wanglab/gogpt-training-data huggingface dataset:
Protein: SRR1-like protein (O60093)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
Sequence:
MDFIVVKRSRKKKNGRGKFPKVSNTITQGDTDLWSQDTLQRKLDNSREKLEYSEFLKSVQSQLSEFKDPIHKCIILGLGRIHTLTASLQLSLFFEIMKIFNLQPRFCSFYDPAFLKDDVEFLENKGFCVLPDPPTPSCLKYTLLYMPHCPTSLYETWLAAYVNDDPRHFIMCGNNLQLYVDNKPSKEIVSTYPNVYKMCTKNYYTRLLFPEFPNVYAFNDLSFHFHDAQSFVEKKQPSKFVDASSVAEHPS
Protein: TNF receptor-associated factor 6 (EC 2.3.2.27) (E3 ubiquitin-protein ligase TRAF6) (RING-type E3 ubiquitin transferase TRAF6) (P70196)
Organism: Mus musculus (Mouse)
Function: E3 ubiquitin ligase that, together with UBE2N and UBE2V1, mediates the synthesis of 'Lys-63'-linked-polyubiquitin chains conjugated to proteins, such as IKBKG, IRAK1, AKT1 and AKT2. Also mediates ubiquitination of free/unanchored polyubiquitin chain that leads to MAP3K7 activation (By similarity). Leads to the activation of NF-kappa-B and JUN. Seems to also play a role in dendritic cells (DCs) maturation and/or activation. Represses c-Myb-mediated transactivation, in B-lymphocytes (By similarity). Adapter protein that seems to play a role in signal transduction initiated via TNF receptor, IL-1 receptor and IL-17 receptor. Regulates osteoclast differentiation by mediating the activation of adapter protein complex 1 (AP-1) and NF-kappa-B, in response to RANK-L stimulation. Together with MAP3K8, mediates CD40 signals that activate ERK in B-cells and macrophages, and thus may play a role in the regulation of immunoglobulin production. Participates also in the TCR signaling by ubiquitinating LAT (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9Y4K3}. Cytoplasm, cell cortex {ECO:0000250|UniProtKB:Q9Y4K3}. Nucleus {ECO:0000250|UniProtKB:Q9Y4K3}. Lipid droplet {ECO:0000269|PubMed:21435586}. Note=RSAD2/viperin recruits it to the lipid droplet.
Interaction partners:
- Tumor necrosis factor receptor superfamily member 5
- Receptor-interacting serine/threonine-protein kinase 1
- TNF receptor-associated factor 3
- Mitogen-activated protein kinase kinase kinase 7
- TGF-beta-activated kinase 1 and MAP3K7-binding protein 3
- Toll-like receptor 3
- Toll-like receptor 4
- Sequestosome-1
- Evolutionarily conserved signaling intermediate in Toll pathway, mitochondrial
- Interferon regulatory factor 7
Sequence:
MSLLNCENSCGSSQSSSDCCAAMAASCSAAVKDDSVSGSASTGNLSSSFMEEIQGYDVEFDPPLESKYECPICLMALREAVQTPCGHRFCKACIIKSIRDAGHKCPVDNEILLENQLFPDNFAKREILSLTVKCPNKGCLQKMELRHLEDHQVHCEFALVNCPQCQRPFQKCQVNTHIIEDCPRRQVSCVNCAVSMAYEEKEIHDQSCPLANIICEYCGTILIREQMPNHYDLDCPTAPIPCTFSVFGCHEKMQRNHLARHLQENTQLHMRLLAQAVHNVNLALRPCDAASPSRGCRPEDPNYEETIKQLESRLVRQDHQIRELTAKMETQSMYVGELKRTIRTLEDKVAEMEAQQCNGIYIWKIGNFGMHLKSQEEERPVVIHSPGFYTGRPGYKLCMRLHLQLPTAQRCANYISLFVHTMQGEYDSHLPWPFQGTIRLTILDQSEALIRQNHEEVMDAKPELLAFQRPTIPRNPKGFGYVTFMHLEALRQGTFIKDDTLLVRCEVSTRFDMGGLRKEGFQPRSTDAGV
Protein: Peptide ABC transporter, peptide-binding protein (O69634)
Organism: Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Interaction partners:
Sequence:
MVRQMRAALAALATGLLVLAPVAGCGGGVLSPDVVLVNGGEPPNPLIPTGTNDSNGGRIIDRLFAGLMSYDAVGKPSLEVAQSIESADNVNYRITVKPGWKFTDGSPVTAHSFVDAWNYGALSTNAQLQQHFFSPIEGFDDVAGAPGDKSRTTMSGLRVVNDLEFTVRLKAPTIDFTLRLGHSSFYPLPDSAFRDMAAFGRNPIGNGPYKLADGPAGPAWEHNVRIDLVPNPDYHGNRKPRNKGLRFEFYANLDTAYADLLSGNLDVLDTIPPSALTVYQRDLGDHATSGPAAINQTLDTPLRLPHFGGEEGRLRRLALSAAINRPQICQQIFAGTRSPARDFTARSLPGFDPNLPGNEVLDYDPQRARRLWAQADAISPWSGRYAIAYNADAGHRDWVDAVANSIKNVLGIDAVAAPQPTFAGFRTQITNRAIDSAFRAGWRGDYPSMIEFLAPLFTAGAGSNDVGYINPEFDAALAAAEAAPTLTESHELVNDAQRILFHDMPVVPLWDYISVVGWSSQVSNVTVTWNGLPDYENIVKA
Protein: TATA-box binding protein (Q7Z6S5)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MDQNNSLPPYAQGLASPQGAMTPGIPIFSPMMPYGTGLTPQPIQNTNSLSILEEQQRQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQAVAAAAVQQSTSQQATQGTSGQAPQLFHSQTLTTAPLPGTTPLYPSPMTPMTPITPATPASESSGIVPQLQNIVSTVNLGCKLDLKTIALRARNAEYNPKRFAAVIMRIREPR
Protein: Two pore channel protein 2 (Two pore calcium channel protein 2) (Voltage-dependent calcium channel protein TPC2) (Q8BWC0)
Organism: Mus musculus (Mouse)
Function: Intracellular channel initially characterized as a non-selective Ca(2+)-permeable channel activated by NAADP (nicotinic acid adenine dinucleotide phosphate), it is also a highly-selective Na(+) channel activated directly by PI(3,5)P2 (phosphatidylinositol 3,5-bisphosphate). Localizes to the lysosomal and late endosome membranes where it regulates organellar membrane excitability, membrane trafficking, and pH homeostasis. Is associated with a plethora of physiological processes, including mTOR-dependent nutrient sensing, skin pigmentation and autophagy. Ion selectivity is not fixed but rather agonist-dependent and under defined ionic conditions, can be readily activated by both NAADP and PI(3,5)P2. As calcium channel, it increases the pH in the lysosomal lumen, as sodium channel, it promotes lysosomal exocytosis. Plays a crucial role in endolysosomal trafficking in the endolysosomal degradation pathway and is potentially involved in the homeostatic control of many macromolecules and cell metabolites. Also expressed in melanosomes of pigmented cells where mediates a Ca(2+) channel and/or PI(3,5)P2-activated melanosomal Na(+) channel to acidify pH and inhibit tyrosinase activity required for melanogenesis and pigmentation. Unlike the voltage-dependent TPCN1, TPCN2 is voltage independent and can be activated solely by PI(3,5)P2 binding. In contrast, PI(4,5)P2, PI(3,4)P2, PI(3)P and PI(5)P have no obvious effect on channel activation (By similarity).
Subcellular location: Late endosome membrane {ECO:0000305|PubMed:25144390}; Multi-pass membrane protein {ECO:0000255}. Lysosome membrane {ECO:0000269|PubMed:19557428, ECO:0000269|PubMed:20495006, ECO:0000269|PubMed:25144390, ECO:0000269|PubMed:32167471}; Multi-pass membrane protein {ECO:0000269|PubMed:19557428, ECO:0000269|PubMed:20495006}. Melanosome membrane {ECO:0000269|PubMed:27231233}; Multi-pass membrane protein {ECO:0000255}. Note=Only the acidic lysosomal fraction is sensitive to NAADP.
