPLFGAVKLELPSFQYSETSAFDQWKTTPSPPHSDLLDSVDAYIQSPPPSQVEESDCFSSCDTGLLDMLLHEAKIKTSAKHSLLMSSPQKSFSSTTCTTNVTQNVPRGSENLIKSGEYEDSQKYLGRSEITSPSQLSAGGFSSAFAGNVVKTEELDQVWEPKRVDITRPDVLLASSWLDQGCYGIVSDTSSMSDALALLGGDDIGNSYVTVGSSSGQAPRGVGSYGWTNMPPVWSL
Protein: Liprin-alpha-4 (Protein tyrosine phosphatase receptor type f polypeptide-interacting protein alpha-4) (PTPRF-interacting protein alpha-4) (O75335)
Organism: Homo sapiens (Human)
Function: May regulate the disassembly of focal adhesions. May localize receptor-like tyrosine phosphatases type 2A at specific sites on the plasma membrane, possibly regulating their interaction with the extracellular environment and their association with substrates (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Cell surface {ECO:0000250}. Note=Colocalizes with PTPRF at the cell surface. {ECO:0000250}.
Interaction partners:
- Liprin-beta-1
- Liprin-beta-2
- ARF GTPase-activating protein GIT1
Sequence:
MCEVMPTINEGDRLGPPHGADADANFEQLMVNMLDEREKLLESLRESQETLAATQSRLQDAIHERDQLQRHLNSALPQEFATLTRELSMCREQLLEREEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSPSGVSSEVEVLKALKSLFEHHKALDEKVRERLRAALERVTTLEEQLAGAHQQVSALQQGAGVRDGAAEEEGTVELGPKRLWKEDTGRVEELQELLEKQNFELSQARERLVTLTTTVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARTAVQVRQREKMNEDHNKRLSDTVDRLLSESNERLQLHLKERMAALEEKNTLIQELESSQRQIEEQHHHKGRLSEEIEKLRQEVDQLKGRGGPFVDGVHSRSHMGSAADVRFSLGTTTHAPPGVHRRYSALREESAKLALPLTVTLRSPTWMRMSQGVCCNLEYHSSGTLCGSSGPLPVPEMIQEEKESTELRAEEIETRVTSGSMEALNLKQLRKRGSIPTSLTALSLASASPPLSGRSTPKLTSRSAAQDLDRMGVMTLPSDLRKHRRKLLSPVSREENREDKATIKCETSPPSSPRTLRLEKLGHPALSQEEGKSALEDQGSNPSSSNSSQDSLHKGAKRKGIKSSIGRLFGKKEKGRLIQLSRDGATGHVLLTDSEFSMQEPMVPAKLGTQAEKDRRLKKKHQLLEDARRKGMPFAQWDGPTVVSWLELWVGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNALHRLKLRLAIQEMVSLTSPSAPPTSRTSSGNVWVTHEEMETLETSTKTDSEEGSWAQTLAYGDMNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLKRLNYDRKELEKRREESQHEIKDVLVWTNDQVVHWVQSIGLRDYAGNLHESGVHGALLALDENFDHNTLALILQIPTQNTQARQVMEREFNNLLALGTDRKLDDGDDKVFRRAPSWRKRFRPREHHGRGGMLSASAETLPAGFRVSTLGTLQPPPAPPKKIMPEAHSHYLYGHMLSAFRD
Protein: Akap2 protein (Q99L95)
Organism: Mus musculus (Mouse)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004342}; Lipid-anchor {ECO:0000256|ARBA:ARBA00004342}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004342}.
