wanglab/gogpt-training-data huggingface dataset:
Protein: 2-oxoglutarate oxidoreductase subunit KorA (EC 1.2.7.3) (Alpha-ketoglutarate oxidoreductase subunit alpha/gamma) (KG oxidoreductase subunit alpha/gamma) (KGO subunit alpha/gamma) (KOR subunit alpha/gamma) (O53182)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Component of KG oxidoreductase (KOR) that catalyzes the CoA-dependent oxidative decarboxylation of 2-oxoglutarate (alpha-ketoglutarate, KG) to succinyl-CoA. Methyl viologen can act as electron acceptor in vitro; the physiologic electron acceptor is unknown. Is involved in the alternative TCA pathway that functions concurrently with fatty acid beta-oxidation. Since a growing body of evidence indicates that lipids (for example cholesterol and fatty acids) are a predominant growth substrate for M.tuberculosis during infection, flux through KOR likely represents an important step in intermediary metabolism in vivo. KOR-dependent decarboxylation of KG also appears to be an important source of CO(2) in M.tuberculosis metabolism.
Interaction partners:
- 2-oxoglutarate oxidoreductase subunit KorB
- Isocitrate dehydrogenase 2
- Phosphate acetyltransferase
- Succinate--CoA ligase subunit alpha
- Succinate--CoA ligase subunit beta
- Probable molybdenum cofactor guanylyltransferase
- NADH-quinone oxidoreductase subunit I
- Chorismate synthase
- Pyruvate kinase
- Acetyl-coenzyme A synthetase
Sequence:
MDPNGSGAGPESHDAAFHAAPDRQRLENVVIRFAGDSGDGMQLTGDRFTSEAALFGNDLATQPNYPAEIRAPAGTLPGVSSFQIQIADYDILTAGDRPDVLVAMNPAALKANIGDLPLGGMVIVNSDEFTKRNLTKVGYVTNPLESGELSDYVVHTVAMTTLTLGAVEAIGASKKDGQRAKNMFALGLLSWMYGRELEHSEAFIREKFARKPEIAEANVLALKAGWNYGETTEAFGTTYEIPPATLPPGEYRQISGNTALAYGIVVAGQLAGLPVVLGSYPITPASDILHELSKHKNFNVVTFQAEDEIGGICAALGAAYGGALGVTSTSGPGISLKSEALGLGVMTELPLLVIDVQRGGPSTGLPTKTEQADLLQALYGRNGESPVAVLAPRSPADCFETALEAVRIAVSYHTPVILLSDGAIANGSEPWRIPDVNALPPIKHTFAKPGEPFQPYARDRETLARQFAIPGTPGLEHRIGGLEAANGSGDISYEPTNHDLMVRLRQAKIDGIHVPDLEVDDPTGDAELLLIGWGSSYGPIGEACRRARRRGTKVAHAHLRYLNPFPANLGEVLRRYPKVVAPELNLGQLAQVLRGKYLVDVQSVTKVKGVSFLADEIGRFIRAALAGRLAELEQDKTLVARLSAATAGAGANG
Protein: Uncharacterized protein (Q38CA3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSASCFTVCESLTTRSSWLARNGWTALPGQSRALSDFLAFLGRISRCRKVHRYVTAGCICVVAVTCVMRHFRHPIARRGVSGPWKLLKGCQVWLRRARSCDPPFRQQEDAVSVEGSFCSYQSSSITSTSTSSTPLSPGATLCVDEDVNSTDVAERSFDWHRRRLERKYVAPLLLMLAEVECVGQRLLHAATLVRGAVSVPVGEKVAGAKGSSVKNEEAGSLRKLLHIKTMDADDLLTQLITQLTMIPVGDNLSLKLRREALMSSTSVFAECIAKWMYLPLGTW
Protein: Sulfotransferase 1C2 (ST1C2) (rSULT1C2) (EC 2.8.2.1) (Sulfotransferase K1) (Q9WUW8)
Organism: Rattus norvegicus (Rat)
Function: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation. Sulfonates p-nitrophenol, a small phenolic compond. Does not sulfonate steroids, dopamine, acetaminophen, or alpha-naphthol.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:O46503}. Lysosome {ECO:0000269|PubMed:10872834}. Mitochondrion {ECO:0000269|PubMed:39194960}.
