wanglab/gogpt-training-data huggingface dataset:
Protein: Anoctamin-4 (Transmembrane protein 16D) (Q8C5H1)
Organism: Mus musculus (Mouse)
Function: Has calcium-dependent phospholipid scramblase activity; scrambles phosphatidylserine, phosphatidylcholine and galactosylceramide. Does not exhibit calcium-activated chloride channel (CaCC) activity.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q32M45}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q32M45}. Note=Shows an intracellular localization according to PubMed:22075693. {ECO:0000269|PubMed:22075693}.
Interaction partners:
Sequence:
MEASSSGITNGKNKVFHAEGGLDLQSHQLDMQILPDGPKSDVDFSEILNAIQEMAKDVNILFDELEAVNSPCKDDDSLLHPGNLTSTSEDTSRLEAGGETVRERNKSNGLYFRDGKCRIDYILVYRKSNPQTEKREVFERNIRAEGLQMEKESSLINSDIIFVKLHAPWEVLGRYAEQMNVRMPFRRKIYYLPRRYKFMSRIDKQISRFRRWLPKKPMRLDKETLPDLEENDCYTAPFSQQRIHHFIIHNKDTFFNNATRSRIVHHILQRIKYEEGKNKIGLNRLLTNGSYEAAFPLHEGSYRSKNSIKTHGAVNHRHLLYECWASWGVWYKYQPLDLVRRYFGEKIGLYFAWLGWYTGMLFPAAFIGLFVFLYGVTTLDHCQVSKEVCQATDIIMCPVCDKYCPFMRLSDSCVYAKVTHLFDNGATVFFAVFMAVWATVFLEFWKRRRAVIAYDWDLIDWEEEEEEIRPQFEAKYSKKERMNPISGKPEPYQAFTDKCSRLIVSASGIFFMICVVIAAVFGIVIYRVVTVSTFAAFKWALIRNNSQVATTGTAVCINFCIIMLLNVLYEKVALLLTNLEQPRTESEWENSFTLKMFLFQFVNLNSSTFYIAFFLGRFTGHPGAYLRLINRWRLEECHPSGCLIDLCMQMGIIMVLKQTWNNFMELGYPLIQNWWTRRKVRQEHGTERKINFPQWEKDYNLQPMNAYGLFDEYLEMILQFGFTTIFVAAFPLAPLLALLNNIIEIRLDAYKFVTQWRRPLASRAKDIGIWYGILEGIGILSVITNAFVIAITSDFIPRLVYAYKYGPCAGQGEAGQKCMVGYVNASLSVFRISDFENRSEPESDGSEFSGTPLKYCRYRDYRDPPHSLAPYGYTLQFWHVLAARLAFIIVFEHLVFCIKHLISYLIPDLPKDLRDRMRREKYLIQEMMYEAELERLQKERKERKKNGKAHHNEWP
Protein: Ras-related protein Rab-6A (Rab-6) (EC 3.6.5.2) (P20340)
Organism: Homo sapiens (Human)
Function: Regulator of COPI-independent retrograde transport from the Golgi apparatus towards the endoplasmic reticulum (ER). Has a low GTPase activity. Recruits VPS13B to the Golgi membrane. Plays a role in neuron projection development (Probable).
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:23091056, ECO:0000269|PubMed:25962623}; Lipid-anchor {ECO:0000269|PubMed:25962623}. Cytoplasmic vesicle, secretory vesicle, acrosome membrane {ECO:0000250|UniProtKB:P35279}; Peripheral membrane protein {ECO:0000305}. Note=BICD2 facilitates its targeting to Golgi apparatus membrane. {ECO:0000269|PubMed:25962623}.; SUBCELLULAR LOCATION: [Isoform 1]: Golgi apparatus membrane {ECO:0000269|PubMed:11071909}; Lipid-anchor {ECO:0000305}.; SUBCELLULAR LOCATION: [Isoform 2]: Golgi apparatus membrane {ECO:0000269|PubMed:11071909}; Lipid-anchor {ECO:0000305}.
