wanglab/gogpt-training-data huggingface dataset:
Protein: Cuticlin-6 (Cuticulin 6) (Q21540)
Organism: Caenorhabditis elegans
Function: Plays a role in alae formation in dauer larvae probably by regulating cuticle assembly.
Subcellular location: Cell membrane {ECO:0000255}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MRPIPYDISLSITSFLSLILICSANPIDNGLVDSELIHECVTHKAVEVILLLDASGSIGDDTFKKQLSFAMHLASRLNISEDGSHMALIQYAETPKLEFSLGQFNHPTQLEWAIQRIEYQSGATNTGQALRLTLEKGLQGARPGIPKVAIVITDGQSQDDVSEPSQLLRDADVMVYAIGVTNLVNVHQLHQMTGNPVRVFTVESFEQLDRALADSLTWSMCKTEFRPGTPEIICGPDRIGVKASTKQPFEGNVFVMDHYHDEECRAGPEKFPDSRSIGLTVPFSACNVHRYRSLNPKGIFVEVSIVFMFHSLFMTKTDQTVKVQCFYMEADKHVTVPLSVSMITTVFREQIYQMPQCAYTLRKGAPDGPIVRFATLGESVYHRWECIEVEGADKDTFGMLVHSCYVDNGYGDRVDILDSNGCGLDAVLLSTPDYDTSLRLATKPYHVFKYADRPVLQFQCQITLCLKYDGGCEGITPPQNCKKLPGEDGHHHHHHPEKRRKLVRRLADGVGTIDVFTDSVTVLEQEPACQQPLPYPLINTNLWIMGIITLTNIFVFILTVWFTFRKRRCKPA
Protein: Protein N-terminal asparagine amidohydrolase (EC 3.5.1.121) (Protein NH2-terminal asparagine amidohydrolase) (PNAA) (Protein NH2-terminal asparagine deamidase) (PNAD) (Protein N-terminal Asn amidase) (Protein N-terminal asparagine amidase) (Protein NTN-amidase) (Q96AB6)
Organism: Homo sapiens (Human)
Function: N-terminal asparagine deamidase that mediates deamidation of N-terminal asparagine residues to aspartate. Required for the ubiquitin-dependent turnover of intracellular proteins that initiate with Met-Asn. These proteins are acetylated on the retained initiator methionine and can subsequently be modified by the removal of N-acetyl methionine by acylaminoacid hydrolase (AAH). Conversion of the resulting N-terminal asparagine to aspartate by NTAN1/PNAD renders the protein susceptible to arginylation, polyubiquitination and degradation as specified by the N-end rule. This enzyme does not act on substrates with internal or C-terminal asparagines and does not act on glutamine residues in any position, nor on acetylated N-terminal peptidyl Asn.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q28955}.
Interaction partners:
- L-selectin
- Carbohydrate sulfotransferase 4
- Carbohydrate sulfotransferase 2
- Mucosal addressin cell adhesion molecule 1
- C-C chemokine receptor type 7
- Protein N-terminal glutamine amidohydrolase
- E3 ubiquitin-protein ligase UBR2
- Pyridoxal-dependent decarboxylase domain-containing protein 1
- Arginyl-tRNA--protein transferase 1
- C-C motif chemokine 21
Sequence:
MPLLVEGRRVRLPQSAGDLVRAHPPLEERARLLRGQSVQQVGPQGLLYVQQRELAVTSPKDGSISILGSDDATTCHIVVLRHTGNGATCLTHCDGTDTKAEVPLIMNSIKSFSDHAQCGRLEVHLVGGFSDDRQLSQKLTHQLLSEFDRQEDDIHLVTLCVTELNDREENENHFPVIYGIAVNIKTAEIYRASFQDRGPEEQLRAARTLAGGPMISIYDAETEQLRIGPYSWTPFPHVDFWLHQDDKQILENLSTSPLAEPPHFVEHIRSTLMFLKKHPSPAHTLFSGNKALLYKKNEDGLWEKISSPGS
Protein: Protein PIN-LIKES 6 (Auxin efflux carrier-like protein 6) (Q9LZN2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in cellular auxin homeostasis by regulating auxin metabolism. Regulates intracellular auxin accumulation at the endoplasmic reticulum and thus auxin availability for nuclear auxin signaling.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:22504182}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Auxin efflux carrier component 5
