wanglab/gogpt-training-data huggingface dataset:
Protein: Vacuolar protein sorting-associated protein 29 (Vesicle protein sorting 29) (Q9QZ88)
Organism: Mus musculus (Mouse)
Function: Acts as component of the retromer cargo-selective complex (CSC). The CSC is believed to be the core functional component of retromer or respective retromer complex variants acting to prevent missorting of selected transmembrane cargo proteins into the lysosomal degradation pathway. The recruitment of the CSC to the endosomal membrane involves RAB7A and SNX3. The SNX-BAR retromer mediates retrograde transport of cargo proteins from endosomes to the trans-Golgi network (TGN) and is involved in endosome-to-plasma membrane transport for cargo protein recycling. The SNX3-retromer mediates the retrograde endosome-to-TGN transport of WLS distinct from the SNX-BAR retromer pathway. The SNX27-retromer is believed to be involved in endosome-to-plasma membrane trafficking and recycling of a broad spectrum of cargo proteins. The CSC seems to act as recruitment hub for other proteins, such as the WASH complex and TBC1D5. Required to regulate transcytosis of the polymeric immunoglobulin receptor (pIgR-pIgA) (By similarity). Acts also as component of the retriever complex. The retriever complex is a heterotrimeric complex related to retromer cargo-selective complex (CSC) and essential for retromer-independent retrieval and recycling of numerous cargos such as integrin alpha-5/beta-1 (ITGA5:ITGB1). In the endosomes, retriever complex drives the retrieval and recycling of NxxY-motif-containing cargo proteins by coupling to SNX17, a cargo essential for the homeostatic maintenance of numerous cell surface proteins associated with processes that include cell migration, cell adhesion, nutrient supply and cell signaling. The recruitment of the retriever complex to the endosomal membrane involves CCC and WASH complexes. Involved in GLUT1 endosome-to-plasma membrane trafficking; the function is dependent of association with ANKRD27 (By similarity). Has no activity towards p-nitrophenylphosphate, p-nitrophenylphosphorylcholine or phosphatidylinositlphosphates or a phosphorylated peptide derived from retromer cargo (in vitro).
Subcellular location: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Endosome membrane {ECO:0000269|PubMed:15965486}; Peripheral membrane protein {ECO:0000269|PubMed:15965486}.
Interaction partners:
- Vacuolar protein sorting-associated protein 35
- TBC1 domain family member 5
- Sorting nexin-1
- Sorting nexin-2
- Vacuolar protein sorting-associated protein 26B
- Vacuolar protein sorting-associated protein 26A
- Vacuolar protein sorting-associated protein 26C
- Sorting nexin-5
- Sorting nexin-6
- Sorting nexin-27
Sequence:
MLVLVLGDLHIPHRCNSLPAKFKKLLVPGKIQHILCTGNLCTKESYDYLKTLAGDVHIVRGDFDENLNYPEQKVVTVGQFKIGLIHGHQVIPWGDMASLALLQRQFDVDILISGHTHKFEAFEHENKFYINPGSATGAYNALETNIIPSFVLMDIQASTVVTYVYQLIGDDVKVERIEYKKS
Protein: Potassium channel subfamily K member 16 (2P domain potassium channel Talk-1) (TWIK-related alkaline pH-activated K(+) channel 1) (TALK-1) (Q96T55)
Organism: Homo sapiens (Human)
Function: Outward rectifying potassium channel. Produces rapidly activating and non-inactivating outward rectifier K(+) currents.