Interaction partners:
- GRIP and coiled-coil domain-containing protein 2
- Kinesin-like protein KIF20A
- DENN domain-containing protein 5A
- Protein bicaudal D homolog 2
- Protein bicaudal D homolog 1
- RAB6-interacting golgin
- ELKS/Rab6-interacting/CAST family member 1
- Inositol polyphosphate 5-phosphatase OCRL
- Rab GDP dissociation inhibitor alpha
- Vacuolar protein sorting-associated protein 53 homolog
Sequence:
MSTGGDFGNPLRKFKLVFLGEQSVGKTSLITRFMYDSFDNTYQATIGIDFLSKTMYLEDRTVRLQLWDTAGQERFRSLIPSYIRDSTVAVVVYDITNVNSFQQTTKWIDDVRTERGSDVIIMLVGNKTDLADKRQVSIEEGERKAKELNVMFIETSAKAGYNVKQLFRRVAAALPGMESTQDRSREDMIDIKLEKPQEQPVSEGGCSC
Protein: Legumain (EC 3.4.22.34) (Asparaginyl endopeptidase) (Protease, cysteine 1) (Q9R0J8)
Organism: Rattus norvegicus (Rat)
Function: Has a strict specificity for hydrolysis of asparaginyl bonds. Can also cleave aspartyl bonds slowly, especially under acidic conditions. Required for normal lysosomal protein degradation in renal proximal tubules. Required for normal degradation of internalized EGFR. Plays a role in the regulation of cell proliferation via its role in EGFR degradation. May be involved in the processing of proteins for MHC class II antigen presentation in the lysosomal/endosomal system (By similarity).
Subcellular location: Lysosome {ECO:0000269|PubMed:9742219}.
Interaction partners:
- Cystatin E/M.
- Cathepsin B
- Cathepsin S
- Procathepsin L
- Cathepsin Z
- Cubilin
- Vitamin D-binding protein
- Dipeptidyl peptidase 1
Sequence:
MTWRVAVLLSLVLGAGAVHIGVDDPEDGGKHWVVIVAGSNGWYNYRHQADACHAYQIIHRNGIPDEQIIVMMYDDIANNEENPTPGVVINRPNGTDVYKGVPKDYTGEDVTPENFLAVLRGDEEAVKGKGSGKVLKSGPRDHVFVYFTDHGATGILVFPNEDLHVKDLNKTIRYMYEHKMYQKMVFYIEACESGSMMNHLPDDIDVYATTAANPNESSYACYYDEERSTYLGDWYSVNWMEDSDVEDLTKETLHKQYHLVKSHTNTSHVMQYGNKSISTMKVMQFQGMKHRASSPISLPPVTHLDLTPSPDVPLTILKRKLLRTNNMKESQVLVGQIQHLLDARHIIEKSVQKIVSLLAGFGETAQKHLSERAMLTAHDCHQEAVTHFRTHCFNWHSVTYEHALRYLYVLANLCEKPYPIDRIKMAMDKVCLSHY
Protein: Dual specificity protein kinase CLK3 (EC 2.7.12.1) (CDC-like kinase 3) (P49761)
Organism: Homo sapiens (Human)
Function: Dual specificity kinase acting on both serine/threonine and tyrosine-containing substrates. Phosphorylates serine- and arginine-rich (SR) proteins of the spliceosomal complex. May be a constituent of a network of regulatory mechanisms that enable SR proteins to control RNA splicing and can cause redistribution of SR proteins from speckles to a diffuse nucleoplasmic distribution. Phosphorylates SRSF1 and SRSF3. Regulates the alternative splicing of tissue factor (F3) pre-mRNA in endothelial cells.
Subcellular location: [Isoform 1]: Nucleus. Cytoplasm {ECO:0000250}. Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000250}.; SUBCELLULAR LOCATION: [Isoform 2]: Nucleus speckle. Note=Co-localizes with serine- and arginine-rich (SR) proteins in the nuclear speckles.
