wanglab/gogpt-training-data huggingface dataset:
Protein: Sodium voltage-gated channel alpha subunit 7 (A0A8I6GH51)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MLTSPEPKGLVPFTAESLELIKNHIAKKCNEEHEEEDLKPSWGLEAGKKLPFAYGTLPQGTVSEPLEDVDPYYYVKRNLTNVNPYFLIKITFIFNICKIIFHLNLQMQFVLTDSILMCMSNLPEWILAVENTLLGIYTFEILVKVIARGIWAGSFSFLGDLWNWLDFSVTLFELITRSSPLSSLPMFKTIRTLRILKIIPLNHGLQSIVVTLVQCLKKLLGAIALALFFLTVSSLFGMGLFMGNLKHKCVRWPQEDGNDVMYNGTGSQYHILERENFYYMEGARYALLCGNKTDAGLCPEGYMCVKEGSNPDNGFTSFDNFGWALLAMFRLMTQDYPELLYHQILYASGKIYMIFFVLISFWFAFYMASLFLGILTMAYEQEKQRASEESRDMDSKCHQTVKEFEEEHEGAELQCIWFYEEVLDLLGLELCTRRSPTSINTTLDILEDTALGHKEEPETSRKECPLCWYKFTKTCFIWKCSPCWIKLNEFADRIITHPLFDLFLVICIILNICFLALEHFPMSEELMSLLAIGNLVFIGIYTIEMILKIIAMHPYGYFQISWHIFDSILVVLGLTEMLLADIEEITVFILVPLIFIKLGKYAPPFKNLMRILGRALVALKDLVLLVSIFIYFSAVFGMKLFGRSYKDCVCHVDQDCQRQRWHMSDFLHAYVTVFRILCGEWIETLWECMEVAGEAWCIPFYMMVILIGNLLILYLFVALVSSFASYDATTEVSKEAKNLQLAVAWIKMVINCVLLKILCKEKTVSTEATDQTCDPSVKENISGHTLSELSNTQTFLRYKDQSSGTEKTPVTESESQSLIASPSVSETVPIASGESDIENLDNKETRSKSANGSSKEKMKQSSSSECSTVDIAISEEEEMVYEHEKSKLHKNGYERKSSAGQVSRESRNGKIWRNIRKTCCKIVENSWFECFIGLVTLLCTGTLALEDIYIDQRKTIKIFLEYGDMIFAYIFILEMLLKWVAYGFKAYFSNNWYKLDFMVVIVLCLSLIGKTREDLNPLASIKFLRALRVLSQFERMKVVLRALIKTTLPAVSVFLVCLMIWLLFSVMGVFLFAGKFYECIDPTRGERFSVFEVMNKSQCENLVFNESMPWENAKLNFDNVGNGFLSLFQVATFNGWISIMNSAIDSVGVYMQPSFEHSLHMYTYFIIFVVFGLFLPLCMLIGVIIRNFNKQKIKIRSNIFITVKQKKQYRALKKLLYADSQKPAARPRNKFQGFICDVVTHRVFNVIIILLICFQATTIMIQNDEQSPQIETAVFWMNSLFTMLFTLECILKLTAFRCHYFTSAWNVHDFMVVVFSITGLLLPLSIGQYFVPPSLVQLLLLSRIIHVLRPGKGPKVFHDLMLPLMLSLPALLNIALLIFLVMFIYAIFGMYNFAYVKKEAGINDVSNFETFGSSMLCLFQVTTFSGWDGMLDAIFNSQWSDCDPDKINPGTQVRGDCGSPSVGIFYFVSYILISWLIIVNMYVVLIMEFLSIPSKRKNRTLSEDDFRRFFKVWNRFDPDRTQYIDSTKLSDFAAALDPPLFMAKPNKGQLVAMDLPMAAGDRIHCLDILLAFTKRVMGKDERVEKILSEIESGFMLANPFKITYEPITTTLKRKQEAVSATIIQRAYKSYRLRQSDKKIQDIPEIDDGREDPNSKGVHSGQIEEKASIQTQI
Protein: Tetratricopeptide repeat protein 4 (TPR repeat protein 4) (O95801)
Organism: Homo sapiens (Human)
Function: May act as a co-chaperone for HSP90AB1. Promotes Sendai virus (SeV)-induced host cell innate immune responses.