Sequence:
MIARILAALADSMEMPVAAGGGSVLGTIKIAVMPIAKVFTMCFLGLLMASKYVNILPPSGRKLLNGLVFSLLLPCLIFSQLGQAVTLQKMLQWWFIPVNVVLGTISGSIIGFIVASIVRPPYPYFKFTIIQIGVGNIGNVPLVLLAALCRDTSNPFGDSEKCSIDGTAYISFGQWVGAIILYTYVYQMFAPPPEGFDAEEENLALKTLPVDAAPEQVPLLTQNFPKDFSPTQDLLPVQSTEPRGRGVSRKGKIAQIFVFLYEKLKLKQIVQPAIVASILAMILGAIPFTKKLIFTNGAPLFFFTDSCMILGDAMIPCILLALGGNLINGPGSSKLGFKTTAAIIIGRLVLVPPVGLGIVTVADKLGFLPADDKMFRFVLLLQHTMPTSVLSGAVANLRGCGRESAAVLFWVHIFAIFSMAGWMVLYINILF
Protein: Leukocyte immunoglobulin-like receptor subfamily B member 2 (LIR-2) (Leukocyte immunoglobulin-like receptor 2) (CD85 antigen-like family member D) (Immunoglobulin-like transcript 4) (ILT-4) (Monocyte/macrophage immunoglobulin-like receptor 10) (MIR-10) (CD antigen CD85d) (Q8N423)
Organism: Homo sapiens (Human)
Function: Receptor for class I MHC antigens. Recognizes a broad spectrum of HLA-A, HLA-B, HLA-C, HLA-G and HLA-F alleles. Involved in the down-regulation of the immune response and the development of tolerance. Recognizes HLA-G in complex with B2M/beta-2 microglobulin and a nonamer self-peptide (peptide-bound HLA-G-B2M) triggering differentiation of type 1 regulatory T cells and myeloid-derived suppressor cells, both of which actively maintain maternal-fetal tolerance. Competes with CD8A for binding to class I MHC antigens. Inhibits FCGR1A-mediated phosphorylation of cellular proteins and mobilization of intracellular calcium ions.
Subcellular location: Cell membrane {ECO:0000269|PubMed:20448110}; Single-pass type I membrane protein.
Interaction partners:
- HLA class I histocompatibility antigen, alpha chain G
- HLA class I histocompatibility antigen, alpha chain F
- Beta-2-microglobulin
- HLA class I histocompatibility antigen, B alpha chain
- HLA class I histocompatibility antigen, A alpha chain
- Angiopoietin-related protein 2
- Tyrosine-protein phosphatase non-receptor type 6
- HLA class I histocompatibility antigen, C alpha chain
- Tyrosine-protein kinase SYK
- CMRF35-like molecule 6
Sequence:
MTPIVTVLICLGLSLGPRTRVQTGTIPKPTLWAEPDSVITQGSPVTLSCQGSLEAQEYRLYREKKSASWITRIRPELVKNGQFHIPSITWEHTGRYGCQYYSRARWSELSDPLVLVMTGAYPKPTLSAQPSPVVTSGGRVTLQCESQVAFGGFILCKEGEDEHPQCLNSQPHARGSSRAIFSVGPVSPNRRWSHRCYGYDLNSPYVWSSPSDLLELLVPGVSKKPSLSVQPGPVMAPGESLTLQCVSDVGYDRFVLYKEGERDLRQLPGRQPQAGLSQANFTLGPVSRSYGGQYRCYGAHNLSSECSAPSDPLDILITGQIRGTPFISVQPGPTVASGENVTLLCQSWRQFHTFLLTKAGAADAPLRLRSIHEYPKYQAEFPMSPVTSAHAGTYRCYGSLNSDPYLLSHPSEPLELVVSGPSMGSSPPPTGPISTPGPEDQPLTPTGSDPQSGLGRHLGVVIGILVAVVLLLLLLLLLFLILRHRRQGKHWTSTQRKADFQHPAGAVGPEPTDRGLQWRSSPAADAQEENLYAAVKDTQPEDGVEMDTRAAASEAPQDVTYAQLHSLTLRRKATEPPPSQEREPPAEPSIYATLAIH
Protein: Uncharacterized protein YhhA (ORFQ) (P0ADX7)
Organism: Escherichia coli (strain K12)
Interaction partners:
- Uncharacterized protein YhgE
Sequence:
MKRLLILTALLPFVGFAQPINTLNNPNQPGYQIPSQQRMQTQMQTQQIQQKGMLNQQLKTQTQLQQQHLENQINNNSQRVLQSQPGERNPARQQMLPNTNGGMLNSNRNPDSSLNQQHMLPERRNGDMLNQPSTPQPDIPLKTIGP