Interaction partners:
Sequence:
MEIGVSVAECKSVPGVTSTPHSKDHSSPFYSPSHNGLLADHHESLDNDVAREIQYLDEVLEANCCDSSADGTYNGISSPEPGAAILVSSLGSPAHSVTEAEPTEKASGRQVPPHIELSRSPSDRMAEGERANGHSTDQPQDLLGNSLQAPASPSSSTSSHCSSRDGEFTLTTLKKEAKFELRAFHEDKKPSKLFEEDEREKEQFCVRKVRPSEEMIELEKERRELIRSQAVKKNPGIAAKWWNPPQEKTIEEQLDEEHLESHRKYKERKEKRAQQEQLQLQQQQQQQLQQQQLQQQLQQQQLQQQQLQQQQLQQQLQQQQLSTSQPCTAPAAHKHLDGIEHTKEDVVTEQIDFSAARKQFQLMENSRQTLAKGQSTPRLFSIKPYYKPLGSIHSDKPPTILRPATVGGTLEDGGTQAAKEQKAPCVSESQSAGAGPANAATQGKEGPYSEPSKRGPLSKLWAEDGEFTSARAVLTVVKDEDHGILDQFSRSVNVSLTQEELDSGLDELSVRSQDTTVLETLSNDFSMDNISDSGASNETPSALQENSLADFSLPQTPQTDNPSEGREGVSKSFSDHGFYSPSSTLGDSPSVDDPLEYQAGLLVQNAIQQAIAEQVDKAEAHTSKERSEQQEPEAGSQTPGSEKPQGMFAPPQVSSPVQEKRDILPKNLPAEDRALREKGPSQPPTAAQPSGPVNMEETRPEGGYFSKYSEAAELRSTASLLATQESDVMVGPFKLRSRKQRTLSMIEEEIRAAQEREEELKRQRQVRQSTPSPRAKNAPSLPSRTTCYKTAPGPGGHTG
Protein: Flagellar motor switch Domain/YscQ family (Type III secretion translocase SctQ) (Q9Z7K1)
Organism: Chlamydia pneumoniae (Chlamydophila pneumoniae)
Interaction partners:
- Type 3 secretion system ATPase
- Flagellar Secretion Protein
- Flagellar M-Ring Protein
- Flagellar assembly protein FliH
- Flagellum-specific ATP synthase
- Adenylate cyclase-like protein
- Flagellar assembly protein FliH
- Flagellar protein
- Pathogenicity-related ORF2
- Outer membrane secretion protein Q
Sequence:
MAVAADSSASWLKSRNNFLSSLGKTEEQVAAPEFPKELCQHKIREKFRLEDVQVSIKFRGSITAVEATKEFGVHLLIQPMVVQPWEVENLLFLTSEEDLQELMVAVFDDASLASYFYEKDKLLGFHYYFVAEACKLFEELQWVPSLSAKVGGDAIFTATSLQGSFQVVDISLRLDGKNVRCRLLLPEDTFQSCQKFFSGLHDESDLHNIDQTQQISLSVEVGYSQLTQEEWHQVVPGSFIMLDSCLYDPETEESGALLTVQKHQFFGGRFLTPSSGEFKITSYPNLTHEDPPLPENPQASAAPLPGYSRLVVEVARYSLAVSEFIKLNLGSILSLGNHPAYGVDIILDGAKVGRGEIIALGDVLGIRVLEV
Protein: Proteasome subunit alpha (20S proteasome alpha subunit) (Proteasome core protein PsmA) (Q6M0L9)
Organism: Methanococcus maripaludis (strain DSM 14266 / JCM 13030 / NBRC 101832 / S2 / LL)
Function: Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00289}.
Interaction partners:
- Proteasome subunit beta
- Proteasome-activating nucleotidase
- CDC48 cell division cycle protein family member
- Large ribosomal subunit protein eL40
- Conserved hypothetical archaeal protein
- Uncharacterized protein
- Large ribosomal subunit protein eL15
- Ribosome maturation protein SDO1
- Large ribosomal subunit protein eL43
- Proteasome assembly chaperone family protein
Sequence:
MQQMVPASGYDRAITIFSPEGRLYQVEYAREAVRRGTTAVGIKCKDGVVLAVDRRITSKLIDVSSIEKIFQIDDHIVAATSGLVADARVLIDRARIEAQMNRVSYGEAITVEALAKKICDIKQAYTQHGGARPFGLALLITGIDRHSARLFETDPSGALIEYKATAIGSGRPIAMEVLESKYDENMTVSEGMELALYALSKTTEELKPENIDMAIIKDSGKLVEKISVDEIEKIVKAVYEKVKAEEEEAEKNKGEEDSE
Protein: Peptide methionine sulfoxide reductase MsrA (Protein-methionine-S-oxide reductase) (EC 1.8.4.11) (Peptide-methionine (S)-S-oxide reductase) (Peptide Met(O) reductase) (P9WJM5)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine.