Subcellular location: [Isoform a]: Endoplasmic reticulum membrane {ECO:0000269|PubMed:28928238}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:26239056}; Multi-pass membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Isoform b]: Endoplasmic reticulum membrane {ECO:0000269|PubMed:28928238, ECO:0000305|PubMed:38206814}; Multi-pass membrane protein {ECO:0000255}. Mitochondrion inner membrane {ECO:0000305|PubMed:38206814}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Potassium channel subfamily K member 17 channel 4) channel 2)
- Keratin, type II cytoskeletal 2 oral
Sequence:
MPSAGLCSCWGGRVLPLLLAYVCYLLLGATIFQLLERQAEAQSRDQFQLEKLRFLENYTCLDQWAMEQFVQVIMEAWVKGVNPKGNSTNPSNWDFGSSFFFAGTVVTTIGYGNLAPSTEAGQVFCVFYALLGIPLNVIFLNHLGTGLRAHLAAIERWEDRPRRSQVLQVLGLALFLTLGTLVILIFPPMVFSHVEGWSFSEGFYFAFITLSTIGFGDYVVGTDPSKHYISVYRSLAAIWILLGLAWLALILPLGPLLLHRCCQLWLLSLRQGCGAKAAPGRRPRRGSTAARGVQVTPQDFPISKKGLGS
Protein: Hemagglutinin glycoprotein (A0SNV4)
Organism: Measles morbillivirus
Subcellular location: Host cell membrane {ECO:0000256|ARBA:ARBA00004336}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004336}. Virion membrane {ECO:0000256|ARBA:ARBA00004208}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004208}.
Interaction partners:
Sequence:
MSPHRDRINAFYKDNPHPKGSRIVINREHLMIDRPYVLLAVLFVMFLSLIGLLAIAGIRLHRAAIYTAEIHKSLSTNLDVTNSIEHQVKDVLTPLFKIIGDEVGLRTPQRFTDLVKFISDKIKFLNPDREYDFRDLTWCIDPPERIKLDYDQYCADVAAEELMNALVNSTLLEARATNQFLAVSKGNCSGPTTIRGQFSNMSLSLLDLYLSRGYNVSSIVTMTSQGMYGGTYLVGKPNLSSKGSELSQLSMHRVFEVGVIRNPGLGAPVFHMTNYFEQPVSNDFSNCMVALGELRFAALCHREDSVTVPYQGSGKGVSFQLVKLGVWKSPTDMQSWVPLSTDDPVIDRLYLSSHRGVIADNQAKWAVPTTRTDDKLRMETCFQQACKGKNQALCENPEWAPLKDNRIPSYGVLSVNLSLTVELKIKIASGFGPLITHGSGMDLYKTNHNNVYWLTIPPMKNLALGVINTLEWIPRFKVSPNLFTVPIKEAGEDCHAPTYLPAEVDGDVKLSSNLVILPGQDLQYVLATYDTSRVEHAVVYYVYSPGRSFSYFYPFRLPIKGVPIELQVECFTWDQKLWCRHFCVLADSESGGHITHSGMVGMGVSCTVTREDGTNRR
Protein: Cleavage and polyadenylation specificity factor subunit 6 (Q6NVF9)
Organism: Mus musculus (Mouse)
Function: Component of the cleavage factor Im (CFIm) complex that functions as an activator of the pre-mRNA 3'-end cleavage and polyadenylation processing required for the maturation of pre-mRNA into functional mRNAs. CFIm contributes to the recruitment of multiprotein complexes on specific sequences on the pre-mRNA 3'-end, so called cleavage and polyadenylation signals (pA signals). Most pre-mRNAs contain multiple pA signals, resulting in alternative cleavage and polyadenylation (APA) producing mRNAs with variable 3'-end formation. The CFIm complex acts as a key regulator of cleavage and polyadenylation site choice during APA through its binding to 5'-UGUA-3' elements localized in the 3'-untranslated region (UTR) for a huge number of pre-mRNAs. CPSF6 enhances NUDT21/CPSF5 binding to 5'-UGUA-3' elements localized upstream of pA signals and promotes RNA looping, and hence activates directly the mRNA 3'-processing machinery. Plays a role in mRNA export.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q16630}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q16630}. Nucleus speckle {ECO:0000250|UniProtKB:Q16630}. Cytoplasm {ECO:0000250|UniProtKB:Q16630}. Note=Shuttles between the nucleus and the cytoplasm in a transcription- and XPO1/CRM1-independent manner, most probably in complex with the cleavage factor Im complex (CFIm). Colocalizes with PSPC1 in punctate subnuclear structures often located adjacent to nuclear speckles, called paraspeckles, and corresponding to interchromatin granules-associated zones (IGAZs). Distribution in speckles and paraspeckles varies during the cell cycle. Associates at sites of active transcription on nascent perichromatin fibrils (PFs) and perichromatin granules. Nuclear import is mediated via interaction with TNPO3 independently of CPSF6 phosphorylation status. {ECO:0000250|UniProtKB:Q16630}.