Interaction partners:
- Carbohydrate sulfotransferase 10
Sequence:
MALAPELSRQTKLKEVAGIPLQAPTVDNWSQIQTFKAKPDDLLICTYPKSGTTWIQEIVDMIEQNGDVEKCQRTIIQHRHPFIEWARPPQPSGVDKANAMPAPRILRTHLPTQLLPPSFWTNNCKFLYVARNAKDCMVSYYHFYRMSQVLPDPGTWNEYFETFINGKVSWGSWFDHVKGWWEIRDRYQILFLFYEDMKRDPKREIQKVMQFMGKNLDEEVVDKIVLETSFEKMKENPMTNRSTVPKSVLDQSISPFMRKGTVGDWKNHFTVAQNDRFDEIYKQKMGGTSLNFCMEL
Protein: Soluble starch synthase 1, chloroplastic/amyloplastic (EC 2.4.1.21) (Starch synthase I) (Q0DEC8)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Involved in starch synthesis in endosperm amyloplasts. Plays a role in the elongation of amylopectin chains. Synthesizes preferentially amylopectin chains with a degree of polymerization (DP) of 7 to 11 by elongating chains with a DP of 4 to 7. Generates distincly chains with a DP of 8 to 12 chains from short chains with a DP of 6 to 7.
Subcellular location: Plastid, chloroplast. Plastid, amyloplast. Note=Amyloplast or chloroplast, soluble. {ECO:0000305}.
Interaction partners:
- 4-alpha-glucanotransferase DPE2
- Granule-bound starch synthase 1, chloroplastic/amyloplastic
- 1,4-alpha-glucan-branching enzyme, chloroplastic/amyloplastic
- Glucose-1-phosphate adenylyltransferase small subunit 2, chloroplastic/amyloplastic/cytosolic
- 4-alpha-glucanotransferase DPE1, chloroplastic/amyloplastic
- starch synthase
- Glucose-1-phosphate adenylyltransferase large subunit 1, chloroplastic/amyloplastic
- Starch synthase, chloroplastic/amyloplastic
- Glucose-1-phosphate adenylyltransferase large subunit 2, cytosolic
- Glucose-1-phosphate adenylyltransferase small subunit 1, chloroplastic/amyloplastic
Sequence:
MATAAGMGIGAACLVAPQVRPGRRLRLQRVRRRCVAELSRDGGSAQRPLAPAPLVKQPVLPTFLVPTSTPPAPTQSPAPAPTPPPLPDSGVGEIEPDLEGLTEDSIDKTIFVASEQESEIMDVKEQAQAKVTRSVVFVTGEASPYAKSGGLGDVCGSLPIALALRGHRVMVVMPRYMNGALNKNFANAFYTEKHIKIPCFGGEHEVTFFHEYRDSVDWVFVDHPSYHRPGNLYGDNFGAFGDNQFRYTLLCYAACEAPLILELGGYIYGQKCMFVVNDWHASLVPVLLAAKYRPYGVYRDARSVLVIHNLAHQGVEPASTYPDLGLPPEWYGALEWVFPEWARRHALDKGEAVNFLKGAVVTADRIVTVSQGYSWEVTTAEGGQGLNELLSSRKSVLNGIVNGIDINDWNPSTDKFLPYHYSVDDLSGKAKCKAELQKELGLPIRPDVPLIGFIGRLDYQKGIDLIKLAIPDLMRDNIQFVMLGSGDPGFEGWMRSTESGYRDKFRGWVGFSVPVSHRITAGCDILLMPSRFEPCGLNQLYAMQYGTVPVVHGTGGLRDTVENFNPFAEKGEQGTGWAFSPLTIEKMLWALRMAISTYREHKSSWEGLMKRGMSSDFTWDHAASQYEQIFEWAFMDQPYVM
Protein: Homeobox protein Meis1b (Meis homeobox 1 b) (Myeloid ecotropic viral integration 1) (Transcription factor Meis1.1) (Q90XH2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|PROSITE-ProRule:PRU00108}.
