wanglab/gogpt-training-data huggingface dataset:
Protein: DNA dC->dU-editing enzyme APOBEC-3D (A3D) (A3DE) (EC 3.5.4.38) (Q96AK3)
Organism: Homo sapiens (Human)
Function: DNA deaminase (cytidine deaminase) which acts as an inhibitor of retrovirus replication and retrotransposon mobility via deaminase-dependent and -independent mechanisms. Exhibits antiviral activity against HIV-1. After the penetration of retroviral nucleocapsids into target cells of infection and the initiation of reverse transcription, it can induce the conversion of cytosine to uracil in the minus-sense single-strand viral DNA, leading to G-to-A hypermutations in the subsequent plus-strand viral DNA. The resultant detrimental levels of mutations in the proviral genome, along with a deamination-independent mechanism that works prior to the proviral integration, together exert efficient antiretroviral effects in infected target cells. Selectively targets single-stranded DNA and does not deaminate double-stranded DNA or single- or double-stranded RNA. Inhibits also the mobility of LTR and non-LTR retrotransposons.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:27289067, ECO:0000269|PubMed:27428332}. Cytoplasm, P-body.
Interaction partners:
- Cytidine deaminase
- Cytochrome c oxidase subunit 5A, mitochondrial
- Putative C->U-editing enzyme APOBEC-4
- Cytochrome c1, heme protein, mitochondrial
- Cytochrome c oxidase subunit 7C, mitochondrial
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
- Cytochrome b-c1 complex subunit 8
- Cytochrome b-c1 complex subunit 7
- Cytochrome c oxidase subunit 5B, mitochondrial
- Uncharacterized protein C1orf198
Sequence:
MNPQIRNPMERMYRDTFYDNFENEPILYGRSYTWLCYEVKIKRGRSNLLWDTGVFRGPVLPKRQSNHRQEVYFRFENHAEMCFLSWFCGNRLPANRRFQITWFVSWNPCLPCVVKVTKFLAEHPNVTLTISAARLYYYRDRDWRWVLLRLHKAGARVKIMDYEDFAYCWENFVCNEGQPFMPWYKFDDNYASLHRTLKEILRNPMEAMYPHIFYFHFKNLLKACGRNESWLCFTMEVTKHHSAVFRKRGVFRNQVDPETHCHAERCFLSWFCDDILSPNTNYEVTWYTSWSPCPECAGEVAEFLARHSNVNLTIFTARLCYFWDTDYQEGLCSLSQEGASVKIMGYKDFVSCWKNFVYSDDEPFKPWKGLQTNFRLLKRRLREILQ
Protein: Epsin 1 (B2MVI1)
Organism: Lampetra fluviatilis (European river lamprey) (Petromyzon fluviatilis)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MATSSLRRQMKNIVNNFSEAEVKVREATSNDPWGPSSSLMSEIADLTYNVVAFSEIMSMIWKRLNDHGKNWRHVYKALTLLDYLIKTGSERVAQQCKENIFAIQTLKDFQYVDRDGKDQGVNVREKSKQLVALLRDEDRLRGEREHALKTKERLAQGATGMGSNNKVTFGRGSSQPNLSTSYSDEYGKAGGSPASYHGYLEQARPQTSGEEELQLQLALAMSREEAEQEEHDKEERMRRGDDLRLQMALEESKRAKLAAKKEESSLLDLVDAFRPTVPQPSADPWGATPPPPAQADPWGAAAAAGGAQADPWPTIAGRAGVQAVSAPDPWLTSQPKAADPWNATGGGAGISIGGPSPTRSAHSDPWGPPPSKPLAAADPWGGGGGGTPSQAKPADPWGSMPSPASSQSGVNGSAGDDLSEFDSIRSSSRGHRGMAGGMDLLGGDDSGSRSPDAFELSGLSNSLSQQGMMAPPSCRKTPESFLGPNAALVNLDSLVSKSAPPPVPQAKNPFLGVAPAPAPSASSTPSATNPFQLNQPPSLTLNQLRSSPGLPAQAFAGGAVPLAPMPLVGGPPLGVIGMGPLPIGMPVMPGMPGALPMMPPGMMGNMPLSIPGVMGTLPPQPLAWAGDVSSAQSGQPGG