Interaction partners:
- NADPH-dependent 3-demethoxyubiquinone 3-hydroxylase, mitochondrial
- Transformer-2 protein homolog beta
- Dual specificity protein kinase CLK2
- Transformer-2 protein homolog alpha
- Arginine/serine-rich protein 1
- Serine/arginine-rich splicing factor 10
- Serine/arginine-rich splicing factor 8
- Serine/arginine-rich splicing factor 1
- Telomere length regulation protein TEL2 homolog
- MICOS complex subunit MIC60
Sequence:
MHHCKRYRSPEPDPYLSYRWKRRRSYSREHEGRLRYPSRREPPPRRSRSRSHDRLPYQRRYRERRDSDTYRCEERSPSFGEDYYGPSRSRHRRRSRERGPYRTRKHAHHCHKRRTRSCSSASSRSQQSSKRSSRSVEDDKEGHLVCRIGDWLQERYEIVGNLGEGTFGKVVECLDHARGKSQVALKIIRNVGKYREAARLEINVLKKIKEKDKENKFLCVLMSDWFNFHGHMCIAFELLGKNTFEFLKENNFQPYPLPHVRHMAYQLCHALRFLHENQLTHTDLKPENILFVNSEFETLYNEHKSCEEKSVKNTSIRVADFGSATFDHEHHTTIVATRHYRPPEVILELGWAQPCDVWSIGCILFEYYRGFTLFQTHENREHLVMMEKILGPIPSHMIHRTRKQKYFYKGGLVWDENSSDGRYVKENCKPLKSYMLQDSLEHVQLFDLMRRMLEFDPAQRITLAEALLHPFFAGLTPEERSFHTSRNPSR
Protein: Receptor interacting serine/threonine kinase 1 (D3ZYL0)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- FAS-associated death domain protein
- NF-kappa-B essential modulator
- TNF receptor-associated factor
- Caspase-8
- Tumor necrosis factor receptor type 1-associated DEATH domain protein
- Receptor-interacting serine/threonine-protein kinase 3
- Tumor necrosis factor receptor superfamily member 1A
- TGF-beta-activated kinase 1 and MAP3K7-binding protein 2
- TNF receptor-associated factor 6
- RING-type E3 ubiquitin transferase
Sequence:
MQPDMSLDNIKMASDDLLERKDLDSGGFGKVSLCFHRTHGFVILKKVYTGPNRAEYNEALLEEGKMMHRLRHDRVVKLLGIIIEEGNYSLVMEYMEQGNLMHVLKTKESVPLSVKGRIIVEIIEGMHYLHDEGVIHKDLKPENILVDRDFHIKIADLGVASFKTWSKLTKEEHNKQREASSVTKKNGGTLYYMAPEHLTDINTKPTEKSDVYSFAIVLWAIFANKEPYENVICTEQFLVCINSGNRPNVEDILEFCPREIISLMERCWQTNPEDRPTFFGIEKEFKPFYLSQFEEYVEEDVASLKKEYPSQSPVLKRMFSLQHDCVPLPPSRSNSEQPGSLHSSQGLPMGPVEESWFSSSPEYPQEENERSVQAKLQEEASYHAFGIFAEKQTKSQPRLNEAYNREEERKRRVSHDPFAQQRVHENVKSAGAKGLPYPSTTSHGNAAHQLSGPASQIKVPLWNNGVYNHHGFGATGTGVWYGPSVSQSYNAYKTPVPETNLPGSIPTMPYISLAPPDDSIRCTIYNSSRVQIGNYNYMDLGPSSQPPTNTCKVESTSRHQAVFANTTSLTDKHLNPIRENMGKQWKNCARKLGFTESQIDEIDHDYERDGLKEKVYQMLQKWLMREGTKGATVGKLAQALHQCCRTDLLNQLIQASQS
Protein: NAD(P)H dehydrogenase (quinone) FQR1 (EC 1.6.5.2) (Flavodoxin-like quinone reductase 1) (Q9LSQ5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the transfer of electrons from NADH and NADPH to several quinones in vitro. May act as detoxification enzyme, and protect against auxin-induced oxidative stress.
Subcellular location: Cell membrane {ECO:0000269|PubMed:15060130}.
Interaction partners:
- 2-phytyl-1,4-beta-naphthoquinone methyltransferase, chloroplastic
- ATP binding protein
- Uclacyanin-3
- Nitroreductase family protein
Sequence:
MATKVYIVYYSMYGHVEKLAEEIRKGAASVEGVEAKLWQVPETLHEEALSKMSAPPKSESPIITPNELAEADGFVFGFPTRFGMMAAQFKAFLDATGGLWRAQALAGKPAGIFYSTGSQGGGQETTALTAITQLVHHGMLFVPIGYTFGAGMFEMENVKGGSPYGAGTFAGDGSRQPTELELQQAFHQGQYIASITKKLKGSTA
Protein: Heterogeneous nuclear ribonucleoprotein K homolog (hnRNP K) (P91277)
Organism: Caenorhabditis elegans
Function: RNA-binding protein which functions together with alg-1, a component of the miRNA loading complex, to modulate the processing and activity of specific miRNAs such as miR-58 and let-7 to regulate gene expression at the post-transcriptional level during embryonic, hypodermal and neuronal development. Promotes the lsy-6-mediated repression of cog-1 in uterine cells. In embryos, may play a role in the DNA damage response.
