wanglab/gogpt-training-data huggingface dataset:
Protein: Prefoldin subunit 2 (O70591)
Organism: Mus musculus (Mouse)
Function: Binds specifically to cytosolic chaperonin (c-CPN) and transfers target proteins to it. Binds to nascent polypeptide chain and promotes folding in an environment in which there are many competing pathways for nonnative proteins.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9UHV9}. Cytoplasm {ECO:0000250|UniProtKB:Q9UHV9}. Mitochondrion {ECO:0000250|UniProtKB:Q9UHV9}.
Interaction partners:
- Prefoldin subunit 5
- Prefoldin subunit 6
- p53 and DNA damage-regulated protein 1
- Prefoldin subunit 1
- Prefoldin subunit 3
- Prefoldin subunit 4
- Protein UXT
- Dynein axonemal assembly factor 10
- DNA-directed RNA polymerases I, II, and III subunit RPABC1
- Unconventional prefoldin RPB5 interactor
Sequence:
MADSSGRVGKSGGSGAGKGAVSAEQVIAGFNRLRQEQRGLASKAAELEMELNEHSLVIDTLKEVDETRKCYRMVGGVLVERTVKEVLPALEGNKEQIQKIIETLSQQLQAKGKELNEFREKHNIRLMGEDEKPAAKENSEGAGAKASSAGVLVS
Protein: Dual specificity protein phosphatase 16 (EC 3.1.3.16) (EC 3.1.3.48) (Mitogen-activated protein kinase phosphatase 7) (MAP kinase phosphatase 7) (MKP-7) (Q9BY84)
Organism: Homo sapiens (Human)
Function: Dual specificity protein phosphatase involved in the inactivation of MAP kinases. Dephosphorylates MAPK10 bound to ARRB2.
Subcellular location: Cytoplasm. Nucleus. Cytoplasmic vesicle. Note=After dissociation upon AGTR stimulation, re-associates with ARRB2 on endocytic vesicles.
Interaction partners:
- Mitogen-activated protein kinase 8
- Mitogen-activated protein kinase 9
- Mitogen-activated protein kinase 14
- Mitogen-activated protein kinase 12
- Mitogen-activated protein kinase 13
- Mitogen-activated protein kinase 11
- Mitogen-activated protein kinase 1
- DNA-directed RNA polymerase I subunit RPA43
- Mitogen-activated protein kinase 3
- C-Jun-amino-terminal kinase-interacting protein 1
Sequence:
MAHEMIGTQIVTERLVALLESGTEKVLLIDSRPFVEYNTSHILEAININCSKLMKRRLQQDKVLITELIQHSAKHKVDIDCSQKVVVYDQSSQDVASLSSDCFLTVLLGKLEKSFNSVHLLAGGFAEFSRCFPGLCEGKSTLVPTCISQPCLPVANIGPTRILPNLYLGCQRDVLNKELMQQNGIGYVLNASNTCPKPDFIPESHFLRVPVNDSFCEKILPWLDKSVDFIEKAKASNGCVLVHCLAGISRSATIAIAYIMKRMDMSLDEAYRFVKEKRPTISPNFNFLGQLLDYEKKIKNQTGASGPKSKLKLLHLEKPNEPVPAVSEGGQKSETPLSPPCADSATSEAAGQRPVHPASVPSVPSVQPSLLEDSPLVQALSGLHLSADRLEDSNKLKRSFSLDIKSVSYSASMAASLHGFSSSEDALEYYKPSTTLDGTNKLCQFSPVQELSEQTPETSPDKEEASIPKKLQTARPSDSQSKRLHSVRTSSSGTAQRSLLSPLHRSGSVEDNYHTSFLFGLSTSQQHLTKSAGLGLKGWHSDILAPQTSTPSLTSSWYFATESSHFYSASAIYGGSASYSAYSCSQLPTCGDQVYSVRRRQKPSDRADSRRSWHEESPFEKQFKRRSCQMEFGESIMSENRSREELGKVGSQSSFSGSMEIIEVS
Protein: Inner membrane-spanning protein YciB (P0A710)
Organism: Escherichia coli (strain K12)
Function: Plays a role in cell envelope biogenesis, maintenance of cell envelope integrity and membrane homeostasis. Required for the normal cell elongation. May participate in the cell division process. Important for the septum site localization of the essential divisome protein ZipA.