Interaction partners:
- peptide-methionine
- Putative glutaredoxin Rv3198A
- Protein DipZ
- DNA polymerase I
- Probable thioredoxin ThiX
- Possible thioredoxin protein
- Possible membrane-anchored thioredoxin-like protein
- Soluble secreted antigen MPT53
- Soluble secreted antigen MPT53
- Possible oxidoreductase
Sequence:
MTSNQKAILAGGCFWGLQDLIRNQPGVVSTRVGYSGGNIPNATYRNHGTHAEAVEIIFDPTVTDYRTLLEFFFQIHDPTTKDRQGNDRGTSYRSAIFYFDEQQKRIALDTIADVEASGLWPGKVVTEVSPAGDFWEAEPEHQDYLQRYPNGYTCHFVRPGWRLPRRTAESALRASLSPELGT
Protein: Very-long-chain aldehyde decarbonylase GL1-5 (EC 4.1.99.5) (Protein GLOSSY 1-5) (Protein WAX-DEFICIENT ANTHER 1) (Q7XDI3)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Aldehyde decarbonylase involved in the conversion of aldehydes to alkanes. Core component of a very-long-chain alkane synthesis complex (By similarity). Required for the biosynthesis of very-long-chain fatty acids (including polyesters) in cuticles, anther tapetum and pollen exine.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:F4HVY0}; Multi-pass membrane protein {ECO:0000250|UniProtKB:F4HVY0}.
Interaction partners:
- Very-long-chain aldehyde decarbonylase GL1-6
- Very-long-chain aldehyde decarbonylase GL1-3
Sequence:
MATNPGLFTEWPWKKLGSFKYVLLAPWVAHGWYEVATKGWREVDLGYIAILPSLLLRMLHNQAWITISRLQNARGRRQIVRRGIEFDQVDRERNWDDQIILSGILLYLGALYVPGGQHLPLWRTDGAGLIALLHAGPVEFLYYWFHRALHHHFLYTHYHSHHHSSIVTEPITSVIHPFAELVAYELLFSIPLIACALTGTASIIAFEMYLIYIDFMNNMGHCNFELVPSWLFTWFPPLKYLMYTPSFHSLHHTQFRTNYSLFMPFYDYIYNTMDKSSDTLYENSLKNNEEEEAVDVVHLTHLTTLHSIYHMRPGFAEFASRPYVSRWYMRMMWPLSWLSMVLTWTYGSSFTVERNVMKKIRMQSWAIPRYSFHYGLDWEKEAINDLIEKAVCEADKNGAKVVSLGLLNQAHTLNKSGEQYLLKYPKLGARIVDGTSLAAAVVVNSIPQGTDQVILAGNVSKVARAVAQALCKKNIKVTMTNKQDYHLLKPEIPETVADNLSFSKTGTAKVWLIGDGLDSAEQFRAQKGTLFIPYSQFPPKMVRKDSCSYSTTPAMAVPKTLQNVHSCENWLPRRVMSAWRIAGILHALEGWNEHECGDKVLDMDKVWSAAIMHGFCPVAQG
Protein: RNA helicase (EC 3.6.4.13) (F6S8Q4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSHVAVENALGLDQQFAGLDLNSSDNQSGGSTASKGRYIPPHLRNREATKGFYDKDSSGWSSSKDKDAYSSFGSRSDSRGKSSFFSDRGSGSRGRFDDRGRSDYDGIGSRGDRSGFGKFERGGNSRWCDKSDEDDWSKPLPPSERLEQELFSGGNTGINFEKYDDIPVEATGNNCPPHIESFSDVEMGEIIMGNIELTRYTRPTPVQKHAIPIIKEKRDLMACAQTGSGKTAAFLLPILSQIYSDGPGEALRAMKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDFCKYLVLDEADRMLDMGFEPQIRRIVEQDTMPPKGVRHTMMFSATFPKEIQMLARDFLDEYIFLAVGRVGSTSENITQKVVWVEESDKRSFLLDLLNATGKDSLTLVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSPILVATAVAARGLDISNVKHVINFDLPSDIEEYVHRIGRTGRVGNLGLATSFFNERNINITKDLLDLLVEAKQEVPSWLENMAYEHHYKGSSRGRSKSSRFSGGFGARDYRQSSGASSSSFSSSRASSSRSGGGGHGSSRGFGGGGYGGFYNSDGYGGNYNSQGVDWWGN
Protein: Signal transducing adapter molecule 1 (STAM-1) (Prion-like-(Q/N-rich) domain-bearing protein 19) (O01498)
Organism: Caenorhabditis elegans
Function: Binds, sorts and targets the polycystin complex (lov-1 and pkd-2) for lysosomal degradation, acting on early endosomes located at the ciliary base. Functions in the germline together with the ephrin receptor (vab-1) signaling pathway to negatively regulate MAPK activation. May have a role as a positive regulator of meiotic maturation in oocytes, acting independently of vab-1.