Subcellular location: Nucleus {ECO:0000269|PubMed:31584932}. Cytoplasm {ECO:0000269|PubMed:31584932}. Note=Localizes to the cytoplasm and nucleus in the germline, oocytes and early embryos (PubMed:31584932). Does not localize to the cytoplasm of somatic cells (PubMed:31584932). {ECO:0000269|PubMed:31584932}.
Interaction partners:
- Heterogeneous nuclear ribonucleoprotein A1
- Nucleolin homolog 1
- RRM domain-containing protein
- CCHC-type zinc finger nucleic acid binding protein
- Splicing factor U2AF 65 kDa subunit
- RNA-binding protein 42
- Putative RNA-binding protein PTB-1a
- B30.2/SPRY domain-containing protein
- RRM domain-containing protein
- Branchpoint-bridging protein
Sequence:
MMIKVGAAINGTDSPKAMKREHDNDDGDRTGRHKRPKTDGFTEAIQQGKFEVRLLVSSKSAGAIIGKGGENIKRLRAEFNAHVQVPDSNTPERVCTVTADEKTVLNILKDVLPRLEDNFSERDPCEVRMLVHQSHAGALIGRNGSKIKELREKCSARLKIFTGCAPGSTDRVLITSGEQKNVLGIIEEVMKELKEIPIKGSATPYLPAFNYDPSNISDYGGFPGNMPAGGPPNNRGPAPQRGGQGPPGGPRSYGGAITQGGGQRSFEAGDFQQFRGGPGPVPGYAMSAPGYPPQQGQFGAPNNAGYGYGPGGGGPVTTAQVTIPSDLGGTIIGRGGERIARIRQESGAQITLEQSNGQPERIITIKGTEQQIHSAQYLLQQCVRNSTQGRERFGGSV
Protein: Ribbon, isoform C (A0A0B4KFC4)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00320}.
Interaction partners:
Sequence:
MGGPTAPVASSGEVGQTYCLRWNNHQTNLVQILHALHEVGSYVDCSLVVDDEQFQAHRVVLAANSPYFQHILKDVPQDHCSIILPGVKGFEIAALLQYMYTGETTVTKSQEPEILRTAKELQVKGLYDNLMKFNHASVTPTSSSGAGGAKPQNGSASNHSSSVISTSTHISPSAAISSSCSPPPPPQFGYQPGYSHYPQQQPMSASQIPAGEAPLTPTQATPHSAASGAGEAGGQWPLTPSAAAAMLNSVYESAADMNPLKRKKLSAISSMLLSGNRDTPILRNVLAQANPADSSQPGPMNANGEKTPTHPHQNTQLPAGLGVSGGERNHSFNGSDYGGDKEPLSPYTDRSFEEETGQSGGKKPEWKRYKQYTRADMMCAIQAVREGMSALQASRKYGLPSRTLYDKVRKLNITTGRGTHRTPKRSPPGAESSQGFSYSAAAAAAAHNYGHGHGHHSEVKRDQKVDHVPAHHGMPPTIPPSAAALLDHAFLQQALENRGGDMAGREALHAMALAAAAHAAANRLSSSPAEMDQRSNGHGMRSPSPQGRHYPHEQEAMDLEMEKHEQNIIKRERDQDEREDADDEEDHEQEHVEDLSLARKERPPSPYSPQPTEAGAGVIMHASSASANGKDHVDYPSSPQFVPIGLKRELMEGEDAQARADXLTLTMAWQYATDSLDSLE
Protein: Putative mitochondrial carrier protein PET8 (P38921)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Mitochondrion inner membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Probable serine/threonine-protein kinase RTK1
- Nitrogen permease reactivator protein
- Mitochondrial glycine transporter
- Cysteine desulfurase, mitochondrial
Sequence:
MNTFFLSLLSGAAAGTSTDLVFFPIDTIKTRLQAKGGFFANGGYKGIYRGLGSAVVASAPGASLFFISYDYMKVKSRPYISKLYSQGSEQLIDTTTHMLSSSIGEICACLVRVPAEVVKQRTQVHSTNSSWQTLQSILRNDNKEGLRKNLYRGWSTTIMREIPFTCIQFPLYEYLKKTWAKANGQSQVEPWKGAICGSIAGGIAAATTTPLDFLKTRLMLNKTTASLGSVIIRIYREEGPAVFFSGVGPRTMWISAGGAIFLGMYETVHSLLSKSFPTAGEMRA