Interaction partners:
- Cleavage and polyadenylation specificity factor subunit 5
- Cleavage and polyadenylation specificity factor subunit 7
- Cleavage stimulation factor subunit 2
- Splicing factor U2AF 65 kDa subunit
- Cleavage and polyadenylation specificity factor subunit 1
- Cleavage and polyadenylation specificity factor subunit 3
- Symplekin
- Poly
- Cleavage and polyadenylation specificity factor subunit 2
- Cleavage and polyadenylation specificity factor subunit 4
Sequence:
MADGVDHIDIYADVGEEFNQEAEYGGHDQIDLYDDVISPSANNGDAPEDRDYMDTLPPTVGDDVGKGAAPNVVYTYTGKRIALYIGNLTWWTTDEDLTEAVHSLGVNDILEIKFFENRANGQSKGFALVGVGSEASSKKLMDLLPKRELHGQSPVVTPCNKQFLSQFEMQSRKTTQSGQMSGEGKAGPPGGGSRAAFPQGGRGRGRFPGAVPGGDRFPGPAGPGGPPPPFPAGQTPPRPPLGPPGPPGPPGPPPPGQVLPPPLAGPPNRGDRPPPPVLFPGQPFGQPPLGPLPPGPPPPVPGYGPPPGPPPPQQGPPPPPGPFPPRPPGPLGPPLTLAPPPHLPGPPPGAPPPAPHVNPAFFPPPTNSGMPTSDSRGPPPTDPYGRPPPYDRGDYGPPGREMDTARTPLSEAEFEEIMNRNRAISSSAISRAVSDASAGDYGSAIETLVTAISLIKQSKVSADDRCKVLISSLQDCLHGIESKSYGSGSRRERSRERDHSRSREKSRRHKSRSRDRHDDYYRERSRERERHRDRDRDRDRERDREREYRHR
Protein: FUS protein (Fusion (Involved in t(1216) in malignant liposarcoma), isoform CRA_a) (Fusion, derived from t(12;16) malignant liposarcoma) (Q6IBQ5)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MASNDYTQQATQSYGAYPTQPGQGYSQQSSQPYGQQSYSGYSQSTDTSGYGQSSYSSYGQSQNTGYGTQSTPQGYGSTGGYGSSQSSQSSYGQQSSYPGYGQQPAPSSTSGSYGSSSQSSSYGQPQSGSYSQQPSYGGQQQSYGQQQSYNPPQGYGQQNQYNSSSGGGGGGGGGGNYGQDQSSMSSGGGSGGGYGNQDQSGGGGSGGYGQQDRGGRGRGGSGGGGGGGGGGYNRSSGGYEPRGRGGGRGGRGGMGGSDRGGFNKFGGPRDQGSRHDSEQDNSDNNTIFVQGLGENVTIESVADYFKQIGIIKTNKKTGQPMINLYTDRETGKLKGEATVSFDDPPSAKAAIDWFDGKEFSGNPIKVSFATRRADFNRGGGNGRGGRGRGGPMGRGGYGGGGSGGGGRGGFPSGGGGGGGQQRAGDWKCPNPTCENMNFSWRNECNQCKAPKPDGPGGGPGGSHMGGNYGDDRRGGRGGYDRGGYRGRGGDRGGFRGGRGGGDRGGFGPGKMDSRGEHRQDRRERPY
Protein: Glycine-rich RNA-binding protein blt801 (Low temperature-responsive RNA-binding protein) (Q43472)
Organism: Hordeum vulgare (Barley)
Function: Binds single-stranded DNA and homoribopolymers of guanine, uracil and adenine, but not cytosine. Also binds RNA, with a preference for RNA containing a high proportion of adenine within an open loop structure. Possibly has a role in RNA transcription or processing during stress.
