wanglab/gogpt-training-data huggingface dataset:
Protein: CTP synthase (EC 6.3.4.2) (Cytidine 5'-triphosphate synthase) (Cytidine triphosphate synthetase) (CTP synthetase) (CTPS) (UTP--ammonia ligase) (G0HV10)
Organism: Haloarcula hispanica (strain ATCC 33960 / DSM 4426 / JCM 8911 / NBRC 102182 / NCIMB 2187 / VKM B-1755)
Function: Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:32507415}. Note=Localizes to the cytoophidium, a short subcellular filamentary structure where CTP synthase is compartmentalized. Only a few cells form cytoophidia under standard growth conditions, they are observed in late log phase. Stress conditions such as treatment with 50 uM 6-diazo-5-oxo-l-norleucine (DON, an inhibitor) or growth at low salt (1.5 M instead of the usual 3.4 M) also induces their appearance. In all these conditions cells are barely growing. {ECO:0000269|PubMed:32507415}.
Interaction partners:
- GMP synthase subunit B
- Small ribosomal subunit protein uS2
- Nucleoside diphosphate kinase
- Arginine--tRNA ligase
- dCTP deaminase
- Large ribosomal subunit protein uL13
- Probable translation initiation factor IF-2
- DNA-directed RNA polymerase
- DNA-directed RNA polymerase subunit beta
- Large ribosomal subunit protein uL6
Sequence:
MPTEPETDYDPELGRKFIFVTGGVMSGLGKGITAASTGRLLKNAGFDVTAVKIDPYLNVDAGTMNPFQHGEVYVLKDGGEVDLDLGNYERFLDIDMTFDHNVTTGKTYQHVIEKERSGDYLGRTVQIIPHITDDIKRRIREAAEGNDVCIIEVGGTVGDIEGMPYLEALRQFAHEEDEDDILFTHVTLVPYSKNGEQKTKPTQHSVKELRSIGLQPDILVGRCSDKLDIDTKEKIALFCDVPTEAVFSNPDVDDIYHVPLMVEEEGLDQYVMEELDIATEALPEDERENRWRDLVTQNTEGEVDIALVGKYDLEDAYMSVHEALKHAGLEKNVDVNVQWVNSEKMNDHHADRMREADAIVVPGGFGARGTEGKIEAIRYARENDIPFLGLCLGFQMAVVEYARNVLDLDDAHSAELDEDTPHPVIDILPEQYEIEDMGGTMRLGAHETEIDANTLAATLYGGESCTERHRHRYEVNPEYIDDLEAAGLKFSGYAENRMEILELAPEDHPYFIGTQFHPEFRSRPTRASPPFVGLLEAVLGDDPHTVTTEEVSH
Protein: GDSL esterase/lipase At1g29670 (EC 3.1.1.-) (Extracellular lipase At1g29670) (Q9C7N4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Disease resistance protein
- Actin cross-linking protein
- ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase
- GATA transcription factor 8
- IQ domain-containing protein IQM2
- Actin cross-linking protein
- Actin cross-linking protein
Sequence:
MESYLTKWCVVLVLLCFGFSVVKAQAQAQVPCFFVFGDSLVDNGNNNGLISIARSNYFPYGIDFGGPTGRFSNGKTTVDVIAELLGFNGYIPAYNTVSGRQILSGVNYASAAAGIREETGRQLGQRISFSGQVRNYQTTVSQVVQLLGDETRAADYLKRCIYSVGLGSNDYLNNYFMPTFYSSSRQFTPEQYANDLISRYSTQLNALYNYGARKFALSGIGAVGCSPNALAGSPDGRTCVDRINSANQIFNNKLRSLVDQLNNNHPDAKFIYINAYGIFQDMITNPARFGFRVTNAGCCGIGRNAGQITCLPGQRPCRDRNAYVFWDAFHPTEAANVIIARRSYNAQSASDAYPMDISRLAQL
Protein: Os09g0509000 protein (cDNA clone:001-206-A08, full insert sequence) (Q0J0H6)
Organism: Oryza sativa subsp. japonica (Rice)
Interaction partners:
- Os03g0207900 protein
- Os06g0255200 protein
- Nuclear pore complex protein
Sequence:
MASASRFLLLSRLPAAAASSTSRLLRPLSAAGSLLPAALAPSAPRAAAAAARCFATQPATSSLRDSSPNWSNRPPKETILLDGCDFEHWLVVVEPPPGDPSNPEPTRDEIIDGYIKTLAQVVGSEEEARHKIYSVSTRHYFAFGALVSEELSYKLKELPKVRWVLPDSYLDVRNKDYGGEPFINGEAVPYDPKYHEEWVRNNARANERSRRNDRPRNFDRSRNFERRRENMQNFQNRDVPPGQGFNSPPPPGQGPVPPRDAPPMHHAQGNVPPPPPPNAGPPNYQPHAPNPQGYTNYQQGGAPGYQGGPPGYQGSNQGYQGPPPPPPSAYQGNNPGYQGGGPGYQGGNPPPYQGGNPGYAPGYHGQGGNPSYQQGGDNYNAGVPAYERDGQGRNYQ
Protein: Krueppel-like factor 12 (Transcriptional repressor AP-2rep) (Q9Y4X4)
Organism: Homo sapiens (Human)
Function: Confers strong transcriptional repression to the AP-2-alpha gene. Binds to a regulatory element (A32) in the AP-2-alpha gene promoter.