Subcellular location: Cell projection, cilium {ECO:0000269|PubMed:17581863}. Endosome {ECO:0000269|PubMed:17581863}. Note=Located to early endosomes at the ciliary base but not cilium proper of male-specific sensory neurons. {ECO:0000269|PubMed:17581863}.
Interaction partners:
- Hepatocyte growth factor-regulated tyrosine kinase substrate
- Tumor susceptibility gene 101 protein
- Multivesicular body subunit 12A
- Vacuolar protein sorting-associated protein 28 homolog
- Vacuolar protein-sorting-associated protein 36
- Charged multivesicular body protein 3
- Charged multivesicular body protein 6
- Vacuolar protein-sorting-associated protein 25
- VPS37 C-terminal domain-containing protein
- Polyubiquitin-A
Sequence:
MKKQKSFPMSAYEDLLGKITAPTITVENWEGILAFCDMINNDFEGSKTGIKSLRKRLNNRDPHVVLLAISVLDSCWANCEERFRKEVSSAQFINELKALCTSSQRQVAEKMRLTVQKWVDTECKTEQSLSLIVTLHKNLVADGYSFVVDDPKSKTKAIDAKFANDPNYVGSAQEEEAIAKAIAASLADAEKQEKAKKSTSTMYPSAKASSPAVQTNSNIPEKNVRALYDFEAAESNELSFVAGDIITITDESNPHWWTGRIGTQQGLFPSSFVTNQLDDLKSKETDSSQKAPEVVASINEAILVRCLQVLHECDPTGERQDPEDLAQLEAASYAQGNLIDAHLASIDRQSNSLAQIDVAIRDVLALYDDAIQKGGFQHQSQGMYQQPMQQYNYQQPPNRAYYPPTGPVQQQQPQQYPPQHYPAPGAQPQYACPPNSVPQPQQQQQQWPAPSSQPQQY
Protein: BBSome complex member BBS2 (Bardet-Biedl syndrome 2 protein) (Q9BXC9)
Organism: Homo sapiens (Human)
Function: The BBSome complex is thought to function as a coat complex required for sorting of specific membrane proteins to the primary cilia. The BBSome complex is required for ciliogenesis but is dispensable for centriolar satellite function. This ciliogenic function is mediated in part by the Rab8 GDP/GTP exchange factor, which localizes to the basal body and contacts the BBSome. Rab8(GTP) enters the primary cilium and promotes extension of the ciliary membrane. Firstly the BBSome associates with the ciliary membrane and binds to RAB3IP/Rabin8, the guanosyl exchange factor (GEF) for Rab8 and then the Rab8-GTP localizes to the cilium and promotes docking and fusion of carrier vesicles to the base of the ciliary membrane. The BBSome complex, together with the LTZL1, controls SMO ciliary trafficking and contributes to the sonic hedgehog (SHH) pathway regulation. Required for proper BBSome complex assembly and its ciliary localization.
Subcellular location: Cell projection, cilium membrane. Cytoplasm. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriolar satellite.