Subcellular location: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_00189, ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:26391555, ECO:0000269|PubMed:26454142}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00189, ECO:0000269|PubMed:26454142, ECO:0000305|PubMed:15919996}. Note=Distributed in the inner membrane through the whole cell. {ECO:0000269|PubMed:26391555}.
Interaction partners:
- UPF0259 membrane protein YciC
- Acyl-CoA thioester hydrolase YciA
Sequence:
MKQFLDFLPLVVFFAFYKIYDIYAATAALIVATAIVLIYSWVRFRKVEKMALITFVLVVVFGGLTLFFHNDEFIKWKVTVIYALFAGALLVSQWVMKKPLIQRMLGKELTLPQPVWSKLNLAWAVFFILCGLANIYIAFWLPQNIWVNFKVFGLTALTLIFTLLSGIYIYRHMPQEDKS
Protein: MHC class I antigen (F1CN43)
Organism: Gallus gallus (Chicken)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
Sequence:
MGPCGALGLGLLLAAVCGAAAELHTLRYIRTAMTDPGPGQPWFVTVGYVDGELFVHYNSTARRYVPRTEWIAANTDQQYWDGQTQIGQLNEQINRENLGIRQRRYNQTGGSHTVQWMFGCDILEDGTIRGYRQSAYDGRDFIALDKDMKTFTAAVPEAVPTKRKWEEESEPERWKNYLEETCVEWLRRYVEYGKAELGRRERPEVRVWGKEADGILTLSCRAHGFYPRPIVVSWLKDGAVRGQDAQSGGIVPNGDGTYHTWVTIDAQPGDGDKYQCRVEHASLPQPGLYSWEPPQPNLVPIVAGVAVAIVAIAIVVGVGFIIYRRHAGKKGKGYNIAPGSNPTI
Protein: Large ribosomal subunit protein uL13B (60S ribosomal protein L16-B) (L21) (RP23) (YL15) (P26785)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:22096102}.
Interaction partners:
- Large ribosomal subunit protein uL15
- Large ribosomal subunit protein uL18
- Large ribosomal subunit protein eL15A
- Large ribosomal subunit protein eL13A
- Large ribosomal subunit protein eL32
- Large ribosomal subunit protein uL23
- Large ribosomal subunit protein uL3
- Large ribosomal subunit protein uL10
- Large ribosomal subunit protein eL6A
- Large ribosomal subunit protein eL14A
Sequence:
MSQPVVVIDAKDHLLGRLASTIAKQVLNGQKIVVVRAEALNISGEFFRNKLKYHDFLRKATAFNKTRGPFHFRAPSRILYKAIRGMVSHKTARGKAALERLKIFEGIPPPYDKKKRVVVPQALRVLRLKPGRKYTTLGKLSTSVGWKYEDVVAKLEDKRKVRSAEYYAKKRAFTKKVSSASAAASESDVAKQLASFGY
Protein: Poly(ADP-ribose) glycohydrolase 2 (EC 3.2.1.143) (Poly ADP-ribose metabolism enzyme 4) (Q9N5L4)
Organism: Caenorhabditis elegans
Function: Poly(ADP-ribose) synthesized after DNA damage is only present transiently and is rapidly degraded by poly(ADP-ribose) glycohydrolase. Poly(ADP-ribose) metabolism may be required for maintenance of the normal function of neuronal cells (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:17188026}.