Protein: Interferon-induced protein with tetratricopeptide repeats (Interferon-induced protein with tetratricopeptide repeats 10 isoform X1) (E7FBH4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MTSDVSSMEADRALRTKLHQLECHFTWALIKDDIDINDLLNRLEEQINLDLEKKERLARTYSALAYVQYLLGFHEKAHQSLMTSKKLHIESHGDEFYRTLIVTYGNLAWLNYHMKNYTECESYLNSLQRINETSPAEFSSIPEVLGEKGWTFLKFSRKYYDGAKECFRKAVELEPEEPEWHTGYAIALYRTEFESTVLEDSATVKQLRLAIEMNPDDDVLKVLLSLRLIVYKRYGEAESWVEKALEKSPDHPHVMRYVGKFFRNKGCVDRSIDLLKRALERSPNSSFIHHQLALCYKYKKIQVLQEQSHHARGSRVQQLRDQCIFHLEKATSLTTSFISAMSDLALQYGENGDIPRAEELFQVTFKIAKEKNDGLHVVNYYYAEYQLYCHRCEPLAVQHYMECLKMCPKSVEGRISSTRMKKTAEKWIDRKSQEGKAYGMLAFLHKVKGEIAQAIECYEKALSYEDNNEFLRNLRELRLSLL
Protein: Zinc finger protein ZAT7 (Q42453)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable transcription factor involved in oxidative stress response.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Probable WRKY transcription factor 70
- Probable WRKY transcription factor 25
- Protein HASTY 1
- Metal tolerance protein 1
- C2H2 and C2HC zinc fingers superfamily protein
- Cysteine proteinase inhibitor 2
- C2H2 and C2HC zinc fingers superfamily protein
- C2H2-type zinc finger protein
- L-ascorbate peroxidase 1, cytosolic
- C2H2-type zinc finger family protein
Sequence:
MVARSEEIVIVEEDTTAKCLMLLSRVGECGGGCGGDERVFRCKTCLKEFSSFQALGGHRASHKKLINSDNPSLLGSLSNKKTKTSHPCPICGVKFPMGQALGGHMRRHRNEKVSGSLVTRSFLPETTTVTALKKFSSGKRVACLDLDLDSMESLVNWKLELGRTISWS
Protein: Breast carcinoma-amplified sequence 3 homolog (Protein rudhira) (DRudh) (Q8SY41)
Organism: Drosophila melanogaster (Fruit fly)
Function: Regulates macropinocytosis in pericardial cells.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:18060846}.
Interaction partners:
- PHAF1 protein CG7083
- Autophagy-related 18b, isoform A
- Autophagy-related 18a, isoform E
Sequence:
MSADSPRRHPSGVVGSGIGLGSGSGTGLGSGSTGGSKSGAAVPAIVPPQTVSDRSILDSAIGFINDVTLANQPVQDPKDTITWARFETCADVSDPRFGDDWELEGNAAPPLLLILGYGLGVQVWAIPANGEAVEVLSWRHGVVTALRVLPTPATAAALDENGRADEPVDSFAEKRPLVAFVDGGSAAASGLLAGSSGLGLGGGGGGVTTVGGSVGGVSGIGVSASAQFSAVNFMSLKTGVQVKTIKFKNAVLDIQANRSAVVITFHERIAVFDARTLEDRLTITTCYPSPGINPNPIALGPRWLAYAEHKLLHSKRSGGGCDGEGVPSYTATVLNAAKSLSKGLREFGEQVAAGLTGTTAGSGASSKSSSFDSASGGPDAKQSGVVTIIDVKHPVKDYSPTSGTPLSSTAGSQGGGDPIVAHFVAHSEALVAMEFDSSGMLLLTADRRGHDFHVFRVQPHPVGPSLAAVHHLYVLHRGDTSAKVQHIAFSLDSRWAAVSTLRGTTHVFPITPYGGAMGVRTHTSLHVVNKLSRFHRSAGLGADGRSSSPISHSESTTFVQSLQPYHNPTLPPYPRPSVVQPLAQLRQPFTLGSPPGSAGLGGGVGGGGVMGSGVSAGGHGVGVGVGSNSQRQRQRLSSLSDDSGKPLSVCSIFAKSRSWLLEPPMATREQPHRVQRKAVDSLFVMAGHGALIQYDLDTKLASHVAKEKICDDTPIELEVEARAQWNLGRRKDGSQEIAPPLGLDNWLIKDRHASLLLDSANQFDDPDERTESWLAQVEIITHAGPHRRLWMGPQFVFKNYNTPSGSNLNHVDAEAVEIGVSKTTTTTLPSTAASSALGLGTIIGKDRSSPLNMPLSAATSVGGAGIGSSAVTGRSGAGVPVLIESGSYSSIEQSPKLMDRFRHGHLDSDYGHGDTRLKEDLADAMRESPSTAAARRETTGNYFTTDQLDGLALNNNNNINNNIIPTKDNASPNPNTNTNPNAIPSSNKVQKAEVTDAVDYPIRHSYGDHGELSTVVNIEVFDDQLSMSSISTNSRLSLEGPPSQSSPPLSLTNGLMDTNLMHFSESVTGTGVAQAQVHGRGANRFEVDDDDEEEEEEEEELDEEAEPDDDEREDRPLGRRNL
Protein: Protein LAZ1 (Lazarus1) (F4JTN2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Required for programmed cell death (PCD) associated with hypersensitive response (HR). Involved both in the induction of EDS1/PAD4 mediated HR and in accelerated cell death in the acd11 mutant. Not required for HR induction elicited through pathways exclusively dependent on CC-NB-LRR resistance proteins.
