wanglab/gogpt-training-data huggingface dataset:
Protein: Katanin p60 ATPase-containing subunit A1 (Katanin p60 subunit A1) (EC 5.6.1.1) (p60 katanin) (O75449)
Organism: Homo sapiens (Human)
Function: Catalytic subunit of a complex which severs microtubules in an ATP-dependent manner. Microtubule severing may promote rapid reorganization of cellular microtubule arrays and the release of microtubules from the centrosome following nucleation. Microtubule release from the mitotic spindle poles may allow depolymerization of the microtubule end proximal to the spindle pole, leading to poleward microtubule flux and poleward motion of chromosome. Microtubule release within the cell body of neurons may be required for their transport into neuronal processes by microtubule-dependent motor proteins. This transport is required for axonal growth.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10751153, ECO:0000269|PubMed:26929214, ECO:0000269|PubMed:9658175}. Midbody {ECO:0000269|PubMed:19261606}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000255|HAMAP-Rule:MF_03023}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:10751153, ECO:0000269|PubMed:26929214, ECO:0000269|PubMed:9658175}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:26929214}. Note=Predominantly cytoplasmic (PubMed:9658175). Localized diffusely in the cytoplasm during the interphase (PubMed:10751153). During metaphase is localized throughout the cell and more widely dispersed than the microtubules. In anaphase and telophase is localized at the midbody region (PubMed:19261606). Also localized to the interphase centrosome and the mitotic spindle poles (By similarity). Enhanced recruitment to the mitotic spindle poles requires microtubules and interaction with KATNB1 (PubMed:10751153). Localizes within the cytoplasm, partially overlapping with microtubules, in interphase and to the mitotic spindle and spindle poles during mitosis (PubMed:26929214). {ECO:0000255|HAMAP-Rule:MF_03023, ECO:0000269|PubMed:10751153, ECO:0000269|PubMed:19261606, ECO:0000269|PubMed:26929214, ECO:0000269|PubMed:9658175}.
Interaction partners:
- Katanin p80 WD40 repeat-containing subunit B1
- KATNB1-like protein 1
- Leucine zipper putative tumor suppressor 2
- Nuclear distribution protein nudE-like 1
- Abnormal spindle-like microcephaly-associated protein
- Glycerol-3-phosphate dehydrogenase, mitochondrial
Sequence:
MSLLMISENVKLAREYALLGNYDSAMVYYQGVLDQMNKYLYSVKDTYLQQKWQQVWQEINVEAKHVKDIMKTLESFKLDSTPLKAAQHDLPASEGEVWSMPVPVERRPSPGPRKRQSSQYSDPKSHGNRPSTTVRVHRSSAQNVHNDRGKAVRCREKKEQNKGREEKNKSPAAVTEPETNKFDSTGYDKDLVEALERDIISQNPNVRWDDIADLVEAKKLLKEAVVLPMWMPEFFKGIRRPWKGVLMVGPPGTGKTLLAKAVATECKTTFFNVSSSTLTSKYRGESEKLVRLLFEMARFYSPATIFIDEIDSICSRRGTSEEHEASRRVKAELLVQMDGVGGTSENDDPSKMVMVLAATNFPWDIDEALRRRLEKRIYIPLPSAKGREELLRISLRELELADDVDLASIAENMEGYSGADITNVCRDASLMAMRRRIEGLTPEEIRNLSKEEMHMPTTMEDFEMALKKVSKSVSAADIERYEKWIFEFGSC
Protein: E3 ubiquitin-protein ligase CBL (EC 2.3.2.27) (B9EKI5)