Interaction partners:
- Poly [ADP-ribose] polymerase 2
- Poly [ADP-ribose] polymerase 1
- IBR domain-containing protein
- Poly [ADP-ribose] polymerase tankyrase
Sequence:
MDHENLMKYLEEFRSIRFQPDFQKVDAERNVRYCEITDFPISNISFELLETGVSQQWRNCDQNLFNEYLKTYKNGGYSQFEDLLFKIWGYSEEKERFDLPALKSFYRKMSEIVGEDEVLEKLARLVRITKSACEVLPEKIYRLVGDIESATFSHIQCASLIAWMFFSDTPRLSFIIILQKTTCVAVEKLKFLFTYFDKMSIDPPIGAVSFRKMRITHKQYLENWKLRETNLLPDVQVFDKMSIEETALCTQIDFANKRLGGGVLKGGAVQEEIRFMMCPEMMVAILLNDVTQDLEAISIVGAYVFSSYTGYSNTLKWAKITPKHSAQNNNSFRDQFGRLQTETVAIDAVRNAGTPLECLLNQLTTEKLTREVRKAAIGFLSAGDGFSKIPVVSGWWGCGAFRGNKPLKFLIQVIACGISDRPLQFCTFGDTELAKKCEEMMTLFRNNNVRTGQLFLIINSIGPPLNYSEQYVFDAIRAKINSTKA
Protein: Eukaryotic initiation factor 4B (Eukaryotic translation initiation factor 4B, isoform B) (LD33831p) (Q7PLL3)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Eukaryotic initiation factor 4A
- Eukaryotic translation initiation factor 4E1
- eIF-4F 25 kDa subunit
- eIF-4F 25 kDa subunit
- Eukaryotic translation initiation factor 4G1, isoform B
- eIF-4F 25 kDa subunit
- eIF-4F 25 kDa subunit
- eIF-4F 25 kDa subunit
- Ribosomal protein S6 kinase
- Polyadenylate-binding protein
Sequence:
MASAGKKGKKNKGTVISLQSFLCNSDAPVGTTQVSKKIRNLDGDDSDDGSGTLPLVYQLPTAPRANRIFDDNSIPHKAPFIAYINNLPFDANEDDLYEFFEGINLISLRLPREDGENGRSRGFGYVELENREDLIHVLSLPDPSIKGRRIRIELSNENDQQSRQKSNRRFDGFGNNGDNRDSGNWRRDSQNNGSNFGYSSNFERSFNRERKSLPDRDDVNTPGSWRTSARPQSIDTSPTRREVEQVSEKYREGRVKIADRYSREETSKVEEERPKLNLKPRTLPLPDVKTIEFEKCDVDEFNLDKQGGTSSLNVFGSAKPVDTAARELEIEQRLALARKQDKGRREQGLNEKLAELQVDKNDNESLSATVSWRTNQDYKESDKINKCPGEKQRDEEIHRLNHARGQFNRPELLREKPNANGESKRDCRNDRSVSKKTSQNDLVLQSSNKYSGLDNEGSE
Protein: Protein phosphatase 1J (EC 3.1.3.16) (Protein phosphatase 2C isoform zeta) (PP2C-zeta) (Q5JR12)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MLNRVRSAVAHLVSSGGAPPPRPKSPDLPNAASAPPAAAPEAPRSPPAKAGSGSATPAKAVEARASFSRPTFLQLSPGGLRRADDHAGRAVQSPPDTGRRLPWSTGYAEVINAGKSRHNEDQACCEVVYVEGRRSVTGVPREPSRGQGLCFYYWGLFDGHAGGGAAEMASRLLHRHIREQLKDLVEILQDPSPPPLCLPTTPGTPDSSDPSHLLGPQSCWSSQKEVSHESLVVGAVENAFQLMDEQMARERRGHQVEGGCCALVVIYLLGKVYVANAGDSRAIIVRNGEIIPMSREFTPETERQRLQLLGFLKPELLGSEFTHLEFPRRVLPKELGQRMLYRDQNMTGWAYKKIELEDLRFPLVCGEGKKARVMATIGVTRGLGDHSLKVCSSTLPIKPFLSCFPEVRVYDLTQYEHCPDDVLVLGTDGLWDVTTDCEVAATVDRVLSAYEPNDHSRYTALAQALVLGARGTPRDRGWRLPNNKLGSGDDISVFVIPLGGPGSYS
Protein: Phosphoenolpyruvate carboxylase (PEPC) (PEPCase) (EC 4.1.1.31) (O27026)
Organism: Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum)
Function: Catalyzes the irreversible beta-carboxylation of phosphoenolpyruvate (PEP) to form oxaloacetate (OAA), a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle.
