wanglab/gogpt-training-data huggingface dataset:
Protein: Cyclic nucleotide-gated channel alpha-2 (CNG channel alpha-2) (CNG-2) (CNG2) (Cyclic nucleotide-gated channel alpha 3) (CNCalpha3) (Olfactory cyclic nucleotide-gated channel subunit 1) (OCNC1) (Q00195)
Organism: Rattus norvegicus (Rat)
Function: Odorant signal transduction is probably mediated by a G-protein coupled cascade using cAMP as second messenger. The olfactory channel can be shown to be activated by cyclic nucleotides which leads to a depolarization of olfactory sensory neurons.
Subcellular location: Cell projection, cilium membrane {ECO:0000269|PubMed:10377344}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Cyclic nucleotide-gated channel subunit beta 1.
- Cyclic nucleotide-gated channel alpha-4
- Calmodulin-1
- Calmodulin-like protein 3
- Calmodulin-like protein 4
- Cyclic nucleotide-gated channel alpha-1
- Cyclic nucleotide gated channel subunit beta 3
- PEX5-related protein
- Adenylate cyclase type 3
- Anoctamin
Sequence:
MMTEKSNGVKSSPANNHNHHPPPSIKANGKDDHRAGSRPQSVAADDDTSPELQRLAEMDTPRRGRGGFQRIVRLVGVIRDWANKNFREEEPRPDSFLERFRGPELQTVTTHQGDDKGGKDGEGKGTKKKFELFVLDPAGDWYYRWLFVIAMPVLYNWCLLVARACFSDLQRNYFVVWLVLDYFSDTVYIADLIIRLRTGFLEQGLLVKDPKKLRDNYIHTLQFKLDVASIIPTDLIYFAVGIHSPEVRFNRLLHFARMFEFFDRTETRTSYPNIFRISNLVLYILVIIHWNACIYYVISKSIGFGVDTWVYPNITDPEYGYLAREYIYCLYWSTLTLTTIGETPPPVKDEEYLFVIFDFLIGVLIFATIVGNVGSMISNMNATRAEFQAKIDAVKHYMQFRKVSKDMEAKVIKWFDYLWTNKKTVDEREVLKNLPAKLRAEIAINVHLSTLKKVRIFQDCEAGLLVELVLKLRPQVFSPGDYICRKGDIGKEMYIIKEGKLAVVADDGVTQYALLSAGSCFGEISILNIKGSKMGNRRTANIRSLGYSDLFCLSKDDLMEAVTEYPDAKKVLEERGREILMKEGLLDENEVAASMEVDVQEKLEQLETNMDTLYTRFARLLAEYTGAQQKLKQRITVLETKMKQNHEDDYLSDGINTPEPTAAE
Protein: Myosin regulatory light chain 11 (DTNB) (Fast skeletal myosin light chain 2) (MLC-2) (G2) (LC2f) (Myosin light chain 11) (Myosin regulatory light chain 2, skeletal muscle isoform) (P02609)
Organism: Gallus gallus (Chicken)
Function: Myosin regulatory subunit that plays an essential to maintain muscle integrity during early development (By similarity). Plays a role in muscle contraction.
Interaction partners:
- Troponin C, skeletal muscle
- Myosin light chain 1, skeletal muscle isoform
- Troponin I, fast skeletal muscle
- Myozenin 1.
- Myosin light chain 1, cardiac muscle
- Sarcolipin
Sequence:
MAPKKAKRRAAEGSSNVFSMFDQTQIQEFKEAFTVIDQNRDGIIDKDDLRETFAAMGRLNVKNEELDAMIKEASGPINFTVFLTMFGEKLKGADPEDVIMGAFKVLDPDGKGSIKKSFLEELLTTQCDRFTPEEIKNMWAAFPPDVAGNVDYKNICYVITHGEDKEGE
Protein: Achaete-scute homolog 2 (ASH-2) (mASH-2) (mASH2) (O35885)
Organism: Mus musculus (Mouse)
Function: AS-C proteins are involved in the determination of the neuronal precursors in the peripheral nervous system and the central nervous system.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P19360}.