Interaction partners:
Sequence:
MADVEYRCFVGGLRWATDDQSLQNAFSKYGDVIDSKIITDRETGRSRGFGFVTFASDEAMRQAIEAMNGQDLDGRNITVNEAQSRRSDGGGGFGGGGGGYGGQRREGGGGGYGGGGGGYGGGRSGGGGGYGSRDGGGGGYGGGGGGYGGSRGGSGGGNWRE
Protein: COP9 signalosome complex subunit 1 (CSN complex subunit 1) (Constitutive photomorphogenesis protein 11) (Protein FUSCA 6) (P45432)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of the COP9 signalosome complex (CSN), a complex involved in various cellular and developmental processes such as photomorphogenesis and auxin and jasmonate responses. The CSN complex is an essential regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of SCF-type E3 ligase complexes, leading to decrease the Ubl ligase activity of SCF. It is involved in repression of photomorphogenesis in darkness by regulating the activity of COP1-containing Ubl ligase complexes. The complex is also required for degradation of IAA6 by regulating the activity of the Ubl ligase SCF-TIR complex. In the complex, it plays a central role in CSN assembly.
Subcellular location: Cytoplasm. Nucleus.
Interaction partners:
- COP9 signalosome complex subunit 8
- COP9 signalosome complex subunit 5b
- COP9 signalosome complex subunit 4
- COP9 signalosome complex subunit 3
- COP9 signalosome complex subunit 5a
- COP9 signalosome complex subunit 7
- COP9 signalosome complex subunit 6a
- COP9 signalosome complex subunit 2
- COP9 signalosome complex subunit 6b
- NEDD8-like protein RUB3
Sequence:
MERDEEASGPMMEMCTNGGEETSNRRPIISGEPLDIEAYAALYKGRTKIMRLLFIANHCGGNHALQFDALRMAYDEIKKGENTQLFREVVNKIGNRLGEKYGMDLAWCEAVDRRAEQKKVKLENELSSYRTNLIKESIRMGYNDFGDFYYACGMLGDAFKNYIRTRDYCTTTKHIIHMCMNAILVSIEMGQFTHVTSYVNKAEQNPETLEPMVNAKLRCASGLAHLELKKYKLAARKFLDVNPELGNSYNEVIAPQDIATYGGLCALASFDRSELKQKVIDNINFRNFLELVPDVRELINDFYSSRYASCLEYLASLKSNLLLDIHLHDHVDTLYDQIRKKALIQYTLPFVSVDLSRMADAFKTSVSGLEKELEALITDNQIQARIDSHNKILYARHADQRNATFQKVLQMGNEFDRDVRAMLLRANLLKHEYHARSARKL
Protein: At3g56430 (Import inner membrane translocase subunit) (Q9LXZ7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Mitochondrial import receptor subunit TOM9-2
- Mitochondrial import inner membrane translocase subunit TIM22-1
- Mitochondrial import receptor subunit TOM5 homolog
- Cytochrome b-c1 complex subunit 7-1, mitochondrial
- Mitochondrial import inner membrane translocase subunit TIM22-4
- Mitochondrial import inner membrane translocase subunit TIM44-2
- Outer envelope pore protein 16-3, chloroplastic/mitochondrial
- Probable mitochondrial-processing peptidase subunit alpha-2, chloroplastic/mitochondrial
- Cytochrome c1 1, heme protein, mitochondrial
- Mitochondrial import inner membrane translocase subunit TIM50
Sequence:
MVKPSDFKAVHKLIQLHYSRVNLFTTTGWSKLSALSSPALPSNGVSQLQPKSGFHTFSSRPTSKNFGLSQILPSNGVSQLQPKTSFHSFLSRPTSKNVGLSQILPSPKLVPGLQNCGVALVKPRVNMNFVSAFRLFSSSGFRKVDGNFARKVVDKPIKAVSSTFARYRMALGLHVDAFWKKNNLLVFGAGAVFVCIFLWRVMFGIASTFVGLSEGMAKYGFLALSSAIVAFAGLYLRARFTINPDKVYRITMRKLNTAADVLEVMGAPLAGSDLRAYVMSGGGITFKKFKPTIRNKRCFLLFPVQGSERKGLVSVEVKKKKGQYDMKLLAVDIPMASGPDQRLFLIGDEEEYRVGGGLISELRDPVVKAMAATKEFDNLDRIEEEEDAERELQEAERKEREEIELQEAERKEREEFELQEAERKQREEIEKLEK
Protein: Myoblast determination protein 1 (P10085)
Organism: Mus musculus (Mouse)
Function: Acts as a transcriptional activator that promotes transcription of muscle-specific target genes and plays a role in muscle differentiation. Together with MYF5 and MYOG, co-occupies muscle-specific gene promoter core region during myogenesis. Induces fibroblasts to differentiate into myoblasts. Interacts with and is inhibited by the twist protein. This interaction probably involves the basic domains of both proteins.