Subcellular location: Nucleus {ECO:0000269|PubMed:18320024, ECO:0000269|PubMed:29251827}. Nucleus, nucleoplasm {ECO:0000269|PubMed:18320024}. Cytoplasm {ECO:0000269|PubMed:29251827}. Note=Predominantly nuclear in the G1 and S phases of cell cycle and is evenly distributed between the nucleus and cytoplasm in the G2 phase (By similarity). MSL1 can promote its nuclear localization (By similarity). {ECO:0000250|UniProtKB:Q8R3H9}.
Interaction partners:
- Protein HGH1 homolog
- Heat shock protein HSP 90-beta
- Heat shock protein HSP 90-alpha
- Small ribosomal subunit protein eS7
- Peptidyl-prolyl cis-trans isomerase D
- Mothers against decapentaplegic homolog 3
- Hsp90 co-chaperone Cdc37
- Vacuolar protein sorting-associated protein 29
- Vacuolar protein sorting-associated protein 35
Sequence:
MEQPGQDPTSDDVMDSFLEKFQSQPYRGGFHEDQWEKEFEKVPLFMSRAPSEIDPRENPDLACLQSIIFDEERSPEEQAKTYKDEGNDYFKEKDYKKAVISYTEGLKKKCADPDLNAVLYTNRAAAQYYLGNFRSALNDVTAARKLKPCHLKAIIRGALCHLELKHFAEAVNWCDEGLQIDAKEKKLLEMRAKADKLKRIEQRDVRKANLKEKKERNQNEALLQAIKARNIRLSEAACEDEDSASEGLGELFLDGLSTENPHGARLSLDGQGRLSWPVLFLYPEYAQSDFISAFHEDSRFIDHLMVMFGETPSWDLEQKYCPDNLEVYFEDEDRAELYRVPAKSTLLQVLQHQRYFVKALTPAFLVCVGSSPFCKNFLRGRKVYQIR
Protein: Muscarinic acetylcholine receptor M1 (P11229)
Organism: Homo sapiens (Human)
Function: The muscarinic acetylcholine receptor mediates various cellular responses, including inhibition of adenylate cyclase, breakdown of phosphoinositides and modulation of potassium channels through the action of G proteins. Primary transducing effect is Pi turnover.
Subcellular location: Cell membrane; Multi-pass membrane protein. Postsynaptic cell membrane; Multi-pass membrane protein.
Interaction partners:
- Guanine nucleotide-binding protein G
- Metabotropic glutamate receptor 5
- Lysophosphatidic acid receptor 6
- Guanine nucleotide-binding protein subunit alpha-11
- Lysophosphatidic acid receptor 1
- Kininogen-1
- Guanine nucleotide-binding protein G
- Muscarinic acetylcholine receptor M3
- Lysophosphatidic acid receptor 3
- Muscarinic acetylcholine receptor M2
Sequence:
MNTSAPPAVSPNITVLAPGKGPWQVAFIGITTGLLSLATVTGNLLVLISFKVNTELKTVNNYFLLSLACADLIIGTFSMNLYTTYLLMGHWALGTLACDLWLALDYVASNASVMNLLLISFDRYFSVTRPLSYRAKRTPRRAALMIGLAWLVSFVLWAPAILFWQYLVGERTVLAGQCYIQFLSQPIITFGTAMAAFYLPVTVMCTLYWRIYRETENRARELAALQGSETPGKGGGSSSSSERSQPGAEGSPETPPGRCCRCCRAPRLLQAYSWKEEEEEDEGSMESLTSSEGEEPGSEVVIKMPMVDPEAQAPTKQPPRSSPNTVKRPTKKGRDRAGKGQKPRGKEQLAKRKTFSLVKEKKAARTLSAILLAFILTWTPYNIMVLVSTFCKDCVPETLWELGYWLCYVNSTINPMCYALCNKAFRDTFRLLLLCRWDKRRWRKIPKRPGSVHRTPSRQC
Protein: Homocysteine biosynthesis enzyme sulfur-incorporation domain-containing protein (Q727B7)
Organism: Nitratidesulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / CCUG 34227 / NCIMB 8303 / VKM B-1760 / Hildenborough) (Desulfovibrio vulgaris)
Interaction partners:
- Iron-sulfur cluster-binding protein
- Methionine synthase
- Aspartate-semialdehyde dehydrogenase
- Adenosylhomocysteinase
- cysteine-S-conjugate beta-lyase
- Homoserine dehydrogenase
- 5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase
- ApbE family lipoprotein
- Cysteine synthase
- PP-loop domain protein
Sequence:
MAHFKVNKTIAEINERIKQGKAVVLNAEEMTEAVRRMGKEKAAREVDVVTTGTFSPMCSSGLLFNIGQQEPPTIKTSKVWLNNVPAYAGLAAVDAYIGATEPTEDDPLNKVYPGRFKYGGGHVIEDLVRGKSVHLRAEAYGTDCYPRRSLDKQITLAEMPFAQLWNPRNCYQNYNAAVNLTSRIIYTYMGPLKPNMRNINFATAGRLSPLFNDPYFRTIGLGTRIFLGGSTGYVTGAGTQHVAAPKRTDRGLPLTGAGTLMVQGDLKGMDARYLRGLSFLGYGCTLAVGIGIPIPVLNEEIAWFTGVDDSDILMPVRDYGHDYPNCLPRIIQHVSYEDLKSGEVEVMGKKVESVPLTSYSISLEIADKLKSWIEKGTFTLTQPVELLPSA
Protein: Mitochondrial distribution and morphology protein 31 (Q10070)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Involved in the organization of the mitochondrial membranes and the global structure of the mitochondria. Also required for mitochondrial distribution and mobility as well as for the maintenance of mitochondrial DNA nucleoids structures (By similarity).
Subcellular location: Mitochondrion inner membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Mitochondrial distribution and morphology protein 10
- Mitochondrial distribution and morphology protein 12
- GrpE protein homolog
Sequence:
MLESRLAKNIARIVQARKPYLISYHVRASTQNALLKQTVLQSSSFKSFPTLPRLAARNISNSGILSRTTPVIIKQISMVRSYSSGDVENPEILNKNESNQSSGVKRAMPFRVLKKMKSFLFKQNKPLTVDNVTAFFSWWLVSHIVWIVVGTTTFFSLLLYTLNTVSAQELLGRWIGQLMTKNTGFQFVFESAIVPNWRKGLITFNKISVIRRPDTLNGIGAQNPNNKSDYEKEYMALRKRYDSNEEPDTEALSQGNYTQFELSIDKADVSFSFARFLNGKGIVKELQLKGVRGVVDRRFIEWDPSSDPRDYRRKHNWGDFEIEKFKLEDLRVTLLQPKGFRKFPVSVFFCELPRLRKQWLFYDLMNAKTLTGSFDNSMFTIHRLQLRPYSPYLKVGKQLDDMRHSRLRIDNVAIDHLNRGVSGAFGWINDGSVDFLVNISFPSEPSENSFQKAWISLMDKLKKKEKDEDVYKDVHFDVNVQLHNPKAVIPIFTNQVSYINNALIRPIIAYINSTRTFIPILCHVSKPLSDFDGSWTFYDSGVLQEISAQVYESFARDVLNQEIRRKRIQKVGYWSLRRFLHLVLVSLQELAPTTSSISNFE
Protein: Uncharacterized protein, isoform B (A0A0B4KGJ8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MFNGLLKSQGYPKQTHFDPSRPGETISNLLDHVAKHHLNVKIDSRQYVKPAVGYAKELLKLGQARGLLQFNATEISDKLTDTLNLEVIEPVLKVHRAYRYISKSPQCDRYVLCQLNAAALDQQEKQRQHDQYQQHHQPKQSQLNRPTSASSLIAGVSPKIVKIGSMGAAIFISTETGTPFWTLFGVINAPYNCEAKYPVDCNGFHEGEAKVTTEYIHNEL
Protein: Fibrinogen beta chain (D6REL8)
Organism: Homo sapiens (Human)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MEYCRTPCTVSCNIPVVSGKECEEIIRKGGETSEMYLIQPDSSVKPYRVYCDMNTENGGWTVIQNRQDGSVDFGRKWDPYKQGFGNVATNTDGKNYCGLPGEYWLGNDKISQLTRMGPTELLIEMEDWKGDKVKAHYGGFTVQNEANKYQISVNKYRGTAGNALMDGASQLMGENRTMTIHNGMFFSTYDRDNDGWLTSDPRKQCSKEDGGGWWYNRCHAANPNGRYYWGGQYTWDMAKHGTDDGVVWMNWKGSWYSMRKMSMKIRPFFPQQ
Protein: Corona (IP08467p) (IP08667p) (IP08767p) (Q9VE78)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Protein benign gonial cell neoplasm
- FI02132p
- Crossover suppressor on 2 of manheim
- Corolla, isoform A
Sequence:
MGSNQDWNKEDSKTEVPPEEDDQVTAYIEKSVAQLGSENDHRTALVDEKKKELDVLIAEKYTTLNDLTHVTNSQNLVDDIHFLHTKNAKILESLNQAVTAKRNVSQAYDDHCKKALKVKAEMQEQTKCFDEFTVMNYHDLKKTILNTKKETQEIRAKTALKTEELKKKREFVNTTQKSMANDIRVLGQIEHDLIGIIEDLKSKISAI
Protein: NFATC2-interacting protein (45 kDa NF-AT-interacting protein) (45 kDa NFAT-interacting protein) (Nuclear factor of activated T-cells, cytoplasmic 2-interacting protein) (Q8NCF5)
Organism: Homo sapiens (Human)