Protein: Protein ECM30 (Extracellular mutant protein 30) (Q06673)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Seems to be involved in cell wall organization and biogenesis.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Ubiquitin carboxyl-terminal hydrolase 15
- Uncharacterized protein YCR022C
- Uncharacterized protein YIR020C
- Putative uncharacterized protein YGR176W
Sequence:
MGNTDSKSSSILLNHCIALVRPEDADASSPSRTSSPSPSLSVDADPLSLNLSIFKLDSGPDVEALFSDKPNVPLDTVFNDFYLDFISVDVQDFSINSSFKKILHIISSLNPPNFNNLIVFLSLYIILSANSLPASRTGLHSSRLINAIKTLSILIPIYFDRVKSSTQDHYDVFWATQHEIEGLPLQNIPLGERLLLAILKLAFQDNFTTAVTAHPSELWEIGILTNSNKYRSLLNMHHQWHLFANRLLLLRLLAALFSSDLYTSGGKQDINMFLVYWCTQMPKDKSIQFTSSLLNCTMRFILNNNKDFQSLKANFFSSDATASNWQTLYFQFVQSCLHVLNLSMSYKAQDNVITIFLTQLQREYDLKLILSSFIKIFKYPIDLAIEQESNIFNFTNNKHIDASRRRAVSTSSHDNSSSSHASLPSSSSAAYHTKPQTKPQLPEIHPLLIPMTILMTNLIDCNKCFQNYFADKFASRFIIFSIYYLKYYDYSSLSSSSSTTRSNSSTTSNGTSNDTSNERSIVELNENSVSQILLPLLNHLLLILTSKKLVLFKMLQTFNLNYYTNNLPNFYKLSNINGDINNLTFRDFTVIQLSNLILDNIKFNLQPNPIFYELIYNLLPINDEILTSSHKNDDSHDDLILLSAKKKSASPSAATSSHTSSSKLSYNAAMSLLYVLSKSSNKVYLTTYATPVFKTKDIPYMISPGFKMDLLALLLRSITIFFTLYFDDAENLLFAMVRHQSITHQINDSINSISKALDMNPNLNSHIMTLKQMGFNRKVQWKDFYQFEEITDLPQVNLYSSANQQHQNQQQGQNDNRGQNQNEDPGQENESPTPYLLFNPASLENETPGTVKHFSSTNHDKNYQVIAFIDFKSDSNLNLQHQLEYWPHRPQWPTPLTFTHKCKNPKYENFNEVWSGTVYLQILLRVIKQILSKVPEIPRIKSVQYFETLSKLSALRSDILTTIHPRLPLDVRRLTTFQPLSMHTNDKLLMWFHIATWANIFTQTSFKYEETFSHELRQFESLLDISIDECEGNTISKPTTDRLGYIRRSRGQSSVSLERTISAGSGVSTPTMALNRTKSNGSGNLMNYFFQNTAQNHFQHLRSSSSSSSITLEKTTSNSSSIRTRPNSHHVAPETNNNNSTNGNSNNSSNGGFSFFKWKWGGNNSNGGSDDTKASQRDPNVSTSIITDNLNSYMFEEEISPGVVNNIIENNIWVGTDIRLFKIANFRKESFSFLEMTSSFFKKFKFINSDNDNYNNNEFDDNTQLRYTSRGLYR
Protein: Protein kinase domain-containing protein (A0A178VQN9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
Sequence:
MKLPSILSLVVSSIFLCMSFCSSLNSDGLSLLALKSAVDNDPTRVMTHWSESDPTPCHWSGIVCTNGRVTTLVLFGKSLSGYIPSELGLLNSLNRLDLAHNNFSKTIPVRLFEATKLRYIDLSHNSLSGPIPAQIKSMKSLNHLDFSSNHLNGSLPESLTELGSLVGTLNFSFNQFTGEIPPSYGRFRVHVSLDFSHNNLTGKVPQVGSLLNQGPNAFAGNSHLCGFPLQTPCEKIKTPNFVAAKPEGTQELQKPNPSVISNDDAKEKKQQITGSVTVSLISGVSVVIGAVSLSVWLIRRKRSSDGYNSETKTTTVVSEFDEEGQEGKFVAFDEGFELELEDLLRASAYVIGKSRSGIVYRVVAAESSSTVVAVRRLSDGNDTWRFKDFVNEVESIGRINHPNIVRLRAYYYAEDEKLLITDFINNGSLYSALHGGPSNTRPTLSWAERLCIAQGTARGLMYIHEYSSRKYVHGNLKSSKILLDNELHPHVSGFGLTRLVSGYPKVTDHSLSSMTQSIDQGFATRLSVSAPAAAYLAPEARASSDCKLSHKCDVYSFGVILLELLTGRLPYGSSENEGEEELVNVLRKWHKEERSLAEILDPKLLKQDFANKQVIATIHVALNCTEMDPDMRPRMRSVSEILGRIK
Protein: Probable ergothioneine transporter EgtUBC (Q8Y775)
Organism: Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)
Subcellular location: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Quaternary amine transport ATP-binding protein