Subcellular location: Nucleus {ECO:0000269|PubMed:16901893}.
Interaction partners:
- Transcription factor E2-alpha
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 3
- Transcription factor 4
- TATA-box-binding protein
- Histone acetyltransferase p300
- Mothers against decapentaplegic homolog 3
- F-box only protein 32
- Myoregulin
- Histone acetyltransferase KAT2B
- TATA box-binding protein-like 2
Sequence:
MELLSPPLRDIDLTGPDGSLCSFETADDFYDDPCFDSPDLRFFEDLDPRLVHMGALLKPEEHAHFPTAVHPGPGAREDEHVRAPSGHHQAGRCLLWACKACKRKTTNADRRKAATMRERRRLSKVNEAFETLKRCTSSNPNQRLPKVEILRNAIRYIEGLQALLRDQDAAPPGAAAFYAPGPLPPGRGSEHYSGDSDASSPRSNCSDGMMDYSGPPSGPRRQNGYDTAYYSEAARESRPGKSAAVSSLDCLSSIVERISTDSPAAPALLLADAPPESPPGPPEGASLSDTEQGTQTPSPDAAPQCPAGSNPNAIYQVL
Protein: Midline fasciclin (O61457)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MLRLWACLLLLGSIQIQAVPFYGDFMPHLTHPLPAHRNLFAPLPFAPLAPLEPQDPLHAQASQRMASVWNGPAPLAPQLHSSHLLPLFSSGYDTEFVPLEHQQQPQGRQETAATVPAQTPSGVEQKPFNVDTITTDVNSPNPAIFFQQSFPFFGNEFFNSFGGFGFGAAQEPWWKGPNVCTEKEEDETVASETEAEETVDTFGQERDGVTNVVRSPLFGQFQFSVNSCAEKPNKHVCTKIVNQNGKKKTLTLTRQCCYGYGRPRNADFTTPCEKIDIKDVEATASDMGAKQFLESARTAGELADMLGAGSGKKVTLFVPNDAAFMEYRGHHQQENNVEDAKAEASKPSIYKLHAVLGEVQLEDVPNEKLLQTELPDQKIRINSYQLPAALGLEPYRFAVNCVPIEKHDKLSEQALVHTLGGVLKPLTKNLMDIIRERADMSIMRTVLEKTNLSAMLEDDKPVTIFVPTDAAFDKLEPHLRRALKEGRGCASNILKNHLLDLTFCSLATVPGAKTTAYNLLGEPLLLNRTHRAANQTGPTPIYINNLAKIIDADIMGTNGVLHVIDTILPTESALPMTSLMSQKNLTIFQRLLEASGYDDQFDDLDNVTIFAPTDKALQNTEWARMLKEQPELLNHNLDLLEFLNYHVVKPMIKTCDLSEKSLPTVAGSSVRLNLYSTHALFSDVMNRATVNCARLVHFDDESCGSVLHQVDRALAPPKNNMLKLLEANPNYSKFLELVRKANLTQLLSNDSRSLTLLVPKNDIFEELNESGEGSKPADPMALVKTHIVEDVVCCAGIIPTNWPFVRSIESISGQHLRITRDRRPKIENAGVTKCDVVATNGILHEINDIIVPRPQRQQQQRPQLIPPGAGYQPQGDFDVFF
Protein: DNA mismatch repair protein Msh6 (E1BYJ2)
Organism: Gallus gallus (Chicken)
Function: Component of the post-replicative DNA mismatch repair system (MMR). Involved in B cell growth by positively regulating B cell proliferation and controlling replication efficiency. Controls cell cycle to prevent re-replication and defects in DNA damage-induced G2 checkpoint. Doesn't seem to counteract or control the immunoglobulin gene conversion (Ig GC) and to contribute to guanine/uracil mismatch repair.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P52701}.
Interaction partners:
- DNA mismatch repair protein
- Mismatch repair endonuclease PMS2
- Proliferating cell nuclear antigen
- DNA mismatch repair protein MLH1
- Uncharacterized protein.