Function: In T-helper 2 (Th2) cells, regulates the magnitude of NFAT-driven transcription of a specific subset of cytokine genes, including IL3, IL4, IL5 and IL13, but not IL2. Recruits PRMT1 to the IL4 promoter; this leads to enhancement of histone H4 'Arg-3'-methylation and facilitates subsequent histone acetylation at the IL4 locus, thus promotes robust cytokine expression (By similarity). Down-regulates formation of poly-SUMO chains by UBE2I/UBC9 (By similarity).
Subcellular location: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=TRAF1 is associated with a fraction of NFATC2IP in the cytoplasm and prevents its translocation to the nucleus. {ECO:0000250}.
Interaction partners:
- SUMO-conjugating enzyme UBC9
- Structural maintenance of chromosomes protein 5
- Protein arginine N-methyltransferase 1
- Helicase SRCAP
- Proliferating cell nuclear antigen
- Zinc finger HIT domain-containing protein 1
Sequence:
MAEPVGKRGRWSGGSGAGRGGRGGWGGRGRRPRAQRSPSRGTLDVVSVDLVTDSDEEILEVATARGAADEVEVEPPEPPGPVASRDNSNSDSEGEDRRPAGPPREPVRRRRRLVLDPGEAPLVPVYSGKVKSSLRLIPDDLSLLKLYPPGDEEEAELADSSGLYHEGSPSPGSPWKTKLRTKDKEEKKKTEFLDLDNSPLSPPSPRTKSRTHTRALKKLSEVNKRLQDLRSCLSPKPPQGQEQQGQEDEVVLVEGPTLPETPRLFPLKIRCRADLVRLPLRMSEPLQSVVDHMATHLGVSPSRILLLFGETELSPTATPRTLKLGVADIIDCVVLTSSPEATETSQQLQLRVQGKEKHQTLEVSLSRDSPLKTLMSHYEEAMGLSGRKLSFFFDGTKLSGRELPADLGMESGDLIEVWG
Protein: Cytochrome P450 4A11 (EC 1.14.14.1) (20-hydroxyeicosatetraenoic acid synthase) (20-HETE synthase) (CYP4AII) (CYPIVA11) (Cytochrome P-450HK-omega) (Cytochrome P450HL-omega) (Fatty acid omega-hydroxylase) (Lauric acid omega-hydroxylase) (Long-chain fatty acid omega-monooxygenase) (EC 1.14.14.80) (Q02928)
Organism: Homo sapiens (Human)
Function: A cytochrome P450 monooxygenase involved in the metabolism of fatty acids and their oxygenated derivatives (oxylipins). Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (CPR; NADPH-ferrihemoprotein reductase). Catalyzes predominantly the oxidation of the terminal carbon (omega-oxidation) of saturated and unsaturated fatty acids, the catalytic efficiency decreasing in the following order: dodecanoic > tetradecanoic > (9Z)-octadecenoic > (9Z,12Z)-octadecadienoic > hexadecanoic acid. Acts as a major omega-hydroxylase for dodecanoic (lauric) acid in liver. Participates in omega-hydroxylation of (5Z,8Z,11Z,14Z)-eicosatetraenoic acid (arachidonate) to 20-hydroxyeicosatetraenoic acid (20-HETE), a signaling molecule acting both as vasoconstrictive and natriuretic with overall effect on arterial blood pressure. Can also catalyze the oxidation of the penultimate carbon (omega-1 oxidation) of fatty acids with lower efficiency. May contribute to the degradation of saturated very long-chain fatty acids (VLCFAs) such as docosanoic acid, by catalyzing successive omega-oxidations to the corresponding dicarboxylic acid, thereby initiating chain shortening. Omega-hydroxylates (9R,10S)-epoxy-octadecanoate stereoisomer. Plays a minor role in omega-oxidation of long-chain 3-hydroxy fatty acids. Has little activity toward prostaglandins A1 and E1.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305|PubMed:1739747}; Peripheral membrane protein {ECO:0000305}. Microsome membrane {ECO:0000305|PubMed:1739747}; Peripheral membrane protein {ECO:0000305}.