Interaction partners:
- Homeobox protein Hox-A9b
- T-box transcription factor TBX20
- Homeobox protein Hox-A9a
- Pbxy homeodomain protein
- Runt-related transcription factor
- Homeobox protein Hox-B7a
- Rhombotin-2
Sequence:
MAQRYEDIPHYGMDGVGIPSTMYGDPHAARSMQAVHLNHGPQLHSHQYPHTAHTNAMPPSMGSSVNDALKRDKDSIYGHPLFPLLALIFEKCELATCTPREPGVAGGDVCSSESFNEDIAVFAKQIRAEKPLFSSNPELDNLMIQAIQVLRFHLLELEKVHELCDNFCHRYISCLKGKMPIDLVIDDREGGSKSDSEEITRSSGPLDQTSWNRDHDDTASTRSGGTPGPSSGGHTSHSGDNSSEQGDGLDNSVASPSTGDDDDPDKEKKRNKKRGIFPKVATNIMRAWLFQHLTHPYPSEEQKKQLAQDTGLTILQVNNWFINARRRIVQPMIDQSNRAVSQGAPYNPDGQPMGGFVMDGQQHMGIRPPGPMSGMGMNMGMEGQWHYM
Protein: [histone H3]-trimethyl-L-lysine(4) demethylase (EC 1.14.11.67) (A0A0G2K6G9)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- ATP synthase peripheral stalk subunit OSCP, mitochondrial
- ATP synthase F
- Lysine-specific histone demethylase
- ATP synthase F
- SUZ12 polycomb repressive complex 2 subunit
- Histone-lysine N-methyltransferase EZH2
- Myc proto-oncogene protein
- Uncharacterized protein
- ATP synthase F
- Histone H3
Sequence:
MEPATALPPGPRPALPLGGPGPLGEFLPPPECPVFEPSWEEFADPFAFIHKIRPIAEQTGICKVRPPPDWQPPFACDVDKLHFTPRIQRLNELEAQTRVKLNFLDQIAKYWELQGSTLKIPHVERKILDLFQLNKLVAEEGGFAVVCKDRKWTKIATKMGFAPGKAVGSHIRGHYERILNPYNLFLSGDSLRCLQKPNLTSDTKDKEYKPHDIPQRQSVQPSETCPPARRAKRMRAEAMNIKIEPEEATEARTHNLRRRMGCATPKRENEKEVKSTIKQEPTEKKDCVLESEKDKPKSRAKKTATAVDLYVCLLCGSGNDEDRLLLCDGCDDSYHTFCLLPPLHDVPKGDWRCPKCLAQECSKPQEAFGFEQAARDYTLRTFGEMADAFKSDYFNMPVHMVPTELVEKEFWRLVSTIEEDVTVEYGADIASKEFGSGFPVRDGKIKISPEEEEYLDSGWNLNNMPVMEQSVLAHITADICGMKLPWLYVGMCFSSFCWHIEDHWSYSINYLHWGEPKTWYGVPGYAAEQLENVMKKLAPELFVSQPDLLHQLVTIMNPNTLMTHEVPVYRTNQCAGEFVITFPRAYHSGFNQGFNFAEAVNFCTVDWLPLGRQCVEHYRLLHRYCVFSHDEMICKMASKADVLDVVVASTVQKDMAIMIEDEKALRETVRKLGVIDSERMDFELLPDDERQCIKCKTTCFMSAISCSCKPGLLVCLHHVKELCSCPPYKYNLRYRYTLDDLYPMMNALKLRAESYNEWALNVNEALEAKINKKKSLVSFKALIEESEMKKFPDNDLLRHLRLVTQDAEKCASVAQQLLNGKRQTRYRSGGGKSQSQLTVNELRQFVTQLCALPCVLSQTPLLKDLLNRVEDFQQQSQRLLSEERPRASELQQLLDVSFTFDVELPQLAEMRIRLEQARWLEEVQQACLDSSSLSLDDMRRLIDLGVGLAPYSAVEKAMARLQELLTVSEHWDDKAKSLLRARPRHSLSSLATAVKEMEEIPAYLPNGTVLKDSVQKARDWVQDVDALQAGGRVPVLETLIELVARGRSIPVHLNSLPRLEMLVSEVHAWKESAAKTFLLENSPYSLLEVLCPRCDIGLLGLKRKQRKLKDPLPSGKKRSTKLESLSDLERALTESKETASAMATLGEARLREMEALQSLRFANEEKLLSPAQDVETKVCLCQKTPATPMIQCELCRDAFHTSCVAVSSISQSSRIWLCPHCRRSEKPPLEKILPLLASLQRIRVRLPEGDALRYMIERTVNWQHRAQQLLSSGNLKLVQDQAGSGLLFSRWPASAGTASAADKVSQPPGTTSFSLPEDWDNRTSYLHSPFSTGQSCIPLHGLSPEVNELLMEAQLLQVSLPEVQELYQTLLTKPSSAQQADRSSPVRPSSEKNDCLRGKRDAINSLERKLKRRPEREGLPSERWDRVKKMRTPQKKKIKLSHPKDMNNFKLERERSYDLVRNAETHSLPSDTSYSEQEDSEDEDAICPAVSCLQPEGDEVSEVWAIEDVLSLNSETL
Protein: Integrin subunit alpha 2b (D3ZXC1)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MSHPYSVGSSITKGGNYHLLPRVAKTCPRALHLPSSTAPNLAHLVHRRHDLLVGAPLYMESRVDRKLAEVGRVYLFLQPKGLQALSSPTLVLTGTQVYGRFGSAIAPLGDLNRDGYNDVAVAAPYGGPSGQGQVLIFLGQSEGLSPRPSQVLDSPFPTGSGFGFSLRGSVDIDDNGYPDLIVGAYGASKVAVYRAQPVVMATVQLMVQDSLNPTLKNCVLEQTKTPVSCFNVQMCVGATGHNIPQKLHLKAELQLDLQKPRQARRVLLLASRQASLTLSLDLGGRNKPICHTIKAFLRDEADFRDKLSPIVLSLNVSLPPEETGVAPAVVLHGVTHVQEQTRIILDCGEDNLCVPQLQLTATAGDSPLLIGADNVLELKVNASNDGEGAYEAELAVHLPPGAHYIRAFSNVKGFERLVCTQKKENESRLALCELGNPMKKDTRIGITMLVSVEILEEAGDSVSFQLQIRSKNSQNPNSEAVLLPVAVRAEAAVELRGNSFPASLVVAAEEVDKEQDGLDSWVSRVEHTYELHNNGPGTVNGLSLIIHLPGQSQPSDLLYILDVQPKGGLLCSTQPPPKVDRRLTTPSPSSIRRIHHDRDRREASPQGSKQTEQQDPVLVVRRLSGLQLGPLEEGGRQGQ
Protein: Uncharacterized protein C17H9.06c (O13803)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Nucleus {ECO:0000269|PubMed:10759889, ECO:0000269|PubMed:16823372}.