- Quaternary amine transport ATP-binding protein
- OpuCC protein
- OpuCB protein
- OpuCD protein
- GbuC protein
- Spermidine/putrescine import ATP-binding protein PotA
- Lmo0553 protein
- Quaternary amine transport ATP-binding protein
- Inosine-5'-monophosphate dehydrogenase
Sequence:
MNTLIDTFTVRKDELFTALVQHIQISFVSLFIAVLIALPLGIYLTRHKRLAEPIIQVAAIFQTIPSLALLGLLIPLVGIGIVPAIIALVIYALLPILRNTYTGIKEVDPALVEASRAMGMNKWKRLYKVQLPLAMPVIMAGIRTAMVLIIGTATLAALIGAGGLGDLILLGIDRNDNSLILLGAIPAALLAILFDFLLRFLEKASFKSTIITISAGILLTAAIIVVPYFASDKKEITIAGKLGAEPEILINMYKLVIEDETDLKVNVKPNMGKTSFVFNALKSGDIDIYPEFTGTVLETFLKENAKTHDPEEVYTQARDGLAKDFDMTYLKPMKYNNTYALAVSPEFAKENNLEKISDLGPVSDQVKAGFTLEFKDRSDGYKGIQDKYGLTFSNLKTMEPKLRYNAIKSGDINLLDAYSTDSELAQYKLKVLEDDQQLFPPYQGAPLMLTKTLDKYPELKKPLNKLAGKITDDEMRKMNYEVNVNGKSAYTVAKDYLKDQGIIK
Protein: Adenylosuccinate lyase (ASL) (EC 4.3.2.2) (Adenylosuccinase) (ASase) (P54822)
Organism: Mus musculus (Mouse)
Function: Catalyzes two non-sequential steps in de novo AMP synthesis: converts (S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido)succinate (SAICAR) to fumarate plus 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide, and thereby also contributes to de novo IMP synthesis, and converts succinyladenosine monophosphate (SAMP) to AMP and fumarate.
Interaction partners:
- Bifunctional phosphoribosylaminoimidazole carboxylase/phosphoribosylaminoimidazole succinocarboxamide synthetase
- Bifunctional purine biosynthesis protein ATIC
- Adenylosuccinate synthetase isozyme 2
- Adenylosuccinate synthetase isozyme 1
- Trifunctional purine biosynthetic protein adenosine-3
- Amidophosphoribosyltransferase
- Adenine phosphoribosyltransferase
- Adenosine kinase
- AMP deaminase 2
- AMP deaminase 1
Sequence:
MAASGDPGSAESYRSPLAARYASREMCFLFSDRYKFQTWRQLWLWLAEAEQTLGLPITDEQIQEMKSNLNNIDFQMAAEEEKRLRHDVMAHVHTFGHCCPKAAGIIHLGATSCYVGDNTDLIILRNAFDLLLPKLARVISRLADFAKDRADLPTLGFTHFQPAQLTTVGKRCCLWIQDLCMDLQNLKRVRDELRFRGVKGTTGTQASFLQLFEGDHQKVEQLDKMVTEKAGFKRAFIITGQTYTRKVDIEVLSVLASLGASVHKICTDIRLLANLKEMEEPFEKQQIGSSAMPYKRNPMRSERCCSLARHLMALTMDPLQTASVQWFERTLDDSANRRICLAEAFLTADTILNTLQNISEGLVVYPKVIERRIRQELPFMATENIIMAMVKAGGSRQDCHEKIRVLSQQAAAVVKQEGGDNDLIERIRADAYFSPIHSQLEHLLDPSSFTGRAPQQVHRFLEEEVRPLLKPYGNEMAVKAELCL
Protein: Putative mitochondrial transporter UCP3 (Solute carrier family 25 member 9) (Uncoupling protein-3) (UCP 3) (P55916)
Organism: Homo sapiens (Human)
Function: UCP are mitochondrial transporter proteins that create proton leaks across the inner mitochondrial membrane, thus uncoupling oxidative phosphorylation. As a result, energy is dissipated in the form of heat. May play a role in the modulation of tissue respiratory control. Participates in thermogenesis and energy balance.