Interaction partners:
- Pyruvate carboxylase subunit B
- Pyruvate carboxylase subunit A
- Malate dehydrogenase
- Probable phosphoenolpyruvate synthase
- Enolase
- Citrate synthase I
- Citrate synthase I
Sequence:
MKVPRCMSTQHPDNVNPPFFAEEPELGGEDEIREAYYVFSHLGCDEQMWDCEGKEVDNYVVKKLLTKYQAFFRDHVLGEDLRLTLRVPNPTVERAEAKILLETLESIPRSYDTASLFYGMDAAPVFEVILPMTSSSSCLNRIHSYYLDFVKGKERLQLADGVTVKEWIGEFRPDEINVIPLFEDHEGMLNAAKITGEYLDGKDIQEQRVFLARSDPAMNYGMISATLLNRIALSDFRDLEEESGVKLYPIIGMGSAPFRGNLRPDNVEDVTWEYRGAYTFTVQSSFKYDHEPSDVIRGIKKLRSVKPGRAAEIERESVLEIISAYCREYRRQVMDLVDIINRVARYVPGRRKRKLHIGLFGYSRSMGNVSLPRAITFTAALYSLGVPPELLGFNALSSGDLEFIEEVYPGLGRDLHDAARYANPESPFLSPEVKSSFEEYLEPEYDEGHMKTTEEIIRALRINRTANLQELILEAASQRKFLG
Protein: Moricin (Q86MA1)
Organism: Manduca sexta (Tobacco hawkmoth) (Tobacco hornworm)
Function: Antimicrobial peptide. Active against a broad spectrum of Gram-positive and Gram-negative bacteria including methicillin-resistant S.aureus ATCC 43 300, S.aureus BAA-39, pathogenic strains of L.monocytogenes, K.pneumoniae, E.coli O157:H7, S.typhimurium and multidrug-resistant S.typhimurium DT104 with minimum inhibitory concentration (MIC) of 1.4 uM for all except for S.aureus BAA-39. Also active against Serratia marcescens. Probably acts by disturbing membrane functions with its amphipathic alpha-helical structure. May protect a developing embryo from bacterial infection (Probable).
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
Sequence:
MKLTSLFIFVIVALSLLFSSTDAAPGKIPVKAIKQAGKVIGKGLRAINIAGTTHDVVSFFRPKKKKH
Protein: G protein-coupled receptor class C group 5 member C (A0A0C4DFY5)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MRGRGSQQQQPTRRQGQKLPSPSPAGKYESAQPGGTQPEPGLGARMAIHKALVMCLGLPLFLFPGAWAQGHVPPGCSQGLNPLYYNLCDRSGAWGIVLEAVAGAGIVTTFVLTIILVASLPFVQDTKKRSLLGTQVFFLLGTLGLFCLVFACVVKPDFSTCASRRFLFGVLFAICFSCLAAHVFALNFLARKNHGPRGWVIFTVALLLTLVEVIINTEWLIITLVRGSGEGGPQGNSSAGWAVASPCAIANMDFVMALIYVMLLLLGAFLGAWPALCGRYKRWRKHGVFVLLTTATSVAIWVVWIVMYTYGNKQHNSPTWDDPTLAIALAANAWAFVLFYVIPEVSQVTKSSPEQSYQGDMYPTRGVGYETILKEQKGQSMFVENKAFSMDEPVAAKRPVSPYSGYNGQLLTSVYQPTEMALMHKVPSEGAYDIILPRATANSQVMGSANSTLRAEDMYSAQSHQAATPPKDGKNSQVFRNPYVWD
Protein: Acetate kinase AckA (EC 2.7.2.1) (Acetokinase) (P63411)
Organism: Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Function: Catalyzes the formation of acetyl phosphate from acetate and ATP. Can also catalyze the reverse reaction. Has broad substrate specificity and can also utilize GTP, UTP and CTP. Can also phosphorylate propionate, but has very low activity with formate and is inactive with butyrate.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00020}.
Interaction partners:
- Phosphate acetyltransferase EutD
- Phosphate acetyltransferase
- Phosphate propanoyltransferase
- Acetyl-coenzyme A synthetase
- Pyruvate dehydrogenase
- Acyl carrier protein
- Propionate--CoA ligase
- Aldehyde dehydrogenase B
- Propionate kinase
- Propionate kinase PduW
Sequence:
MSSKLVLVLNCGSSSLKFAIIDAVNGDEYLSGLAECFHLPEARIKWKMDGSKQEAALGAGAAHSEALNFIVNTILAQKPELSAQLTAIGHRIVHGGEKYTSSVVIDESVIQGIKDSASFAPLHNPAHLIGIAEALKSFPQLKDKNVAVFDTAFHQTMPEESYLYALPYSLYKEHGVRRYGAHGTSHFYVTQEAAKMLNKPVEELNIITCHLGNGGSVSAIRNGKCVDTSMGLTPLEGLVMGTRSGDIDPAIIFHLHDTLGMSVDQINKMLTKESGLLGLTEVTSDCRYVEDNYATKEDAKRAMDVYCHRLAKYIGSYTALMDGRLDAVVFTGGIGENAAMVRELSLGKLGVLGFEVDHERNLAARFGKSGFINKEGTRPAVVIPTNEELVIAQDASRLTA
Protein: Beta-galactosidase 11 (Lactase 11) (EC 3.2.1.23) (Q9SCV1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Secreted, extracellular space, apoplast {ECO:0000305}.