Interaction partners:
- BBSome complex member BBS4
- BBSome complex member BBS5
- BBSome complex member BBS1
- BBSome complex member BBS7
- Tetratricopeptide repeat protein 8
- Protein PTHB1
- BBSome complex assembly protein BBS10
- Leucine zipper transcription factor-like protein 1
- Chaperonin-containing T-complex member BBS12
- Rab-3A-interacting protein
Sequence:
MLLPVFTLKLRHKISPRMVAIGRYDGTHPCLAAATQTGKVFIHNPHTRNQHVSASRVFQSPLESDVSLLSINQAVSCLTAGVLNPELGYDALLVGTQTNLLAYDVYNNSDLFYREVADGANAIVLGTLGDISSPLAIIGGNCALQGFNHEGSDLFWTVTGDNVNSLALCDFDGDGKKELLVGSEDFDIRVFKEDEIVAEMTETEIVTSLCPMYGSRFGYALSNGTVGVYDKTSRYWRIKSKNHAMSIHAFDLNSDGVNELITGWSNGKVDARSDRTGEVIFKDNFSSAIAGVVEGDYRMDGHIQLICCSVDGEIRGYLPGTAEMRGNLMDTSAEQDLIRELSQKKQNLLLELRNYEENAKAELASPLNEADGHRGIIPANTRLHTTLSVSLGNETQTAHTELRISTSNDTIIRAVLIFAEGIFTGESHVVHPSIHNLSSSICIPIVPPKDVPVDLHLKAFVGYRSSTQFHVFESTRQLPRFSMYALTSLDPASEPISYVNFTIAERAQRVVVWLGQNFLLPEDTHIQNAPFQVCFTSLRNGGHLHIKIKLSGEITINTDDIDLAGDIIQSMASFFAIEDLQVEADFPVYFEELRKVLVKVDEYHSVHQKLSADMADHSNLIRSLLVGAEDARLMRDMKTMKSRYMELYDLNRDLLNGYKIRCNNHTELLGNLKAVNQAIQRAGRLRVGKPKNQVITACRDAIRSNNINTLFKIMRVGTASS
Protein: Cox11p (Q59PA0)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004243}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004243}; Intermembrane side {ECO:0000256|ARBA:ARBA00004243}.
Interaction partners:
- Copper metallochaperone
- Protoheme IX farnesyltransferase, mitochondrial
- Cu-binding protein
- SURF1-like protein
- Cytochrome c oxidase subunit 2
- Cox15p
- Replication factor C subunit 5
- Large ribosomal subunit protein uL24
- Cytochrome c oxidase subunit 3
- Cytochrome c oxidase subunit 1
Sequence:
MNRLRIYTPIFRSTIVKPAVFRPYAFIVSRGIHTTGKLFQMQHQQQPSVPDQSSIEKQREWVDRLAREREERQKYRNRTATYYTASLGIFFLALAFSAVPIYRAICQRTGWGGIPITDSTKFTPDKLIPVDTNKRIRIQFTCQSSGILPWKFTPLQREVYVVPGETALAFYRAKNMSKEDIIGMATYSISPDNVAGYFNKIQCFCFEEQRLSAGEEVDMPVFFFIDPDFAKDPAMRNIDDVVLHYSFFKAHYSDGELAAAPIGNMEMKASVVS
Protein: IP01149p (No hitter) (Q9VJP5)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Transcription initiation factor TFIID subunit 12
- Transcription initiation factor TFIID subunit 5
- Transcription initiation factor TFIID subunit 6
- Transcription initiation factor TFIID subunit 11
- Transcription initiation factor TFIID subunit 1
- Transcription initiation factor TFIID subunit 8
- Transcription initiation factor TFIID subunit 2
- Transcription initiation factor TFIID subunit 7
- TATA-box-binding protein
- TBP-associated factor 3
Sequence:
MSIISLEVPIQPYAGQLLIINDLILPDSGSQDASKAKVSIKKNQRASFFDRSSIYKKIMKHLSQGNQADDINISEQEWLLDSFLAALETYMKHVVKKTIELCEHRTSYHLHNDERCVMKNDMRVTMMFLNDLEIADYGSSDDETGFYRKRRAENIDEERKVARLESVNDTALLAISGRKRPGEQLAPESAPSGSKVAKLTGAPIQRACAPRFKHMNIRDVLQFMEEDRRYARSNMLFEAYLKYKS
Protein: Protein unc-112 (Mitogen-inducible mig-2 protein-like) (Uncoordinated protein 112) (Q18685)
Organism: Caenorhabditis elegans
Function: Component of an integrin containing attachment complex, which is required for muscle development and maintenance. Probable regulator of cell-extracellular matrix adhesion. Required during initial muscle assembly to form dense bodies and M-lines.