Interaction partners:
- WD repeat-containing protein 5
- Retinoblastoma-binding protein 5
- Leucine-rich repeat-containing G-protein coupled receptor 5
- Olfactomedin-4
- Transcription factor E2-alpha
- Transcription factor Atoh1
- Pleckstrin homology-like domain family A member 2
Sequence:
MEAHLDWYGVPGLQEASDACPRESCSSALPEAREGANVHFPPHPVPREHFSCAAPELVAGAQGLNASLMDGGALPRLMPTSSGVAGACAARRRQASPELLRCSRRRRSGATEASSSSAAVARRNERERNRVKLVNLGFQALRQHVPHGGANKKLSKVETLRSAVEYIRALQRLLAEHDAVRAALAGGLLTPATPPSDECAQPSASPASASLSCASTSPSPDRLGCSEPTSPRSAYSSEESSCEGELSPMEQELLDFSSWLGGY
Protein: Glutamine synthetase (GS) (EC 6.3.1.2) (Glutamate--ammonia ligase) (Glutamine synthetase I alpha) (GSI alpha) (P9WN37)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Glutamine synthetase (GS) is an unusual multitasking protein that functions as an enzyme, a transcription coregulator, and a chaperone in ammonium assimilation and in the regulation of genes involved in nitrogen metabolism. It catalyzes the ATP-dependent biosynthesis of glutamine from glutamate and ammonia. Feedback-inhibited GlnA also interacts with and regulates the activity of the transcriptional regulator TnrA. During nitrogen limitation, TnrA is in its DNA-binding active state and turns on the transcription of genes required for nitrogen assimilation. Under conditions of nitrogen excess, feedback-inhibited GlnA forms a stable complex with TnrA, which inhibits its DNA-binding activity. In contrast, feedback-inhibited GlnA acts as a chaperone to stabilize the DNA-binding activity of GlnR, which represses the transcription of nitrogen assimilation genes.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P12425}.
Interaction partners:
- Glutamate synthase large chain
- Bifunctional glutamine synthetase adenylyltransferase/adenylyl-removing enzyme
- Nitrogen regulatory protein P-II
- NAD-specific glutamate dehydrogenase
- assimilatory sulfite reductase
- Bifunctional uridylyltransferase/uridylyl-removing enzyme
- Glutamine--fructose-6-phosphate aminotransferase
- Nitrite reductase small subunit
- Carbamoyl phosphate synthase large chain
- Carbamoyl phosphate synthase small chain
Sequence:
MDRQKEFVLRTLEERDIRFVRLWFTDVLGFLKSVAIAPAELEGAFEEGIGFDGSSIEGFARVSESDTVAHPDPSTFQVLPWATSSGHHHSARMFCDITMPDGSPSWADPRHVLRRQLTKAGELGFSCYVHPEIEFFLLKPGPEDGSVPVPVDNAGYFDQAVHDSALNFRRHAIDALEFMGISVEFSHHEGAPGQQEIDLRFADALSMADNVMTFRYVIKEVALEEGARASFMPKPFGQHPGSAMHTHMSLFEGDVNAFHSADDPLQLSEVGKSFIAGILEHACEISAVTNQWVNSYKRLVQGGEAPTAASWGAANRSALVRVPMYTPHKTSSRRVEVRSPDSACNPYLTFAVLLAAGLRGVEKGYVLGPQAEDNVWDLTPEERRAMGYRELPSSLDSALRAMEASELVAEALGEHVFDFFLRNKRTEWANYRSHVTPYELRTYLSL
Protein: Tubulin alpha-2 chain (EC 3.6.5.-) (P34690)
Organism: Caenorhabditis elegans
Function: Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P68363}.
Interaction partners:
- Tubulin beta-2 chain
- Tubulin beta chain
- Tubulin beta-4 chain
- Tubulin beta chain
- Tubulin beta-1 chain
- Tubulin beta chain
- WD_REPEATS_REGION domain-containing protein
- Dynein heavy chain, cytoplasmic
- Serine/threonine-protein kinase zyg-8
- Cytoplasmic dynein 2 heavy chain 1
Sequence:
MREVISIHVGQAGVQIGNACWELYCLEHGIQPDGTMPTQSTNEGESFTTFFSDTGSGRYVPRSIFVDLEPTVVDEIRTGTYKKLFHPEQMITGKEDAANNYARGHYTVGKELIDTVLDRIRRLADNCSGLQGFFVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDVERPSYTNLNRIISQVVSSITASLRFDGALNVDLNEFQTNLVPYPRIHFPLAAYTPLISAEKAYHEALSVSDITNSCFEPANQMVKCDPRHGKYMAVCLLYRGDVVPKDVNTAIAAIKTKRTIQFVDWCPTGFKVGINYQPPTVVPGGDLAKVPRAVCMLSNTTAIAEAWSRLDYKFDLMYAKRAFVHWYVGEGMEEGEFTEAREDLAALEKDYEEVGADSNEGGEEEGEEY
Protein: D-aminoacyl-tRNA deacylase (EC 3.1.1.96) (Ethanol tolerance protein GEKO1) (Q9ZPQ3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Hydrolyzes D-aminoacyl-tRNA into D-amino acid and free tRNA. Broad specificity toward the amino acid, but strict specificity toward the D-isomer. Seems to be required for ethanol tolerance.