Interaction partners:
- Two pore calcium channel protein 1
- ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 1
- Mucolipin-1
- Sodium/potassium/calcium exchanger 5
Sequence:
MAAEEQPLLGRDRGSGQVHSGAAADQELCIDQAVVFIEDAIKYRSIYHRMDAGSLWLYRWYYSNVCQRVLGFIIFLILILAFVEVPSSFTKTADVRYRSQPWQPPCGLTETIEAFCLLAFLVDLSVKGYLVGQAQLQQNLWLLAYFMVLVVSVVDWIVSLSLACEEPLRMRRLLRPFFLLQNSSMMKKTLKCIRWSLPEMASVGLLLAIHLCLFTIIGMLLFTIGEKDEAQDQERLAYFRNLPEALTSLLVLLTTSNNPDVMIPAYTQNRAFALFFIVFTLIGSLFLMNLLTAIIYNQFRGYLMKSLQTSLFRRRLGARAAYEVLASRAGPAGTTPELVGVNPETFLPVLQKTQLNKTHKQAIMQKVQSYEGRPMLADEFQKLFDEVDKGLAKERPLKPQYQSPFLQTAQFIFSHHYFDYLGNLVALGNLLSICVFLVLDSDLLPGERDDFVLGILDYIFILYYLLELLFKVFALGLPGYLSYHSNVFDGLLTIILLVSEICTLAVYRLPHSGWKPEQYGPLSLWDMTRLMNTLIVFRFLRIIPNIKPMAEVANTILGLIPNLRAFGGILVVAYYVFAMIGINLFRGVIVPPGNSSLVPDNNSAVCGSFEQLGYWPNNFDDFAAALITLWNVMVVNNWQVILEAYKRYAGPWSMVYFVLWWLVSSVIWINLFLALLLENFLHRWDPQGHKQLLVGTKQMSVELMFRDILEEPKEEELMEKLHKHPHLHLCR
Protein: Sulfate-binding protein (Sulfate starvation-induced protein 2) (SSI2) (P0AG78)
Organism: Escherichia coli (strain K12)
Function: This protein specifically binds sulfate and is involved in its transmembrane transport.
Subcellular location: Periplasm.
Interaction partners:
- Sulfate/thiosulfate import ATP-binding protein CysA
- Sulfate adenylyltransferase subunit 1
- Sulfate transport system permease protein CysT
- Sulfate transport system permease protein CysW
- Sulfate adenylyltransferase subunit 2
- Thiosulfate-binding protein
- Adenylyl-sulfate kinase
- Phosphoadenosine 5'-phosphosulfate reductase
- Sulfite reductase hemoprotein beta-component
- Taurine-binding periplasmic protein
Sequence:
MNKWGVGLTFLLAATSVMAKDIQLLNVSYDPTRELYEQYNKAFSAHWKQQTGDNVVIRQSHGGSGKQATSVINGIEADVVTLALAYDVDAIAERGRIDKEWIKRLPDNSAPYTSTIVFLVRKGNPKQIHDWNDLIKPGVSVITPNPKSSGGARWNYLAAWGYALHHNNNDQAKAQDFVRALYKNVEVLDSGARGSTNTFVERGIGDVLIAWENEALLAANELGKDKFEIVTPSESILAEPTVSVVDKVVEKKGTKEVAEAYLKYLYSPEGQEIAAKNYYRPRDAEVAKKYENAFPKLKLFTIDEEFGGWTKAQKEHFANGGTFDQISKR
Protein: UDP-N-acetylenolpyruvoylglucosamine reductase (EC 1.3.1.98) (UDP-N-acetylmuramate dehydrogenase) (P08373)
Organism: Escherichia coli (strain K12)
Function: Cell wall formation.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- UDP-N-acetylmuramate--L-alanine ligase
- UDP-N-acetylglucosamine 1-carboxyvinyltransferase
- UDP-N-acetylmuramoylalanine--D-glutamate ligase
- UDP-N-acetylglucosamine--N-acetylmuramyl-
- UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase
- UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase
- D-alanine--D-alanine ligase B
- Bifunctional ligase/repressor BirA
- Glutamate racemase
- UDP-N-acetylmuramate--L-alanyl-gamma-D-glutamyl-meso-2,6-diaminoheptandioate ligase
Sequence:
MNHSLKPWNTFGIDHNAQHIVCAEDEQQLLNAWQYATAEGQPVLILGEGSNVLFLEDYRGTVIINRIKGIEIHDEPDAWYLHVGAGENWHRLVKYTLQEGMPGLENLALIPGCVGSSPIQNIGAYGVELQRVCAYVDSVELATGKQVRLTAKECRFGYRDSIFKHEYQDRFAIVAVGLRLPKEWQPVLTYGDLTRLDPTTVTPQQVFNAVCHMRTTKLPDPKVNGNAGSFFKNPVVSAETAKALLSQFPTAPNYPQADGSVKLAAGWLIDQCQLKGMQIGGAAVHRQQALVLINEDNAKSEDVVQLAHHVRQKVGEKFNVWLEPEVRFIGASGEVSAVETIS
Protein: Myosin, light chain 12A, regulatory, non-sarcomeric (D3YV37)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MSSKRAKTKTTKKRPQRATSNVFAMFDQSQIQEFKEAFNMIDQNRDGFIDKEDLHDMLASMGKNPTDEYLDAMMNEAPGPINFTMFLTMFGEKLNGTDPEDVIRNAF
Protein: ELMO domain-containing protein A (Q54YW1)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Functions as a negative regulator of actin polymerization. Modulates actin/myosin II at cortex actinomyosins to prevent excessive F-actin polymerization around the cell periphery, thereby maintaining proper cell shape during phagocytosis and chemotaxis.
Interaction partners:
Sequence:
MKIKVTFQERIIEHNFETEITNLQQVTQKLCSLFLITNYYSYSLFLSSGQLVDNINLIDEGSEIIIKHLNRLGTISIGSGYSNSVVGTTNNNAPSSPSSSININGQQIQQQIQQQIQQQQQQQQQQQQQVQLSPDTLINNLLNNLKDNTFKKKAFFDLKDLKEEILIKKFVEKNGIEVIVCQLKELTGNTLSYALSALQTIMSYEFTITSMTSTDTASLITQLLPLTENTSNPSISKTSLSLLCLFLNQSNNLNFKQFSSTLVLEYNEKTKRNYNHTLVQLLSSSNTVDVQLNALTLINIIIGKTMSTTIPGLENGSVTGGENGFNKLLKELDEYEINQKLKKLVESIIVAPELKRQLYIYQRHRFQVITNRKNVTFNKESSEHDALLMKLWSLTYPGVKLESRVSEQWKQMGFQGTDPCTDFRAMGIWGLDNLIYFAQNYNEKFRKIVNSQIDRKEREYPTATAGIVLTFELYNSIFKMGTPNLNPYNSTTSNTTSNTTSTTNIDDLPFFPLFFSHPHAFEEVYCTTFQILDSTWDDMNGTYMHFQKIMSSVKNLIITALESKPTTLEAFDWKCQKNTKNSNGGTNSNQNNSSSNLLLSNFANGSSLLSLLNDLSSSSRDDMKKLLTGVNYQVLDLIKSQKISYFQEGFQFKLHKQLKTKQSLPLNWIFIRLFNNNNNNNNNNENCSYEIQYCFLSTELNQPPLPNQSIPTNYNTIKISDLFFNGESTNSNNKKKDKSLSYFNISIKDEQIQSLIQNQLPLSNLNNSSNSLQLDSSTSMNSIKDSIINISSSNNNIKDNLTNNNTNTNTNNTNNNTSNGNGNSNSVSMSSININNSGQLSPNTTSPILIPQQQQQQPQSSSLSVQHQQSSTPTPSSPVLLSSPSLQSSSSSSSSSSNPNLFTIDLISSNRDDVSNFWDSIKLLSGQEIKSQEGLDDYHSLLSINTSVKLLDLDGIDIPKETPQIPILPDNFDFRTV
Protein: Nicotinate phosphoribosyltransferase (NAPRTase) (EC 6.3.4.21) (Nicotinate phosphoribosyltransferase domain-containing protein 1) (Q6XQN1)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the first step in the biosynthesis of NAD from nicotinic acid, the ATP-dependent synthesis of beta-nicotinate D-ribonucleotide from nicotinate and 5-phospho-D-ribose 1-phosphate. Helps prevent cellular oxidative stress via its role in NAD biosynthesis.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q6XQN6}.