Interaction partners:
- Cytochrome P450 1A2
- Cytochrome P450 2A6
- Cytochrome P450 2B6
- Cytochrome P450 2C8
- Cytochrome P450 2E1
- Cytochrome P450 4A22
- Cytochrome P450 3A4)
- Cytochrome P450 2C19
- Cytochrome P450 2C9
- Cytochrome P450 2J2))
Sequence:
MSVSVLSPSRLLGDVSGILQAASLLILLLLLIKAVQLYLHRQWLLKALQQFPCPPSHWLFGHIQELQQDQELQRIQKWVETFPSACPHWLWGGKVRVQLYDPDYMKVILGRSDPKSHGSYRFLAPWIGYGLLLLNGQTWFQHRRMLTPAFHYDILKPYVGLMADSVRVMLDKWEELLGQDSPLEVFQHVSLMTLDTIMKCAFSHQGSIQVDRNSQSYIQAISDLNNLVFSRVRNAFHQNDTIYSLTSAGRWTHRACQLAHQHTDQVIQLRKAQLQKEGELEKIKRKRHLDFLDILLLAKMENGSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREEIHSLLGDGASITWNHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFPDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFAPGSAQHSHAFLPFSGGSRNCIGKQFAMNELKVATALTLLRFELLPDPTRIPIPIARLVLKSKNGIHLRLRRLPNPCEDKDQL
Protein: G-protein coupled receptors family 1 profile domain-containing protein (Q7JP61)
Organism: Caenorhabditis elegans
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
- Tyramine beta-hydroxylase
- G-protein coupled receptors family 1 profile domain-containing protein
- Activated in Blocked Unfolded protein response
- G_PROTEIN_RECEP_F1_2 domain-containing protein
- Activated in Blocked Unfolded protein response
- Neuropeptide-Like Protein
- Probable G-protein coupled receptor C06G4.5
- Guanine nucleotide-binding protein subunit beta-2
- Guanine nucleotide-binding protein subunit beta-1
- Activated in Blocked Unfolded protein response
Sequence:
MWNLNCSESDTKVACLNLGEAVLTISSMLTVMLLIIFGNLLVVVTVYRDRKLRMQRQNWLIVSLAVADMLVGLLVMPLTLTYEIVGEWTMGNILCEIWLALDVLFVTASILHICAISLDRYFSVTSPLTYPATRTPLRMFIYIGVSWIVSLLICLPPIFGWRPERAEGECSVSTDLGYVLYSSLGSFYIPVVILIIVYAKIYSITIRHSRQRLKETERRDHTLNMLTIRSSTNERYNMEYELEENSDPIEDEKEKVVTNRDMINKVCWQLRKISEELPRQGVKVSIALDTNHNSPPASDLTRKLEEKKFCEKRKRKLKAKERQATLLLGIILSAFILSWLPFFLIYVIGAFGHEAPPLVFKFFFWLGYCNSGINPVIYTVFNREFKRGLCKQLHKFERFIHPLMEFYK
Protein: Mitochondrial coenzyme A diphosphatase NUDT8 (EC 3.6.1.-) (EC 3.6.1.77) (Nucleoside diphosphate-linked moiety X motif 8) (Nudix motif 8) (Q9CR24)
Organism: Mus musculus (Mouse)
Function: Acyl-CoA diphosphatase that mediates the hydrolysis of a wide range of CoA and CoA esters yielding 3',5'-ADP and the corresponding 4'-phosphopantetheine derivative as products. Hydrolyzes short- and medium-chain acyl-CoAs, exhibiting the highest activity toward free CoA, hexanoyl-CoA, and octanoyl-CoA and the lowest activity against acetyl-CoA. Exhibits decapping activity towards dpCoA-capped RNAs in vitro.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:31004344}.