Subcellular location: Endomembrane system {ECO:0000269|PubMed:20830211}; Multi-pass membrane protein {ECO:0000269|PubMed:20830211}. Cell membrane {ECO:0000269|PubMed:20830211}; Multi-pass membrane protein {ECO:0000269|PubMed:20830211}. Cytoplasm, cytosol {ECO:0000269|PubMed:20830211}.
Interaction partners:
- Accelerated cell death 11
- Probable L-type lectin-domain containing receptor kinase S.7
- Protein BONZAI 3
Sequence:
MDILKSYHLLAAAYSAPAWASFMAGAFLVLTLSLSLFLVFDHLSTYKNPEEQKFLIGVILMVPCYSIESFASLVKPSISVDCGILRDCYESFAMYCFGRYLVACIGGEERTIEFMERQGRKSFKTPLLDHKDEKGIIKHPFPMNLFLKPWRLSPWFYQVVKFGIVQYMIIKSLTALTALILEAFGVYCEGEFKWGCGYPYLAVVLNFSQSWALYCLVQFYGATKDELAHIQPLAKFLTFKSIVFLTWWQGVAIALLSSLGLFKSSIAQSLQLKTSVQDFIICIEMGIASVVHLYVFPAKPYGLMGDRFTGSVSVLGDYASVDCPIDPDEIRDSERPTKVRLPHPDVDIRSGMTIKESMRDVFVGGGEYIVKDVRFTVTQAVEPMEKSITKFNEKLHKISQNIKKHDKEKRRVKDDSCMSSSPSRRVIRGIDDPLLNGSFSDSGVTRTKKHRRKSGYTSAESGGESSSDQAYGGFEVRGRRWITKD
Protein: Mitochondrial thiamine pyrophosphate carrier 1 (A0A1D8PPR4)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MSPAAQSSSDKKQSGIARVLGSATAGIAEIGVFHPVDTISKRLMSNHTKVTSLHELNKVIFRDQASQALGKRLFSLFPGLGYAACYKILQRVYKYGGQPFANEFLTKNFKDTYDAAFGPKTGKALMSATAGSLIGIGEVVLLPLDVLKIKRQTNPESFRGRGFLKIIQDEGLGLYRGWGWTMARNAPGSFALFGGNSFAKEYIFGLKDYSQATWSQNFITSIFGASASLIVSAPLDVIKTRIQNRNFENPESGFTILKNMFKNEGITAFFKGLTPKLLTTGPKLVFSFALAQSLIPAFDKLLSK
Protein: Chaperone protein DNAJ, putative (Q388L6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Uncharacterized protein
- Ubiquitin-conjugating enzyme E2, putative
Sequence:
MWRSQCCLFVGGRTCRRLLTPTSSRRMAAGAMGAAPLFVQLRLASEVKNPYTVLGVKQGASKEDIKKAYRVLARKHHPDAPGGSHEKFQEIQMAYEQVKSGIWIPKDSNGGTDGAGGTTNANRYSNFRFTTRQHKSRISYDEFYEEMHTGKVRKDPFGDDDGTEEATSKDPRRRAFAGNEEFFQAWFRVILMWSALFVTLRIVLFMLFPPRHEAVRRAPMPKEPRKPPPPKPLMNNSLVA
Protein: Transmembrane protein 229B (Q8BFQ2)
Organism: Mus musculus (Mouse)
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Transmembrane protein 131-like
Sequence:
MASAEPLTALSRWYLYAIHGYFCEVMFTAAWEFVVNFNWKFPGVTSVWALFIYGTSILIVERMYLRLRGRCPLLVRCVIYTLWTYLWEFTTGFILRQFNACPWDYSQFDFDFMGLITLEYAVPWFCGALIMEQFIIRNTLRLRFDKDAEPGEPASPPALANGHVKTD
Protein: Dicer-related helicase (RNA helicase) (G5EDI8)
Organism: Caenorhabditis elegans
Interaction partners:
- Piwi domain-containing protein
- DRBM domain-containing protein
- Endoribonuclease dcr-1
- RNA-directed RNA polymerase
- DNA topoisomerase 3
- ATP-dependent helicase wrn-1
- RecQ-like DNA helicase blm-1
- Tudor domain-containing protein
- RNA-directed RNA polymerase
- Structural maintenance of chromosomes protein 5
Sequence:
MRKKQCSSILSLYDKEIILCLEPIYRDPEKGDGFSELLPLGRIDELKIQSENAQEFSKQLYHDLKNSILSNADDERLYKDIMTYLQTYLPKCTVHKLLNCSNREVKLSDFHYILDHFEGFLRFIEPKVVLAYLDSYPQYIDAVAVLRKEIERNEEDNQDSDFIKKLILRTVPLLGEQAVYDIMYTISEKSSNNLDVEAKQFIAKVLRLKNDGFLRFYQIINASRRQLNGRIYICPVHESATEMMVYLGTAALNTNRYRMINIRVDNIVQENSTPRLVIESVRQRIHRQRQLCLRNYQEELCQVALQGKNTIVTAPTGSGKTVIAANIIKEHFESRSSEGKRFKALFMTPNSMILNQQAASISSYLDHVYHTQIIQGSDNVPTRNVIQSKDLIVATPQMIVNLCNEHRNSLDDESRLDQFFLSTFTIIFFDECHNTVKNSPYSNIMREYHYLKNMGNMPEGHSLPQIIGLTASLGTGDKNDCLQVRNYIAGLCASMDVKDLSIVKDNLEELRGYSPIVPDKVLLCERSTDGPIGMFTNRLTLMMQEVEGLIRTALRNEHIGIEQRRQIETTERDFRPDSSFLDPPADKEHAGYQNWVCNQMNLVSGTSFRETGTRTIINEALDVLKECFCTLSYNINFHPEVALNYLKDEMEYRTPNFTVNMIRIWERYHNQLVGTGSAENPMISKTVQYIVEQNLQRADSRTIIFVRTRYEATILNKVLNSNEELLMLGIKSEWMSGLNKSTASSADISASKQKQMEKLKMFADGEIRILVSTSVAEEGLDVPECSLVIKYNYATNEIAHVQRRGRGRALNSECVLITNSIALRDQESNNRDKESLMSETISLIQNSPAEFRKCVDEESNKIWPRILREDTDKAQKIEEQINRNIVYKIICKKCEAILCTSKDIRSRNTQYLVCDPGFWSLVRKTRLTDEQQALIKYNATGSINCRRENCGLKLGQLIEVNTVDLPCLSALSIVLLVEGTDKRIIVKKWKNILDKYFTPTEIRQLDVQTMRDADQARTPMVFEHHANGEVVNLIREA
Protein: Protein adenylyltransferase SelO, mitochondrial (EC 2.7.7.-) (Selenoprotein O) (SelO) (O13890)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalyzes the transfer of adenosine 5'-monophosphate (AMP) to Tyr residues of target mitochondrial proteins (AMPylation). Involved in redox homeostasis by regulating the cellular response to oxidative stress. Regulates protein S-glutathionylation levels possibly by AMPylation of deglutathionylation enzymes such as glutaredoxins.
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:Q08968}.
Interaction partners:
- PAN2-PAN3 deadenylation complex subunit pan3
Sequence:
MSKKLKDLPVSSTFTSNLPPDPLVPTVQAMKKADDRILHVPRFVEGGGLFTYLTPSLKANSQLLAYSPSSVKSLGLEESETQTEAFQQLVVGSNVDVNKCCPWAQCYGGYQFGDWAGQLGDGRVVSLCELTNPETGKRFEIQVKGAGRTPYSRFADGKAVLRSSIREYLCCEALYALGIPTTQALAISNLEGVVAQRETVEPCAVVCRMAPSWIRIGTFDLQGINNQIESLRKLADYCLNFVLKDGFHGGDTGNRYEKLLRDVAYRNAKTVAKWQAYGFMNGVLNTDNTSILGLSIDYGPFGFLDVYNPSFTPNHDDVFLRYSYRNQPDIIIWNLSKLASALVELIGACDKVDDLQYMEQLHNSTDLLKKAFAYTSEVFEKIVEEYKNIVQNDFYDLMFKRVGLPSDSSNKILITDLLQILEDYELDMPNCFSFLSRNSPSSMENEEYAAKLMQACICLNPNNERVRNESVKAFTNWVGRYSEATKTQEDSSRLASMKKVNPHFTLRNWVLEEVIKEAYIGKFELFKKVCKMAACPFEDTWGFSKEEEDYLCYNTTPSKSQIQCSCSS
Protein: Actin-binding Rho-activating protein (MS1) (Striated muscle activator of Rho-dependent signaling) (STARS) (Q8K4K7)
Organism: Rattus norvegicus (Rat)
Function: Acts as an activator of serum response factor (SRF)-dependent transcription possibly by inducing nuclear translocation of MKL1 or MKL2 and through a mechanism requiring Rho-actin signaling.
Subcellular location: Cytoplasm, myofibril, sarcomere {ECO:0000269|PubMed:11983702}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:11983702}. Note=Localized to the I-band of the sarcomere and to a lesser extent to the sarcomeric structure between Z-lines.