Subcellular location: Nucleus {ECO:0000269|PubMed:15215500}. Cytoplasm {ECO:0000269|PubMed:15215500}.
Interaction partners:
- mRNA-decapping enzyme-like protein
- mRNA-decapping enzyme subunit 2
- Sm-like protein LSM3A
- Sm-like protein LSM3B
- Ribosomal RNA-processing protein 42
- Protein LAZY 2
- Sm-like protein LSM1A
- Sm-like protein LSM1B
- Sm-like protein LSM4
- Exosome complex component RRP4 homolog
Sequence:
MVTLIVATTADPASINPAAALLAMPGWTAGPILPPDIKSFSNKQTRVIQHDRSIVKEDDLDLRWEEATGEVVDEVIFLSRHTAVSNRPALTVHPIGVLHLKDGESPPQGGKPGWAALPSTRIGPWFRLLKKMAEAHGLVPEFEITLEATHHGPITNKPTMFLEIGSTEEYWKRQDAAQVMALLMWEGLGLGGSEEVGKWKSETGKRKVLLGIGGGHYAPRHMDIALKDDIWVGHLLSGYSLPMEDPTQTKTTPGENYIGGNWRQSIKAAFEATKASFPGGEILAHLDHKSFKGWQKKAITEFLAEESINVGKPNDFT
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (A0A5F9W493)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MASSSGSKAEFIVGGKYKLVRKIGSGSFGDIYLAINITNGEEVAVKLESQKARHPQLLYESKLYKILQGGVGIPHIRWYGQEKDYNVLVMDLLGPSLEDLFNFCSRRFTMKTVLMLADQMISRIEYVHTKNFIHRDIKPDNFLMGIGRHCNKCLESPVGKRKRSMTVSTSQDPSFSGLNQLFLIDFGLAKKYRDNRTRQHIPYREDKNLTGTARYASINAHLGIEQSRRDDMESLGYVLMYFNRTSLPWQGLKAATKKQKYEKISEKKMSTPVEVLCKGFPAEFAMYLNYCRGLRFEEAPDYMYLRQLFRILFRTLNHQYDYTFDWTMLKQKAAQQAASSSGQGQQAQTPTGF
Protein: Dystroglycan-type cadherin-like domain-containing protein (H2L0C3)
Organism: Caenorhabditis elegans
Subcellular location: Cell membrane, sarcolemma {ECO:0000256|ARBA:ARBA00004135}.
Interaction partners:
- Beta-sarcoglycan
- Sarcoglycan complex subunit protein
- Syntrophin-1
- Dystrophin-1
- Protein KTI12 homolog
- Dystrobrevin-1
- PDZ domain-containing protein
- Dystroglycan 1
- Dystrophin-like protein 1
- Interactor with SLO-1
Sequence:
MKIRLLDFSIFSILLLFRTSKSFKAPTHVTATKGKFFVHTLHSAHFFPSTVKVKWEATLNKKPALPNWLRLLPSRHPEIAYLIGTPVTNVQHVTLHVIAKRLDNFDIQQRMVVINLVEDSLYQGNTQQVFELPINGLDVEDLVSNRDRKISQLENSLRNTFRGRNVNPYIAGVRSRYIIPRGKEHIFKNSFGTMVYVGTQQKFYPGTMSIVHNLQTMPEFCSNPSSVVMNKYFAPTFPVDWCNVAVRNISSLEGEGIDELIKDEQEEKLTKANPDQNLNEKPEQPPRELYGYSEHGFSIVLFAIILGVSILFVFALVLIFFGSREGQKWRDDKTSGETLGEFISIRDNQKKLRELSLQRQLLSMGPDTNSTAPSGIHSYLQSRSRAPSTSIARFSKSASRLNDKEDTIELLPSVDHVPVGKQTVAEAAKQCGSSLHLYRNPLSNESDEQDTESSDEDN
Protein: Follicle stimulating hormone beta subunit (Q5QHN8)
Organism: Oncorhynchus tshawytscha (Chinook salmon) (Salmo tshawytscha)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613, ECO:0000256|RuleBase:RU004069}.