Subcellular location: Nucleus.
Interaction partners:
- Transcription factor AP-2-alpha
Sequence:
MNIHMKRKTIKNINTFENRMLMLDGMPAVRVKTELLESEQGSPNVHNYPDMEAVPLLLNNVKGEPPEDSLSVDHFQTQTEPVDLSINKARTSPTAVSSSPVSMTASASSPSSTSTSSSSSSRLASSPTVITSVSSASSSSTVLTPGPLVASASGVGGQQFLHIIHPVPPSSPMNLQSNKLSHVHRIPVVVQSVPVVYTAVRSPGNVNNTIVVPLLEDGRGHGKAQMDPRGLSPRQSKSDSDDDDLPNVTLDSVNETGSTALSIARAVQEVHPSPVSRVRGNRMNNQKFPCSISPFSIESTRRQRRSESPDSRKRRIHRCDFEGCNKVYTKSSHLKAHRRTHTGEKPYKCTWEGCTWKFARSDELTRHYRKHTGVKPFKCADCDRSFSRSDHLALHRRRHMLV
Protein: Myocyte-specific enhancer factor 2A (Serum response factor-like protein 1) (Q02078)
Organism: Homo sapiens (Human)
Function: Transcriptional activator which binds specifically to the MEF2 element, 5'-YTA[AT](4)TAR-3', found in numerous muscle-specific genes. Also involved in the activation of numerous growth factor- and stress-induced genes. Mediates cellular functions not only in skeletal and cardiac muscle development, but also in neuronal differentiation and survival. Plays diverse roles in the control of cell growth, survival and apoptosis via p38 MAPK signaling in muscle-specific and/or growth factor-related transcription. In cerebellar granule neurons, phosphorylated and sumoylated MEF2A represses transcription of NUR77 promoting synaptic differentiation. Associates with chromatin to the ZNF16 promoter.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00251, ECO:0000269|PubMed:12691662, ECO:0000269|PubMed:16563226}.
Interaction partners:
- Myocyte-specific enhancer factor 2D
- Histone acetyltransferase p300
- Myocyte-specific enhancer factor 2B
- Histone deacetylase 4
- Mitogen-activated protein kinase 7
- Myoblast determination protein 1
- Mitogen-activated protein kinase 14
- Histone deacetylase 7
- Histone deacetylase 9
- Myogenin
Sequence:
MGRKKIQITRIMDERNRQVTFTKRKFGLMKKAYELSVLCDCEIALIIFNSSNKLFQYASTDMDKVLLKYTEYNEPHESRTNSDIVEALNKKEHRGCDSPDPDTSYVLTPHTEEKYKKINEEFDNMMRNHKIAPGLPPQNFSMSVTVPVTSPNALSYTNPGSSLVSPSLAASSTLTDSSMLSPPQTTLHRNVSPGAPQRPPSTGNAGGMLSTTDLTVPNGAGSSPVGNGFVNSRASPNLIGATGANSLGKVMPTKSPPPPGGGNLGMNSRKPDLRVVIPPSSKGMMPPLSEEEELELNTQRISSSQATQPLATPVVSVTTPSLPPQGLVYSAMPTAYNTDYSLTSADLSALQGFNSPGMLSLGQVSAWQQHHLGQAALSSLVAGGQLSQGSNLSINTNQNISIKSEPISPPRDRMTPSGFQQQQQQQQQQQPPPPPQPQPQPPQPQPRQEMGRSPVDSLSSSSSSYDGSDREDPRGDFHSPIVLGRPPNTEDRESPSVKRMRMDAWVT
Protein: Structural maintenance of chromosomes protein 5 (SMC protein 5) (SMC-5) (mSMC5) (Protein expressed in male leptotene and zygotene spermatocytes 453) (MLZ-453) (Q8CG46)
Organism: Mus musculus (Mouse)
Function: Core component of the SMC5-SMC6 complex, a complex involved in repair of DNA double-strand breaks by homologous recombination. The complex may promote sister chromatid homologous recombination by recruiting the SMC1-SMC3 cohesin complex to double-strand breaks. The complex is required for telomere maintenance via recombination and mediates sumoylation of shelterin complex (telosome) components. Required for sister chromatid cohesion during prometaphase and mitotic progression; the function seems to be independent of SMC6 (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:11408570, ECO:0000269|PubMed:20339383}. Chromosome {ECO:0000269|PubMed:11408570}. Nucleus, PML body {ECO:0000250|UniProtKB:Q8IY18}. Chromosome, telomere {ECO:0000250|UniProtKB:Q8IY18}. Note=Colocalizes with SMC6 on the X-Y chromosome pair within the sex vesicle during late pachytene/diplotene (PubMed:11408570). Associates with chromatin. Localizes to PML nuclear bodies in ALT cell lines. Accumulates with RAD18 and the SLF1-SLF2 complex at replication-coupled DNA interstrand repair and DNA double-strand breaks (DSBs) sites on chromatin in a ubiquitin-dependent manner. {ECO:0000250|UniProtKB:Q8IY18, ECO:0000269|PubMed:11408570}.