Interaction partners:
- Methyl-CpG-binding domain-containing protein 13
Sequence:
MRKHSLDRWLLTAVLVVLLSSSSSFAAKKDAKKKKKSNKEVTYDGTSLIIDGKRELLYSGSIHYPRSTPEMWPSIIKRAKQGGLNTIQTYVFWNVHEPQQGKFNFSGRADLVKFIKLIQKNGMYVTLRLGPFIQAEWTHGGLPYWLREVPGIFFRTDNKQFKEHTERYVRMILDKMKEERLFASQGGPIILGQIENEYSAVQRAYKQDGLNYIKWASNLVDSMKLGIPWVMCKQNDAPDPMINACNGRHCGDTFPGPNRENKPSLWTENWTTQFRVFGDPPTQRSVEDIAYSVARFFSKNGTHVNYYMYHGGTNFGRTSAHYVTTRYYDDAPLDEYGLEKEPKYGHLKHLHNALNLCKKPLLWGQPKTEKPGKDTEIRYYEQPGTKTCAAFLANNNTEAAETIKFKGREYVIAPRSISILPDCKTVVYNTAQIVSQHTSRNFMKSKKANKKFDFKVFTETLPSKLEGNSYIPVELYGLTKDKTDYGWYTTSFKVHKNHLPTKKGVKTFVRIASLGHALHAWLNGEYLGSGHGSHEEKSFVFQKQVTLKAGENHLVMLGVLTGFPDSGSYMEHRYTGPRGISILGLTSGTLDLTESSKWGNKIGMEGEKLGIHTEEGLKKVEWKKFTGKAPGLTWYQTYFDAPESVSAATIRMHGMGKGLIWVNGEGVGRYWQSFLSPLGQPTQIEYHIPRSFLKPKKNLLVIFEEEPNVKPELMDFAIVNRDTVCSYVGENYTPSVRHWTRKKDQVQAITDNVSLTATLKCSGTKKIAAVEFASFGNPIGVCGNFTLGTCNAPVSKQVIEKHCLGKAECVIPVNKSTFQQDKKDSCKNVVKMLAVQVKCGRGKKN
Protein: 2-Cys peroxiredoxin BAS1, chloroplastic (EC 1.11.1.24) (Thiol-specific antioxidant protein) (Thioredoxin-dependent peroxiredoxin BAS1) (Q6ER94)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides. May be an antioxidant enzyme particularly in the developing shoot and photosynthesizing leaf (By similarity).
Subcellular location: Plastid, chloroplast {ECO:0000250|UniProtKB:Q96291}.
Interaction partners:
- Thioredoxin reductase NTRC
- sulfiredoxin
- Os02g0246900 protein
- Os01g0616300 protein
- Os01g0616333 protein
- Os05g0210600 protein
- Peroxiredoxin-2F, mitochondrial
- Os10g0561200 protein
- Peroxiredoxin-2E-1, chloroplastic
- Peroxiredoxin-2C
Sequence:
MAACCSSLATAVSSSSAKPLAGIPPAAPHSLSLPRAPAARPLRLSASSSRSARASSFVARAGGVDDAPLVGNKAPDFDAEAVFDQEFINVKLSDYIGKKYVILFFYPLDFTFVCPTEITAFSDRYDEFEKLNTEILGVSIDSVFSHLAWVQTDRKSGGLGDLKYPLISDVTKSISKSFGVLIPDQGIALRGLFIIDKEGVIQHSTINNLAIGRSVDETMRTLQALQYVQDNPDEVCPAGWKPGDKSMKPDPKGSKEYFAAI
Protein: Eosinophil cationic protein (ECP) (EC 3.1.27.-) (Ribonuclease 3) (RNase 3) (P12724)
Organism: Homo sapiens (Human)
Function: Cytotoxin and helminthotoxin with low-efficiency ribonuclease activity. Possesses a wide variety of biological activities. Exhibits antibacterial activity, including cytoplasmic membrane depolarization of preferentially Gram-negative, but also Gram-positive strains. Promotes E.coli outer membrane detachment, alteration of the overall cell shape and partial loss of cell content.
Subcellular location: Secreted. Note=Located in the matrix of eosinophil large specific granule, which are released following activation by an immune stimulus.