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P56501}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Peroxisome proliferator-activated receptor gamma coactivator 1-alpha
- Carnitine O-palmitoyltransferase 1, muscle isoform
- Palmitoyl thioesterase CPT1C
- Peroxisome proliferator-activated receptor gamma
- Peroxisome proliferator-activated receptor delta
- [Pyruvate dehydrogenase
- Peroxisome proliferator-activated receptor alpha
- Beta-3 adrenergic receptor
- Carnitine O-palmitoyltransferase 1, liver isoform
- Appetite-regulating hormone
Sequence:
MVGLKPSDVPPTMAVKFLGAGTAACFADLVTFPLDTAKVRLQIQGENQAVQTARLVQYRGVLGTILTMVRTEGPCSPYNGLVAGLQRQMSFASIRIGLYDSVKQVYTPKGADNSSLTTRILAGCTTGAMAVTCAQPTDVVKVRFQASIHLGPSRSDRKYSGTMDAYRTIAREEGVRGLWKGTLPNIMRNAIVNCAEVVTYDILKEKLLDYHLLTDNFPCHFVSAFGAGFCATVVASPVDVVKTRYMNSPPGQYFSPLDCMIKMVAQEGPTAFYKGFTPSFLRLGSWNVVMFVTYEQLKRALMKVQMLRESPF
Protein: Spectrin beta chain (A0A0G2JZY6)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
Sequence:
MELQRTSSISGPLSPAYTGQVPYNYNQLEGRFKQLQDEREAVQKKTFTKWVNSHLARVSCRITDLYTDLRDGRMLIKLLEVLSGERLPKPTKGRMRIHCLENVDKALQFLKEQRVHLENMGSHDIVDGNHRLTLGLIWTIILRFQIQDISVETEDNKEKKSAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQHLGLTKLLDPEDISVDHPDEKSIITYVVTYYHYFSKMKALAVEGKRIGKVLDNAIETEKMIEKYESLASDLLEWIEQTIIILNNRKFANSLVGVQQQLQAFNTYRTVEKPPKFTEKGNLEVLLFTIQSKMRANNQKVYMPREGKLISDINKAWERLEKAEHERELALRNELIRQEKLEQLARRFDRKAAMRETWLSENQRLVSQDNFGFDLPAVEAATKKHEAIETDIAAYEERVQAVVAVARELEAESYHDIKRITARKDNVIRLWEYLLELLRARRQRLEMNLGLQKIFQEMLYIMDWMDEMKVLLLSQDYGKHLLGVEDLLQKHALVEADIAIQAERVRGVNASAQKFATDGEGYKPCDPQVIRDRVAHMEFCYQELCQLAAERRARLEESRRLWKFFWEMAEEEGWIREKEKILSSDDYGKDLTSVMRLLSKHRAFEDEMSGRSGHFEQAIKEGEDMIAEEHFGSEIRERISYIREQWANEQLSAIRKKRLEEASLLHQFQADADDIDAWMLDILKIVSSNDVGHDEYSTQSLVKKHKDVAEEISNYRPTIDTLHEQAGALPQAHAESPDVKGRLAGIEERYKEVAELTRLRKQALQDTLALYKMFSEADACELWIDEKEQWLNNMQIPEKLEDLEVIQHRFESLEPEMNNQASRVAVVNQIARQLMHSGHPSEKEIRAQQDKLNTRWSQFRELVDRKKDALLSALSIQNYHLECNETKSWIREKTKVIESTQDLGNDLAGVMALQRKLTGMERDLVAIEAKLSDLQKEAEKLESEHPDQAQAILSRLAEISDVWEEMKTTLKNREASLGEASKLQQFLRDLDDFQSWLSRTQTAIASEDMPNTLTEAEKLLTQHENIKNEIDNYEEDYQKMRDMGEMVTQGQTDAQYMFLRQRLQALDTGWNELHKMWENRQNLLSQSHAYQQFLRDTKQAEAFLNNQEYVLAHTEMPTTLEGAEAAIKKQEDFMTTMDANEEKINAVVETGRRLVSDGNINSDRIQEKVDSIDDRHRKNREAASELLMRLKDNRDLQKFLQDCQELSLWINEKMLTAQDMSYDEARNLHSKWLKHQAFMAELASNKEWLDKIEKEGMQLISEKPETEAVVKEKLTGLHKMWEVLESTTQTKAQRLFDANKAELFTQSCADLDKWLHGLESQIQSDDYGKDLTSVNILLKKQQMLENQMEVRKKEIEELQSQAQALSQEGKSTDEVDSKRLTVQTKFMELLEPLNERKHNLLASKEIHQFNRDVEDEILWVGERMPLATSTDHGHNLQTVQLLIKKNQTLQKEIQGHQPRIDDIFERSQNIITDSSSLNAEAIRQRLADLKQLWGLLIEETEKRHRRLEEAHKAQQYYFDAAEAEAWMSEQELYMMSEEKAKDEQSAVSMLKKHQILEQAVEDYAETVHQLSKTSRALVADSHPESERISMRQSKVDKLYAGLKDLAEERRGKLDERHRLFQLNREVDDLEQWIAEREVVAGSHELGQDYEHVTMLQERFREFARDTGNIGQERVDTVNHMADDLINSGHSDAATIAEWKDGLNEAWADLLELIDTRTQILAASYELHKFYHDAKEIFGRIQDKHKKLPEELGRDQNTVETLQRMHTTFEHDIQALGTQVRQLQEDAARLQAAYAGDKADDIQKRENEVLEAWKSLLDACEGRRVRLVDTGDKFRFFSMVRDLMLWMEDVIRQIEAQEKPRDVSSVELLMNNHQGIKAEIDARNDSFTACIELGKALLARKHYASEEIKEKLLQLTEKRKEMIDKWEDRWEWLRLILEVHQFSRDASVAEAWLLGQEPYLSSREIGQSVDEVEKLIKRHEAFEKSAATWDERFSALERLTTLELLEVRRQQEEEERKRRPPSPEPSAKVSEEAESQQWDTSKGDQVSQNGLPAEQGSPRVSYRSQTYQNYKNFNSRRTASDHSWSGL
Protein: Reduced mechanoreceptor potential A, isoform B (Q7KTZ4)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell projection, cilium {ECO:0000256|ARBA:ARBA00004138}.