Organism: Mus musculus (Mouse)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MANSMNGRNPGGRGGNPRKGRILGIIDAIQDAVGPPKQAAADRRTVEKTWKLMDKVVRLCQNPKLQLKNSPPYILDILPDTYQHLRLILSKYDDNQKLAQLSENEYFKIYIDSLMKKSKRAIRLFKEGKERMYEEQSQDRRNLTKLSLIFSHMLAEIKAIFPNGQFQGDNFRITKADAAEFWRKFFGDKTIVPWKVFRQCLHEVHQISSGLEAMALKSTIDLTCNDYISVFEFDIFTRLFQPWGSILRNWNFLAVTHPGYMAFLTYDEVKARLQKYSTKPGSYIFRLSCTRLGQWAIGYVTGDGNILQTIPHNKPLFQALIDGSREGFYLYPDGRSYNPDLTGLCEPTPHDHIKVTQEQYELYCEMGSTFQLCKICAENDKDVKIEPCGHLMCTSCLTAWQESDGQGCPFCRCEIKGTEPIIVDPFDPRDEGSRCCSIIDPFSIPMLDLDDDDDREESLMMNRLASVRKCTDRQNSPVTSPGSSPLAQRRKPQPDPLQIPHLSLPPVPPRLDLIQKGIVRSPCGSPTGSPKSSPCMVRKQDKPLPAPPPPLRDPPPPPERPPPIPPDNRLSRHFHHGESVPSRDQPMPLEAWCPRDAFGTNQVMGCRILGDGSPKPGVTANSSLNGRHSRMGSEQVLMRKHRRHDLPSEGAKVFSNGHLATEEYDVPPRLSPPPPVTTLLPSIKCTGPLANCLSEKTRDTVEDDDDEYKIPSSHPVSLNSQPSHCHNVKAPVRSCDNGHCILNGTHGAPSEMKKSNIPDLGIYLKGEDAFDALPPSLPPPPPPARHSLIEHSKPPGSSSRPSSGQDLFLLPSDPFFDPTSGQVPLPPARRAAGDSGKANRASQDYDQLPSSSDGSQAPARPPKPRPRRTAPEIHHRKPHGPEAALENVDAKIAKLMGEGYAFEEVKRALEIAQNNVEVARSILREFAFPPPVSPRLNL
Protein: Cytochrome P450 4e2 (EC 1.14.-.-) (CYPIVE2) (Q27606)
Organism: Drosophila melanogaster (Fruit fly)
Function: May be involved in the metabolism of insect hormones and in the breakdown of synthetic insecticides.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. Microsome membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MWFVLYIFLALPLLLVAYLELSTFRRRRVLNKFNGPRGLPLMGNAHQMGKNPSEILDTVFSWWHQYGKDNFVFWIGTYSNVLVTSSKYLEFILSSQTLITKSDIYQLTHPWLGLGLLTSTGSKWHKHRKMITPAFHFNILQDFHEVMNENSTKFIKHLKTVAAGDNIFDFQEQAHYLTLDVICDTAMGVSINAMENRSSSIVQAFKDMCYNINMRAFHPLKRNELLYRLAPDYPAYSRTLKTLQDFTNEIIAKRIEAHKSGAVSTNAGDEFTRKKMAFLDTLLSSTIDGRPLNSKELYEEVSTFMFEGHDTTTSGVSFAVYLLSRHQDEQRKLFKEQREVMGNSELGRDATFQEISQMKYLDLFIKEAQRVYPSVPFIGRFTEKDYVIDGDLVPKGTTLNLGLVMLGYNEKVFKDPHKFRPERFELEKPGPFEYVPFSAGPRNCIGQKFALLEIKTVVSKIIRNFEVLPALDELVSKDGYISTTIGLPDAERKKRDPYRHKYDPILSAVLTLKSENGLYIRLKERH
Protein: TSC22 domain family protein 3 (Glucocorticoid-induced leucine zipper protein) (Q9EQZ1)
Organism: Rattus norvegicus (Rat)
Function: Protects T-cells from IL2 deprivation-induced apoptosis through the inhibition of FOXO3A transcriptional activity that leads to the down-regulation of the pro-apoptotic factor BCL2L11. In macrophages, plays a role in the anti-inflammatory and immunosuppressive effects of glucocorticoids and IL10. In T-cells, inhibits anti-CD3-induced NFKB1 nuclear translocation. In vitro, suppresses AP1 and NFKB1 DNA-binding activities. Inhibits myogenic differentiation and mediates anti-myogenic effects of glucocorticoids by binding and regulating MYOD1 and HDAC1 transcriptional activity resulting in reduced expression of MYOG (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9Z2S7}. Nucleus {ECO:0000250|UniProtKB:Q9Z2S7}. Note=Localization may depend on differentiation status of myoblasts (By similarity). In undifferentiated myoblasts; localizes to the cytoplasm, but in differentiating myoblast; localizes to the nucleus (By similarity). {ECO:0000250|UniProtKB:Q9Z2S7}.
Interaction partners:
- Uncharacterized protein.
- Serine/threonine-protein kinase Sgk1
- RAF proto-oncogene serine/threonine-protein kinase
- peptidylprolyl isomerase
- NEDD4-like E3 ubiquitin protein ligase.