Protein: Ecdysone-inducible gene E3 (LD11958p) (Q9VHW8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MRSGLTVRPMLVVLLVGHLVDPVAPANLLTSYLPASMQALAYYIDLLQYEPLSSTTVEPPFSADEEGMESTTANPRPSTPLPTRMRTTTTRRPIGAGASGSGGMGWWQPPSWWETPKRSSTTERPTSPPTVPHRPAIFAPTAPPEKSLEGNDLFAEIKDDSDFDTLPLSLIRDIQSERYDFTNDVESLDNFLRLYDDNYGRAAFGSESAMDRWSTASIAGKKRVPPTKPYVDFLLVYDLLKRDAKAASLSKYEGYSENLLVELHALSQVSAARQLYTLFKRMLDRGDIQRSDVVARVQGIAKDLGNPKSPTSKALTFIPSMQFLP
Protein: E3 ubiquitin-protein ligase makorin-1 (EC 2.3.2.27) (RING-type E3 ubiquitin transferase makorin-1) (Q9QXP6)
Organism: Mus musculus (Mouse)
Function: E3 ubiquitin ligase catalyzing the covalent attachment of ubiquitin moieties onto substrate proteins. These substrates include FILIP1, p53/TP53, CDKN1A and TERT. Keeps cells alive by suppressing p53/TP53 under normal conditions, but stimulates apoptosis by repressing CDKN1A under stress conditions. Acts as a negative regulator of telomerase (By similarity). Has negative and positive effects on RNA polymerase II-dependent transcription.
Interaction partners:
Sequence:
MAEAAAPGTTATTSGAGAAAAAVAAASLTSIPTVAAPSPGAGGGGGGSDGSGGGWTKQVTCRYFMHGVCKEGDNCRYSHDLSDSPYGVVCKYFQRGYCVYGDRCRYEHSKPLKQEEVTATDLSAKPSLAASSSLSSGVGSLAEMNSGEAESRNPSFPTVGAGSEDWVNAIEFVPGQPYCGRTAPSCTEVPPQGSVTKEESEKEPTTVETKKQLCPYAAVGECRYGENCVYLHGDSCDMCGLQVLHPVDAAQRSQHIKSCIEAHEKDMELSFAVQRTKDMVCGICMEVVYEKANPSERRFGILSNCNHTYCLKCIRKWRSAKQFESKIIKSCPECRITSNFVIPSEYWVEEKEEKQKLIQKYKEAMSNKACRYFDEGRGSCPFGGNCFYKHAYPDGRREEPQRQKVGTSSRYRAQRRSHFWELIEERENNPFDNDEEEVVTFELGEMLLMLLAAGGDDELTDSEDEWDLFHDELEDFYDLDL
Protein: Lipase member K (EC 3.1.1.-) (Lipase-like abhydrolase domain-containing protein 2) (Q5VXJ0)
Organism: Homo sapiens (Human)
Function: Plays a highly specific role in the last step of keratinocyte differentiation. May have an essential function in lipid metabolism of the most differentiated epidermal layers.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
Sequence:
MWQLLAAACWMLLLGSMYGYDKKGNNANPEANMNISQIISYWGYPYEEYDVTTKDGYILGIYRIPHGRGCPGRTAPKPAVYLQHGLIASASNWICNLPNNSLAFLLADSGYDVWLGNSRGNTWSRKHLKLSPKSPEYWAFSLDEMAKYDLPATINFIIEKTGQKRLYYVGHSQGTTIAFIAFSTNPELAKKIKIFFALAPVVTVKYTQSPMKKLTTLSRRVVKVLFGDKMFHPHTLFDQFIATKVCNRKLFRRICSNFLFTLSGFDPQNLNMSRLDVYLSHNPAGTSVQNMLHWAQAVNSGQLQAFDWGNSDQNMMHFHQLTPPLYNITKMEVPTAIWNGGQDIVADPKDVENLLPQIANLIYYKLIPHYNHVDFYLGEDAPQEIYQDLIILMEEYLQN
Protein: Kinesin-like protein KIP1 (Chromosome instability protein 9) (P28742)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for assembly of the mitotic spindle. Interacts with spindle microtubules to produce an outwardly directed force acting upon the poles. Following spindle assembly, CIN8 and KIP1 apparently act to oppose a force that draws separated poles back together. This force seems to be mediate by KAR3.