Interaction partners:
- Outer segment 6
- Intraflagellar transport protein 122 homolog
- Intraflagellar transport 43
- WD repeat-containing protein 35
- Intraflagellar transport 52
- No mechanoreceptor potential B, isoform D
- Intraflagellar transport protein 57 homolog
- Outer segment 5
- Intraflagellar transport 20
- Intraflagellar transport protein 46 homolog
Sequence:
MTLYFDTKIEFLDSDAVSTISSWHPSEPLFAVASFSPERGGSVTIFADTGEPQRDVTYPVHATSQATALCWHPEKALLASGWEHGDIHVWFAGHREFASVNAPHKAAIVLLQFSEQGGRMVTADAMGLVTGWRCDGQYQFLTMFSHDLREVLLLICFRLTVESEVREEMANLAKAAVAGDENALDTLTNWRPRTAARSMTHSGVRDNHCFYACTQGGVVYYINQGGACVEVMKCGSLPPIVQMLWHPRKDAVICLMEDLTVTLFLVESTGILTELDRVKMSGRGGGRQGGIAWSGNSLAIITGDFFVRIWDIERSDNYLLKMDLPSGNQPGSSMTTLSNGTMSSSNQFFSHDSSESSGVLRKTPKYGQLNGEMFTCLAYSSTGQTLCAGTSQGNVYTWKRSGSRLVGAPEDAWQLTNISSVRGAIRSCEWGYNELAKPCMLVNCLSNVFMLKEQPLLAVHTRELWAVQRSAKSVQLTHCSGREAIVQSEFAVTAMALSELSLVMSNGRSISSYSLQKVEKSLDEFEEILQTVEGTTPTTESTTTPLSLKLLQTFAAECLALNLCNQNIFCLGSSDVFVYSVGGVVLHRIQASDIEGKIIGMDLSGCYLSVFTMNGYVKAYDVSRHDPKLLFPSKSGHDIFDDFGEFILVKCNSSGSHLAMVIASSNFTPISTLFCWDFERSNLLEYGLLEPETNAKKESSTSLPVRIFWDAEEPRLLATEVKSMIQKTLPQKNSLQPSHFVQSKVVLLFYSEKGCLNVLETQSMSPGCQLLNLCVPNVIRLKINTMEEQPLQDFVDLQQCNPVTRKQVLNFSLYVAEGNMDMAYRSIRSIQSKVIWTNLAKMCVHTNRLDVAKVCMGHLEQARSVRALRQAIEDDDLETEAKVAVLAIELGMIEEAKDLYRRCKRFDLLNKLLQSIGHLDEAVELAEAEDRIHLKHTYYQKAQELRERGDIKGALEYFEKTQNPAQNITQLLLENPGAMKRYIQTTSDPKLLKWWGQYIESSGDMDAALAVYHKAEDWFSQVKILCYLGKISKADAIARQSGDRAACYHLARHYENVGKFQEAIMFFTRAQTFSNAIRICKENDFQEELWTVASSSRQRDKAIAAAYFEECGNFKHAVELYHRAGMLHKALEMAFESQQPEILEIIASDLAPDSDAELINRCADFFCSIEQFQKAVHLLAKTRHLERALGICSEKGVPVTEELSEMLTPEKGEFEEATRVHILVQLGEFLQQQGDYHSATKKFTQAGDKIRAMKSLLKSGNTDKIIFFANMSRQREVYIMAANYLQALDWQSDPQVLKHIVTFYTKGQAFDSLANFYAICAQIEIEEFQDYGKALTAMQEASKCLEKLSHAQHVYNNLQRTVADVKAILEIQQALREGDHQLVIGSCRSMLIKPELPPIRHAHILAMLIRALVYVKDYSEAGRALKELTVKDSTWSASGLLDRSIVHKIAQECHLEFDLIWNAGRQVTASTSGTAATGMSSTSGMTTTDDDDADDEEITEELH
Protein: Type 1 phosphatases regulator YPI1 (P43587)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Regulator of type 1 phosphatases which maintains protein phosphatase activity under strict control. Regulates the nuclear localization of type 1 phosphatase GLC7 and SDS22, and is involved in the regulation of mRNA 3'-end processing. May also regulate the activity of type 1 phosphatase PPZ1.