- DNA mismatch repair protein
- HMG box domain-containing protein.
- MutL homolog 3.
- Fanconi anemia group M protein
- Uracil-DNA glycosylase
Sequence:
MMSASNLSVIHEVLLVLLNHQRINLPYENLEASLSRMLFLSSFVQEVVQVPIPCNVSANRSVSGVYSPGDLVWAKMEGYPWWPCLIYNHPTEGTIVRGKGSSARIHVQFFDVSPTRGWVSIKYLRPYKGSSDREVLKGGMFYSMKPEIKKAMELADDAMSKDKTKRLELAVCSEPSDTEEAEEEEMEQMSGSASGDSDDSNSEEDVKGNKRVPNRGSAIKAKRRRVLDSDSDRDGSDVEFKPDVKEASSEEASSGVDENEATDVETDEESIEESPIKVPSKRKRGNVSKPSKRSSLENEHSEAPKRAAPVSLEAKSKLTLFAAPENFESQANACSGGTNGFAAWEHEKLEWLQEGKKKDAHRRRQNHPDYDPCTLYVPEDYLNKCTPGMRRWWQLKSQNFDAVICYKVGKFYELYHMDAVTGVNELGLIFMKGSWAHSGFPETAFGRFSAILVQKGYKIARVEQTETPEMMEARCKATAHTTKFDKVVRREICRIITKGTQTYSIIDCDPTENHNKYLLCVKEKEDSSGQRVYGVCFVDTSVGKFYVGQFSDDRHCSRFRTLVAHYTPVQVLFEKGNLTVDTQKILKGSLISCIQEGLISGSQFWSASKTLKVLLEEEYFKENQNTESGCVLPSVIKSLTSESDSLGLTPGENSELALSALGGIVFYLKKCLIDQELLSLANFEKYIPVDADNAKTVSSSNFFARTDRRMVLDGVTLMNLEVLQNGTNGTTEGTLLERIDSCCTPFGKRLLKQWLCAPLCNPTSINDRLDAVEDLLAVPAKLTEITEHLKKLPDLERLLSKIHSIGSPLKSQNHPDSRAIFYEEIKYSKKKIADFLSALEGFKVMNEIVDAMEEVASDFKSQVLKQLVTRKAKHPDGRFPDLSAELKRWDTAFDHNQARKTGVITPKAGFDPDYDKALQDIKTVEEDFRTYLDKQRKLLGLKSVLYWGTGKNRYQMEIPETATSRNLPEEYELKSTRKGYKRYWTKEIEKMLAELINAEERRDAALKDCMRRLFYNFDKNSQDWQTAVQCIAVLDVLMSLANYSQDGDGPLCRPVILLPVDSAPPFLELKNARHPCITKTFFGDDFIPNDIVIGSKDEDGGSEASCVLVTGPNMGGKSTLMRQAGLLVIMAQLGCYVPAEVCRLTPIDRVFTRLGASDRIMSGESTFFVELSETSSILQHATEHSLVLVDELGRGTATFDGTAIASAVVRELAENIKCRTLFSTHYHSLVEDYSGSAAVRLGHMACMVENESEDPSQETITFLYKFIEGACPKSYGFNAARLADIPEEIIQKGHRKAKEFEKKTMSLRIFRFLCRVVDGVTHDANAVGKLTTMLSHL
Protein: Ankyrin repeat domain-containing protein 13A (Protein KE03) (Q8IZ07)
Organism: Homo sapiens (Human)
Function: Ubiquitin-binding protein that specifically recognizes and binds 'Lys-63'-linked ubiquitin. Does not bind 'Lys-48'-linked ubiquitin. Positively regulates the internalization of ligand-activated EGFR by binding to the Ub moiety of ubiquitinated EGFR at the cell membrane.
Subcellular location: Cell membrane {ECO:0000269|PubMed:22298428}. Late endosome {ECO:0000269|PubMed:22298428}. Note=Interaction with EGFR may enhance association with the cell membrane.