Sequence:
MNTEMYQTPMEVAVYQLHNFSISFFSSLLGGDVVSVKLDNSASGASVVALDNKIEQAMDLVKNHLMYAVREEVEVLKEQIRELVEKNSQLERENTLLKTLASPEQLEKFQSRLSPEEPAPEAPETPEAPGGSAV
Protein: ArfGAP with RhoGAP domain, ankyrin repeat and PH domain 1 (E7EU13)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MTKKEEPPPSRVPRAVRVASLLSEGEELSGDDQGDEEEDDHAYEGVPNGGWHTSSLSLSLPSTIAAPHPMDGPPGGSTPVTPVIKAGWLDKNPPQGSYIYQKRWVRLDTDHLRYFDSNKDAYSKRFISVACISHVAAIGDQKFEVITNNRTFAFRAESDVERKEWMQALQQAMAEQRARARLSSAYLLGVPGSEQPDRAGSLELRGFKNKLYVAVVGDKVQLYKNLEEYHLGIGITFIDMSVGNVKEVDRRSFDLTTPYRIFSFSADSELEKEQWLEAMQGAIAEALSTSEVAERIWAAAPNRFCADCGAPQPDWASINLCVVICKRCAGEHRGLGAGVSKVRSLKMDRKVWTETLIELFLQLGNGAGNRFWAANVPPSEALQPSSSPSTRRCHLEAKYREGKYRRYHPLFGNQEELDKALCAAVTTTDLAETQALLGCGAGINCFSGDPEAPTPLALAEQAGQTLQMEFLRNNRTTEVPRLDSMKPLEKHYSVVLPTVSHSGFLYKTASAGKLLQDRRAREEFSRRWCVLGDGVLSYFENERAVTPNGEIRASEIVCLAVPPPDTHGFEHTFEVYTEGERLYLFGLESAEQAHEWVKCIAKAFVPPLAEDLLARDFERLGRLPYKAGLSLQRAQEGWFSLSGSELRAVFPEGPCEEPLQLRKLQELSIQGDSENQVLVLVERRRTLYIQGERRLDFMGWLGAIQKAAASMGDTLSEQQLGDSDIPVIVYRCVDYITQCGLTSEGIYRKCGQTSKTQRLLESLRQDARSVHLKEGEQHVDDVSSALKRFLRDLPDGLFTRAQRLTWLEASEIEDEEEKVSRYRELLVRLPPVNRATVKALISHLYCVQCFSDTNQMNVHNLAIVFGPTLFQTDGQDYKAGRVVEDLINHYVVVFSVDEEELRKQREEITAIVKMRVAGTASGTQHAGDFICTVYLEEKKAETEQHIKVPASMTAEELTLEILDRRNVGIREKDYWTCFEVNEREEAERPLHFAEKVLPILHGLGTDSHLVVKKHQAMEAMLLYLASRVGDTKHGMMKFREDRSLLGLGLPSGGFHDRYFILNSSCLRLYKEVRSHRPEKEWPIKSLKVYLGVKKKLRPPTCWGFTVVHETEKHEKQQWYLCCDTQMELREWFATFLFVQHDGLVWPSEPSRVSRAVPEVRLGSVSLIPLRGSENEMRRSVAAFTADPLSLLRNV
Protein: Guanylate-binding family protein (F4ITY5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Purple acid phosphatase 3
Sequence:
MEIPRRTFVFFFSLCLLSSTSLSIDNFHQAFPIVEPAPGHTKLQLSREGLEAISRITTPISAVAVIGPYRSGKSFLLNQLLSLSCYEGFGVGHMRDTKTKGIWVWGTPLELEIDGVKTSVIYLDTEGFESVGKSNVYDDRIFALATVMSSVLIYNLPETIREADISRLSFAVELAEEFYGRVKGEDVAFEPSKLLWLIQRDFLQGKSVKQMVDEALRHVPNEDGNKNIDQVNQIRDSLAIMGDNSTAFSLPQPHLMRTKLCDLKDEDLDSTYVARRDQLKKLVASIIRPKIVQGKTLNGKEFISFLEQILDALNKGEIPSTGSLVEVFNKDIVERCVKLYNEKMVRVRLPMSEESLQSAHEMAHNEAIKAFDAQHFGRQHAKKSVDQLDEQMQEVYKNFVLANEYQSSKLCEALYTSCEDDMDHLQALRLPSMAKFNAGFVYCNKTFEQQCVGPSKQNYEQRLTKMMGKSRSLFIKEYNNRLFNWLVGFSLVMVVVGRFIIKFILLEMAAWILFIFLETYTRMFWTAEALYYNPVWHFIVGTWENVVYSPVLDLDRWAIPIVCIIALCVLYWRCYGKRKHGARWLLPLYNNQKNGRNRERSE
Protein: Anthrone oxygenase encC (EC 1.-.-.-) (Endocrocin synthesis protein C) (A4DA85)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Function: Anthrone oxygenase; part of the gene cluster that mediates the biosynthesis of endocrocin, a simple anthraquinone interesting for many biotechnological applications. The pathway begins with the synthesis of atrochrysone thioester by the polyketide synthase (PKS) encA. The atrochrysone carboxyl ACP thioesterase encB then breaks the thioester bond and releases the atrochrysone carboxylic acid from encA. The atrochrysone carboxylic acid is then converted to endocrocin anthrone which is further oxidized into endocrocin by the anthrone oxygenase encC. The exact function of encD has not been identified yet, but it negatively regulates endocrocin production, likely through the modification of endocrocin itself.