Subcellular location: Cytoplasm, cytoskeleton, spindle. Note=Spindle microtubules that lie between the poles.
Interaction partners:
- Anaphase spindle elongation protein
- Kinesin-like protein KIP3
- Kinesin-like protein KIP2
- Tubulin beta chain
- Cell cycle serine/threonine-protein kinase CDC5/MSD2
- Spindle pole body-associated protein VIK1
- Spindle pole body-associated protein CIK1
- Kinesin-like protein KAR3
- Securin
- Tubulin alpha-3 chain
Sequence:
MARSSLPNRRTAQFEANKRRTIAHAPSPSLSNGMHTLTPPTCNNGAATSDSNIHVYVRCRSRNKREIEEKSSVVISTLGPQGKEIILSNGSHQSYSSSKKTYQFDQVFGAESDQETVFNATAKNYIKEMLHGYNCTIFAYGQTGTGKTYTMSGDINILGDVQSTDNLLLGEHAGIIPRVLVDLFKELSSLNKEYSVKISFLELYNENLKDLLSDSEDDDPAVNDPKRQIRIFDNNNNNSSIMVKGMQEIFINSAHEGLNLLMQGSLKRKVAATKCNDLSSRSHTVFTITTNIVEQDSKDHGQNKNFVKIGKLNLVDLAGSENINRSGAENKRAQEAGLINKSLLTLGRVINALVDHSNHIPYRESKLTRLLQDSLGGMTKTCIIATISPAKISMEETASTLEYATRAKSIKNTPQVNQSLSKDTCLKDYIQEIEKLRNDLKNSRNKQGIFITQDQLDLYESNSILIDEQNLKIHNLREQIKKFKENYLNQLDINNLLQSEKEKLIAIIQNFNVDFSNFYSEIQKIHHTNLELMNEVIQQRDFSLENSQKQYNTNQNMQLKISQQVLQTLNTLQGSLNNYNSKCSEVIKGVTEELTRNVNTHKAKHDSTLKSLLNITTNLLMNQMNELVRSISTSLEIFQSDSTSHYRKDLNEIYQSHQQFLKNLQNDIKSCLDSIGSSILTSINEISQNCTTNLNSMNVLIENQQSGSSKLIKEQDLEIKKLKNDLINERRISNQFNQQLAEMKRYFQDHVSRTRSEFHDELNKCIDNLKDKQSKLDQDIWQKTASIFNETDIVVNKIHSDSIASLAHNAENTLKTVSQNNESFTNDLISLSRGMNMDISSKLRSLPINEFLNKISQTICETCGDDNTIASNPVLTSIKKFQNIICSDIALTNEKIMSLIDEIQSQIETISNENNINLIAINENFNSLCNFILTDYDENIMQISKTQDEVLSEHCEKLQSLKILGMDIFTAHSIEKPLHEHTRPEASVIKALPLLDYPKQFQIYRDAENKSKDDTSNSRTCIPNLSTNENFPLSQFSPKTPVPVPDQPLPKVLIPKSINSAKSNRSKTLPNTEGTGRESQNNLKRRFTTEPILKGEETENNDILQNKKLHQ
Protein: Sensor histidine kinase YpdA (EC 2.7.13.3) (P0AA93)
Organism: Escherichia coli (strain K12)
Function: Member of the two-component regulatory system YpdA/YpdB, which is part of a nutrient-sensing regulatory network composed of YpdA/YpdB, the high-affinity pyruvate signaling system BtsS/BtsR and their respective target proteins, YhjX and BtsT. YpdA activates YpdB by phosphorylation in response to high concentrations of extracellular pyruvate. Activation of the YpdA/YpdB signaling cascade also promotes BtsS/BtsR-mediated btsT expression.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Transcriptional regulatory protein YpdB
- Transcriptional regulatory protein BtsR
- Uncharacterized MFS-type transporter YhjX
- Pyruvate/proton symporter BtsT
- Sensor histidine kinase ZraS
- Aerobic respiration control sensor protein ArcB
- Uncharacterized permease YjhF
- Uncharacterized HTH-type transcriptional regulator YpdC
Sequence:
MHEIFNMLLAVFDRAALMLICLFFLIRIRLFRELLHKSAHSPKELLAVTAIFSLFALFSTWSGVPVEGSLVNVRIIAVMSGGILFGPWVGIITGVIAGIHRYLIDIGGVTAIPCFITSILAGCISGWINLKIPKAQRWRVGILGGMLCETLTMILVIVWAPTTALGIDIVSKIGIPMILGSVCIGFIVLLVQSVEGEKEASAARQAKLALDIANKTLPLFRHVNSESLRKVCEIIRDDIHADAVAITNTDHVLAYVGVGEHNYQNGDDFISPTTRQAMNYGKIIIKNNDEAHRTPEIHSMLVIPLWEKGVVTGTLKIYYCHAHQITSSLQEMAVGLSQIISTQLEVSRAEQLREMANKAELRALQSKINPHFLFNALNAISSSIRLNPDTARQLIFNLSRYLRYNIELKDDEQIDIKKELYQIKDYIAIEQARFGDKLTVIYDIDEEVNCCIPSLLIQPLVENAIVHGIQPCKGKGVVTISVAECGNRVRIAVRDTGHGIDPKVIERVEANEMPGNKIGLLNVHHRVKLLYGEGLHIRRLEPGTEIAFYIPNQRTPVASQATLLL