Interaction partners:
Sequence:
MLPDGLSAEDEQRCRQLLARTTARLRSRPAAAAVLVPLCLVRGVPALLYTLRSSRLVGRHKGEVSFPGGKCDPDDQDVIHTALRETQEELGLEVPKEHVWGVLQPVYDREKATIVPVLANVGPLDLQSLRPNLEEVDEVFEMSLAHLLQTQNQGYTHFCQGGHFSYTLPVFLHGPHRVWGLTAVITELTLKLLAPGFYQPSLAVPELPRG
Protein: Lysosomal alpha-mannosidase (Laman) (EC 3.2.1.24) (Alpha-D-mannoside mannohydrolase) (Alpha-mannosidase A) [Cleaved into: Alpha-mannosidase 60 kDa subunit; Alpha-mannosidase 58 kDa subunit] (P34098)
Organism: Dictyostelium discoideum (Social amoeba)
Subcellular location: [Alpha-mannosidase 60 kDa subunit]: Lysosome. Note=A few precursors are secreted. The mature 58 and 60 kDa subunits are lysosomal.; SUBCELLULAR LOCATION: [Alpha-mannosidase 58 kDa subunit]: Lysosome.
Interaction partners:
- Alpha-mannosidase G
- BEACH domain-containing protein lvsE
Sequence:
MVIKKLFILIFCLFLIINEINGKKTKINDIKKSKPKLSSTLLNVHIVAHTHDDVGWLKTVDEYYYGSNMSIAFAGVQYTLDTAITCLLANPERKFIYVEIAFFQRWWDEQSTTMQNIVKGLVESGQLEFINGGYCMNDEATTYYDDTIDQMTLGHQFLWENFGVMPKIGWHIDPFGHSATQARIFGQLGFDAFIIGRMDYQDIEARLENKQMEFMWRSTQSTPENQVFTSVLRAMYCTPDGFNFEQGDDPIQDDPNLFDNNVDSRAEQFTQVALEYATHYRTNNVLIPFGCDFAYLNAQMYYKNIDKLIAHINSNPDKYGLNLLYSTPSIYIDAVNDANLVWEVKTDDLFPYADNEFSYWTGYFVSRPALKGYVRQNNALLHVVEQMLVTSSNLMPSSRSEQLVDDIVIMREVMGIAQHHDAVSGTEQQHVADDYAERLSIGNCASLETINTVVGTLLTANGNSKSAAATPTISFCPLLNQSICPATDPLSSGTSVPVLIYNSLSWTRNEPVRIPIPIANVTVTSSSNGSITSQVNQINGTFILEFLATIPPLGYSTYIITSTASDFVEPNSIPAIIIQDEIIVSGGGKINEKVSYNDPIILENDYINVQFSSQDGSILSITNKTSGVTSSITQEYIWYNPSVGNDDSAQCSGAYIFRPVEDFAYPYNNATPSVSIIRGEISSSIRRFWSNEMVQTFRLYSNADHLEVEEIIGPIDISDGIGKEIVSRYTTTLVTDQTWYSDSQGMEMQKRITNYRPSWNLTVVQPTSGNYVPVNAIAYIQDPNQSLQFTIVTDRSRGCASLRDGQLDMMMHRRTLKDDGRGVGQPMNESTQIVTTSKLIFHDISSYAQSHYRPAALSLSHPLLPMFTTTQQSSNDWNSQYQGVYSPLTSASPLPNGLKIQTLQWLDNQDNTILLRIENIYQIDGQDSQDPQTITLDLSTIFSTITITSATEMNLTGVQKLSNLSRLKWKTVDGKNYDHKSSSSTKEDSSNGFVFTFSPMQIRTFIITTN
Protein: Zinc finger protein 250 (Zinc finger protein 647) (P15622)
Organism: Homo sapiens (Human)
Function: May be involved in transcriptional regulation.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Transcription intermediary factor 1-beta
Sequence:
MAAARLLPVPAGPQPLSFQAKLTFEDVAVLLSQDEWDRLCPAQRGLYRNVMMETYGNVVSLGLPGSKPDIISQLERGEDPWVLDRKGAKKSQGLWSDYSDNLKYDHTTACTQQDSLSCPWECETKGESQNTDLSPKPLISEQTVILGKTPLGRIDQENNETKQSFCLSPNSVDHREVQVLSQSMPLTPHQAVPSGERPYMCVECGKCFGRSSHLLQHQRIHTGEKPYVCSVCGKAFSQSSVLSKHRRIHTGEKPYECNECGKAFRVSSDLAQHHKIHTGEKPHECLECRKAFTQLSHLIQHQRIHTGERPYVCPLCGKAFNHSTVLRSHQRVHTGEKPHRCNECGKTFSVKRTLLQHQRIHTGEKPYTCSECGKAFSDRSVLIQHHNVHTGEKPYECSECGKTFSHRSTLMNHERIHTEEKPYACYECGKAFVQHSHLIQHQRVHTGEKPYVCGECGHAFSARRSLIQHERIHTGEKPFQCTECGKAFSLKATLIVHLRTHTGEKPYECNSCGKAFSQYSVLIQHQRIHTGEKPYECGECGRAFNQHGHLIQHQKVHRKL
Protein: ATP-dependent DNA helicase HMI1, mitochondrial (EC 5.6.2.4) (DNA 3'-5' helicase) (Q12039)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for mitochondrial genome maintenance and mitochondrial DNA inheritance.