Interaction partners:
- E3 SUMO-protein ligase NSE2
- Non-structural maintenance of chromosomes element 1 homolog
- Structural maintenance of chromosomes protein 6
- Non-structural maintenance of chromosomes element 4
- EP300-interacting inhibitor of differentiation 3
- Non-structural maintenance of chromosomes element 3 homolog
- Structural maintenance of chromosomes protein 3
- Nipped-B-like protein
- Double-strand-break repair protein rad21 homolog
- Small ubiquitin-related modifier 3
Sequence:
MATPSGKAAPPNPQVSKRSLPRDASSEVPSKRKNSNPLPTLPRPSGTFVEGSIVRIAMENFLTYDICEVSPGPHLNMIIGANGTGKSSIVCAICLGLAGKPAFMGRADKVGFFVKRGCSKGLVEIELFRTSGNLIITREIDVIKNQSFWFINKKPVTQKIVEEQVAALNIQVGNLCQFLPQDKVGEFAKLSKIELLEATEKSVGPPEMHRYHCELKNFREKEKQLETSCKEKTEYLEKMVQRNERYKQDVERFYERKRHLDLIEMLEAKRPWVEYENVRQEYEGVKLIRDRVKEEVRKLKEGQIPMTRRIEEIDRQRHTLEVRIKEKSTDIKEASQKCKQRQDLIERKDRQIKELQQALTVKQNEELDRQKRISNTRKMIEDLQSELKTAENCENLQPQIDTVTNDLRRVQEEKALCEGEIIDKQREKEMLEKQRRSVSDHITRFDNLMNQKEDKLRQRYRDTYDAVLWLRNNRDRFKQRVCEPIMLTINMKDNKNAKYVENHISSNDLRAFVFESQEDMEIFLREVRDNKKLRVNAVIAPKISYADKAPSRSLNDLKQYGFFSYLRELFDAPDPVMSYLCCQYHIHEVPVGTERTRERIERVIQETRLKQIYTAEEKYVLKTSVYSNKVISSNTSLKVAQFLTVTVDLEQRRHLEEQLKEMNRQLEAVDSGLAALRDTNRHLELKDNELRLKKKELLERKTRKRQLEQKISSKLASIRLMEQDTCNLEEEERKASTKIKEINVQKAKLVTELTGLVKICTSFQIQKVDLILQNTTVISEKNKLEADYMASSSQLRVTEQQFIELDDNRQRLLQKCKELMKKARQVCNLSADQAVPQEFQTQVPTIPNGHSSSPPMAFQDLPNTLDEIDALLTEERSRASCFTGLNPSVVEEYSKREVEIQQLTEELQGKKVELDEYRENISQVKERWLNPLKELVEKINEKFSNFFSSMQCAGEVDLHTENEEDYDKYGIRIRVKFRSSTQLHELTPHHQSGGERSVSTMLYLMALQELNRCPFRVVDEINQGMDPINERRVFEMVVNTACKENTSQYFFITPKLLQNLPYSEKMTVLFVYNGPHMLEPNRWNLKAFQRRRRRITFTQPQ
Protein: tRNA modification GTPase MSS1, mitochondrial (P32559)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: GTPase involved in the 5-carboxymethylaminomethyl modification (mnm(5)s(2)U34) of the wobble uridine base in mitochondrial tRNAs. Involved in the expression of cytochrome c oxidase subunit 1 (COX1). Works in association with the small subunit of mitoribosomes.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Mitochondrial translation optimization protein 1
- MIOREX complex component 8
- Large ribosomal subunit protein uL15m
- Large ribosomal subunit protein uL11m
- Mitochondrial GTPase 1
- Large ribosomal subunit protein uL13m
- Multisubstrate pseudouridine synthase 7
- Large ribosomal subunit protein uL3m
- Large ribosomal subunit protein bL17m
- Acyl carrier protein, mitochondrial
Sequence:
MNSASFLQSRLISRSFLVRRSLKRYSGLAKPYTFQQPTIYALSTPANQTSAIAIIRISGTHAKYIYNRLVDSSTVPPIRKAILRNIYSPSSCSVKPHDQKESKILLDTSLLLYFQAPYSFTGEDVLELHVHGGKAVVNSILKAIGSLHDRSSGKDIRFALPGDFSRRAFQNGKFDLTQLEGIKDLIDSETESQRRSALSSFNGDNKILFENWRETIIENMAQLTAIIDFADDNSQEIQNTDEIFHNVEKNIICLRDQIVTFMQKVEKSTILQNGIKLVLLGAPNVGKSSLVNSLTNDDISIVSDIPGTTRDSIDAMINVNGYKVIICDTAGIREKSSDKIEMLGIDRAKKKSVQSDLCLFIVDPTDLSKLLPEDILAHLSSKTFGNKRIIIVVNKSDLVSDDEMTKVLNKLQTRLGSKYPILSVSCKTKEGIESLISTLTSNFESLSQSSADASPVIVSKRVSEILKNDVLYGLEEFFKSKDFHNDIVLATENLRYASDGIAKITGQAIGIEEILDSVFSKFCIGK