Interaction partners:
Sequence:
MSSACDAGDHYPLHLLVWKNDYRQLEKELQGQNVEAVDPRGRTLLHLAVSLGHLESARVLLRHKADVTKENRQGWTVLHEAVSTGDPEMVYTVLQHRDYHNTSMALEGVPELLQKILEAPDFYVQMKWEFTSWVPLVSRICPNDVCRIWKSGAKLRVDITLLGFENMSWIRGRRSFIFKGEDNWAELMEVNHDDKVVTTERFDLSQEMERLTLDLMKPKSREVERRLTSPVINTSLDTKNIAFERTKSGFWGWRTDKAEVVNGYEAKVYTVNNVNVITKIRTEHLTEEEKKRYKADRNPLESLLGTVEHQFGAQGDLTTECATANNPTAITPDEYFNEEFDLKDRDIGRPKELTIRTQKFKAMLWMCEEFPLSLVEQVIPIIDLMARTSAHFARLRDFIKLEFPPGFPVKIEIPLFHVLNARITFGNVNGCSTAEESVSQNVEGTQADSASHITNFEVDQSVFEIPESYYVQDNGRNVHLQDEDYEIMQFAIQQSLLESSRSQELSGPASNGGISQTNTYDAQYERAIQESLLTSTEGLCPSALSETSRFDNDLQLAMELSAKELEEWELRLQEEEAELQQVLQLSLTDK
Protein: Putative mitochondrial ATP-dependent helicase irc3 (EC 3.6.4.-) (Q1MTR1)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Mitochondrion {ECO:0000250}.
Interaction partners:
- Dihydrolipoyl dehydrogenase, mitochondrial
- Probable citrate synthase, mitochondrial
Sequence:
MLLNACCKKNLWPRNGSTIFRRFALKLRPYQEECLSACLNAFDEGKRRIAVSLATGSGKTALFPHFIKYAPTLRPNSEQCLILVHRKELALQALKHCRESLPNKSIEIDMGNQCASGLADVTVASVFSLKNERLLKYNPLNFKLLIFDEVHHMASPSYLRILEHFGAESEKSKVNVIGLTATLFRADGKGLACGLDEIVYHRHFVDMIKDNWLVEPKVINIKWSTDLVLADSSSFLDQEKLKKEAQSEKAIFEIPRAWLEHASNRSSTLVFCINVEHSLKVCNAFRKLGIDARALFGETNDSERETLIQDFRKKKFPVLVNCMVLTEGTDIPNIDCLMIARPTSSPNLLTQMIGRGLRLHEGKRDCLILDFCDSLRRVSLHVDPTLAGLSPDEVENFYNKSKNSLANPDYDPKIYGLQSVLWYSKLRKLIEMMDNIKNKDRSIFNLSTNAWVAVGMGRYVLSFLQKVLIIDTNFEDGTHKISEYTKEKLGTRVYNRKRIVSDRIPSLKFAIRAAETYISNLKTPRSLISRKAVWRMRPASVRQINFLKKSNLKLDEKLLTAGVAADMITKVIYGGKGRQVRTDKLQSYLKHDANLKRITTLKELKG
Protein: B4 protein (O16865)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MQRTNIELERQRHLANWLMNSRPHMPGGPAAATTTSAAAATTPAASATKGATTTTTTTTNPGSTVGGAGAGTVGGNGVATAAAAGAPSNSVAAAAAAACNGGAAVGAHHGHHSAAGARKPKLRRFNSHDTSSNMFSVADFENARLARRNEIELNQRRARRVRGSANNSTYGLGSGSGLLGGAHSGYCDALNGSGDYSTGDSKASKGSSEGALTAIEFLERNSLPRVVRILHASKSSNETLQSSSSHGSSTAASSSSSTGANPFGSGGSGGGNISSGNIDTGTHSSSSGGSATGNGTGSGPGLSSGSGSGSGSGHQNNNGRHSSNGGTPPGHDELFLLYRLVRQRNIYHGHNAKTQASQRKKTLLIPQEFPGYFSMLSEKGLPTATQYGSLIQLVRERVYKFVSVDNMPAFTESSPNSTSSPTHEGCLPINKGRPQYVKTTARGGQVFRLLAVFEDGKQDQVNMSQHGNGNATRSHGSGYMGREKEKNRYAQLLNENRQVLYVPLSTKGKFYEIEPGIPQLLQKLGDAQRKLNPECVHRLSALVTAAKQLPLTLRYISGPGGPDIPEQLCISQVSKEDVVVGCSIEDVDTQTPLQLRKFYPSRDIQLVKSYLGFDSEQRMLANTNVQNMLKFCQFNCDPFLKLVEIELIQRSERSGSKNREGLRILKPLHFPKILRREKSSMAAAHEKEDSIIFLSKSDLENLEAKEAAASAAAHSESSLNRISERMRVFQSTKKKWFGKHHPQQQQPQIEKHQSDLDLDEQAKRMSMERYTDMSKLLQERFGSNPEQPEQDAISLNSTAASDTETTMLTTMEPRSLDTMMQKSMSLQDIELLNGQCKQRPDLLASHNHNDAISEAGTELEDVENQTPPPQSFITEKLYNEFHVKTRQYSKSSSSLHQLPLFSLPQKLQLHEAEKEKRHLMLLKAQQQALTKEPVTGRRAAGGVSLLGGGLNQLAISPASLVEDDLPYSSVRDSLVISGGDCLRSESASRPVPAVDYTKENIYAEICPSHTVDTFSGATQLTHVPDDDGDYASLKYSVNGPQSVSRIEVNGATAAVKSSAISYHTVYLGEEPLGERHAAHITTVELAGEDNIYNTLK