Interaction partners:
Sequence:
MYCTHLKTLQLVVMATLWVTPVRAGTDCRYGCRLNNMTITVEREDCHGSITITTCAGLCETTDLNYQSTWLPRSQGVCNFKEWSYEKVYLEGCPSGVDPFFIPVAKSCDCIKCKTDNTDCDRISMATPSCIVNPLEM
Protein: Non-disjunction protein 1 (Telomere-associated meiosis protein 1) (Q12366)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for telomeric clustering (bouquet stage) during meiosis 1 prophase, formation and efficient homolog pairing, meiosis 1 disjunction, and telomere deletion during meiosis. Promotes also meiotic recombination.
Subcellular location: Nucleus {ECO:0000269|PubMed:11018056, ECO:0000269|PubMed:16254243, ECO:0000269|PubMed:9157883, ECO:0000269|PubMed:9242487}. Chromosome, telomere {ECO:0000269|PubMed:11018056, ECO:0000269|PubMed:16254243, ECO:0000269|PubMed:9157883, ECO:0000269|PubMed:9242487}.
Interaction partners:
- Spindle pole body assembly component MPS3
- Chromosome segregation in meiosis protein 4
- Meiosis-specific protein SPO11
- Meiosis-specific protein HOP1
- MutS protein homolog 4
- Synaptonemal complex protein ZIP1
- Actin
Sequence:
MSKDNRLASILLQPVASSSGNCTEFHDSKLHTLQEELNFLPLEGVASNVCPPMFRGHKNYVFVLYCLNQVDLVTNLQDSTKRYYPLQIFKDCQLSSLVQKDFSHYFQLSRQKEGEDRNDSDTTLVNVVNSGVSRHRSQLLKMCIIPRICSFDKSNSKTYKLIQEYVNRFETVLTKFGPEKDFTKVYANWSKLIESFNELILHDLLVKWQQWSELTQPNATVHQNIPNVLRELVIKLTQRYFTFQPSYSCSIDEFTTILLNKNALSLLDVFRKPRKYKLNFGLWLDCQNGILIFTNGIVQMADEITSERVKSFVRPAHLLVLEDHSNDEAVKKLMFFTFSAILQCFTDEILNC
Protein: Transcription elongation factor A protein-like 1 (TCEA-like protein 1) (Nuclear phosphoprotein p21/SIIR) (Transcription elongation factor S-II protein-like 1) (Q15170)
Organism: Homo sapiens (Human)
Function: May be involved in transcriptional regulation. Modulates various viral and cellular promoters in a promoter context-dependent manner. For example, transcription from the FOS promoter is increased, while Rous sarcoma virus (RSV) long terminal repeat (LTR) promoter activity is repressed. Does not bind DNA directly.
Subcellular location: Nucleus.
Interaction partners:
- Transcription elongation factor A protein-like 4
- Transcription elongation factor A protein-like 7
- Protein BEX3
- Ubiquitin carboxyl-terminal hydrolase 11
- Transcription elongation factor A protein-like 2
- Transcription elongation factor A protein-like 3
- Transcription elongation factor A protein 1
- Heme-binding protein 2
- E3 ubiquitin-protein ligase PHF7
Sequence:
MDKPRKENEEEPQSAPKTDEERPPVEHSPEKQSPEEQSSEEQSSEEEFFPEELLPELLPEMLLSEERPPQEGLSRKDLFEGRPPMEQPPCGVGKHKLEEGSFKERLARSRPQFRGDIHGRNLSNEEMIQAADELEEMKRVRNKLMIMHWKAKRSRPYPI