Subcellular location: Mitochondrion inner membrane {ECO:0000305|PubMed:10669756}; Peripheral membrane protein {ECO:0000305|PubMed:10669756}.
Interaction partners:
- Suppressor of kinetochore protein 1
- Putative ATP-dependent helicase IRC3
- DNA polymerase gamma
Sequence:
MDKLTPSQWKVINKSYEPASTIKVIAGPGSGKTLTLLYKVLHLITVENIKPEEILIFSLTNKAVDSIIENLLSIFENSHTNKEIVHQIGCYTVHGLANRIVVENEGMINIIEEIGWRGLMKLLPPSKRTPHHFRSYKELEKVVKDYKLNNAKNNNPVIEKLVELMDNCKVMTNDDLIIRAKKYLELDSSDSDASSFTQDLRNKYKVVLIDEFQDLYPSLAPLITMICKGKQLIMFGDTNQSIYGFLGSNNEIMSQLDNLHPKNSTTVLKLFDNFRSTPEIISLASKIINRPLAEKQIIDDTDETPSELVRKLPSGVSPQIMTFDDLAAESEFIIDKITQLICSSAKFSDIAILSRTNSHLTAIASILKKYGIPYQKLKSQPDWMDDLRIQFLLDILKVCSLASDEKHNREFNTGDKWQSNFSILVTMSALKGIGDASIQALYKACSLKNLSIWKYLTMVPNFEWPLGLSIKKKMENYTSNLYEMIENDQVHQLDDPMELLEKVASITNNLNLNPTYFQSLSDAQSSLEFKTHLQEMAQVMKVSKSNKPPGISFVKWFLETYFDQTMVFHQSQQALQTTGPGTVKLSTIHSAKGLEFPIVFLTNGSMSNFPMDTNALYVGITRARNLLYMCNMKHERLVSKSSPYSRNIMSNNLFWTYYNKDLKRSVCDVKVTHGYNVQRYNQLRKNFGFYRAYSSLRGCKSVFRRI
Protein: SHC-transforming protein 1 (SHC-transforming protein A) (Src homology 2 domain-containing-transforming protein C1) (SH2 domain protein C1) (P98083)
Organism: Mus musculus (Mouse)
Function: Signaling adapter that couples activated growth factor receptors to signaling pathways. Participates in signaling downstream of the angiopoietin receptor TEK/TIE2, and plays a role in the regulation of endothelial cell migration and sprouting angiogenesis (By similarity). Participates in a signaling cascade initiated by activated KIT and KITLG/SCF. Isoform p47Shc and isoform p52Shc, once phosphorylated, couple activated receptor kinases to Ras via the recruitment of the GRB2/SOS complex and are implicated in the cytoplasmic propagation of mitogenic signals. Isoform p47Shc and isoform p52 may thus function as initiators of the Ras signaling cascade in various non-neuronal systems. Isoform p66Shc does not mediate Ras activation, but is involved in signal transduction pathways that regulate the cellular response to oxidative stress and life span. Isoform p66Shc acts as a downstream target of the tumor suppressor p53 and is indispensable for the ability of stress-activated p53 to induce elevation of intracellular oxidants, cytochrome c release and apoptosis. The expression of isoform p66Shc has been correlated with life span.