Subcellular location: Nucleus {ECO:0000269|PubMed:17142459, ECO:0000269|PubMed:18172024}.
Interaction partners:
- Protein phosphatase 1 regulatory subunit SDS22
- Serine/threonine-protein phosphatase PP1-2
- UBX domain-containing protein 1
- Protein GLC8
- Serine/threonine-protein phosphatase PP-Z1
- Serine/threonine-protein phosphatase PP-Z2
- Serine/threonine-protein phosphatase PPQ
- Aurora kinase
- GLC7-interacting protein 2
Sequence:
MSGNQMAMGSEQQQTVGSRTVSVEEVPAVLQLRATQDPPRSQEAMPTRHNVRWEENVIDNENMNKKKTKICCIFHPQNEDEEECNHHSDDDGSSSSGSSSSESENEKDLDFNERRQRRLERRHRKLEKKRSYSPNAYEIQPDYSEYRRKQQEKKD
Protein: Protein FRG1 homolog (Q9VWA8)
Organism: Drosophila melanogaster (Fruit fly)
Function: May have a role in processing of pre-rRNA or in the assembly of rRNA into ribosomal subunits (By similarity). May be involved in epigenetic regulation of muscle differentiation through regulation of the activity of the histone-lysine N-methyltransferase Suv4-20.
Subcellular location: Nucleus, Cajal body {ECO:0000250}. Nucleus, nucleolus {ECO:0000250}. Cytoplasm {ECO:0000250}. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000250}.
Interaction partners:
- Pre-mRNA-splicing factor CWC22 homolog
- Pre-mRNA-processing-splicing factor 8
- Pre-mRNA-processing factor 19
- Pre-mRNA-processing factor 17
- Pre-mRNA-splicing factor syf1 homolog
- Small nuclear ribonucleoprotein F
- 116 kDa U5 small nuclear ribonucleoprotein component
Sequence:
MSDYDHARIKKLVLKGEKLKKSKKRKKEKDEAGSSKKAKVVVDEDAVKHGGWWAAKTAADITGTVSIEFGDRSYLKAMDNGLFTLGAPHNAGDGPDPEEIFTAFPINDRKVAFKSGYGKYLKIEKDGMVTGRSEAVGGMEQWEPVFEEQRMALLSETGHFMSIDPQDDACVALRKKVGQHEICKVRSNASRDVVIDTEPKEEKGDLGEVEKNYVKKFQKFQDKKMRINQNDVKELEQAKAQGSLHETLLDRRSKMKADRYCK
Protein: Apoptosis-stimulating of p53 protein 1 (Protein phosphatase 1 regulatory subunit 13B) (Q96KQ4)
Organism: Homo sapiens (Human)
Function: Regulator that plays a central role in regulation of apoptosis via its interaction with p53/TP53. Regulates TP53 by enhancing the DNA binding and transactivation function of TP53 on the promoters of proapoptotic genes in vivo.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11684014}. Nucleus {ECO:0000269|PubMed:11684014}. Note=Predominantly cytoplasmic. Some fraction is nuclear.