Protein: KCNQ potassium channel, isoform I (A0A0B4KEH2)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MDPDNDIYAFYDIRGYKGKCRPGRPNSERILQPRMSLLGKPLNYNRGTRRDVRYRRLQSRLYNFLERPRGLHAIFYHVMVFLMVFTCLALSVFSTIKEYEEDAVYILFRMEILVVIWFTMEFGARLWSSGCRSRYQGCLGRLKFVKRPFCIIDIVTILASIVVLGMGTSGQVFATSALRGLRFFQILRMVRMDRRGGTWKLLGSVVYAHRQELITTMYIGFLGLIFASFLVYMWEKDVNDKFSNFAQALWWGVITLCTVGYGDMVPITWQGKLIASCCALLGISFFALPAGILGSGFALKVQQQQRQKHMIRRRQPAATLIQAVWRCYAADEHSVSVATWNIHRVALPSPPASRASSSFKHNTSFVARLPTIRRHKSQTIQTPGGGDGGGVSKPPGSSRASTRYTRTIRDINASVENLEVVQNGKSMNPSFSEDSVAETTCLKNIKNSDDEEDEPRCTQLTNRHKTAIRFIRKLKYFVARRKFKEALKPYDVKDVMEQYAAGHVDLLGRVKMLHLRLDQILGKQGSKAKDVYASKISLASRVVKVERQVADIEEKLDILIKAYMEDRDRFLALPLPAKPKIHSISPSHKPLHHAHNLAMIDVWKRTAALSVHPEQVTTTPLLNPSAPDSSELRSLTATQTPTTTTDAIATQTPMPPHVQHTATNTKSSVLNSYQLGSEKQQHNDVFMTELENRTKKRVTLSLHRSTSEPYSKQEQRITIPDEGADSLDSSAKPTPPDSSIILIDEYEDFEEEDLNCEGEMDHFPTWEIDSDIGVEVDVDADADGDCDESTEDTALLQCATRTAIVITPISPVSSAHNLQQLNDQTTTLNKSNLLPPDSG
Protein: Large ribosomal subunit protein P2 (60S acidic ribosomal protein P2) (Acidic ribosomal protein RPA1) (P05389)
Organism: Drosophila melanogaster (Fruit fly)
Function: Plays an important role in the elongation step of protein synthesis.
Interaction partners:
- Small ribosomal subunit protein eS4
- Small ribosomal subunit protein uS12
- Large ribosomal subunit protein eL20
- 40S ribosomal protein S24
- Large ribosomal subunit protein eL43
- Large ribosomal subunit protein eL19
- Small ribosomal subunit protein eS26
- Large ribosomal subunit protein uL10
- Large ribosomal subunit protein eL8
- Small ribosomal subunit protein uS15
Sequence:
MRYVAAYLLAVLGGKDSPANSDLEKILSSVGVEVDAERLTKVIKELAGKSIDDLIKEGREKLSSMPVGGGGAVAAADAAPAAAAGGDKKEAKKEEKKEESESEDDDMGFALFE
Protein: Ras-associated and pleckstrin homology domains-containing protein 1 (RAPH1) (Amyotrophic lateral sclerosis 2 chromosomal region candidate gene 18 protein) (Amyotrophic lateral sclerosis 2 chromosomal region candidate gene 9 protein) (Lamellipodin) (Proline-rich EVH1 ligand 2) (PREL-2) (Protein RMO1) (Q70E73)
Organism: Homo sapiens (Human)
Function: Mediator of localized membrane signals. Implicated in the regulation of lamellipodial dynamics. Negatively regulates cell adhesion.
Subcellular location: Cell membrane {ECO:0000269|PubMed:15469845}; Peripheral membrane protein {ECO:0000269|PubMed:15469845}; Cytoplasmic side {ECO:0000269|PubMed:15469845}. Cell projection, lamellipodium {ECO:0000269|PubMed:15469845}. Cell projection, filopodium {ECO:0000269|PubMed:15469845}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:15469845}. Note=Recruited to the membrane, via the PH domain, by the phosphoinositide, PI(3,4)P2. Colocalizes with ENAH/VASP at the tips of lamellipodia and filopodia. Also colocalizes with the pathogens, Vaccinia and Enteropathogenic E.coli (EPEC) at the interface between the pathogen and their actin.