Interaction partners:
Sequence:
MAPGETEREAGPAKSALQKVRRATLVINLARGWQQWANENSTRQAQEPAGWLPGATQDLPHTPKEPGPRQHAPKPPSPKPDGDREGRGSEEATEVSHIKRKEVTRTVVSKAYERGGDVNYLSHRYEHDGGVSEAVQPDNDIDRILLSHDSPTRRRKCTNLVSELTKGWKVMEQEEPKWKSDSIDTEDSGYGGDMEERPEQDVAQVAAARIKRPLHSQANRYSETLNCKAHRKYSQVDNLKGRWQQWADEHIQSQKLNPFSDEFDYDLAMSTRLHKGDEGYGRPKEGSKTAERAKRAEEHIYREIMELCFVIRTMARHRRDGKIQVTFGELFDRYVRISDKVVGILMRARKHGLVHFEGEMLWQGKDDHVVITLLE
Protein: Potassium channel subfamily T member 2 (Sequence like an intermediate conductance potassium channel subunit) (Sodium and chloride-activated ATP-sensitive potassium channel Slo2.1) (Q6UVM4)
Organism: Rattus norvegicus (Rat)
Function: Outward rectifying potassium channel. Produces rapidly activating outward rectifier K(+) currents. Activated by high intracellular sodium and chloride levels. Channel activity is inhibited by ATP and by inhalation anesthetics, such as isoflurane. Inhibited upon stimulation of G-protein coupled receptors, such as CHRM1 and GRM1 (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:15717307, ECO:0000269|PubMed:16687497, ECO:0000269|PubMed:19403831}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Short coiled-coil protein
Sequence:
MVDLESEVPPLPPRYRFRDLLLGDQGWQNDDRVQVEFYMNENTFKERLKLFFIKNQRSSLRIRLFNFSLKLLSCLLYIIRVLLEKPSQGNDWSHIFWVNRSLPLWGLQVSVALISLFETILLGYLSYKGNIWEQILRVPFILEIINAVPFIISIFWPTLRNLFVPVFLNCWLAKHALENMINDLHRAIQRTQSAMFNQVLILISTLLCLIFTCICGIQHLERIGKKLNLFDSLYFCIVTFSTVGFGDVTPETWSSKLFVVAMICVALVVLPIQFEQLAYLWMERQKSGGNYSRHRAQTEKHVVLCVSSLKIDLLMDFLNEFYAHPRLQDYYVVILCPTEMDVQVRRVLQIPMWSQRVIYLQGSALKDQDLLRAKMDNAEACFILSSRCEVDRTSSDHQTILRAWAVKDFAPNCPLYVQILKPENKFHIKFADHVVCEEEFKYAMLALNCICPATSTLITLLVHTSRGQCVCLCCREGQQSPEQWQKTYGRCSGNEVYHIVLEESTFFAEYEGKSFTYASFHAHKKFGVCLVGVRREDNKNILLNPGPRYIMNASDICFYINITKEENSAFKNQDQQRKSNVSRSFYHGPSRLPVHSIIASMGTVAIDLQDTSCRAASGPTLALPSEGGKELRRPSIAPVLEVADTSSIQTCDLLSDQSEDETTPDEETSSNLEYAKGYPPYSPYIGSSPTFCHLLQEKVPFCCLRLDKSCQHNYYEDAKAYGFKNKLIIVAAETAGNGLYNFIVPLRAYYRPKKELNPIVLLLDNPPDMHFLDAICWFPMVYYMVGSIDNLDDLLRCGVTFAANMVVVDKESTMSAEEDYMADAKTIVNVQTLFRLFSSLSIITELTHPANMRFMQFRAKDCYSLALSKLEKKERERGSNLAFMFRLPFAAGRVFSISMLDTLLYQSFVKDYMISITRLLLGLDTIPGSGFLCSMKITEDDLWIRTYARLYQKLCSSTGDVPIGIYRTESQKLTTSESQISISVEEWEDTKDVKDPGHHRSIHRNSTSSDQSDHPLLRRKSMQWARRLSRKGPKHSGKTAEKITQQRLNLYRRSERQELAELVKNRMKHLGLSTVGYDEMNDHQSTLSYILINPSPDTRLELNDVVYLIRPDPLSYLPNSEPSRKNSICNAAVQDSREETQL
Protein: Protein FAM220A (Acrosomal protein ACPIN1) (STAT3-interacting protein as a repressor) (Q3ZN08)
Organism: Mus musculus (Mouse)
Function: May negatively regulate STAT3.
Subcellular location: Nucleus {ECO:0000269|PubMed:23917203, ECO:0000269|PubMed:26026268}. Cytoplasm {ECO:0000269|PubMed:23917203}. Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000269|PubMed:19659802}. Note=Localizes to both nucleus and cytoplasm but located predominantly in the nucleus (PubMed:23917203). Detected in the sperm acrosome prior to the acrosome reaction and is likely to be released from acrosome-reacted sperm (PubMed:19659802). {ECO:0000269|PubMed:19659802, ECO:0000269|PubMed:23917203}.