Protein: Xylan O-acetyltransferase 2 (EC 2.3.1.-) (Protein trichome birefringence-like 11) (OsTBL11) (B9FKP6)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Xylan acetyltransferase required for 2-O- and 3-O-monoacetylation of xylosyl residues in xylan. Catalyzes the 2-O-acetylation of xylan, followed by nonenzymatic acetyl migration to the O-3 position, resulting in products that are monoacetylated at both O-2 and O-3 positions (By similarity).
Subcellular location: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q2QYU2}; Single-pass type II membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MGLPGRRNPLLSARRAAASLRRSRRLPVYVAAVFFVASVLLMFRDEILYLTTARSPSSSLPTTGGSAGGAGLARKEELVSVNKPVLLGHGGKPEKHHSVTERHRPKVSAKRRPNKKAAKAARKKFMASPSVAAGAEVNVPETCNLSKGKWVFDNATYPLYREQECEYLTAQVTCTRNGRRDDGYQKWRWQPRDCDLPLAFDARLFMERLRGKRLMFVGDSLNRNQWESMVCLVRPALSPGKSYVTWWDGQRVVLHAWEYNATVEFYWAPFLVESNSDDPKAHSIRDRVIKPEAIAAHAGDWVGVDYLVFNTYIWWMNTVNMKVVRPTGKTWEEYDEVGRIEAYRRVLDTWATWVNDNVDPARTSVFFMSVSPLHISPEAWGNPGGVRCAKEDAPVQNWHGPLWLGTDWDMFRAARNASRAAGRVPVTFVDVTAMSELRKDGHTSVHTIRQGRVLTPEQQADPATYADCIHWCLPGVPDVWNLMLYARILSRPPAAAGHVA
Protein: Protein gamma response 1 (COM1/SAE2-like protein) (Protein gamma response I) (Q9ZRT1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Seems to mediate cell cycle arrest before mitosis in response to DNA damage. Is probably also involved in the transition from mitosis to endoreduplication.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- DNA-damage-repair/toleration protein 111
- RNA polymerase II C-terminal domain phosphatase-like 4
- Protein POOR HOMOLOGOUS SYNAPSIS 1
- Proton pump-interactor 2
- Serine/threonine-protein kinase ATM
- Meiosis-specific protein ASY3
- Peptide methionine sulfoxide reductase B4
- Serine/threonine-protein phosphatase PP1 isozyme 3
- Meiotic recombination protein SPO11-2
- Probable calcium-binding protein CML28
Sequence:
MGDETVDGIEAKYISGLSTIMVATIQEAKDRISQIEYIFCSQLFPNFQSKSKAFEKVYSEARLAACDTWKDREKSLLDQIEELKVENQQIKSDKEKLAEELGKTASMPLRLTSLQGYIDHLKKKMKSRSKMVGDARDLYYRLVELLQVKGLDELSEDGINMIVSEVKSLKMKTEFLQEELSKKTLVTENLLKKLEYLSTEAADGERKLSSVEEEKQRLKTRLQVFEENVGRLEEILRQKTDEVEEGKTALEVLQGKLKLTEREMLNCKQKIADHEKEKTVVMGKAKDDMQGRHGSYLADLEALRCQSEEKSFELAMEIKKNKELSRTCKKWKSQHTFLCKRFNFTPDSVLHQSSLEDENKEIGQHEKSAISSYLERKHSETAEGADKVRIGTGSSGNNYEKESIIKTVQTPITSISPIVRSPGAAKPPQLSGLKRPASIWRDTRSRQSPGGHDPHDDFLDTPIENVKRVAGEEKHVHDVAKKDDSDDETQDMNPKPSPSRQRIQIAETSKKSFKHVESVRKKAERENLKGIECKQCKKFYDAVHPENEGNGNKSLRCEHHEGVSRHRYRYAPPMTPEGFWNIGFESEM
Protein: CST complex subunit STN1 (Oligonucleotide/oligosaccharide-binding fold-containing protein 1) (Suppressor of cdc thirteen homolog) (B8JKF4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Component of the CST complex proposed to act as a specialized replication factor promoting DNA replication under conditions of replication stress or natural replication barriers such as the telomere duplex. The CST complex binds single-stranded DNA with high affinity in a sequence-independent manner, while isolated subunits bind DNA with low affinity by themselves. Initially the CST complex has been proposed to protect telomeres from DNA degradation. However, the CST complex has been shown to be involved in several aspects of telomere replication.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9H668}. Chromosome, telomere {ECO:0000250|UniProtKB:Q9H668}.