Subcellular location: Cell membrane {ECO:0000269|PubMed:10893272}; Peripheral membrane protein {ECO:0000269|PubMed:10893272}. Cytoplasm, myofibril, sarcomere, M line {ECO:0000269|PubMed:23283987}. Note=Colocalizes with pat-3/beta-integrin in body wall muscles. Requires unc-52/perlecan and pat-3 to be localized to the muscle cell membrane (PubMed:10893272). Colocalizes with cpna-1 in M line and dense bodies (PubMed:23283987). {ECO:0000269|PubMed:10893272, ECO:0000269|PubMed:23283987}.
Interaction partners:
- Integrin-linked protein kinase homolog pat-4
- Paralyzed arrest at two-fold protein 6
- LIM domain-containing protein unc-97
- Zyxin
- Integrin beta pat-3
- FERM domain-containing protein
- Vinculin
- Paxillin homolog 1
- Alpha-actinin, sarcomeric
- Protein vav
Sequence:
MAHLVEGTSIIDGKWQLPILVTDLNIQRSISVLGNLNVGGLMLELVSECDVERDWSDHALWWPEKRRWLQHTRSTLDQNGITAETQLEFTPMHKEARIQLPDMQMIDARVDFSVNSFKATKKLCRDLGIRYSEELSLKRYIPPEDLRRGTSDADNMNGPLSMRPGEESVGPMTLRKAAPIFASQSNLDMRRRGQSPALSQSGHIFNAHEMGTLPRHGTLPRGVSPSPGAYNDTMRRTPIMPSISFSEGLENEQFDDALIHSPRLAPSRDTPVFRPQNYVEKAAINRGWLDSSRSLMEQGIFEGDIILLRFKFMNFFDLNPKYDPVRINQLYEQAKWSILLDEFDHTEEEATLFAALQLQATLQRDSPEPEENNKDDVDILLDELEQNLDAAALNRRSDLTQVPELADYLKYMKPKKLAAFKGFKRAFFSFRDLYLSYHQSSSDVNSAPLGHFSLKGCEVSQDVSVGQQKYHIKLLLPTAEGMIDFILKCDSEHQYARWMAACRLASRGKSMADSSYQQEVESIKNLLKMQSGNGNENGNSNTASRKAAAVKLPNDFNVDEYISSKYVRRARSKQQIQQRVSDAHGNVRQLTATEAKLQYIRAWQALPEHGIHYFIVRFRNARKAELVAVAVNRLAKLNMDNGESLKTWRFANMKKWHVNWEIRHLKIQFEDEDIEFKPLSADCKVVHEFIGGYIFLSMRSKEHSQNLDEELFHKLTGGWA
Protein: Baculoviral IAP repeat-containing 8 (Q6PIA0)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MTGYEARLITFGTWMYSVNKEQLARAGFYAIGQEDKVQCFHCGGGLANWKPKEDPWEQHAKWYPGCKYLLEEKGHEYINNIHLTRSLEGALVQTTKKTPSLTKRISDTIFPNPMLQEAIRMGFDFKDVKKIMEERIQTSGSNYKTLGVLVADLVSAQKDTTENELNQTSLQREISPEEPLRRLQEEKLCKICMDRHIAVVFIPCGHLVTCKQCAEAVDRCPMCSMVIDFKQRVFMS
Protein: Uncharacterized protein (Q381C2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MQAEVDGEMVSLLKLHDLRHQQELLEKELSAVHPTPETLQMPEPVDANTFQSQTADFHNTRAISPVERLDEIRRRHRREAHRTMQRYFSALNNFRDYQERRMEKLRNVQPFSFEARELRRPRGIHARRMEEDRLKREQEEQRELNRRFKSNPVPPSTYMNKYDLMVEEWRQRRVMVEALAAEKAERIREEKEFMQLCVSGLRNVREVMGARRQRGSESDYSRGHNARDCRQVSEIRDVPVEVALKLWPAIEEHEQIRVERIKQRAVHQMEEVKAEESQRVAAAEQTGRTQPWFGMTPVEFLQLHQRQQQQQVQQQGDRAANIVPVSGPVVTVSSQHTTTAPPPSSAVPSSSPPTGVLVMAPLSKPKVSGGVSESKEDKTPKRRSRSTSAKRNPNLTFKPKIRGGVPNFEALWAEERLALAERKLKRQPTQVEPFKLTVSGKEEVIRGRSLHRKKQQRPGSATRPARRKRSVPKPPEGKEGSSGGTGEAEDKRGLSVPKGTRAHAMRTQAVFERYITAAEAKQYQDKRSEETAALKEAYQRQKRVNARLKEYLKSTQVNTDDVIRKKVTELRRLGREAEREAAEQLNEMLSRVVQIPPIFVEPVHLHSAAKVRAETEKEILRLLKESGVDGGTLSAIIQGCADASDDDNAAGADNAATAAAAAGEASKKSEPDGEARDNDEKDEPSKSGSDGEVDSGEKGSRRQSTEGSSSESESHEGTKEGKDSESKETSEGKSDSDSKGKSGTEKEDSDREHDDKDSEYGTDFESTSSKSAVSV
Protein: Receptor-binding cancer antigen expressed on SiSo cells (Estrogen receptor-binding fragment-associated gene 9 protein) (Q5PQP2)
Organism: Rattus norvegicus (Rat)
Function: May participate in suppression of cell proliferation and induces apoptotic cell death through activation of interleukin-1-beta converting enzyme (ICE)-like proteases.
Subcellular location: Golgi apparatus membrane {ECO:0000250}; Single-pass type III membrane protein {ECO:0000250}. Note=Predominantly located in the Golgi. {ECO:0000250}.
Interaction partners:
- Estrogen receptor
Sequence:
MAITQFRLFKVCTCLATVLSFLKRLICRSGRGRKLSGDQITLPTTVDYSSVPKQTDVEEWTSWDEDAPTSVKIEGGTGNAAAQQNSLEQLEPDYFKDMTPTIRKTQKIVIKKREPLSFGVPDGSTGFSSRLAATQDMPFIHQSSELGDLDTWQENSNAWEEEEDAAWQAEEVLRQQKIADREKRAAEQQRKKMEKEAQRLLKKEQNKMGVKLS
Protein: Protein-lysine myristoyltransferase RtxC (EC 2.3.1.-) (A1YKW8)
Organism: Kingella kingae
Function: Protein-lysine myristoyltransferase that catalyzes myristoylation of the protoxin (RtxA) at two internal lysine residues, thereby converting it to the active toxin.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
Sequence:
MDKFSELGSIAWLWTNSELHQNWPLSLFSTNVIPAIETQQYVLLVRDGMPIAYCSWARLNLETEVKYINDVTSLKLEDWQSGDRYWFIDWIAPFGDSYLLTKHMRKLFSDGLFRAIRVDAGSPNGKISEFYGRNVDAKLAMQSFEQYQKELMNALSQQDNFIISTSK
Protein: STARD3 N-terminal like (C9JKL2)
Organism: Homo sapiens (Human)
Subcellular location: Late endosome membrane {ECO:0000256|ARBA:ARBA00004107}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004107}.
Interaction partners:
Sequence:
MNHLPEDMENALTGSQSSHASLRNIHSINPTQLMARIESYEGREKKGISDVRRTFCLFVTFDLLFVTLLWIIELNVNGGIENTLEKEVMQYDYYSSYFDIFLLAVFRFKVLILAYAVCRLRHWWAIALFSQGAFGYVLPIISFILAWIETWFLDFKVLPQEAEEENRLLIVQDASERAALIPGGLSDGQFYSPPESEAGSEEAEEKQDSEKPLLEL