Protein: L-serine dehydratase (EC 4.3.1.17) (Q9HTI5)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- Probable D-serine dehydratase
- Serine hydroxymethyltransferase 1
- Serine hydroxymethyltransferase 3
- Serine hydroxymethyltransferase 2
- Phosphoserine phosphatase
- L-threonine dehydratase
- Tryptophan synthase beta chain-like PALP domain-containing protein
- L-threonine dehydratase
- Cysteine synthase B
- serine O-acetyltransferase
Sequence:
MAISVFDLFKIGIGPSSSHTVGPMRAAALFTAALRQRQALSAVRRLEVRLYGSLSATGVGHGTDRAVIMGLMGEWPDRIDPTQIAPRMAALLDSGLLQLDGRVAVPFDWVRDMRLLDENLPYHPNAMTLVAYGEQGELHQETYYSVGGGFVVDAAQAASGQLDQDHTVLPYDFSSAEELLLLCKRHNLRVSELMLANERIWRSETDIREGLRRIWQAMRDCVDNGLRNEGILPGGLNVQRRAARLHRNLQEIGKPNVIGSTLSAMEWVNLFALAVNEENAAGGRMVTAPTNGAAGIIPAVLHYYMKFNPDAQDRDVVDYLLAAAAVGILCKKNASISGAEVGCQGEVGSACAMAAAGLAEVLGATPAQVENAAEIGLEHNLGLTCDPVGGLVQVPCIERNAIAAVKAINAAQMALRGDGQHFISLDKVIRTMRDTGADMHDKYKETSRGGLAVNAIEC
Protein: HECT and RLD domain containing E3 ubiquitin protein ligase 4 (D6RCL5)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MLCWGNASFGQLGLGGIDEEIVLEPRKSDFFINKRVRDVGCGLRHTVFVLDDGTVYTCGCNDLGQLGHEKSRKKPEQVVALDAQNIVAVSCGEAHTLALNDKGQVYAWGLDSDGQLGLVGSEECIRVPSCFPKIMCVDSLVRICSGLSYGRIRNIKSLSDIQIVQVACGYYHSLALSKASEVFCWGQNKYGQLGLGTDCKKQTSPQLLKSLLGIPFMQVAAGGAHSFVLTLSGAIFGWGR
Protein: Putative 1,2-phenylacetyl-CoA epoxidase, subunit D (1,2-phenylacetyl-CoA monooxygenase, subunit D) (P76080)
Organism: Escherichia coli (strain K12)
Function: Possible component of 1,2-phenylacetyl-CoA epoxidase multicomponent enzyme system which catalyzes the reduction of phenylacetyl-CoA (PA-CoA) to form 1,2-epoxyphenylacetyl-CoA. The subunit D may have a function related to the maturation of the monooxygenase complex, rather than direct involvement in catalysis. PaaD could assist either in maturation of PaaE or PaaA.
Interaction partners:
- Acyl-coenzyme A thioesterase PaaI
- 1,2-epoxyphenylacetyl-CoA isomerase
- 1,2-phenylacetyl-CoA epoxidase, subunit C
- 1,2-phenylacetyl-CoA epoxidase, subunit E
- 1,2-phenylacetyl-CoA epoxidase, subunit B
- 1,2-phenylacetyl-CoA epoxidase, subunit A
- Phenylacetate-coenzyme A ligase
- Bifunctional protein PaaZ
- 2,3-dehydroadipyl-CoA hydratase
- 3-hydroxyadipyl-CoA dehydrogenase
Sequence:
MQRLATIAPPQVHEIWALLSQIPDPEIPVLTITDLGMVRNVTQMGEGWVIGFTPTYSGCPATEHLIGAIREAMTTNGFTPVQVVLQLDPAWTTDWMTPDARERLREYGISPPAGHSCHAHLPPEVRCPRCASVHTTLISEFGSTACKALYRCDSCREPFDYFKCI
Protein: Phospholipid-transporting ATPase (EC 7.6.2.1) (F4IE35)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU362033}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU362033}.