Interaction partners:
- Vasodilator-stimulated phosphoprotein
- Talin-1
- Profilin-1
- Profilin-4
- Profilin-3
- Abl interactor 1
- Talin-2
- Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 2
- Abl interactor 2
- Protein enabled homolog
Sequence:
MEQLSDEEIDHGAEEDSDKEDQDLDKMFGAWLGELDKLTQSLDSDKPMEPVKRSPLRQETNMANFSYRFSIYNLNEALNQGETVDLDALMADLCSIEQELSSIGSGNSKRQITETKATQKLPVSRHTLKHGTLKGLSSSSNRIAKPSHASYSLDDVTAQLEQASLSMDEAAQQSVLEDTKPLVTNQHRRTASAGTVSDAEVHSISNSSHSSITSAASSMDSLDIDKVTRPQELDLTHQGQPITEEEQAAKLKAEKIRVALEKIKEAQVKKLVIRVHMSDDSSKTMMVDERQTVRQVLDNLMDKSHCGYSLDWSLVETVSELQMERIFEDHENLVENLLNWTRDSQNKLIFMERIEKYALFKNPQNYLLGKKETAEMADRNKEVLLEECFCGSSVTVPEIEGVLWLKDDGKKSWKKRYFLLRASGIYYVPKGKAKVSRDLVCFLQLDHVNVYYGQDYRNKYKAPTDYCLVLKHPQIQKKSQYIKYLCCDDVRTLHQWVNGIRIAKYGKQLYMNYQEALKRTESAYDWTSLSSSSIKSGSSSSSIPESQSNHSNQSDSGVSDTQPAGHVRSQSIVSSVFSEAWKRGTQLEESSKARMESMNRPYTSLVPPLSPQPKIVTPYTASQPSPPLPPPPPPPPPPPPPPPPPPPPLPSQSAPSAGSAAPMFVKYSTITRLQNASQHSGALFKPPTPPVMQSQSVKPQILVPPNGVVPPPPPPPPPPTPGSAMAQLKPAPCAPSLPQFSAPPPPLKIHQVQHITQVAPPTPPPPPPIPAPLPPQAPPKPLVTIPAPTSTKTVAPVVTQAAPPTPTPPVPPAKKQPAFPASYIPPSPPTPPVPVPPPTLPKQQSFCAKPPPSPLSPVPSVVKQIASQFPPPPTPPAMESQPLKPVPANVAPQSPPAVKAKPKWQPSSIPVPSPDFPPPPPESSLVFPPPPPSPVPAPPPPPPPTASPTPDKSGSPGKKTSKTSSPGGKKPPPTPQRNSSIKSSSGAEHPEPKRPSVDSLVSKFTPPAESGSPSKETLPPPAAPPKPGKLNLSGVNLPGVLQQGCVSAKAPVLSGRGKDSVVEFPSPPSDSDFPPPPPETELPLPPIEIPAVFSGNTSPKVAVVNPQPQQWSKMSVKKAPPPTRPKRNDSTRLTQAEISEQPTMATVVPQVPTSPKSSLSVQPGFLADLNRTLQRKSITRHGSLSSRMSRAEPTATMDDMALPPPPPELLSDQQKAGYGGSHISGYATLRRGPPPAPPKRDQNTKLSRDW
Protein: Imidazole glycerol phosphate synthase subunit HisH (EC 4.3.2.10) (IGP synthase glutaminase subunit) (EC 3.5.1.2) (IGP synthase subunit HisH) (ImGP synthase subunit HisH) (IGPS subunit HisH) (TmHisH) (Q9X0C8)
Organism: Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)
Function: IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisH subunit catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the synthesis of IGP and AICAR. The resulting ammonia molecule is channeled to the active site of HisF.
Subcellular location: Cytoplasm.
Interaction partners:
- Histidine biosynthesis bifunctional protein HisIE
- 1-
- Imidazoleglycerol-phosphate dehydratase
- Imidazole glycerol phosphate synthase subunit HisF
- Histidinol-phosphate aminotransferase
- Histidinol dehydrogenase
- ATP phosphoribosyltransferase
- Bifunctional purine biosynthesis protein PurH
- Adenylosuccinate lyase
- Adenine phosphoribosyltransferase
Sequence:
MRIGIISVGPGNIMNLYRGVKRASENFEDVSIELVESPRNDLYDLLFIPGVGHFGEGMRRLRENDLIDFVRKHVEDERYVVGVCLGMQLLFEESEEAPGVKGLSLIEGNVVKLRSRRLPHMGWNEVIFKDTFPNGYYYFVHTYRAVCEEEHVLGTTEYDGEIFPSAVRKGRILGFQFHPEKSSKIGRKLLEKVIECSLSRR
Protein: RNA helicase (EC 3.6.4.13) (A0A1X7SBZ2)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
LPTGFVAPILCVLLPSPTREAATVASATGDSASERESAAPAAAPTAEAPPPSVVTRPEPQALPSPAIRAPLPDLYPFGTMRGGGFGDRDRDRDRGGFGARGGGGLPPKKFGNPGERLRKKKWDLSELPKFEKNFYVEHPEVARLTPYEVDELRRKKEITVRGGDVCPKPVFAFHHANFPQYVMDVLMDQHFTEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHQPYLERGDGPICLVLAPTRELAQQVQQVADDYGKCSRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLESGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLRDYTQINVGNLELSANHNILQIVDVCMESEKDHKLIQLMEEIMAEKENKTIIFVETKRRCDDLTRRMRRDGWPAMCIHGDKSQPERDWVLNEFRSGKAPILIATDVASRGLDVEDVKFVINYDYPNSSEDYVHRIGRTARSTNKGTAYTFFTPGNLKQARELIKVLEEANQAINPKLMQLVDHRGGGGGGGGRSRYRTTSSANNPNLMYQDECDRRLRGVKDGGRRDSASYRDRSETDRAGYANGSGYGSPNSAFGAQAGQYTYGQGTYGAAAYGTSSYTAQEYGAGTYGASSTTSTGRSSQSSSQQFSGIGRSGQQPQPLMSQQFAQPPGATNMIGYMGQTAYQYPPPPPPPPPSRK