Interaction partners:
- SAGA complex/transcription factor TFIID complex subunit Taf10
- SAGA complex/transcription factor TFIID complex subunit Taf12
- SAGA complex/transcription factor TFIID complex subunit Taf9
- SAGA complex/transcription factor TFIID complex subunit Taf6
- Transcription initiation factor TFIID subunit 2
- Transcription initiation factor TFIID subunit 7
- Transcription initiation factor TFIID subunit 11
- Putative transcription initiation factor TFIID 111 kDa subunit
- Transcription initiation factor TFIID subunit 4
- Transcription initiation factor TFIID subunit 8
Sequence:
MVSNQDNVQRNDVQKYPITRFVKRKSNVVLKKNKGAMKSNSNSRSRGNKKLKESQFSSRDNFRTTQTQASSSSEPSDNTNRLVPVVIIDNNTPKKEESNAEKLKLDKDSSSVNYENQISKPLITFSDIHETVNVPFLCLDKHDSKNEVAINSHEDSPVCLEDITGSLSSTYGNDSLGESNLEELPTSDKIKGENMGSRKKRKGFVIDSEDSDTGIPREENVTITRKTKLSSNILYSDSDTERQSDSGSKNVARQFSRIKRKRKVLSSSSEDDESSSPEDLLKPIIRSTEEMENLNELEQEVQDLDPIDEGFEEKVPRFRNPSKKAFYEKLHSLRNRSYSKLESLTSEKSDTLITKSELANESEEDDFIVDDEDTEVMMNARSLLPAEFSMTSHQGLKAHFRNFMMFIVQQAIDPIDASDISDHYLFSRRTIRKQLYSSVDSNIISSIWQSEFIKLIKTVPNMKSAKIDATYGCDACNIHTRMSTQIVYFKGMPYNEHNYKELDSFEPITKEAWMLGNSCFNRARIAHSIYHWEYKVSRHIQVELKFREASNTSEQGKNIVESIYEDLKDSNFFETTWVELCNLLKLASSSFESNFHSRSSM
Protein: Peroxisomal biogenesis factor 5 (F5H5C0)
Organism: Homo sapiens (Human)
Subcellular location: Peroxisome {ECO:0000256|ARBA:ARBA00004275}.