Interaction partners:
Sequence:
MATVSGRRRKRKIQLSKLFTLTGAKACFKPDHSKIGRSGFSRVVFCNQPDSPEAESRNYCDNYVRTTKYTLATFLPKSLFEQFRRVANFYFLVVGILSFTPLAPYTAVSAIVPLTFVILATMFKEGVEDWRRKQQDIEVNNRKVRVHRGNGNFDLREWKTLRVGDILKVEKNEFFPADLVLLSSSYEDAVCYVETMNLDGETNLKLKQGLEVTLSLREELNFRDFEAFIKCEDPNANLYSFVGTMDLKGEKYPLSPQQLLLRGSKLRNTDYIYGVVIFTGPDTKVVQNSTDPPSKRSMIERKMDKIIYLMFLMVFSLAFFGSVLFGIWTRDDFQNGVMERWYLKPDDSSIFFDPKRAPMAAIYHFLTALMLNSYFIPISLYVSIEIVKVLQSIFINQDIHMYYEEADKPAHARTSNLNEELGQVGTILSDKTGTLTCNSMEFIKCSIAGTAYGRGVTEVEMAMDKRKGSALVNQSNGNSTEDAVAAEPAVKGFNFRDERIMDGNWVTETHADVIQKFFQLLAVCHTVIPEVDEDTGKISYEAESPDEAAFVIAARELGFEFFTRTQTTISVRELDLVTGERVERLYSVLNVLEFSSSKKRMSVIVQDQDGKLLLLCKGADSVMFERLSESGRKYEKETRDHVNEYADAGLRTLILAYRELDENEYEVFTERISEAKNSVSADREALIDEVTEKIEKNLVLLGATAVEDKLQNGVPDCINKLAQAGIKIWVLTGDKMETAINIGFACSLLRRDMKQIIINLETPEIQQLEKSGEKDAIAAALKENVLHQITSGKAQLKASGGNAKAFALIIDGKSLAYALEEDMKGIFLELAIGCASVICCRSSPKQKALVTRLVKTGSGQTTLAIGDGANDVGMLQEADIGVGISGVEGMQAVMSSDIAIAQFRYLERLLLVHGHWCYRRISKMICYFFYKNITFGFTLFLYEAYTSFSATPAYNDWYLSLYSVFFTSLPVICLGIFDQDVSAPFCLKFPVLYQEGVQNLLFSWRRILSWMFHGFCSAIIIFFLCKTSLESQAFNHEGKTAGRDILGGTMYTCVVWVVSLQMVLTISYFTLIQHVVVWGSVVIWYLFLMVYGSLPIRMSTDAYMVFLEALAPAPSYWITTLFVVLSTMMPYFIFSAIQMRFFPMSHGTVQLLRYEDQCSNSGNFEMGRQGSVRPTLVMRSHQPES
Protein: LD33192p (Q960V4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MFFFMFYFISLPFREYANGFKQLQTMSRFTYWFAHFTFDMLILIFVCVALFSLQSLMMPSELYTTAELKVIVLSIFFYGCSYLPILYALGNNFKSISTISTYLLLMLIVSAIAPLITSSNAAAMKLHETKIAFLCFLPDFNLNHQFRIINENFITRRHPALIKGLISQDTFFAYATAVGVMVMAFFTIVLEHKYLRRRIHDGIWEWAFQRKKYNSTGTLPSTPISEIDDCAREEKRVTDLIKDPLNDHSLIVHNLRKRYGDKLAVDGVSFAAAQGECFGLLGVNGAGKTSTFQMIAANLPLDGGTIRIKGADIREHELKYREYFGYCPQYDALNKFMTAEQCLYYMALLRGLSRRRTDGPASCKEHVKYWLEKMHLTKYQKVQVRHYSGGTKRKLLAAMAMIGAPALVLLDEPTTGVDPISRRFLWQCIKDFQGKDRTVVLTSHSMDECEELCNRLAIMAHGKFKCLNNICALKRLSGFTIKLKMKADTETEMNVSTITGTLKSEFPGLELRESHAGTLTYFVSTQESVVLWSSVFKIAEEYLGDRLSALVADYSVNECTLEDIFLKFEREAKSQSTSRQTSVQRRPECSYV
Protein: RE01528p (Q9W171)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Peroxisome {ECO:0000256|ARBA:ARBA00004275}.