Subcellular location: Cytoplasm {ECO:0000250}. Cell junction, focal adhesion {ECO:0000250|UniProtKB:P29353}.; SUBCELLULAR LOCATION: [Isoform p47Shc]: Mitochondrion matrix {ECO:0000250}. Note=Targeting of isoform p47Shc to mitochondria is mediated by its first 32 amino acids, which behave as a bona fide mitochondrial targeting sequence. Isoform p52Shc and isoform p66Shc, that contain the same sequence but more internally located, display a different subcellular localization (By similarity). {ECO:0000250}.; SUBCELLULAR LOCATION: [Isoform p66Shc]: Mitochondrion {ECO:0000269|PubMed:17272725}. Note=In case of oxidative conditions, phosphorylation at 'Ser-36' of isoform p66Shc, leads to mitochondrial accumulation.
Interaction partners:
- High affinity nerve growth factor receptor
- Epidermal growth factor receptor
- Insulin-like growth factor 1 receptor
- Son of sevenless homolog 1
- Son of sevenless homolog 2
- Growth factor receptor-bound protein 2
- GRB2-associated-binding protein 1
- Proto-oncogene tyrosine-protein kinase Src
- Receptor tyrosine-protein kinase erbB-2
- Receptor tyrosine-protein kinase erbB-3
Sequence:
MDLLPPKPKYNPLRNESLSSLEEGASGSTPPEELPSPSASSLGPILPPLPGDDSPTTLCSFFPRMSNLKLANPAGGRLGPKGEPGKAAEDGEGSAGAALRDSGLLPLLQDMNKLSGGGGRRTRVEGGQLGGEEWTRHGSFVNKPTRGWLHPNDKVMGPGVSYLVRYMGCVEVLQSMRALDFNTRTQVTREAISLVCEAVPGAKGATRRRKPCSRPLSSILGRSNLKFAGMPITLTVSTSSLNLMAADCKQIIANHHMQSISFASGGDPDTAEYVAYVAKDPVNQRACHILECPEGLAQDVISTIGQAFELRFKQYLRNPPKLVTPHDRMAGFDGSAWDEEEEEPPDHQYYNDFPGKEPPLGGVVDMRLREGAARPTLPSAQMSSHLGATLPIGQHAAGDHEVRKQMLPPPPCPGRELFDDPSYVNIQNLDKARQAGGGAGPPNPSLNGSAPRDLFDMKPFEDALRVPPPPQSMSMAEQLQGEPWFHGKLSRREAEALLQLNGDFLVRESTTTPGQYVLTGLQSGQPKHLLLVDPEGVVRTKDHRFESVSHLISYHMDNHLPIISAGSELCLQQPVDRKV
Protein: Beta-defensin 127 (Beta-defensin 27) (DEFB-27) (Defensin, beta 127) (Q9H1M4)
Organism: Homo sapiens (Human)
Function: Has antibacterial activity.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Beta-defensin 125
- Beta-defensin 114
- Beta-defensin 134
- Beta-defensin 129
- Beta-defensin 126
- Beta-defensin 132
- Beta-defensin 124
- Defensin beta 118
- Beta-defensin 135
- Beta-defensin 110
Sequence:
MGLFMIIAILLFQKPTVTEQLKKCWNNYVQGHCRKICRVNEVPEALCENGRYCCLNIKELEACKKITKPPRPKPATLALTLQDYVTIIENFPSLKTQST
Protein: S-phase kinase-associated protein, putative (Q385F6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Polyubiquitin, putative
- Ubiquitin, putative
- Cyclin-dependent kinases regulatory subunit
- RING-type domain-containing protein
- RING-type domain-containing protein
- COP9 signalosome complex subunit 5
- uracil phosphoribosyltransferase
- DNA 3'-5' helicase
- Cullin, putative
- Cullin, putative
Sequence:
MAEEVSVQDVDFTEYCILESNDPTPVKFKVRREAAMMSGLLKDMLEDQNGGDPIIPIPNVSARTLKLVIKYMEHHHKERADPIEKPLKSNIEKIISPWDHDFLYTELVKDHDEKQHEVLIDVIMAANFLNVRDLLDLTCACVANMIRGKSAEQIRELFNIESDFTPEEEEKIREENRWCEEA