Interaction partners:
Sequence:
MAMRELVEAECGGANPLMKLAGHFTQDKALRQEGLRPGPWPPGAPASEALVAEFLQDQNAPLVSRAPQTFKMDDLLAEMQQIEQSNFRQAPQRAPGVADLALSENWAQEFLAAGDAVDVTQDYNETDWSQEFISEVTDPLSVSPARWAEEYLEQSEEKLWLGEPEGTATDRWYDEYHPEEDLQHTASDFVAKVDDPKLANSEGTSDAWVDQFTRPVNTSALDMEFERAKSAIESDVDFWDKLQAELEEMAKRDAEAHPWLSDYDDLTSATYD
Protein: CLIP domain-containing serine protease B8 (EC 3.4.21.-) [Cleaved into: CLIP domain-containing serine protease B8 light chain; CLIP domain-containing serine protease B8 heavy chain] (Q8MZM7)
Organism: Anopheles gambiae (African malaria mosquito)
Function: Serine protease that functions in the melanization-mediated immune response. Preferentially, cleaves substrates with an arginine at the P1 site. May be involved in the activation of the prophenoloxidase cascade upstream of CLIPB9; does not cleave prophenoloxidase.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Serine protease inhibitor 2
Sequence:
MSSAVLLLLVCGCALAVLSPVAYGAPMDTDDRPVWDSIRLCDIPNEPNPGQCMLPAECVAYGKINDVSSLSSIERFSFIKQIQCNGSDTVPYVCCPRDSDAYREPYVNETMVPKNRVASRIAFDADSCGIQSYVAKIRGGQLAEIDEFPWMAMLLYERDNNALTQGCGGALISRTYVITAAHCVTGKNFQQTKGRLKFVRLREYNIHTNPDCVYENDLKDCSDDMIDLVPQAVIPHPEYDSESSNQQHDIALIRIEQTPPFTDFLRSICLPEQNFESSATPGKKLSVSGWGRTDIFKDNLGPDVLSPIKLKLSLPYVEREKCSKTFRPWSFALGPGQMCAGGERAKDTCAGDSGSPLMSYDMKRAIWYITGIVSLGVRGCGVEGLPGVYTNVHHYLPWIKMYTGA
Protein: Actin-12 (EC 3.6.4.-) (P53497)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. Essential component of cell cytoskeleton; plays an important role in cytoplasmic streaming, cell shape determination, cell division, organelle movement and extension growth. This is considered as one of the reproductive actins.
Subcellular location: Cytoplasm, cytoskeleton.
Interaction partners:
- Actin-interacting protein 1-2
- Actin-depolymerizing factor 6
- Tubulin alpha-3 chain
- Actin-related protein 4
- Actin-related protein 2
- Actin-related protein 2/3 complex subunit 3
- Tubulin alpha-6 chain
- F-actin-capping protein subunit beta
- Tubulin alpha-1 chain
- Actin-related protein 9
Sequence:
MADGEDIQPLVCDNGTGMVKAGFAGDDAPRAVFPSIVGRPRHTGVMVGMGQKDAYVGDEAQSKRGILTLKYPIEHGIVNNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPIYEGYALPHAILRLDLAGRDLTDHLMKILTERGYSFTTTAEREIVRDMKEKLSYIALDYEQELETSKTSSSVEKSFELPDGQVITIGAERFRCPEVLFQPSMIGMENPGIHETTYNSIMKCDVDIRKDLYGNIVLSGGTTMFGGIGDRMSKEITALAPSSMKIKVVAPPERKYSVWIGGSILASLSTFQQMWIAKAEYDESGPSIVHRKCF
Protein: Gtt11p (A0A1D8PJR2)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Gst2p
- Glutathione reductase
- Gst1p
- Gst3p
- Thioredoxin peroxidase
- Ecm38p
- Glutathione hydrolase
- Glutathione synthetase
- Gtt1p
- Gtt13p
Sequence:
MSDTKIIVHWLNYSRSQRVIWLLEELNIPFELKVYLRNKQFRAPKELENVHPLGKSPVIEVIDTKTGESEVIAETGHIFNYILSNYDTTNILTPANRKLQNQVDYFLHYAEGTLQPNLVALLVHGFAKQQAPFGTKFLMGLLVNGIDSMFYIPELKKNLNYLEDIMRKQHENGSNYFVGDKLSGADIILEFPVITNIFQNKRGAEQLGAGDVEKEYPHLNQWAEDIKKEPKYIKAQELVAKHETVKPNI
Protein: Calcium-transporting ATPase (EC 7.2.2.10) (Q9V4C7)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane {ECO:0000256|RuleBase:RU361146}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU361146}.