Subcellular location: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Atrochrysone carboxyl ACP thioesterase
- Atrochrysone carboxylic acid synthase
Sequence:
MASVQGLIKIVAITGGVWLSGKITAHSLVSVPALLQTRSADGLSPCTILRVWRRIYEQGHRHSPQIAACTSTAFAYLAWCASDRTPRLLYGTAACSVMGIVPYTLLFMGPTNSRLLERSAAEEEKVPGATRGEDMVNVPSEMTTEELLSHWRFLAGIRGLLPLAGGILGLFAALYSNEGAR
Protein: CDK-activating kinase assembly factor MAT1 (CDK7/cyclin-H assembly factor) (Menage a trois) (RING finger protein MAT1) (A0A8I6ATM4)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR003338}.
Interaction partners:
Sequence:
MDDQGCPRCKTTKYRNPSLKLMVNVCGHTLCESCVDLLFVRGAGNCPECGTPLRKSNFRVQLFEDPTVDKEVEIRKKVLKIYNKREEDFPSLREYNDFLEEVEEIVFNLTNNVDLENTKKKMEIYQKENKDVIQKNKLKLTREQEELEEALEVERQESEQRRLFIQKEEELQQILKRKNKQAFLDELESSDLPVALLLAQHKDRSTQLEMQLEKPKSMKPVTFSTGIKMGSLISLAPIQKLEEALYEYQPLQIETCGPQVPEQELLGRLGKVMVEGVTEINS
Protein: Pyrroline-5-carboxylate reductase (P5C reductase) (P5CR) (EC 1.5.1.2) (PCA reductase) (P22008)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Catalyzes the reduction of 1-pyrroline-5-carboxylate (PCA) to L-proline.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01925}.
Interaction partners:
- Bifunctional protein PutA
- Ornithine cyclodeaminase
- 4-hydroxyproline 2-epimerase
- Proline iminopeptidase
- Uncharacterized protein PA0392
- Pyridoxal phosphate homeostasis protein
- Glutamate 5-kinase
- Gamma-glutamyl phosphate reductase
Sequence:
MSTPRIAFIGAGNMAASLIGGLRAQGVPAAQIRASDPGAEQRAKIAGEFAIDVVESNAEAVADADVVVLSVKPQAMKAVCQALAPALKPEQLIVSIAAGIPCASLEAWLGQPRPVVRCMPNTPALLRQGASGLYANAQVSAAQCEQAGQLLSAVGIALWLDDEAQIDAVTAVSGSGPAYFFLLMQAMTDAGEKLGLSRETASRLTLQTALGAAQMALSSEVEPAELRRRVTSPNGTTEAAIKSFQANGFEALVEQALNAASQRSAELAEQLGQ
Protein: Replicase large subunit (EC 2.1.1.-) (EC 2.7.7.-) (EC 2.7.7.48) (EC 3.6.4.13) (183 kDa protein) (RNA-directed RNA polymerase) [Cleaved into: Replicase small subunit (EC 2.1.1.-) (EC 2.7.7.-) (EC 3.6.4.13) (126 kDa protein) (Methyltransferase/RNA helicase) (MT/HEL)] (P18339)
Organism: Tobacco mild green mosaic virus (TMGMV) (TMV strain U2)
Function: Is an RNA-dependent RNA polymerase active in viral RNA replication.