Protein: Xyloglucan 6-xylosyltransferase 1 (AtXT1) (EC 2.4.2.39) (Q9LZJ3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Xylosyltransferase specific to UDP-D-xylose that accepts both cellopentaose and cellohexaose as substrates, with a better use of cellohexaose, to produce xyloglucan. Adds preferentially the first xylosyl residue to the fourth glucosyl residue from the reducing end of both acceptors. Transfer one xylose mainly to the second glucose residue from the non-reducing end. The acceptor should have a minimum of four glucose residues.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:21143678, ECO:0000269|PubMed:22665445}; Single-pass type II membrane protein {ECO:0000305}. Note=Mainly located in the cis and medial cisternae of Golgi apparatus. {ECO:0000269|PubMed:21143678}.
Interaction partners:
- Xyloglucan galactosyltransferase MUR3
- Xyloglucan glycosyltransferase 4
- Xyloglucan galactosyltransferase XLT2
- Galactoside 2-alpha-L-fucosyltransferase
- Cellulose synthase-like protein D2
- UDP-D-xylose:L-fucose alpha-1,3-D-xylosyltransferase
- Probable galacturonosyltransferase 7
- Probable arabinosyltransferase ARAD1
- Polygalacturonate 4-alpha-galacturonosyltransferase
- UDP-D-xylose:L-fucose alpha-1,3-D-xylosyltransferase 3
Sequence:
MIEKCIGAHRFRRLQRFMRQGKVTILCLVLTVIVLRGTIGAGKFGTPEKDIEEIREHFFYTRKRGEPHRVLVEVSSKTTSSEDGGNGGNSYETFDINKLFVDEGDEEKSRDRTNKPYSLGPKISDWDEQRRDWLKQNPSFPNFVAPNKPRVLLVTGSAPKPCENPVGDHYLLKSIKNKIDYCRIHGIEIFYNMALLDAEMAGFWAKLPLIRKLLLSHPEIEFLWWMDSDAMFTDMVFELPWERYKDYNLVMHGWNEMVYDQKNWIGLNTGSFLLRNSQWSLDLLDAWAPMGPKGKIREEAGKVLTRELKDRPAFEADDQSAMVYLLATEREKWGGKVYLESGYYLHGYWGILVDRYEEMIENHKPGFGDHRWPLVTHFVGCKPCGKFGDYPVERCLRQMDRAFNFGDNQILQMYGFTHKSLGSRRVKPTRNQTDRPLDAKDEFGLLHPPFKAAKLSTTTT
Protein: Ciz1 protein (Q6GQU3)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MFNPQLQQQQQLQQQQQQLQQQLQQQQLQQQQQQILQLQQLLQQSPPQASLSIPVSRGLPQQSSPQQLLSLQGLHSTSLLNGPMLQRALLLQQLQGLDQFAMPPATYDGASLTMPTATLGNLRAFNVTAPSLAAPSLTPPQMVTPNLQQFFPQATRQSLLGPPPVGVPINPSQLNHSGRNTQKQARTPSSTTPNRKDSSSQTVPLEDREDPTEGSEEATELQMDTCEDQDSLVGPDSMLSEPQVPEPEPFETLEPPAKRCRSSEESTEKGPTGQPQARVQPQTQMTAPKQTQTPDRLPEPPEVQMLPRIQPQALQIQTQPKLLRQAQTQTSPEHLAPQQDQVEPQVPTQAQSQEQTSEKTQDQPQTWPQGSVPPPEQASGPACATEPQLSSHAAEAGSDPDKALPEPVSAQSSEDRSREASAGGLDLGECEKRAGEMLGMWGAGSSLKVTILQSSNSRAFNTTPLTSGPRPGDSTSATPAIASTPSKQSLQFFCYICKASSSSQQEFQDHMSEAQHQQRLGEIQHSSQTCLLSLLPMPRDILEKEAE
Protein: Proto-oncogene Mas (P12526)
Organism: Rattus norvegicus (Rat)
Function: Receptor for angiotensin 1-7 (By similarity). Acts specifically as a functional antagonist of AGTR1 (angiotensin-2 type 1 receptor), although it up-regulates AGTR1 receptor levels. Positive regulation of AGTR1 levels occurs through activation of the G-proteins GNA11 and GNAQ, and stimulation of the protein kinase C signaling cascade. The antagonist effect on AGTR1 function is probably due to AGTR1 being physically altered by MAS1 (By similarity).