Interaction partners:
- Eosinophil peroxidase
- Non-secretory ribonuclease
- Myeloperoxidase
- Azurocidin
- Cathepsin G
- Neutrophil elastase
- Angiogenin
- Membrane-spanning 4-domains subfamily A member 3
- Bone marrow proteoglycan
- Interleukin-5
Sequence:
MVPKLFTSQICLLLLLGLMGVEGSLHARPPQFTRAQWFAIQHISLNPPRCTIAMRAINNYRWRCKNQNTFLRTTFANVVNVCGNQSIRCPHNRTLNNCHRSRFRVPLLHCDLINPGAQNISNCTYADRPGRRFYVVACDNRDPRDSPRYPVVPVHLDTTI
Protein: Urease subunit beta (EC 3.5.1.5) (Urea amidohydrolase subunit beta) (D3UJ80)
Organism: Helicobacter mustelae (strain ATCC 43772 / CCUG 25715 / CIP 103759 / LMG 18044 / NCTC 12198 / R85-136P) (Campylobacter mustelae)
Subcellular location: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01953, ECO:0000256|PROSITE-ProRule:PRU00700}.
Interaction partners:
- Urease subunit alpha
- urease
- Urease accessory protein UreF
- Urease accessory protein UreG
- Arginase
- Urease accessory protein UreE
- Urease subunit beta
- Putative urease accessory protein UreH
- Hydrogenase isoenzymes formation protein
Sequence:
MKMKRQEYVNTYGPTTGDKVRLGDTDLWAEVEHDYTVYGEELKFGAGKTIREGMGQSNSPDENTLDLVITNALIIDYTGIYKADIGIKNGKIHGIGKAGNKDMQDGVTPHMVVGVGTEALAGEGMIITAGGIDSHTHFLSPQQFPTALANGVTTMFGGGTGPVDGTNATTITPGVWNLHRMLRAAEEYGMNVGLLGKGNSSSRAQLVEQVKAGAIGFKLHEDWGTTPSAIDHCLSVADEYDVQVCIHTDTVNEAGYVDDTLRAMNGRAIHAYHIEGAGGGHSPDVITMAGEVNILPSSTTPTIPYTINTVAEHLDMLMTCHHLDKRIREDLQFSQSRIRPGSIAAEDTLHDMGVIAMTSSDSQAMGRAGEVIPRTWQTADKNKKEFGRLTEEKGDNDNFRIKRYISKYTINPAITHGVSEYIGSVEEGKIADLVVWNPAFFGVKPKIIIKGGMVVFSEMGDSNASVPTPQPVYYREMFGHHGKAKFDTSITFVSKVAYENGIKEKLGLERKVLPVKNCRNVTKKDFKFNNTTAKITVNPETFEVFVNGKLCTSKPATEVALASRYTFF
Protein: Molybdopterin synthase catalytic subunit (EC 2.8.1.12) (MPT synthase subunit 2) (Molybdenum cofactor biosynthesis protein E) (Molybdopterin-converting factor large subunit) (Molybdopterin-converting factor subunit 2) (P56422)
Organism: Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori)
Function: Converts molybdopterin precursor Z into molybdopterin. This requires the incorporation of two sulfur atoms into precursor Z to generate a dithiolene group. The sulfur is provided by MoaD (By similarity).
Interaction partners:
- Cyclic pyranopterin monophosphate synthase
- Molybdopterin converting factor, subunit 1
- Molybdopterin adenylyltransferase
- Thiamin biosynthesis protein
- Molybdopterin molybdenumtransferase
- GTP 3',8-cyclase
- Potassium channel protein, putative
- Molybdenum cofactor guanylyltransferase
- SurA N-terminal domain-containing protein
- YjgP/YjgQ family permease
Sequence:
MLKIIQGALDTRELLKAYQEEACAKNFGAFCVFVGIVRKEDNIQGLSFDIYEALLKTWFEKWHHKAKDLGVVLKMAHSLGDVLIGQSSFLCVSMGKNRKNALELYENFIEDFKHNAPIWKYDLIHNKRIYAKERSHPLKGSGLLA
Protein: WRKY transcription factor WRKY24 (OsWRKY24) (Q6B6R4)
Organism: Oryza sativa subsp. indica (Rice)
Function: Transcription repressor (By similarity). Interacts specifically with the W box (5'-(T)TGAC[CT]-3'), a frequently occurring elicitor-responsive cis-acting element. Negative regulator of both gibberellic acid (GA) and abscisic acid (ABA) signaling in aleurone cells, probably by interfering with GAM1, via the specific repression of GA- and ABA-induced promoters (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q6QHD1, ECO:0000255|PROSITE-ProRule:PRU00223}.