Interaction partners:
Sequence:
MATIDGRPAQYGISLKQLRELMEHRGREGVMKIAENGGIHELCKKLYTSPNEGLSGSKADEEHRRETFGSNVIPPKPPKTFLTLVWEALQDVTLIILEVAALVSLGLSFYKPADEDAPVLQEEEEHHGWIEGLAILISVIVVVIVTAFNDYSKERQFRGLQNRIEGEHKFSVIRGGEVCQISVGDILVGDIAQVKYGDLLPADGCLIQSNDLKVDESSLTGESDHVKKGPDVDPMVLSGTHVMEGSGKMVVTAVGVNSQAGIIFTLLGAAVDEQEAEIKKMKKEAKRANKQKNLTGENDGRSQIKGSQAPSQRETVTSEITKSESEGNHLPQSSSSGAAETGHKKEKSVLQAKLTKLAIQIGYAGSTIAVLTVIILIIQFCIKTFVIDEKPWKNTYANNLVKHLIIGVTVLVVAVPEGLPLAVTLSLAYSVKKMMKDNNLVRHLDACETMGNATAICSDKTGTLTTNRMTVVQSYICEKLCKVLPTLSDIPQHVGNLITMGISVNSAYTSNIMAGHNPGDLPIQVGNKTECALLGFVQGLGVKYQSIRDEITEDKFTRVYTFNSVRKSMGTVIPRPNGGYRLYTKGASEIIMKKCAFIYGHEGTLEKFTRDMQERLIREVIEPMACDGLRTISVAYRDFVPGKAAINEVHIDGEPNWDDEENIMTNLTCLCVVGIEDPVRPEVPDAIRKCQRAGITVRMVTGDNINTARSIASKCGILRPNDDFLILEGKEFNRRIRDSNGDIQQHLIDKVWPKLRVLARSSPTDKYTLVKGIIDSTVSENREVVAVTGDGTNDGPALKKADVGFAMGIAGTDVAKEASDIILTDDNFSSIVKAVMWGRNVYDSIAKFLQFQLTVNVVAVIVAFIGACAVQDSPLKAVQMLWVNLIMDTLASLALATEFPTPDLLLRKPYGRTKPLISRTMMKNILGQALYQLIIIFGLLFVGDVILDIESGRGQELNAGPTQHFTIIFNTFVMMTLFNEINARKIHGQRNVIEGLLTNPIFYTIWIFTMISQVLIIQYGKMAFSTKALTLDQWLWCIFFGIGTLVWGQLITSVPTRKLPKILSWGRGHPEEYTDGMNLGEERFDSIDSDKKPRAGQILWIRGLTRLQTQVIGGELQERLIPVPYSKSNTDQAIRVVNAFRQGLDARYGDHTNTSLAEVLRKQTSLSKRLSETSSIEYADNIPDELTIPEIDVERLSSHSHTETAV
Protein: Na(+)/H(+) antiporter 1 (MjNhaP1) (Q60362)
Organism: Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
Function: This is a Na(+)/H(+) antiporter. Can also transport lithium.
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Uncharacterized membrane protein MJ0091
- Riboflavin kinase
- 3,4-dihydroxy-2-butanone 4-phosphate synthase
- Uncharacterized ATP-dependent helicase MJ0104
- Uncharacterized protein MJ0912
Sequence:
MELMMAIGYLGLALVLGSLVAKIAEKLKIPDIPLLLLLGLIIGPFLQIIPSDSAMEIFEYAGPIGLIFILLGGAFTMRISLLKRVIKTVVRLDTITFLITLLISGFIFNMVLNLPYTSPVGYLFGAITAATDPATLIPVFSRVRTNPEVAITLEAESIFNDPLGIVSTSVILGLFGLFSSSNPLIDLITLAGGAIVVGLLLAKIYEKIIIHCDFHEYVAPLVLGGAMLLLYVGDDLLPSICGYGFSGYMAVAIMGLYLGDALFRADDIDYKYIVSFCDDLSLLARVFIFVFLGACIKLSMLENYFIPGLLVALGSIFLARPLGVFLGLIGSKHSFKEKLYFALEGPRGVVPAALAVTVGIEILKNADKIPASITKYITPTDIAGTIIIGTFMTILLSVILEASWAGMLALKLLGEYKPKYKEESHH
Protein: DnaJ heat shock protein family (Hsp40) member C7 (K7ER44)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MCPKNASYYGNRAATLMMLGRFREALGDAQQSVRLDDSFVRGHLREGKCHLSLGNAMAACRSFQRALELDHKNAQAQQEFKNANAVMEYEKIAETDFEKRDFRKVVFCMDRALEFAPACHRFKILKAECLAMLGRYPEAQSVASDILRMDSTNADALYVRGLCLYYEDCIEKAVQFFVQALRMAPDHEKACIACRNAKALKAKKEDGNKAFKEGNYKLAYELYTEALGIDPNNIKTNAKLYCNRGTVNSKYEEAVRDYEKVYQTEKTKEHKQLLKNAQLELKKSKRKDYYKILGVDKNASEDEIKKAYRKRALMHHPDRHSGASAEVQKEEEKKFKEVGEAFTILSDPKKKTRYDSGQDLDEEGMNMGDFDPNNIFKAFFGGPGGFSFEASGPGNFFFQFG
Protein: Sphingosine-1-phosphate phosphatase 1 (SPP) (SPPase1) (mSPP1) (EC 3.1.3.-) (Sphingosine-1-phosphatase 1) (Q9JI99)
Organism: Mus musculus (Mouse)