Interaction partners:
Sequence:
MAHIQSIISNALLESVSGKNTLVNDLARRRMYDTAVEEFNARDRRPKVNFSKTISEEQTLLVSNAYPEFQITFYNTQNAVHSLAGGLRALELEYLMLQVPYGSPTYDIGGNFAAHLFKGRDYVHCCMPNLDIRDIMRHEGQKDSIEMYLSRLSRSNKVIPEFQREAFNRYAEAPNEVCCSKTFQDCRIHPPENSGRRYAVALHSLYDIPVHEFGAALISKNIHVCYAASILAEALLLDQTEVTLNEIGATFKREGDDVSFFFADESTLNYSHKYKNILHYVVKSYFPASSRIVYFKEFLVTRVNTWFCKFTKVDTYILYKSVRQVGCDSDQFYEAMEDAFAYKKTLAMFNTERAIFRDTASVNFWFPKMKDMVIVPLFEGSITSKKMTRSEVIVNRDFVYTVLNHIRTYQAKALTYQNVLSFVESIRSRVIINGVTARSEWDVDKAILQPLSMTFFLQTKLAALQDDIVMGKFRCLDKTTSELIWDEVGKFFGNVFPTIKERLVSRKILDVSENALKIKIPDLYVTWKDRFVAEYTKSEELPHLDIKKDLEEAEQMYDALSELSILKGADNFDIAKFKDMCKALDVSPDVAARVIVAVAENRSGLTLTFDKPTEENVAKALKSTASEAVVCLEPTSEEVNVNKFSIAEKGRLPVCAESHGLTNANLEHQELESLNDFHKACVDSVITKQMASVVYTGSLKVQQMKNYVDSLAASLSATVSNLCKSLKDEVGYDSDSREKVGVWDVTLKKWLLKPAAKGHSWGVVLDYKGKMFTALLSYEGDRMVTESDWRRVAVSSDTMVYSDIAKLQNLRKTMRDGEPHEPTAKMVLVDGVPGCGKYKGDFERFDLDEDLILVPGKQAAAMIRRRANSSGLIRATMDNVRTVDSLLMHPKPRSHKRLFIDEGLMLHTGCVNFLVLISGCDIAYIYGDTQQIPFINRVQNFPYPKHFEKLQVDEVEMRRTTLRCPGDVNFFLQSKYEGAVTTTSTVQRSVSSEMIGGKGVLNSVSKPLKGKIVTFTQADKFELEEKGYKNVNTVHEIQGETFEDVSLVRLTATPLTLISKSSPHVLVALTRHTKSFKYYTVVLDPLVQIISDLSSLSSFLLEMYMVEAGSRXQLQMDAVFKGHNLFVATPKSGDFPDLQFYYDVCLPGNSTILNKYDAVTMRLRDNSLNVKDCVLDFSKSIPMPKEVKPCLEPVLRTAAEPPRAAGLLENLVAMIKRNFNAPDLTGTIDIESTASVVVDKFFDSYFIKKEKYTKNIAGVMTKDSMMRWLENRKEVLLDDLANYNFTDLPAIDQYKHMIKAQPKQKLDLSIQNEYPALQTIVYHSKQINGILAGFSELTRLLLEAFDSKKFLFFTRKTPEQIQEFFSDLDSHVPMDVLELDISKYDKSQNEFHCAVEYEIWKRLGLNEFLAEVWKQGHRKTTLKDYIAGIKTCLWYQRKSGDVTTFIGNTVIIAACLGSMLPMEKVIKGAFCGDDSVLYFPKGLDFPDIQSCANLMWNFEAKLYRKRYGYFCGRYIIHHDKGAIVYYDPLKLISKLGAKHIKDYDHLEELRVSLCDVACSLGNWCLGFPQLNAAIKEVHKTAIDGSFAFNCVNKFLCDKFLFRTLFLNGC
Protein: Activator of stress genes 1 (P40467)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Probable transcription factor involved in the stress response.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00227, ECO:0000269|PubMed:14562095}.
Interaction partners:
- Protein GIS4
- Serine/threonine-protein kinase SKS1
Sequence:
MPEQAQQGEQSVKRRRVTRACDECRKKKVKCDGQQPCIHCTVYSYECTYKKPTKRTQNSGNSGVLTLGNVTTGPSSSTVVAAAASNPNKLLSNIKTERAILPGASTIPASNNPSKPRKYKTKSTRLQSKIDRYKQIFDEVFPQLPDIDNLDIPVFLQIFHNFKRDSQSFLDDTVKEYTLIVNDSSSPIQPVLSSNSKNSTPDEFLPNMKSDSNSASSNREQDSVDTYSNIPVGREIKIILPPKAIALQFVKSTWEHCCVLLRFYHRPSFIRQLDELYETDPNNYTSKQMQFLPLCYAAIAVGALFSKSIVSNDSSREKFLQDEGYKYFIAARKLIDITNARDLNSIQAILMLIIFLQCSARLSTCYTYIGVAMRSALRAGFHRKLSPNSGFSPIEIEMRKRLFYTIYKLDVYINAMLGLPRSISPDDFDQTLPLDLSDENITEVAYLPENQHSVLSSTGISNEHTKLFLILNEIISELYPIKKTSNIISHETVTSLELKLRNWLDSLPKELIPNAENIDPEYERANRLLHLSFLHVQIILYRPFIHYLSRNMNAENVDPLCYRRARNSIAVARTVIKLAKEMVSNNLLTGSYWYACYTIFYSVAGLLFYIHEAQLPDKDSAREYYDILKDAETGRSVLIQLKDSSMAASRTYNLLNQIFEKLNSKTIQLTALHSSPSNESAFLVTNNSSALKPHLGDSLQPPVFFSSQDTKNSFSLAKSEESTNDYAMANYLNNTPISENPLNEAQQQDQVSQGTTNMSNERDPNNFLSIDIRLDNNGQSNILDATDDVFIRNDGDIPTNSAFDFSSSKSNASNNSNPDTINNNYNNVSGKNNNNNNITNNSNNNHNNNNNDNNNNNNNNNNNNNNNNNSGNSSNNNNNNNNNKNNNDFGIKIDNNSPSYEGFPQLQIPLSQDNLNIEDKEEMSPNIEIKNEQNMTDSNDILGVFDQLDAQLFGKYLPLNYPSE
Protein: NADH-quinone oxidoreductase subunit G (EC 7.1.1.-) (NADH dehydrogenase I subunit G) (NDH-1 subunit G) (P9WIV9)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient (By similarity).