Interaction partners:
- Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 2
- Nicotinamide-nucleotide adenylyltransferase
- Nicotinate-nucleotide pyrophosphorylase [carboxylating]
- Nicotinamide riboside kinase 1
- Nicotinamide riboside kinase 2
- Purine nucleoside phosphorylase
- NAD-capped RNA hydrolase NUDT12
- 5'-nucleotidase, cytosolic IA
- Ectonucleotide pyrophosphatase/phosphodiesterase family member 1
- Nicotinamide-nucleotide adenylyltransferase
Sequence:
MEMELDDQGRMVVRPLLTDLYQATMGLGYWRAGRACEEAEFELFFRHCPFGGSFALTAGLQDCIRFLRAFRLRDADVQFLASVLPPDTDPAFFEHLRALDCSRVSVRALPEGSLAFPGVPLLQVSGPLLLVQLLETPLLCLVSYASLVATNAARLRLIAGPDKRLLEMGLRRAQGPDGGFTASIYSYLGGFDSSSNTLAGQLRGVPVAGTLAHSFITSFLGSEVPPDPMLAPASSEGPAVDLPASVNLWLKHVCIYLGLEEREPHLGERAAFVAYALAFPRAFQGLLDSYSVRRSGLPNFLAVALALGELGYRAVGVRLDSGDLLQQAKEIRGIFRTVGAEFQMPWLEFVPIAVSNNIDEKELARLAQKGSEVNVIGIGTNVVTCPKQPSMGCVYKLVSVGGQPRIKLTEESQKETLPGSKAAFRFLVSEGSLLLDLLQLAEEPPPKAGQELRVWLQGAQEPCTVKPAQVEPLLRLYLQQGQPYEPLPSLEESRAFAQQSLSRLRPAHKQLQNPAVYQVALSEKLRALVDSLSARGAL
Protein: WD repeat domain 74 (E9PS41)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MLVGCADRTVKHFSTEDGIFQGQRHCPGGEGMFRGLAQADGTLITCVDSGILRVWHDKDKDTSSDPLLELRVGPGVCRMRQDPAHPHVVATGGKENALKIWDLQGSEEPVFRAKNVRNDWLDLRVPIWDQDIQFLPGSQKLVTCTGYHQVRVYDPASPQRRPVLETTYGEYPLTAMTLTPGGNSVIVGNTHGQLAEIDLRQGRLLGCLKGLAGSVRGLQCHPSKPLLASCGLDRVLRIHRIQNPRGLEHKVYLKSQLNCLLLSGRDNWEDEPQEPQEPNKVPLEDTETDELWASLEAAAKRKLSGLEQPQGALQTRRRKKKRPGSTSP
Protein: Cell division protein FtsQ (A0A1D3FIJ4)
Organism: Neisseria gonorrhoeae
Subcellular location: Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_00911}; Single-pass type II membrane protein {ECO:0000256|HAMAP-Rule:MF_00911}. Membrane {ECO:0000256|ARBA:ARBA00004370}. Note=Localizes to the division septum. {ECO:0000256|HAMAP-Rule:MF_00911}.