Interaction partners:
Sequence:
MKAGRGTLGVCLAKQSQGGDPDKLACGLKKRSQKRNPSPSVVPSWTDQPVADSHGKSRATGAAASEMKHGQSKASLLHHGGFKVLQSLKGSVGRSSAPAASLGKAVALSPAPSEEQLAGMSHGIGDALGSDWPGREPRATDNRGQYLKGESWVSGRPGHPKLREVGFLRGEPPSAGPKGLGTWSELSHRYFELGQLPYAYPYYKVLPEGELRCVSLDRFNPGLSEETVEDEKTLKFFRWSADSRGVTGSAIFQISKSLMP
Protein: High mobility group B protein 3 (High mobility group protein B 2) (AtHMGbeta2) (HMG beta 2) (Nucleosome/chromatin assembly factor group D 03) (Nucleosome/chromatin assembly factor group D 3) (P93047)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Binds preferentially double-stranded DNA.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267, ECO:0000269|PubMed:20123078}. Cytoplasm, cytosol {ECO:0000269|PubMed:20123078}.
Interaction partners:
- Actin-related protein 9
- RuvB-like protein 1
- GATA transcription factor 6
Sequence:
MKGAKSKAETRSTKLSVTKKPAKGAKGAAKDPNKPKRPSSAFFVFMEDFRVTYKEEHPKNKSVAAVGKAGGEKWKSLSDSEKAPYVAKADKRKVEYEKNMKAYNKKLEEGPKEDEESDKSVSEVNDEDDAEDGSEEEEDDD
Protein: Urokinase-type plasminogen activator (U-plasminogen activator) (uPA) (EC 3.4.21.73) [Cleaved into: Urokinase-type plasminogen activator long chain A; Urokinase-type plasminogen activator short chain A; Urokinase-type plasminogen activator chain B] (P29598)
Organism: Rattus norvegicus (Rat)
Function: Specifically cleaves the zymogen plasminogen to form the active enzyme plasmin.
Subcellular location: Secreted {ECO:0000250|UniProtKB:P00749}.
Interaction partners:
- Plasminogen activator inhibitor 1
- Urokinase plasminogen activator surface receptor
- Aa1018
- Plasminogen
- Glia-derived nexin
- Plasminogen activator inhibitor 2 type A
- Cathepsin B
- Tissue factor
- Thrombomodulin
- Serpin family A member 5
Sequence:
MRVWLASLFLCALVANSEGGSELEASDESNCGCQNGGVCVSYKYFSSIRRCSCPKKFKGEHCEIDTSKTCYHGNGQSYRGKANTDTKGRPCLAWNSPAVLQQTYNAHRSDALSLGLGKHNYCRNPDNQRRPWCYVQIGLKQFVQECMVQDCSLSKKPSSTVDQQGFQCGQKALRPRFKIVGGEFTVVENQPWFAAIYLKNKGGSPPSFKCGGSLISPCWVASATHCFVNQPKKEEYVVYLGQSKRNSYNPGEMKFEVEQLILHEDFSDETLAFHNDIALLKIRTSTGQCAQPSRTIQTICLPPRFGDAPFGSDCEITGFGQESATDYFYPKDLKMSVVKIISHEQCKQPHYYGSEINYKMLCAADPEWKTDSCSGDSGGPLICNIDGRPTLSGIVSWGSGCAEKNKPGVYTRVSYFLNWIQSHIGEENGLAF
Protein: Supervillin (Archvillin) (p205/p250) (O95425)
Organism: Homo sapiens (Human)
Function: Forms a high-affinity link between the actin cytoskeleton and the membrane. Is among the first costameric proteins to assemble during myogenesis and it contributes to myogenic membrane structure and differentiation. Appears to be involved in myosin II assembly. May modulate myosin II regulation through MLCK during cell spreading, an initial step in cell migration. May play a role in invadopodial function.
Subcellular location: Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm, cytoskeleton. Cell projection, invadopodium. Cell projection, podosome. Midbody {ECO:0000250|UniProtKB:O46385}. Cleavage furrow {ECO:0000250|UniProtKB:O46385}. Note=Tightly associated with both actin filaments and plasma membranes.