Interaction partners:
- VQ domain-containing protein
Sequence:
MTTSSSGSVETSANSRPGTFSFASASFTDLLGGNAGAGGGGVSRYKAMTPPSLPLSPPPVSPSSFFNSPIGMNQADFLGSPVLLTSSIFPSPTTGAFASQHFDWRPEVAAAQSADQGGKDEQRNSYSDFSFQTAPASEEAARTTTFQPPVPPALLGDEAYRSQQQQQPWGYQQQPAGMDAGANAASFGAAPFQATSSEMAPQVQGGGGYSQPQSQRRSSDDGYNWRKYGQKQVKGSENPRSYYKCTFPNCPTKKKVERSLDGQITEIVYKGTHNHAKPQNTRRNSGSSAAQVLQSGGDMSEHSFGGMSGTAATPENSSASFGDDEIGVGSPRAGNGGGDEFDDDEPDSKRWRKDGDGEGISMAGNRTVREPRVVVQTMSDIDILDDGYRWRKYGQKVVKGNPNPRSYYKCTTAGCPVRKHVERASHDLRAVITTYEGKHNHDVPAARGSAALYRPAPPAAAATSSHPYLPNQPPPMSYQPTGPQPYALRPDGFGGQGPFGGVVGGSSFGGLSGFDDARGSYMSQHQQQQRQNDAMHASRAKEEPGDDMFFQNSLY
Protein: EMAP like 4 (B5MBZ0)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MDGFAGSLDDSISAASTSDVQDRLSALESRVQQQEDEITVLKAALADVLRRLAISEDHVASVKKSVSSKGQPSPRAVIPMSCITNGSGANRKPSHTSAVSIAGKETLSSAAKSGTEKKKEKPQGQREKKEESHSNDQSPQIRASPSPQPSSQPLQIHRQTPESKNATPTKSIKRPSPAEKSHNSWENSDDSRNKLSKIPSTPKLIPKVTKTADKHKDVIINQAKMSTREKNSQEGEYIKMFMRGRPITMFIPSDVDNYDDIRTELPPEKLKLEWAYGYRGKDCRANVYLLPTGKIVYFIASVVVLFNYEERTQRHYLGHTDCVKCLAIHPDKIRIATGQIAGVDKDGRPLQPHVRVWDSVTLSTLQIIGLGTFERGVGCLDFSKADSGVHLCIIDDSNEHMLTVWDWQKKAKGAEIKTTNEVVLAVEFHPTDANTIITCGKSHIFFWTWSGNSLTRKQGIFGKYEKPKFVQCLAFLGNGDVLTGDSGGVMLIWSKTTVEPTPGKGPKGVYQISKQIKAHDGSVFTLCQMRNGMLLTGGGKDRKIILWDHDLNPEREIEVPDQYGTIRAVAEGKADQFLVGTSRNFILRGTFNDGFQIEVQGHTDELWGLATHPFKDLLLTCAQDRQVCLWNSMEHRLEWTRLVDEPGHCADFHPSGTVVAIGTHSGRWFVLDAETRDLVSIHTDGNEQLSVMRYSIDGTFLAVGSHDNFIYLYVVSENGRKYSRYGRCTGHSSYITHLDWSPDNKYIMSNSGDYEILYWDIPNGCKLIRNRSDCKDIDWTTYTCVLGFQVFGVWPEGSDGTDINALVRSHNRKVIAVADDFCKVHLFQYPCSKAKAPSHKYSAHSSHVTNVSFTHNDSHLISTGGKDMSIIQWKLVEKLSLPQNETVADTTLTKAPVSSTESVIQSNTPTPPPSQPLNETAEEESRISSSPTLLENSLEQTVEPSEDHSEEESEEGSGDLGEPLYEEPCNEISKEQAKATLLEDQQDPSPSS
Protein: Ribonuclease VapC1 (RNase VapC) (EC 3.1.-.-) (NTHi VapC1) (Toxin VapC) (Q4QNL7)
Organism: Haemophilus influenzae (strain 86-028NP)
Function: Toxic component of a type II toxin-antitoxin (TA) system. Acts as an RNase (Probable). Its toxic effect is neutralized by cognate antitoxin VapB1 but not by non-cognate antitoxin VapB2.