Protein: RNA-binding protein FUS (75 kDa DNA-pairing protein) (Oncogene FUS) (Oncogene TLS) (POMp75) (Translocated in liposarcoma protein) (P35637)
Organism: Homo sapiens (Human)
Function: DNA/RNA-binding protein that plays a role in various cellular processes such as transcription regulation, RNA splicing, RNA transport, DNA repair and damage response. Binds to nascent pre-mRNAs and acts as a molecular mediator between RNA polymerase II and U1 small nuclear ribonucleoprotein thereby coupling transcription and splicing. Binds also its own pre-mRNA and autoregulates its expression; this autoregulation mechanism is mediated by non-sense-mediated decay. Plays a role in DNA repair mechanisms by promoting D-loop formation and homologous recombination during DNA double-strand break repair. In neuronal cells, plays crucial roles in dendritic spine formation and stability, RNA transport, mRNA stability and synaptic homeostasis (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:19251627, ECO:0000269|PubMed:19251628, ECO:0000269|PubMed:24204307, ECO:0000269|PubMed:25453086, ECO:0000269|PubMed:30354839}. Note=Displays a punctate pattern inside the nucleus and is excluded from nucleoli. {ECO:0000269|PubMed:25453086}.
Interaction partners:
- TAR DNA-binding protein 43
- Transportin-1
- Superoxide dismutase
- Ribonuclease 3
- Heterogeneous nuclear ribonucleoproteins A2/B1
- TAR DNA binding protein
- Splicing factor, proline- and glutamine-rich
- Serine/arginine-rich splicing factor 10
- Interleukin enhancer-binding factor 3
- Heterogeneous nuclear ribonucleoproteins C1/C2
Sequence:
MASNDYTQQATQSYGAYPTQPGQGYSQQSSQPYGQQSYSGYSQSTDTSGYGQSSYSSYGQSQNTGYGTQSTPQGYGSTGGYGSSQSSQSSYGQQSSYPGYGQQPAPSSTSGSYGSSSQSSSYGQPQSGSYSQQPSYGGQQQSYGQQQSYNPPQGYGQQNQYNSSSGGGGGGGGGGNYGQDQSSMSSGGGSGGGYGNQDQSGGGGSGGYGQQDRGGRGRGGSGGGGGGGGGGYNRSSGGYEPRGRGGGRGGRGGMGGSDRGGFNKFGGPRDQGSRHDSEQDNSDNNTIFVQGLGENVTIESVADYFKQIGIIKTNKKTGQPMINLYTDRETGKLKGEATVSFDDPPSAKAAIDWFDGKEFSGNPIKVSFATRRADFNRGGGNGRGGRGRGGPMGRGGYGGGGSGGGGRGGFPSGGGGGGGQQRAGDWKCPNPTCENMNFSWRNECNQCKAPKPDGPGGGPGGSHMGGNYGDDRRGGRGGYDRGGYRGRGGDRGGFRGGRGGGDRGGFGPGKMDSRGEHRQDRRERPY