Interaction partners:
Sequence:
MWDNAEAMERLTRWLLVMMAMLLAASGLVWFYNSNHLPVKQVSLKGNLVYSDKKALGSLAKEYIHGNILRTDINGAQEAYRRYPWIASVMVRRRFPDTVEVVLTERKPVARWGDHALVDGEGNVFEARLDRPGMPVFRGAEGTSAEMLRRYDEFSTVLAKQGLGIKEMTYTARSAWNVVLDNGITVRLGRENEMKRLRLFTEAWQHLLRKNKNRLSYVDMRYKDGFSVRHAPDGLPEKESEE
Protein: ATP synthase F(1) complex subunit gamma, mitochondrial (ATP synthase F1 subunit gamma) (F-ATPase gamma subunit) (Q54DF1)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(1) domain and the central stalk which is part of the complex rotary element. The gamma subunit protrudes into the catalytic domain formed of alpha(3)beta(3). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits (By similarity).
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P05631}; Peripheral membrane protein {ECO:0000250|UniProtKB:P05631}; Matrix side {ECO:0000250|UniProtKB:P05631}.
Interaction partners:
- ATP synthase subunit alpha
- ATP synthase F
- ATP synthase peripheral stalk subunit OSCP, mitochondrial
- ATP synthase subunit a
- ATP synthase subunit 9, mitochondrial
- ATP synthase F
- ATP synthase F
- V-type proton ATPase proteolipid subunit
- V-ATPase proteolipid subunit C-like domain-containing protein
- ARID/BRIGHT DNA binding domain-containing protein
Sequence:
MNSASKLFVVLASPANQRNMATLKDLKIRLGTVKTISKLTKTLHMVASSKLRSAEKKAEESGPYSVGPQKVLGVVETADAFNTATEPIEDRSNKQLLIAITTDTGMCGPVNHQIIKTIKALLKDDAKQEILVSTTGLKGVAPIVADFPNQFLINGRDFGKADYSFPEVLLFLNEIISKVPNYDSALVVYNKFKNALSYSVDRQFIPGFNLLELNRDKFYEYTTSEDRAATMKDLSEFYLASSLWTGLYQNRASEMAARMVAMDNASKNGESISQALGLQYNRARQAMITSELIEIVSGASAIESSD
Protein: Fidgetin-like protein 1 (EC 3.6.4.-) (Q8BPY9)
Organism: Mus musculus (Mouse)
Function: Involved in DNA double-strand break (DBS) repair via homologous recombination (HR). Recruited at DSB sites independently of BRCA2, RAD51 and RAD51 paralogs in a H2AX-dependent manner. May regulate osteoblast proliferation and differentiation. May play a role in the control of male meiosis dynamic.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q6PIW4}. Cytoplasm {ECO:0000269|PubMed:22110678}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:22110678}. Note=Together with RAD51 and a subset of H2A histone proteins, redistributed in discrete nuclear DNA damage-induced foci after ionizing radiation (IR) treatment. {ECO:0000250|UniProtKB:Q6PIW4}.