Interaction partners:
Sequence:
MPTKAVFPTFFNKETQVWSGPPRPTVYDHNTSVGQIVFNSLRCWPTNVIQITDDDGTVLTNADMLAYATRIALFFKSEGLTQEDRVGIIANSSTFVIPVATACFFQATPFHAVNYSREPAIVQGLYSVTKPKIMFIDGPDYDRIKEITKEWSPKLITLTGKVEGVTSIEDLVKPHPAEKIYVPASLATGGDQIAVVLCSSGTAGLPKAVALSHRHIASTNSLCISTDVLYTSATIDWMTGFSITVMNLTCGFTRIISRRTFSAETALYLVSKYKVTCLAMAPWQAYELFTSPLATSEQLESLKIAFVIGGWISLALLRRAQELLPKTYVMFSYGTTETGVVTINIDHSLECSVGRLAPGMRIKIQGEDGQQLGVNQTGEVLIDIGLKWEGYLSNPEDTATTLQDGWINLGDLGYFDEDNNLYLVDRKKDLLKYKSKHYWPNEIEQIIAELPEVEHVCVVGVRDARYGDAAGALIIKKEGAEIADQKVIDHVAQRVVVDYKQLNAGVIFVDKFPKNANGKVMRSLAREVFEKTKPITF
Protein: Inosine-5'-monophosphate dehydrogenase (IMP dehydrogenase) (IMPD) (IMPDH) (EC 1.1.1.205) (C9J381)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03156}. Nucleus {ECO:0000256|HAMAP-Rule:MF_03156}.
Interaction partners:
Sequence:
MADYLISGGTGYVPEDGLTAQQLFASADGLTYNDFLILPGFIDFIADEVDLTSALTRKITLKTPLISSPMDTVTEADMAIAMALMGGIGFIHHNCTPEFQANEVRKVKFEQGFITDPVVLSPSHTVGDVLEAKMRHGFSGIPITETGTMGSKLVGIVTSRDIDFLAEKDHTTLLSEVMTPRIELVVAPAGVTLKEANEILQRSKKGKLPIVNDCDELVAIIARTDLKKNRDYPLASKDSQKQLLCGAAVGTREDDKYRLDLLTQAGVDVIVLDSSQGNSVYQIAMVHYIKQKYPHLQVIGGNVVTAAQAKNLIDAGVDGLRVGMGCGSICITQEVMACGRPQGTAVYKVAEYARRFGVPIIADGGIQTVGHVVKALALGASTVMMGSLLAATTEAPGEYFFSDGVRLKKYRGMGSLDAMEKSSSSQKRYFSEGDKVKIAQGVSGSIQDKGSIQKFVPYLIAGIQHGCQDIGARSLSVLRSMMYSGELKFEKRTMSAQIEGGVHGLHSYEKRLY
Protein: Peroxisomal leader peptide-processing protease (EC 3.4.21.-) (Trypsin domain-containing protein 1) [Cleaved into: Peroxisomal leader peptide-processing protease, 15 kDa form; Peroxisomal leader peptide-processing protease, 45 kDa form] (Q2T9J0)
Organism: Homo sapiens (Human)
Function: Peroxisomal protease that mediates both the removal of the leader peptide from proteins containing a PTS2 target sequence and processes several PTS1-containing proteins. Catalyzes the processing of PTS1-proteins involved in the peroxisomal beta-oxidation of fatty acids.
Subcellular location: Peroxisome {ECO:0000269|PubMed:22002062}.
Interaction partners:
- Peroxisomal acyl-coenzyme A oxidase 1
- 3-ketoacyl-CoA thiolase, peroxisomal
- Lon protease homolog 2, peroxisomal
- Peroxisomal targeting signal 1 receptor
- Alkyldihydroxyacetonephosphate synthase, peroxisomal
- Peroxisomal multifunctional enzyme type 2
- Sterol carrier protein 2
- Phytanoyl-CoA dioxygenase, peroxisomal
- Peroxisomal membrane protein PEX14
- Peroxisomal targeting signal 2 receptor
Sequence:
MRRQWGSAMRAAEQAGCMVSASRAGQPEAGPWSCSGVILSRSPGLVLCHGGIFVPFLRAGSEVLTAAGAVFLPGDSCRDDLRLHVQWAPTAAGPGGGAERGRPGLCTPQCASLEPGPPAPSRGRPLQPRLPAELLLLLSCPAFWAHFARLFGDEAAEQWRFSSAARDDEVSEDEEADQLRALGWFALLGVRLGQEEVEEERGPAMAVSPLGAVPKGAPLLVCGSPFGAFCPDIFLNTLSCGVLSNVAGPLLLTDARCLPGTEGGGVFTARPAGALVALVVAPLCWKAGEWVGFTLLCAAAPLFRAARDALHRLPHSTAALAALLPPEVGVPWGLPLRDSGPLWAAAAVLVECGTVWGSGVAVAPRLVVTCRHVSPREAARVLVRSTTPKSVAIWGRVVFATQETCPYDIAVVSLEEDLDDVPIPVPAEHFHEGEAVSVVGFGVFGQSCGPSVTSGILSAVVQVNGTPVMLQTTCAVHSGSSGGPLFSNHSGNLLGIITSNTRDNNTGATYPHLNFSIPITVLQPALQQYSQTQDLGGLRELDRAAEPVRVVWRLQRPLAEAPRSKL
Protein: MIP16918p (Steppke, isoform C) (Steppke, isoform D) (Steppke, isoform E) (Q0E8N2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- RE36140p
- ADP-ribosylation factor 6
- ADP-ribosylation factor 1
- ADP-ribosylation factor-like protein 11
Sequence:
MASLHQKRPSISNWFSSLRRQPKNKKCSPGLGGSESVGRKQPLQRSCLDLSTTRVGCDGCVSLEFFQSESPESRRSNSTFYVNTQNVSSAVFKDNRQPLLERGSGSDSSPSSVCVRCSCNSITKSGDRNETPTMATPKSDIKIALKPPPKPRSPSMAPYTSVATYNITKLAPDSPPPASPTLSTQTVNCSDVTTKVTEVQRLPCDEPNTELISKRTEYKHTTITTTTRTLIVSRPVELLLNENGEIIARRSPRKSRSNSLGRMLDVQNEIGTGGLFMEADPCSKNSLPPPPYIDDMRFIDDSSNSQSESERNSNIHKTNKYTSKNNNNDSKRESQQSNLCESCRMLLDRNYINTEQSDNLVILRRPSKQIKDELCEVVSEMEALDVPEDCKHSNKDKQMSIGRKKFNMDPKKGIEYLVENRLLRHDPQDVAHFLYKGEGLNKTAIGDYLGEKNDFNEDVLKAFVALHDFTNLILVQALRQFLWSFRLPGEAQKIDRMMETFAQRYCQLNPDIFTNTDTCYVLSFAIIMLNTSLHNPSVKDKPTVDQFISMNRGINNGGDLPRGLLESLYESIRTEPFKIPQDDGNDLMHTFFNPDKEGWLWKQGGRYKSWKRRWFILNDNCLYYFEYTTDKEPRGIIPLENISVREIHDRSKPHCFELFATGGADIIKACKTDSEGKVVEGKHTVYRMSAATEEDQQEWIKRLTQSISHNPFYDILVQRKKKALSKS
Protein: Olfactory receptor 2W3 (Olfactory receptor 2W8) (Olfactory receptor OR1-49) (Q7Z3T1)
Organism: Homo sapiens (Human)
Function: Odorant receptor.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- E3 ubiquitin-protein ligase TRIM58
Sequence:
MDGTNGSTQTHFILLGFSDRPHLERILFVVILIAYLLTLVGNTTIILVSRLDPHLHTPMYFFLAHLSFLDLSFTTSSIPQLLYNLNGCDKTISYMGCAIQLFLFLGLGGVECLLLAVMAYDRCVAICKPLHYMVIMNPRLCRGLVSVTWGCGVANSLAMSPVTLRLPRCGHHEVDHFLREMPALIRMACVSTVAIEGTVFVLAVGVVLSPLVFILLSYSYIVRAVLQIRSASGRQKAFGTCGSHLTVVSLFYGNIIYMYMQPGASSSQDQGMFLMLFYNIVTPLLNPLIYTLRNREVKGALGRLLLGKRELGKE
Protein: Nucleolar protein 16 (A0A0C4DGU5)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus, nucleolus {ECO:0000256|ARBA:ARBA00004604}.
Interaction partners:
Sequence:
MPKAKGKTRRQKFGYSVNRKRLNRNARRKAAPRIECSHIRHAWDHAKSVRQNLAEMGLAVDPNRAVPLRKRKVKAMEVDIEERPKELVRKPYVLNDLEAEASLPEKKGNTLSRDLIDYVRYMVENHGEDYKSGKTSSILCRRGRWRWSDWFTSQLPQAEASPGPVKLEPGCKARRCCVAPEELARSHGIRRLHTHVHTPRSGEGTVLRGSNLYSSGGSRKSQNLLFSGWVM
Protein: Cytochrome P450 3A (EC 1.14.14.-) (X5L565)
Organism: Canis lupus familiaris (Dog) (Canis familiaris)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004406, ECO:0000256|RuleBase:RU368049}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004406}. Microsome membrane {ECO:0000256|ARBA:ARBA00004174, ECO:0000256|RuleBase:RU368049}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004174}.