Interaction partners:
- Cellular tumor antigen p53
- Serine/threonine-protein phosphatase PP1-alpha catalytic subunit
- Ras association domain-containing protein 8
- Ras association domain-containing protein 7
- Hypoxia-inducible factor 1-alpha inhibitor
- Serine/threonine-protein phosphatase PP1-gamma catalytic subunit
- Serine/threonine-protein phosphatase PP1-beta catalytic subunit
- Tumor protein p73
- Apoptosis-stimulating of p53 protein 2
Sequence:
MMPMILTVFLSNNEQILTEVPITPETTCRDVVEFCKEPGEGSCHLAEVWRGNERPIPFDHMMYEHLQKWGPRREEVKFFLRHEDSPTENSEQGGRQTQEQRTQRNVINVPGEKRTENGVGNPRVELTLSELQDMAARQQQQIENQQQMLVAKEQRLHFLKQQERRQQQSISENEKLQKLKERVEAQENKLKKIRAMRGQVDYSKIMNGNLSAEIERFSAMFQEKKQEVQTAILRVDQLSQQLEDLKKGKLNGFQSYNGKLTGPAAVELKRLYQELQIRNQLNQEQNSKLQQQKELLNKRNMEVAMMDKRISELRERLYGKKIQLNRVNGTSSPQSPLSTSGRVAAVGPYIQVPSAGSFPVLGDPIKPQSLSIASNAAHGRSKSANDGNWPTLKQNSSSSVKPVQVAGADWKDPSVEGSVKQGTVSSQPVPFSALGPTEKPGIEIGKVPPPIPGVGKQLPPSYGTYPSPTPLGPGSTSSLERRKEGSLPRPSAGLPSRQRPTLLPATGSTPQPGSSQQIQQRISVPPSPTYPPAGPPAFPAGDSKPELPLTVAIRPFLADKGSRPQSPRKGPQTVNSSSIYSMYLQQATPPKNYQPAAHSALNKSVKAVYGKPVLPSGSTSPSPLPFLHGSLSTGTPQPQPPSESTEKEPEQDGPAAPADGSTVESLPRPLSPTKLTPIVHSPLRYQSDADLEALRRKLANAPRPLKKRSSITEPEGPGGPNIQKLLYQRFNTLAGGMEGTPFYQPSPSQDFMGTLADVDNGNTNANGNLEELPPAQPTAPLPAEPAPSSDANDNELPSPEPEELICPQTTHQTAEPAEDNNNNVATVPTTEQIPSPVAEAPSPGEEQVPPAPLPPASHPPATSTNKRTNLKKPNSERTGHGLRVRFNPLALLLDASLEGEFDLVQRIIYEVEDPSKPNDEGITPLHNAVCAGHHHIVKFLLDFGVNVNAADSDGWTPLHCAASCNSVHLCKQLVESGAAIFASTISDIETAADKCEEMEEGYIQCSQFLYGVQEKLGVMNKGVAYALWDYEAQNSDELSFHEGDALTILRRKDESETEWWWARLGDREGYVPKNLLGLYPRIKPRQRTLA
Protein: Aquaporin (Q8IG23)
Organism: Caenorhabditis elegans
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MTAEEDTLPERLRFHGVHTNILARNLIAEFFGTFLLCFIGLSIVFQFHAGGGKTTEWIGVNIGWGFAIMFAVMATARMSGGHLNPAVSLLLWSLGHLKLAWVPLYAIAQTAGAFVASLGMYSYYYEQFNAFDGGNRTILGATGTAGCFASYPSPNLGVWGPYIDQCVGTGVLAYFLCVVIDERNQIPKIWHPMFFGFLVMMIGTGFGMNIGYPINPARDLGPRLFSYFIYGPGVFHSPYPNYWLAPAIAPFVGALVGGWFYHFSLGMHNPDIEEADDIFVQQPPKSVEQQKLLQA
Protein: Flotillin (C0H9R4)
Organism: Salmo salar (Atlantic salmon)
Subcellular location: Membrane {ECO:0000256|RuleBase:RU366054}. Endosome {ECO:0000256|RuleBase:RU366054}.
Interaction partners:
- Sorbin and SH3 domain-containing protein 1-like isoform X1
Sequence:
MFHTCGPNEAMVVSGFGRSPPLMIAGGRVFVLPCIQQIQRITLNTLTLNVKSDKVYTRHGVPISVTGIAQVKIQGQNKEMLATACQMFMGKSEAEVSNIALETLEGHQRAIIAHLTVEEIYQDRKKFSEQVFKVASSDLVNMGIGVVSYTLKDVHDDQDYLNSLGKARTAQVQKDARIGEAQYKRDAVIREAQAMQEKVSAQYLNEIEMAKAQRDYELKKASYDYEVNTKKAESEMAYQLQVAKTKQRIEEETMQVKVVERSQQIMLQEQEITRKEMELEAKVKKPAEAERYRLERLAEAERAQLIMEAEAEAESIRMRGDAEAFALEAKGRAEAEQMAKKAEAFKQYGEGAMVDMLLEKLPLIAEEISRPLSMAQKVTMVSSGGGEVGAAKLTGEVLDIMTRLPAAVEKLTGINISQVGLSTRMG
Protein: Small ubiquitin-related modifier 1 (AtSUMO1) (Ubiquitin-like protein SMT3) (P55852)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Ubiquitin-like protein which can be covalently attached to target lysines as a monomer. Does not seem to be involved in protein degradation and may function as an antagonist of ubiquitin in the degradation process. Required for the massive protein sumoylation in the nucleus induced by heat shock and controlled by SIZ1. Involved in the regulation of the heat stress transcription factor HSFA2 in acquired thermotolerance.
Subcellular location: Nucleus {ECO:0000269|PubMed:20521085}. Cytoplasm {ECO:0000250|UniProtKB:Q9FLP6}.