Interaction partners:
- Kinesin-like protein KIF14
- Actin, cytoplasmic 1
- Src substrate cortactin
Sequence:
MKRKERIARRLEGIENDTQPILLQSCTGLVTHRLLEEDTPRYMRASDPASPHIGRSNEEEETSDSSLEKQTRSKYCTETSGVHGDSPYGSGTMDTHSLESKAERIARYKAERRRQLAEKYGLTLDPEADSEYLSRYTKSRKEPDAVEKRGGKSDKQEESSRDASSLYPGTETMGLRTCAGESKDYALHVGDGSSDPEVLLNIENQRRGQELSATRQAHDLSPAAESSSTFSFSGRDSSFTEVPRSPKHAHSSSLQQAASRSPSFGDPQLSPEARPSTGKPKHEWFLQKDSEGDTPSLINWPSRVKVREKLVKEESARNSPELASESVTQRRHQPAPVHYVSFQSEHSAFDRVPSKAAGSTRQPIRGYVQPADTGHTAKLVTPETPENASECSWVASATQNVPKPPSLTVLEGDGRDSPVLHVCESKAEEEEGEGEGEEKEEDVCFTEALEQSKKTLLALEGDGLVRSPEDPSRNEDFGKPAVSTVTLEHQKELENVAQPPQAPHQPTERTGRSEMVLYIQSEPVSQDAKPTGHNREASKKRKVRTRSLSDFTGPPQLQALKYKDPASRRELELPSSKTEGPYGEISMLDTKVSVAQLRSAFLASANACRRPELKSRVERSAEGPGLPTGVERERGSRKPRRYFSPGESRKTSERFRTQPITSAERKESDRCTSHSETPTVDDEEKVDERAKLSVAAKRLLFREMEKSFDEQNVPKRRSRNTAVEQRLRRLQDRSLTQPITTEEVVIAATEPIPASCSGGTHPVMARLPSPTVARSAVQPARLQASAHQKALAKDQTNEGKELAEQGEPDSSTLSLAEKLALFNKLSQPVSKAISTRNRIDTRQRRMNARYQTQPVTLGEVEQVQSGKLIPFSPAVNTSVSTVASTVAPMYAGDLRTKPPLDHNASATDYKFSSSIENSDSPVRSILKSQAWQPLVEGSENKGMLREYGETESKRALTGRDSGMEKYGSFEEAEASYPILNRAREGDSHKESKYAVPRRGSLERANPPITHLGDEPKEFSMAKMNAQGNLDLRDRLPFEEKVEVENVMKRKFSLRAAEFGEPTSEQTGTAAGKTIAQTTAPVSWKPQDSSEQPQEKLCKNPCAMFAAGEIKTPTGEGLLDSPSKTMSIKERLALLKKSGEEDWRNRLSRRQEGGKAPASSLHTQEAGRSLIKKRVTESRESQMTIEERKQLITVREEAWKTRGRGAANDSTQFTVAGRMVKKGLASPTAITPVASPICGKTRGTTPVSKPLEDIEARPDMQLESDLKLDRLETFLRRLNNKVGGMHETVLTVTGKSVKEVMKPDDDETFAKFYRSVDYNMPRSPVEMDEDFDVIFDPYAPKLTSSVAEHKRAVRPKRRVQASKNPLKMLAAREDLLQEYTEQRLNVAFMESKRMKVEKMSSNSNFSEVTLAGLASKENFSNVSLRSVNLTEQNSNNSAVPYKRLMLLQIKGRRHVQTRLVEPRASALNSGDCFLLLSPHCCFLWVGEFANVIEKAKASELATLIQTKRELGCRATYIQTIEEGINTHTHAAKDFWKLLGGQTSYQSAGDPKEDELYEAAIIETNCIYRLMDDKLVPDDDYWGKIPKCSLLQPKEVLVFDFGSEVYVWHGKEVTLAQRKIAFQLAKHLWNGTFDYENCDINPLDPGECNPLIPRKGQGRPDWAIFGRLTEHNETILFKEKFLDWTELKRSNEKNPGELAQHKEDPRTDVKAYDVTRMVSMPQTTAGTILDGVNVGRGYGLVEGHDRRQFEITSVSVDVWHILEFDYSRLPKQSIGQFHEGDAYVVKWKFMVSTAVGSRQKGEHSVRAAGKEKCVYFFWQGRHSTVSEKGTSALMTVELDEERGAQVQVLQGKEPPCFLQCFQGGMVVHSGRREEEEENVQSEWRLYCVRGEVPVEGNLLEVACHCSSLRSRTSMVVLNVNKALIYLWHGCKAQAHTKEVGRTAANKIKEQCPLEAGLHSSSKVTIHECDEGSEPLGFWDALGRRDRKAYDCMLQDPGSFNFAPRLFILSSSSGDFAATEFVYPARAPSVVSSMPFLQEDLYSAPQPALFLVDNHHEVYLWQGWWPIENKITGSARIRWASDRKSAMETVLQYCKGKNLKKPAPKSYLIHAGLEPLTFTNMFPSWEHREDIAEITEMDTEVSNQITLVEDVLAKLCKTIYPLADLLARPLPEGVDPLKLEIYLTDEDFEFALDMTRDEYNALPAWKQVNLKKAKGLF