Interaction partners:
- NADH-quinone oxidoreductase subunit D
- NADH-quinone oxidoreductase subunit F
- NADH-quinone oxidoreductase subunit M
- NADH-quinone oxidoreductase subunit L
- Uncharacterized response regulatory protein Rv3143
- NADH-quinone oxidoreductase subunit A
- NADH-quinone oxidoreductase subunit N
- NADH-quinone oxidoreductase subunit C
- NADH-quinone oxidoreductase subunit J
- NADH-quinone oxidoreductase subunit H
Sequence:
MTQAADTDIRVGQPEMVTLTIDGVEISVPKGTLVIRAAELMGIQIPRFCDHPLLEPVGACRQCLVEVEGQRKPLASCTTVATDDMVVRTQLTSEIADKAQHGVMELLLINHPLDCPMCDKGGECPLQNQAMSNGRTDSRFTEAKRTFAKPINISAQVLLDRERCILCARCTRFSDQIAGDPFIDMQERGALQQVGIYADEPFESYFSGNTVQICPVGALTGTAYRFRARPFDLVSSPSVCEHCASGCAQRTDHRRGKVLRRLAGDDPEVNEEWNCDKGRWAFTYATQPDVITTPLIRDGGDPKGALVPTSWSHAMAVAAQGLAAARGRTGVLVGGRVTWEDAYAYAKFARITLGTNDIDFRARPHSAEEADFLAARIAGRHMAVSYADLESAPVVLLVGFEPEDESPIVFLRLRKAARRHRVPVYTIAPFATGGLHKMSGRLIKTVPGGEPAALDDLATGAVGDLLATPGAVIIVGERLATVPGGLSAAARLADTTGARLAWVPRRAGERGALEAGALPTLLPGGRPLADEVARAQVCAAWHIAELPAAAGRDADGILAAAADETLAALLVGGIEPADFADPDAVLAALDATGFVVSLELRHSTVTERADVVFPVAPTTQKAGAFVNWEGRYRTFEPALRGSTLQAGQSDHRVLDALADDMGVHLGVPTVEAAREELAALGIWDGKHAAGPHIAATGPTQPEAGEAILTGWRMLLDEGRLQDGEPYLAGTARTPVVRLSPDTAAEIGAADGEAVTVSTSRGSITLPCSVTDMPDRVVWLPLNSAGSTVHRQLRVTIGSIVKIGAGS
Protein: Protein RarD (P27844)
Organism: Escherichia coli (strain K12)
Subcellular location: Cell inner membrane; Multi-pass membrane protein.
Interaction partners:
- Uncharacterized protein YigF
- Inner membrane protein YigG
- Probable amino-acid metabolite efflux pump
- UPF0178 protein YaiI
- UPF0324 inner membrane protein YeiH
- Medium/long-chain acyl-CoA thioesterase YigI
Sequence:
MDAKQTRQGVLLALAAYFIWGIAPAYFKLIYYVPADEILTHRVIWSFFFMVVLMSICRQWSYLKTLIQTPQKIFMLAVSAVLIGGNWLLFIWAVNNHHMLEASLGYFINPLVNIVLGMIFLGERFRRMQWLAVILAICGVLVQLWTFGSLPIIALGLAFSFAFYGLVRKKIAVEAQTGMLIETMWLLPVAAIYLFAIADSSTSHMGQNPMSLNLLLIAAGIVTTVPLLCFTAAATRLRLSTLGFFQYIGPTLMFLLAVTFYGEKPGADKMVTFAFIWVALAIFVMDAIYTQRRTSK
Protein: Glycerol-3-phosphate dehydrogenase 1-like protein (GPD1-L) (EC 1.1.1.8) (Q8N335)
Organism: Homo sapiens (Human)
Function: Plays a role in regulating cardiac sodium current; decreased enzymatic activity with resulting increased levels of glycerol 3-phosphate activating the DPD1L-dependent SCN5A phosphorylation pathway, may ultimately lead to decreased sodium current; cardiac sodium current may also be reduced due to alterations of NAD(H) balance induced by DPD1L.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:17967977}. Note=Localized to the region of the plasma membrane.