Interaction partners:
Sequence:
MDLIPSFSTETWLLLAISLVLLYLYGTYTHGIFRKLGIPGPTPLPFVGTALGYRNGFYVFDMKCFSKYGRMWGFYDGRQPVLAITDPDMIKTVLVKECYSVFTNRRTLGPVGFMKSAISLSEDEEWKRMRTLLSPTFTTGKLKEMFPIIGQYGDVLVNNLRKEAEKGKAINLKDVFGAYSMDVITSTSFGVNIDSLNHPQDPFVENTKKLLKFDFLDPFLFSILLFPFLTPVFEILNIWLFPKKVTDFFRKSVERMKESRLKDKQKHRVDFLQLMINSQNSKEMDTHKALSDLELVAQSIIFIFAGYETTSTSLSFLMYELATHPDVQQKLQEEIDATFPNKALPTYDALVQMEYLDMVLNETLRLYPIAGRLERVCKKDVEISGVFIPKGTVVMVPTFTLHRDQSLWPEPEEFRPERFSRKNKDSINPYTYLPFGTGPRNCIGMRFAIMNMKLALVRVLQNFSFKPCKETQIPLKLNAQGIIQPEKPIVLKVEPRDGSVNGA
Protein: IRK-interacting protein (Q9LXU9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Probable LRR receptor-like serine/threonine-protein kinase IRK
Sequence:
MASSETRMNKAREKEEAIANGVKLRALQASLMQMKSSPSSNYSLRNPSSSSAASPASRPLPNLSAHDYPVFTPSYEDEPVSAFHHKNLTLSETWDEDGVGLVDGDTYLSDSYKTSTSRKTVMMPHQDSHHHVYTMSDALRSPPLHFYTTGRSNCGSVDFRSVSSCNDYNKQKGFDTKSLKSSNLVVPLTDSHSAVVSSQPRNRGGRVMSWLFPKLKKKQKSNSIFNSPSITEKSEEVSEVLKDSGSGVEKLKRELMEANRSRDAALTQVSEMKSSLGELSEKLQYLESYCDNLKKALREATEVVSQENSGGRSSGKKNSEMPVSEEVMVEGFLQIVSEARLSIKQFLKTLVSEIDEEDSTLIGNINTLLQPHNLSFTSKYSKIIQYHLEAIISQSVYQDFENCVFQKNGKPKLLDPEQDRQANFSSFASLRNLSWNEVLKKGTKYYSDEFSRFCDEKMSLIITTLNWTRPWSEQMLQAFFVAAKCVWLLHLLAFSFNPALGILRVEENREFESSFMEDMGADRQRSALSRGPARVKVMVMPGFYVLDRVLRCKVLCRYKSLG
Protein: Phosphocarrier protein HPr (A0A0H2UQ34)
Organism: Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MASKDFHVVAETGIHARPATLLVQTASKFASDITLEYKGKSVNLKSIMGVMSLGVGQGADVTISAEGADADDAIAAISETMEKEGLA
Protein: Acid-sensing ion channel 3 (ASIC3) (hASIC3) (Amiloride-sensitive cation channel 3) (Neuronal amiloride-sensitive cation channel 3) (Testis sodium channel 1) (hTNaC1) (Q9UHC3)
Organism: Homo sapiens (Human)
Function: Cation channel with high affinity for sodium, which is gated by extracellular protons and inhibited by the diuretic amiloride. Generates a biphasic current with a fast inactivating and a slow sustained phase. In sensory neurons is proposed to mediate the pain induced by acidosis that occurs in ischemic, damaged or inflamed tissue. May be involved in hyperalgesia. May play a role in mechanoreception. Heteromeric channel assembly seems to modulate channel properties.
Subcellular location: Cell membrane {ECO:0000269|PubMed:10842183, ECO:0000269|PubMed:15317815, ECO:0000269|PubMed:9744806, ECO:0000269|PubMed:9886053}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000250|UniProtKB:Q6X1Y6}. Note=Preferentially expressed at the plasma membrane of the soma and cellular processes of neurons (By similarity). In part cytoplasmic in cochlea cells (By similarity). Localized in specialized sensory nerve endings (By similarity). {ECO:0000250|UniProtKB:O35240, ECO:0000250|UniProtKB:Q6X1Y6}.
Interaction partners:
- Acid-sensing ion channel 4
- Bile acid-sensitive ion channel
- Stomatin
- Transient receptor potential cation channel subfamily V member 1
- Stomatin-like protein 3
- Acid-sensing ion channel 2
- P2X purinoceptor 5
Sequence:
MKPTSGPEEARRPASDIRVFASNCSMHGLGHVFGPGSLSLRRGMWAAAVVLSVATFLYQVAERVRYYREFHHQTALDERESHRLIFPAVTLCNINPLRRSRLTPNDLHWAGSALLGLDPAEHAAFLRALGRPPAPPGFMPSPTFDMAQLYARAGHSLDDMLLDCRFRGQPCGPENFTTIFTRMGKCYTFNSGADGAELLTTTRGGMGNGLDIMLDVQQEEYLPVWRDNEETPFEVGIRVQIHSQEEPPIIDQLGLGVSPGYQTFVSCQQQQLSFLPPPWGDCSSASLNPNYEPEPSDPLGSPSPSPSPPYTLMGCRLACETRYVARKCGCRMVYMPGDVPVCSPQQYKNCAHPAIDAMLRKDSCACPNPCASTRYAKELSMVRIPSRAAARFLARKLNRSEAYIAENVLALDIFFEALNYETVEQKKAYEMSELLGDIGGQMGLFIGASLLTILEILDYLCEVFRDKVLGYFWNRQHSQRHSSTNLLQEGLGSHRTQVPHLSLGPRPPTPPCAVTKTLSASHRTCYLVTQL