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Angiotensinogen
- Angiotensin-converting enzyme 2
Sequence:
MDQSNMTSFAEEKAMNTSSRNASLGTSHPPIPIVHWVIMSISPLGFVENGILLWFLCFRMRRNPFTVYITHLSIADISLLFCIFILSIDYALDYELSSGHYYTIVTLSVTFLFGYNTGLYLLTAISVERCLSVLYPIWYRCHRPKHQSAFVCALLWALSCLVTTMEYVMCIDSGEESHSQSDCRAVIIFIAILSFLVFTPLMLVSSTILVVKIRKNTWASHSSKLYIVIMVTIIIFLIFAMPMRVLYLLYYEYWSTFGNLHNISLLFSTINSSANPFIYFFVGSSKKKRFRESLKVVLTRAFKDEMQPRRQEGNGNTVSIETVV
Protein: COP9 signalosome complex subunit 7b (SGN7b) (Signalosome subunit 7b) (JAB1-containing signalosome subunit 7b) (Q9H9Q2)
Organism: Homo sapiens (Human)
Function: Component of the COP9 signalosome complex (CSN), a complex involved in various cellular and developmental processes. The CSN complex is an essential regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of SCF-type E3 ligase complexes, leading to decrease the Ubl ligase activity of SCF-type complexes such as SCF, CSA or DDB2. The complex is also involved in phosphorylation of p53/TP53, JUN, I-kappa-B-alpha/NFKBIA, ITPK1 and IRF8/ICSBP, possibly via its association with CK2 and PKD kinases. CSN-dependent phosphorylation of TP53 and JUN promotes and protects degradation by the Ubl system, respectively.
Subcellular location: Cytoplasm. Nucleus.
Interaction partners:
- COP9 signalosome complex subunit 1
- COP9 signalosome complex subunit 3
- COP9 signalosome complex subunit 2
- COP9 signalosome complex subunit 6
- COP9 signalosome complex subunit 8
- COP9 signalosome complex subunit 4
- COP9 signalosome complex subunit 5
- COP9 signalosome complex subunit 7a
- COP9 signalosome complex subunit 9
- Ubiquitin-like protein NEDD8
Sequence:
MAGEQKPSSNLLEQFILLAKGTSGSALTALISQVLEAPGVYVFGELLELANVQELAEGANAAYLQLLNLFAYGTYPDYIANKESLPELSTAQQNKLKHLTIVSLASRMKCIPYSVLLKDLEMRNLRELEDLIIEAVYTDIIQGKLDQRNQLLEVDFCIGRDIRKKDINNIVKTLHEWCDGCEAVLLGIEQQVLRANQYKENHNRTQQQVEAEVTNIKKTLKATASSSAQEMEQQLAERECPPHAEQRQPTKKMSKVKGLVSSRH
Protein: Ras-like protein family member 10B (EC 3.6.5.2) (Q5SSG5)
Organism: Mus musculus (Mouse)
Function: May facilitate the release of atrial natriuretic peptide by cardiomyocytes and hence play a role in the regulation of arterial pressure.
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
Interaction partners:
Sequence:
MVSTYRVAVLGARGVGKSAIVRQFLYNEFSEVCVPTTTRRLYLPAVVMNGHVHDLQILDFPPISAFPVNTLQEWADACCRGLRSVHAYILVYDICCFDSFEYVKTIRQQILETRVIGTSETPIIIVGNKRDLQRGRVIPRWNVSHLVRKTWKCGYVECSAKYNWHILLLFSELLKSVGCARCKHVHAALRFQGALRRNRCAIM