Function: Specifically dephosphorylates sphingosine 1-phosphate (S1P), dihydro-S1P, and phyto-S1P. Does not act on ceramide 1-phosphate, lysophosphatidic acid or phosphatidic acid. Sphingosine-1-phosphate phosphatase activity is needed for efficient recycling of sphingosine into the sphingolipid synthesis pathway. Regulates the intracellular levels of the bioactive sphingolipid metabolite S1P that regulates diverse biological processes acting both as an extracellular receptor ligand or as an intracellular second messenger. Involved in efficient ceramide synthesis from exogenous sphingoid bases. Converts S1P to sphingosine, which is readily metabolized to ceramide via ceramide synthase. In concert with sphingosine kinase 2 (SphK2), recycles sphingosine into ceramide through a phosphorylation/dephosphorylation cycle. Regulates endoplasmic-to-Golgi trafficking of ceramides, resulting in the regulation of ceramide levels in the endoplasmic reticulum, preferentially long-chain ceramide species, and influences the anterograde membrane transport of both ceramide and proteins from the endoplasmic reticulum to the Golgi apparatus (By similarity). The modulation of intracellular ceramide levels in turn regulates apoptosis. Via S1P levels, modulates resting tone, intracellular Ca(2+) and myogenic vasoconstriction in resistance arteries. Also involved in unfolded protein response (UPR) and ER stress-induced autophagy via regulation of intracellular S1P levels (By similarity). Involved in the regulation of epidermal homeostasis and keratinocyte differentiation.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:12235122}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:12235122}; Multi-pass membrane protein {ECO:0000255}. Note=Mainly found in intracellular membrane fractions. {ECO:0000269|PubMed:12235122}.
Interaction partners:
- Sphingosine-1-phosphate lyase 1
- Sphingosine kinase 2
- Sphingosine kinase 1
- Ceramide synthase 2
- Acid ceramidase
- Ceramide synthase 4
- Ceramide glucosyltransferase
- Alkaline ceramidase 3
- Ceramide synthase 5
- Sphingolipid delta
Sequence:
MSLGQRLALLASRLQEPQRVASFQRLCGVEVPLSSPAADEDAETEVRGAPGEPRRRGRQPGAEDSPAKADCCGAPNGVRNGLAAEPGPTGPRRAGSQRRNSLTGEEGELVKVSNLPLYYLFCLGTELGNELFYILFFPFWIWNLDPFVGRRLVIIWVLVMYLGQCTKDIIRWPRPASPPVIKLEVFYNSEYSMPSTHAMSGTAIPIAMFLLTYGRWQYPLIYGLILIPCWSSLVCLSRIYMGMHSILDVIAGFLYTILILIIFYPLVDLIDNFNQTYKYAPLIIIGLHLILGIFSFTLDTWSTSRGDTAEILGSGAGIACGSHAAYTLGLSLEPSLHMLPLAIPPLTVTLFGKAILRIVLGMLLVLFVRDIMKKITIPLACKLSSIPCHDIRQARQHMEVELPYRYITYGMVGFSITFLVPYVFSFIGIS
Protein: Desmoglein-4 (Q6W3B0)
Organism: Rattus norvegicus (Rat)
Function: Component of intercellular desmosome junctions. Involved in the interaction of plaque proteins and intermediate filaments mediating cell-cell adhesion. Coordinates the transition from proliferation to differentiation in hair follicle keratinocytes (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q86SJ6}; Single-pass type I membrane protein {ECO:0000255}. Cell junction, desmosome {ECO:0000250|UniProtKB:Q86SJ6}. Note=Colocalizes with JUP at desmosomes. {ECO:0000250|UniProtKB:Q86SJ6}.