Interaction partners:
- Exonuclease 1
- UBX domain-containing protein 7
- DNA repair and recombination protein RAD54-like
- DNA repair-scaffolding protein
- DNA excision repair protein ERCC-6-like
- FIGNL1-interacting regulator of recombination and mitosis
- Condensin complex subunit 2
- Mitotic spindle assembly checkpoint protein MAD2A
- Kinetochore-associated protein 1
- Protein SPMIP7
Sequence:
METSSSMSVETTRSVQVDEWQKNYCVVTSSICTPKQKADAYRALLLHIQYAYANSEISQVFATNLFKRYTEKYSAIIDSDNVVTGLNNYAESIFALAGSRQADSNKWQSGLSIDNVFKMSCVQEMMQAGKKFEESLLEPADASVVLCKEPTAFEVPQLSVCGGSEDADILSSSGHDTDKTQAIPGSSLRCSPFQSARLPKETNTTKTCLTSSTSLGESATAAFHMTPLFGNTEKDTQSFPKTSTGLNMFLSNLSCVPSGCENPQERKAFNDSDIIDILSNPTLNKAPSKTEDRGRREDNSLPTFKTAKEQLWVDQKKKGHQSQHTSKSSNGVMKKSLGAGRSRGIFGKFVPPVSNKQDGSEQHAKKHKSSRAGSAEPAHLTDDCLKNVEPRMVELIMNEIMDHGPPVHWDDIAGVEFAKATIKEIVVWPMMRPDIFTGLRGPPKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKWVGEGEKMVRALFAVARCQQPAVIFIDEIDSLLSQRGDGEHESSRRIKTEFLVQLDGATTSSEDRILVVGATNRPQEIDEAARRRLVKRLYIPLPEASARKQIVGNLMSKEQCCLSDEETDLVVQQSDGFSGADMTQLCREASLGPIRSLHAADIATISPDQVRPIAYIDFENAFKTVRPTVSPKDLELYENWNETFGCGK
Protein: Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial (EC 2.3.1.61) (2-oxoglutarate dehydrogenase complex component E2) (OGDC-E2) (Dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complex) (E2K) (Q9D2G2)
Organism: Mus musculus (Mouse)
Function: Dihydrolipoamide succinyltransferase (E2) component of the 2-oxoglutarate dehydrogenase complex (By similarity). The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2) (By similarity). The 2-oxoglutarate dehydrogenase complex is mainly active in the mitochondrion. A fraction of the 2-oxoglutarate dehydrogenase complex also localizes in the nucleus and is required for lysine succinylation of histones: associates with KAT2A on chromatin and provides succinyl-CoA to histone succinyltransferase KAT2A (By similarity).
Subcellular location: Mitochondrion matrix {ECO:0000250|UniProtKB:P36957}. Nucleus {ECO:0000250|UniProtKB:P36957}. Note=Mainly localizes in the mitochondrion. A small fraction localizes to the nucleus, where the 2-oxoglutarate dehydrogenase complex is required for histone succinylation. {ECO:0000250|UniProtKB:P36957}.
Interaction partners:
- 2-oxoglutarate dehydrogenase-like, mitochondrial
- 2-oxoglutarate dehydrogenase complex component E1
- Dihydrolipoyl dehydrogenase, mitochondrial
- 2-oxoadipate dehydrogenase complex component E1
- Succinate--CoA ligase subunit alpha, mitochondrial
- Succinate--CoA ligase subunit beta, mitochondrial
- Succinate--CoA ligase [GDP-forming] subunit beta, mitochondrial
- Pyruvate dehydrogenase E1 component subunit beta, mitochondrial
- Isocitrate dehydrogenase subunit alpha, mitochondrial
- 2-oxoisovalerate dehydrogenase subunit beta, mitochondrial
Sequence:
MLSRSRCVSRAFSRSLSAFQKGNCPLGRRSLPGVSLCRGPGYPDNRKMVINSGSVFRVRFFQTTAVCKNDVITVQTPAFAESVTEGDVRWEKAVGDAVAEDEVVCEIETDKTSVQVPSPANGIIEALLVPDGGKVEGGTPLFTLRKTGAAPAKAKPAETPAPAHKAEPAAPAAPPPPAAPVLTQMPPVPSPSQPPSSKPVSAIKPTAAPPLAEAGAAKGLRSEHREKMNRMRQRIAQRLKEAQNTCAMLTTFNEVDMSNIQEMRARHKDAFLKKHNLKLGFMSAFVKASAFALQEQPVVNAVIDDATKEVVYRDYIDISVAVATPRGLVVPVIRNVETMNYADIERTINELGEKARKNELAIEDMDGGTFTISNGGVFGSLFGTPIINPPQSAILGMHAIFDRPVAVGGKVEVRPMMYVALTYDHRLIDGREAVTFLRKIKAAVEDPRVLLLDL
Protein: Immune induced molecule 33, isoform A (Immune induced molecule 33, isoform B) (RH05411p) (RH38008p) (Q9VQT8)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
- RH15675p
- Fondue, isoform B
- FI01556p
Sequence:
MKFIAAVCLMFALVAVALGLKDPICGLPAGIDGNGLIKCAAFIPSFSYHPETNSCEKFIYGGCGGNENRFGTQELCEQKCKE
Protein: DNA-binding transcriptional activator AdeR (PucR-type transcriptional activator AdeR) (P71073)
Organism: Bacillus subtilis (strain 168)
Function: Activates ald expression in response to alanine availability and is important for normal sporulation in B.subtilis.