Interaction partners:
Sequence:
MIYMLDTNIIIYLMKNRPKIIAERVSQLLPNDRLVMSFITYAELIKGAFGSQNYEQSIRAIELLTERVNVLYPNEQICLHYGKWANTLKKQGRPIGNNDLWIACHALSLNAVLITHNVKEFQRITDLQWQDWTK
Protein: Major urinary protein 11 (P04938)
Organism: Mus musculus (Mouse)
Function: Major urinary proteins (Mups) bind pheromones, and thus stabilize them to allow slow release into the air from urine marks. May protect pheromones from oxidation. May also act as pheromones themselves. In this context, they play a role in the regulation of social behaviors, such as aggression, mating, pup-suckling, territory establishment and dominance (Probable). Binds the pheromone analog 2-sec-butyl-4,5-dihydrothiazole (SBT) in vitro.
Subcellular location: Secreted {ECO:0000250|UniProtKB:Q5FW60}.
Interaction partners:
- Major urinary protein 6
Sequence:
MKMLLLLLCLGLTLVCVHAEEASSTGRNFNVEKINGEWHTIILASDKREKIEDNGNFRLFLEQIHVLENSLVLKFHTVRDEECSELSMVADKTEKAGEYSVTYDGFNTFTIPKTDYDNFLMAHLINEKDGETFQLMGLYGREPDLSSDIKERFAQLCEEHGILRENIIDLSNANRCLQARE
Protein: cGMP-specific 3',5'-cyclic phosphodiesterase (EC 3.1.4.35) (cGMP-binding cGMP-specific phosphodiesterase) (CGB-PDE) (Q8CG03)
Organism: Mus musculus (Mouse)
Function: Plays a role in signal transduction by regulating the intracellular concentration of cyclic nucleotides. This phosphodiesterase catalyzes the specific hydrolysis of cGMP to 5'-GMP. Specifically regulates nitric-oxide-generated cGMP.
Interaction partners:
- Adenine phosphoribosyltransferase
- Inosine triphosphate pyrophosphatase
- Guanylate kinase
- Hypoxanthine-guanine phosphoribosyltransferase
- GMP synthase
- Guanylate cyclase soluble subunit beta-1
- Guanylate cyclase soluble subunit alpha-1
- Atrial natriuretic peptide receptor 2
- Atrial natriuretic peptide receptor 1
- Adenylate cyclase type 3
Sequence:
MERAGPNSVRSQQQRDPDWVEAWLDDHRDFTFSYFIRKATRDMVNAWFSERVHNIPVCKEGIRAHTESCSCSLQQSPHADNTTPGAPARKISASEFDRPLRPIVVKDSEGTVSFLSDSGKKEQMPLTPPRFDSDEGDQCSRLLELVKDISSHLDVTALCHKIFLHIHGLISADRYSLFLVCEDSSKDKFLISRLFDVAEGSTLEEASNNCIRLEWNKGIVGHVAAFGEPLNIKDAYEDPRFNAEVDQITGYKTQSILCMPIKNHREEVVGVAQAINKKSGNGGTFTEKDEKDFAAYLAFCGIVLHNAQLYETSLLENKRNQVLLDLASLIFEEQQSLEVILKKIAATIISFMQVQKCTIFIVDEDCPDSFSRVFHMECEEVGKPSDPLTREQDANKINYMYAQYVKNTMEPLNIPDVTKDKRFPWTNENMGHVNTPCIGSLLCTPIKNGKKNKVIGVCQLVNKMEENTGKIKAFNQNDEQFLEAFVIFCGLGIQNTQMYEAVERAMAKQMVTLEVLSYHASAAEEETRELQALSAAVVPSAQTLKITDFSFSDFELSDLETALCTIRMFTDLNLVQNFQMKHEVLCRWILSVKKNYRKNVAYHNWRHAFNTAQCMFAALKAGKIQNKLTDLETLALLIAALSHDLDHRGVNNSYIQRSEHPLAQLYCHSIMEHHHFDQCLMILNSPGNQILSGLSIDEYKTTLKIIKQAILATDLALYIKRRGEFFELIRKNQFSFEDPLQKELFLAMLMTACDLSAITKPWPIQQRIAELVAAEFFDQGDRERKELNMEPADLMNREKKNKIPSMQVGFIDAICLQLYEALTHVSEDCLPLLDGCRKNRQKWQALAEQQEKMLLNGESSQGKRD