Interaction partners:
- Gasdermin A
- Plakophilin-1
- Plakophilin-3
- Desmoplakin
- Junction plakoglobin
Sequence:
MDWLLFRNICLLILFMVVLGVNSEFIVEVKELDIENGTTTWQTVRRQKREWIKFAAACREGEDNSKRNPIARIRSDCEVSQRITYRISGAGIDRPPYGVFTINPRTGEINITSVVDREITPLFLIHCRALNSRGEDLERPLELRVKVMDVNDNPPVFTQNVYTANIEENSDANALVVKLSATDADEDNHLNSKIAYKIISQEPAGAPMFMVNRYTGEVRTMSNFLDREQHSMYNLLVRGSDRDGATDGLSSECDCRIKILDVNDNFPILEKTSYSASIEENCLSSELIRLQAIDLDEEGTDNWLAQYSILSGNDGNWFEIQTDPKTNEGILKLVKMLDYEQEPNIYLSIGVRNQAEFHHSVASQFQMHSTPVRIQVINVREGPTFRPSSMTFSLRGGMRGDSLMNYVLGTYTAIDMDTGSPATNVRYVIGHDAGSWLKVDSRTGEIQFSREFDTKSKYITDGMYAAEILAIDDGSGRTATGTICIEVPDANDYCPVIYAESRSVCTHASSVRIYVNDHSFGAPFTFCVVDESPDTADIWDIRSINGTSAILMTEQTLSPGPYQIPILVKDSHNRACELPQTVLLDACLCDDYHVCLHSSTTGIYTGDTIWVTDDMGTVTDDGLRQSNVGLGPAGIGMIILGLLLLFLSPLLLLMCCCKRRQPEGLGTRFAPVPEGGEGVMQPWRIEGAHPEDRDVSNICVPMTASNTQDRIDSSEIYTNTYAGGGTVEGGVSGVELNTGVGTAAGIAAGGATGTLRKRSSTIGTLREYQDTGMNMAFLDSYFSEKAYAYADEDEGRPANDCLLIYDHEGTGSPVGSIGCCSWIVDDLDESYMETLDPKFRTLAEICLDTEIEPFPSHQACIPISTDLPLLGPNYFVNESSGMTLSEAEFQAEMAAASEPMIHGDIIVTETYTATDPCVQPTTIVFDSQLPPNVVVTETVMAPVYDVQGNICVPAEIANTHNVYYAERVVASPGVPDMGNGNIGDTCIGPVMSGGILVGPEIQVTQMMSPDIHISQTTRSTSPMTSQHRVTRYSNIHYSRQ
Protein: Fatty-acid amide hydrolase 1 (EC 3.5.1.99) (Anandamide amidase) (Anandamide amidohydrolase 1) (Fatty acid ester hydrolase) (EC 3.1.1.-) (Oleamide hydrolase 1) (P97612)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the hydrolysis of endogenous amidated lipids like the sleep-inducing lipid oleamide ((9Z)-octadecenamide), the endocannabinoid anandamide (N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-ethanolamine), as well as other fatty amides, to their corresponding fatty acids, thereby regulating the signaling functions of these molecules. Hydrolyzes polyunsaturated substrate anandamide preferentially as compared to monounsaturated substrates. It can also catalyze the hydrolysis of the endocannabinoid 2-arachidonoylglycerol (2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-glycerol). FAAH cooperates with PM20D1 in the hydrolysis of amino acid-conjugated fatty acids such as N-fatty acyl glycine and N-fatty acyl-L-serine, thereby acting as a physiological regulator of specific subsets of intracellular, but not of extracellular, N-fatty acyl amino acids (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:9122178, ECO:0000269|PubMed:9790682}; Single-pass membrane protein {ECO:0000269|PubMed:9122178}. Golgi apparatus membrane {ECO:0000269|PubMed:9122178, ECO:0000269|PubMed:9790682}; Single-pass membrane protein {ECO:0000269|PubMed:9122178}. Note=Seems to be associated with the endoplasmic reticulum and/or Golgi apparatus.
Interaction partners:
- Glutamyl-tRNA
- Monoglyceride lipase
- N-acyl-phosphatidylethanolamine-hydrolyzing phospholipase D
- Monoacylglycerol lipase ABHD6
- N-acylethanolamine-hydrolyzing acid amidase
- Bifunctional glutamate/proline--tRNA ligase
- G protein-coupled receptor 55
- Transient receptor potential cation channel subfamily V member 1
- Cannabinoid receptor 1
- Lysophosphatidylserine lipase ABHD12
Sequence:
MVLSEVWTTLSGVSGVCLACSLLSAAVVLRWTGRQKARGAATRARQKQRASLETMDKAVQRFRLQNPDLDSEALLTLPLLQLVQKLQSGELSPEAVFFTYLGKAWEVNKGTNCVTSYLTDCETQLSQAPRQGLLYGVPVSLKECFSYKGHDSTLGLSLNEGMPSESDCVVVQVLKLQGAVPFVHTNVPQSMLSFDCSNPLFGQTMNPWKSSKSPGGSSGGEGALIGSGGSPLGLGTDIGGSIRFPSAFCGICGLKPTGNRLSKSGLKGCVYGQTAVQLSLGPMARDVESLALCLKALLCEHLFTLDPTVPPLPFREEVYRSSRPLRVGYYETDNYTMPSPAMRRALIETKQRLEAAGHTLIPFLPNNIPYALEVLSAGGLFSDGGRSFLQNFKGDFVDPCLGDLILILRLPSWFKRLLSLLLKPLFPRLAAFLNSMRPRSAEKLWKLQHEIEMYRQSVIAQWKAMNLDVLLTPMLGPALDLNTPGRATGAISYTVLYNCLDFPAGVVPVTTVTAEDDAQMELYKGYFGDIWDIILKKAMKNSVGLPVAVQCVALPWQEELCLRFMREVEQLMTPQKQPS