Interaction partners:
- Adenine deaminase
- NTD biosynthesis operon regulator NtdR
- Alanine dehydrogenase
Sequence:
MSKRNQARKVGRFMTMPNDPFKYSFDRLEDVADHISDVLRCPITIEDVNHKLLAYSTHSDCTDPARTSTIIGRRVPEKVINKLWKDGTIPALLKTDQPIRVKQIDEVGLSNRVAISIWKNKQVLGFIWALEIQKTLSDEDLLTLQMAAKAVKNKLLKLQIRKTKNEERSQEFFWKMLTGHIHQEDDMADGFHKLGMAAPSEFSVMIIRINGELTEKIEQQLQYLQETTQQVYVLLATVDSNELIILTSPKTDHPFQDLKQFALSTQKQLKERYKIEDVSIAFGGIYNSISFVSRSYQEALSVLKTKERFAEETKHLFSFSELGIYQYLDVLNEKRKQAGHYNYSLSKLEQYDRDHQSNMVETLERFIEADSNVNTASKLLNIHVNTLNYRLKRISQIAEIDLKNVNQKFTIYLDIKLRHMDL
Protein: Desiccation-related protein clone PCC27-04 (P22238)
Organism: Craterostigma plantagineum (Blue gem) (Torenia plantagineum)
Interaction partners:
Sequence:
MAHSLGEQYDLGKPTEEHHESHPPAHQAPHAGGELGAGQKTSQLARSNSSSSSSSEDDGQGGRRKKPIKEKVKEKLPGGAGGKQTGECGTTTTTAAGGHEEKKGVMEKIKEKLPGQH
Protein: MGC68541 protein (Nucleoporin 54kDa S homeolog) (Q6PAY1)
Organism: Xenopus laevis (African clawed frog)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MAFNFGATTGTPANQGGFGGFGATTTASTGPAFSFTTPANTTSGLFGATQNKGFGFGTGFGSTTTSTGLGTGLGTGLGFTGFNTSQQQQQQSVLGAGLFNQSFQSTPQSNQLINTASALSAPTLLGDERDAILAKWNQLQAFWGTGKGFFMNNTPPVEFTQENPFCRFKAVGFSYIPNNKDEDGMISLIFNKKESDIRGQQQQLVESLHKVLGGHQTLTVNVEGVKTKADNQTEVIIYVVERSPNGTSRRVGASALFSYFEQAHIKANMQQLGVTGAMAQTELSPVQIKQLIQNPLSGVDPIIWEQAKVDNPDPERLIPVPMIGFKELLRRLEVQDQMTKQHQSRLDIISEDIGELQKNQTTTMAKIGQYKRKLMELSHRVLQVLIKQEIQRKSGFAIQAEEEQLRVQLDTIQSELNAPTQFKGRLNELMSQIRMQNHFGAVRSEEKYYVDADLLREIKQHLKQQQEGVSHLISIIKDNHEDIKLIEQGLNDNLHMRTGFLS
Protein: WAP four-disulfide core domain protein 3 (Putative protease inhibitor WAP14) (Q8IUB2)
Organism: Homo sapiens (Human)
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Protein WFDC10B
Sequence:
MMLSCLFLLKALLALGSLESWITAGEHAKEGECPPHKNPCKELCQGDELCPAEQKCCTTGCGRICRDIPKGRKRDCPRVIRKQSCLKRCITDETCPGVKKCCTLGCNKSCVVPISKQKLAEFGGECPADPLPCEELCDGDASCPQGHKCCSTGCGRTCLGDIEGGRGGDCPKVLVGLCIVGCVMDENCQAGEKCCKSGCGRFCVPPVLPPKLTMNPNWTVRSDSELEIPVP