Interaction partners:
- Sodium channel protein type 5 subunit alpha
- Glycerol-3-phosphate acyltransferase 2, mitochondrial
- Glycerol-3-phosphate acyltransferase 1, mitochondrial
- Dihydroxyacetone phosphate acyltransferase
- Glycerol-3-phosphate acyltransferase 3
- Glycerol-3-phosphate dehydrogenase [NAD
- Glycerol-3-phosphate acyltransferase 4
- Glycerol-3-phosphate dehydrogenase, mitochondrial
- Potassium voltage-gated channel subfamily E member 3
- Manganese-dependent ADP-ribose/CDP-alcohol diphosphatase
Sequence:
MAAAPLKVCIVGSGNWGSAVAKIIGNNVKKLQKFASTVKMWVFEETVNGRKLTDIINNDHENVKYLPGHKLPENVVAMSNLSEAVQDADLLVFVIPHQFIHRICDEITGRVPKKALGITLIKGIDEGPEGLKLISDIIREKMGIDISVLMGANIANEVAAEKFCETTIGSKVMENGLLFKELLQTPNFRITVVDDADTVELCGALKNIVAVGAGFCDGLRCGDNTKAAVIRLGLMEMIAFARIFCKGQVSTATFLESCGVADLITTCYGGRNRRVAEAFARTGKTIEELEKEMLNGQKLQGPQTSAEVYRILKQKGLLDKFPLFTAVYQICYESRPVQEMLSCLQSHPEHT
Protein: Glutathione peroxidase 1, mitochondrial (CrGPx1) (EC 1.11.1.9) (P83564)
Organism: Chlamydomonas reinhardtii (Chlamydomonas smithii)
Function: May constitute a glutathione peroxidase-like protective system against oxidative stresses. Hydrogen peroxide, tert-butyl hydroperoxide and cumene, but not phosphatidylcholine hydroperoxide, can act as acceptors.
Subcellular location: Mitochondrion {ECO:0000305}.
Interaction partners:
Sequence:
MLLTRKNVAVRPARAARRDVRAMSLLGNLFGGGSKPTSSTSNFHQLSALDIDKKNVDFKSLNNRVVLVVNVASKUGLTAANYKEFATLLGKYPATDLTIVAFPCNQFGGQEPGTNAEIKAFASARGFSGAGALLMDKVDVNGANASPVYNFLKVAAGDTSDIGWNFGKFLVRPDGTVFGRYAPTTGPLSLEKYIVELINSR
Protein: Nuclear nucleic acid-binding protein C1D (J3KPZ4)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|RuleBase:RU368003}. Nucleus, nucleolus {ECO:0000256|RuleBase:RU368003}.
Interaction partners:
Sequence:
MPSPSVSTSAASVLEGVCGRARSTYRTPEEGEEQSWSAIMAGEEINEDYPVEIHEYLSAFENSIGAVDEMLKTMMSVSRNELLQKLDPLEQAKVDLVSAYTLNSMFWVYLATQGVNPKEHPVKQELERIRVYMNRVKEITDKKKAGKLDRGAASRFVKNALWEPKSKNASKVANKGKSKS
Protein: Nitric oxide synthase 3 (EC 1.14.13.39) (Constitutive NOS) (cNOS) (EC-NOS) (NOS type III) (NOSIII) (Nitric oxide synthase, endothelial) (Endothelial NOS) (eNOS) (P29474)
Organism: Homo sapiens (Human)
Function: Produces nitric oxide (NO) which is implicated in vascular smooth muscle relaxation through a cGMP-mediated signal transduction pathway. NO mediates vascular endothelial growth factor (VEGF)-induced angiogenesis in coronary vessels and promotes blood clotting through the activation of platelets.
Subcellular location: Cell membrane. Membrane, caveola. Cytoplasm, cytoskeleton. Golgi apparatus. Note=Specifically associates with actin cytoskeleton in the G2 phase of the cell cycle; which is favored by interaction with NOSIP and results in a reduced enzymatic activity.