Interaction partners:
- CST complex subunit CTC1
- CST complex subunit TEN1
- DNA primase
- DNA polymerase
- DNA primase large subunit
- Mediator of RNA polymerase II transcription subunit 4
- Mediator of RNA polymerase II transcription subunit 25
- Mediator of RNA polymerase II transcription subunit 14
- Mediator of RNA polymerase II transcription subunit 27
- Mediator of RNA polymerase II transcription subunit 6
Sequence:
MAVSLGDDDADELPSMLWGLDPVFSSYCRLYITDILLMKESRQVPGIYFYKTHPIFQVDVLGIVVYKREREDFYCYGVDDSTGVINCLCWKDEKWRDQGGSTTCGDASGFPRSFNIEDELKGLKEAERKSTVLEIGDLLRVRGTVKTSRDNREIKATSFYKVHDPAMAVQISRMLELPQLYRKCYDQPFKMPSDDLGSTEAGGSSHPQYLLSRAVLTLKEFLLEKEVTRFRPYDVEFLLHPLIQRSSAEQEADQPGTSFATQVGKLLKETLSFLQDEGQIFRKKRTQDEVYNVTEQDKDLHIAIKDVLREDTKREKYAEKGCHVLHILSSVRQRYSQNLSREVLEVALTFLESNSDIISTTEAHYIVL
Protein: Ubiquitin-conjugating enzyme E2 1 (EC 2.3.2.23) (E2 ubiquitin-conjugating enzyme 1) (Ubiquitin carrier protein) (Ubiquitin-conjugating enzyme E2-24 kDa) (Ubiquitin-protein ligase) (P21734)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the covalent attachment of ubiquitin to other proteins. Functions in degradation of misfolded or regulated proteins localized in the endoplasmic reticulum (ER) lumen or membrane via the ubiquitin-proteasome system. Cognate E2 conjugating enzyme for the HRD1 ubiquitin ligase complex, which is part of the ERAD-L and ERAD-M pathways responsible for the rapid degradation of soluble lumenal and membrane proteins with misfolded lumenal domains (ERAD-L), or ER-membrane proteins with misfolded transmembrane domains (ERAD-M).
Interaction partners:
- Polyubiquitin
- Ubiquitin-activating enzyme E1 1
- Ubiquitin-ribosomal protein eS31 fusion protein
- Ubiquitin-ribosomal protein eL40A fusion protein
- E3 ubiquitin-protein ligase RSP5
- SUMO-conjugating enzyme UBC9
- Ubiquitin-conjugating enzyme E2 4
- Ubiquitin-like protein SMT3
- Anaphase-promoting complex subunit 11
- Ubiquitin-conjugating enzyme variant MMS2
Sequence:
MSRAKRIMKEIQAVKDDPAAHITLEFVSESDIHHLKGTFLGPPGTPYEGGKFVVDIEVPMEYPFKPPKMQFDTKVYHPNISSVTGAICLDILKNAWSPVITLKSALISLQALLQSPEPNDPQDAEVAQHYLRDRESFNKTAALWTRLYASETSNGQKGNVEESDLYGIDHDLIDEFESQGFEKDKIVEVLRRLGVKSLDPNDNNTANRIIEELLK