Interaction partners:
- SUMO-conjugating enzyme SCE1
- E3 SUMO-protein ligase SIZ1
- SUMO-activating enzyme subunit 2
- Ubiquitin-like-specific protease ESD4
- E3 SUMO-protein ligase MMS21
- E4 SUMO-protein ligase PIAL2
- SUMO-activating enzyme subunit 1B-1
- E4 SUMO-protein ligase PIAL1
- RAN GTPase-activating protein 1
- SUMO-activating enzyme subunit 1A
Sequence:
MSANQEEDKKPGDGGAHINLKVKGQDGNEVFFRIKRSTQLKKLMNAYCDRQSVDMNSIAFLFDGRRLRAEQTPDELDMEDGDEIDAMLHQTGGSGGGATA
Protein: Extracellular superoxide dismutase [Cu-Zn] (EC-SOD) (EC 1.15.1.1) (Superoxide dismutase B) (Q08420)
Organism: Rattus norvegicus (Rat)
Function: Protect the extracellular space from toxic effect of reactive oxygen intermediates by converting superoxide radicals into hydrogen peroxide and oxygen.
Subcellular location: Secreted, extracellular space. Golgi apparatus, trans-Golgi network {ECO:0000250|UniProtKB:O09164}.
Interaction partners:
- Superoxide dismutase, mitochondrial
- Copper chaperone for superoxide dismutase
- Parkinson disease protein 7 homolog
- Catalase
- Glutathione peroxidase 1
- Glutathione peroxidase 3
- Glutathione peroxidase
- Copper transport protein ATOX1
- Glutathione peroxidase
- Glutathione peroxidase 2
Sequence:
MVAFLFCNLLLVACGSVTWTMSDTGESGVDLADRLDLVEKIGDTHSKDLEIWMELGKQREADAREMHAVCRVQPSAMLPPDQPQITGLVLFRQLGPSSRLEASFNLEGFPAEQNTSNHAIHVHEFGDLSQGCESTGPHYNPLGVPHPQHPGDFGNFVVRDGRLWKHRMGLATSLAGPHSILGRAVVVHAGEDDLGKGGNQASVQNGNAGRRLACCVVGTSNSEAWESQTKERKKRRRESECKTT
Protein: ATP-binding cassette sub-family D member 1 (EC 7.6.2.4) (Q7JUN3)
Organism: Drosophila melanogaster (Fruit fly)
Function: Plays a role in the transport of free very-long-chain fatty acids (VLCFAs) as well as their CoA-esters across the peroxisomal membrane by acting as an ATP-specific binding subunit releasing ADP after ATP hydrolysis. Thus, plays a role in regulation of VLCFAs and energy metabolism namely, in the degradation and biosynthesis of fatty acids by beta-oxidation, mitochondrial function and microsomal fatty acid elongation.
Subcellular location: Peroxisome membrane {ECO:0000250|UniProtKB:P33897}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- ATP binding cassette subfamily A member 3, isoform B
- ATP-binding cassette sub-family D member 3
- Peroxin-19
- Sterol carrier protein 2
- Peroxin 11
- Peroxisomal membrane protein PEX13
- long-chain-fatty-acid--CoA ligase
- Protein Pixie
- Peroxisomal multifunctional enzyme type 2
- ATP-binding cassette sub-family B member 6
Sequence:
MSVLSKYVDRIAEKCEHNGFTKHAFSYALVTSAILALTIKVTIPYVKNVNTTSSVRTQKGKTNGQLSPSTRDSSEEDFKLAEAEKLLVAQQLKKKATNNLVEPGLNKEFLKHLQMLAKIMIPQAFCYETGLLSVHTFCLISRTFLSIYVAALEGALVKFIVRKDIKQFALVLLKWFGIAIPATFVNSMIRFLESKLSLAFRTRLVRHSYRLYFKNQNYYRVSNLDGRIENADHRLTEDISVFANSVAHLYSSLTKPCFDLMLIGLALMRSSKKMKANIITGPALSIGVIALTAHILRIVSPKFGQLVSEEANRYGYLRHIHSRIITNAEEIAFYGGHKVEMQQLRQAYNRLVNQMTTIFNQKLWFIMLEQFFMKYVWSGTGMIMVSLPILTGSDVGLGTVPNTAISESRVSERTQYLTTARNLLISAADAIERLMSSYKEIVSLAGYTFRVAGMMDVFEETALGVYCKTSVMESNQSNGIIEFRNGKPIAKGRIIYSDDPKNMSISLRAVPVVTPNCDIVVPKLTLCIEPGVHLLITGPNGCGKSSLFRILSGLWPIYAGELHIPRPVKDVPCMFYIPQRPYMSIGSLCDQIIYPDTREDMKRKHITENELRSILKMVSLEHIAQRDSFDVVRDWKDILSGGEKQRMAIARLFYHRPRYALLDECTSAVSIDVESSIYEIAKGMGITLLTITHRPTLWKYHTHILEFDGLGNWQFRKMNSDEEQKGQFLS