Interaction partners:
- Calmodulin-like protein 3
- Calmodulin-like protein 6
- Calmodulin-like protein 5
- Calmodulin-1
- Calmodulin-like protein 4
- Caveolin-1
- Heat shock protein HSP 90-alpha
- Heat shock protein HSP 90-beta
- RAC-alpha serine/threonine-protein kinase
- Nitric oxide synthase-interacting protein
Sequence:
MGNLKSVAQEPGPPCGLGLGLGLGLCGKQGPATPAPEPSRAPASLLPPAPEHSPPSSPLTQPPEGPKFPRVKNWEVGSITYDTLSAQAQQDGPCTPRRCLGSLVFPRKLQGRPSPGPPAPEQLLSQARDFINQYYSSIKRSGSQAHEQRLQEVEAEVAATGTYQLRESELVFGAKQAWRNAPRCVGRIQWGKLQVFDARDCRSAQEMFTYICNHIKYATNRGNLRSAITVFPQRCPGRGDFRIWNSQLVRYAGYRQQDGSVRGDPANVEITELCIQHGWTPGNGRFDVLPLLLQAPDDPPELFLLPPELVLEVPLEHPTLEWFAALGLRWYALPAVSNMLLEIGGLEFPAAPFSGWYMSTEIGTRNLCDPHRYNILEDVAVCMDLDTRTTSSLWKDKAAVEINVAVLHSYQLAKVTIVDHHAATASFMKHLENEQKARGGCPADWAWIVPPISGSLTPVFHQEMVNYFLSPAFRYQPDPWKGSAAKGTGITRKKTFKEVANAVKISASLMGTVMAKRVKATILYGSETGRAQSYAQQLGRLFRKAFDPRVLCMDEYDVVSLEHETLVLVVTSTFGNGDPPENGESFAAALMEMSGPYNSSPRPEQHKSYKIRFNSISCSDPLVSSWRRKRKESSNTDSAGALGTLRFCVFGLGSRAYPHFCAFARAVDTRLEELGGERLLQLGQGDELCGQEEAFRGWAQAAFQAACETFCVGEDAKAAARDIFSPKRSWKRQRYRLSAQAEGLQLLPGLIHVHRRKMFQATIRSVENLQSSKSTRATILVRLDTGGQEGLQYQPGDHIGVCPPNRPGLVEALLSRVEDPPAPTEPVAVEQLEKGSPGGPPPGWVRDPRLPPCTLRQALTFFLDITSPPSPQLLRLLSTLAEEPREQQELEALSQDPRRYEEWKWFRCPTLLEVLEQFPSVALPAPLLLTQLPLLQPRYYSVSSAPSTHPGEIHLTVAVLAYRTQDGLGPLHYGVCSTWLSQLKPGDPVPCFIRGAPSFRLPPDPSLPCILVGPGTGIAPFRGFWQERLHDIESKGLQPTPMTLVFGCRCSQLDHLYRDEVQNAQQRGVFGRVLTAFSREPDNPKTYVQDILRTELAAEVHRVLCLERGHMFVCGDVTMATNVLQTVQRILATEGDMELDEAGDVIGVLRDQQRYHEDIFGLTLRTQEVTSRIRTQSFSLQERQLRGAVPWAFDPPGSDTNSP
Protein: DNA helicase (EC 3.6.4.12) (Q9U9L0)
Organism: Trypanosoma brucei
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MADGPTQEQTKKAAFAVAATSKYPNYLADRDLCRRFFEEFRDASGGMKYMDMAARVARRETNVFTVDLDDIQLYGQLYLAQRIQMNVMGYREEVYRVVDEIIPEAYFEEDMIDHLILEAQTAGQHLPPLLTRRYELVVMPLTSFSEPVPLRQLKGGLIGTLVVLRGICIAATAVRPKLSMLVSVCEVCAETTFQQVIGDRLTPLMVCQSQRCRLNNTVGRLLPQYKASKFTKHQELRLQELPQYVPRGAIPRTIRVICEGEQTRIATPGQVVKVVGTYCPDPSTGQGHEAFRASTMVKTLFRALRIELERRSYQEAADDLKIQVDNVKQHPDKEVVIEKLTRSVAPEIWGMEDVKKALLCLLVGGSSIANGIRIRSDTNICLMGDPGVAKSQLLKWIASVAPRSIFTTGKGSSGVGLTAAVTRDTYTGEVMLEGGALVLSDRGICCIDEFDKMDDSDRTALHEVMEQQMVSIAKAGIITSLNARTSILAAANPKYGRWRRNLTPSENVNLPPALLSRFDVLWLLLDESNRERDAELSMHVTYVHLHGVAPGTVSDNGFYGLSSDYFGKDFLQAYVGEAKKIHPIVDSSAAKVISDIYCEMRAQSVRHTNVVTARTLLSIIRLSQACARLRFSDRVVEADVREAGRLLDCSKISLQERVDTGGRRMVTTSDAAIFSTIKELARSRGSIDLAEVRPALMIKGIDESHLQRCLNTYADVGVWEVSGNTVHFSLE