wanglab/gogpt-training-data huggingface dataset:
Protein: Cell division control protein 31 (O74435)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Required for the proper coordination between exit from mitosis and the initiation of septation. Has a role in bipolar spindle formation during spindle pole body (SPB) duplication. Required for the localization of sad1 to the SPB.
Subcellular location: Nucleus {ECO:0000269|PubMed:12857865}. Note=Associates with the half-bridge structure of the SPB.
Interaction partners:
- Protein sfi1
- SAGA complex subunit Sus1
- SAC3 family protein 1
- DNA repair protein rhp41
- SAC3 family protein 2
- Nucleoporin nup124
- PCI domain-containing protein C1105.07c
- Spindle pole body-associated protein sad1
- Protein CSN12 homolog
- UV excision repair protein rhp23
Sequence:
MFANARAKRRSRASSPTPARLGGYAPLRVEITEEQRQDINEAFKLFDSDKDNAIDYHELRAAMRALGFNAEKSEVLKILRDFDKTGKGYLQMEDFVRVMTEKIVERDPLEEIKRAFELFDDDETGKISLRNLRRVAKELNENIDDQELEAMIEEFDLDQDGEINEQEFIAIMMDEA
Protein: Sodium channel protein (A0A590UK43)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU361132}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU361132}.
Interaction partners:
Sequence:
MAARLLAPPGPDSFKPFTPESLANIERRIAESKLKKPPKADGSHREDDEDSKPKPNSDLEAGKSLPFIYGDIPQGLVAVPLEDFDPYYLTQKTFVVLNRGKTLFRFSATPALYILSPFNLIRRIAIKILIHSVFSMIIMCTILTNCVFMTFSNPPDWSKNVEYTFTGIYTFESLVKIIARGFCIDGFTFLRDPWNWLDFSVIMMAYVTEFVDLGNVSALRTFRVLRALKTISVIPGLKTIVGALIQSVKKLSDVMILTVFCLSVFALIGLQLFMGNLRNKCVVWPINFNESYLENGTKGFDWEEYINNKTNFYTVPGMLEPLLCGNSSDAGQCPEGYQCMKAGRNPNYGYTSFDTFSWAFLALFRLMTQDYWENLYQLTLRAAGKTYMIFFVLVIFVGSFYLVNLILAVVAMAYEEQNQATLEEAEQKEAEFKAMLEQLKKQQEEAQAAAMATSAGTVSEDAIEEEGEEGGGSPRSSSEISKLSSKSAKERRNRRKKRKQKELSEGEEKGDPEKVFKSESEDGMRRKAFRLPDNRIGRKFSIMNQSLLSIPGSPFLSRHNSKSSIFSFRGPGRFRDPGSENEFADDEHSTVEESEGRRDSLFIPIRARERRSSYSGYSGYSQGSRSSRIFPSLRRSVKRNSTVDCNGVVSLIGGPGSHIGGRLLPEATTEVEIKKKGPGSLLVSMDQLASYGRKDRINSIMSVVTNTLVEELEESQRKCPPCWYKFANTFLIWECHPYWIKLKEIVNLIVMDPFVDLAITICIVLNTLFMAMEHHPMTPQFEHVLAVGNLVFTGIFTAEMFLKLIAMDPYYYFQEGWNIFDGFIVSLSLMELSLADVEGLSVLRSFRLLRVFKLAKSWPTLNMLIKIIGNSVGALGNLTLVLAIIVFIFAVVGMQLFGKSYKECVCKINQDCELPRWHMHDFFHSFLIVFRVLCGEWIETMWDCMEVAGQAMCLIVFMMVMVIGNLVVLNLFLALLLSSFSADNLAATDDDGEMNNLQISVIRIKKGVAWTKLKVHAFMQAHFKQREADEVKPLDELYEKKANCIANHTGADIHRNGDFQKNGNGTTSGIGSSVEKYIIDEDHMSFINNPNLTVRVPIAVGESDFENLNTEDVSSESDPEGSKDKLDDTSSSEGSTIDIKPEVEEVPVEQPEEYLDPDACFTEGCVQRFKCCQVNIEEGLGKSWWILRKTCFLIVEHNWFETFIIFMILLSSGALAFEDIYIEQRKTIRTILEYADKVFTYIFILEMLLKWTAYGFVKFFTNAWCWLDFLIVAVVVNALVGAIPSIMNVLLVCLIFWLIFSIMGVNLFAGKYHYCFNETSEIRFEIEDVNNKTECEKLMEGNNTEIRWKNVKINFDNVGAGYLALLQVATFKGWMDIMYAAVDSRKPDEQPKYEDNIYMYIYFVIFIIFGSFFTLNLFIGVIIDNFNQQKKKFGGQDIFMTEEQKKYYNAMKKLGSKKPQKPIPRPLNKIQGIVFDFVTQQAFDIVIMMLICLNMVTMMVETDTQSKQMENILYWINLVFVIFFTCECVLKMFALRHYYFTIGWNIFDFVVVILSIVGMFLADIIEKYFVSPTLFRVIRLARIGRILRLIKGAKGIRTLLFALMMSLPALFNIGLLLFLVMFIFSIFGMSNFAYVKHEAGIDDMFNFETFGNSMICLFQITTSAGWDGLLLPILNRPPDCSLDKEHPGSGFKGDCGNPSVGIFFFVSYIIISFLIVVNMYIAIILENFSVATEESADPLSEDDFETFYEIWEKFDPDATQFIEYCKLADFADALEHPLRVPKPNTIELIAMDLPMVSGDRIHCLDILFAFTKRVLGDSGELDILRQQMEERFVASNPSKVSYEPITTTLRRKQEEVSAVVLQRAYRGHLARRGFICKKTTSNKLENGGTHREKKESTPSTASLPSYDSVTKPEKEKQQRAEEGRRERAKRQKEVRESKC
Protein: TNFAIP3-interacting protein 2 (A20-binding inhibitor of NF-kappa-B activation 2) (ABIN-2) (Fetal liver LKB1-interacting protein) (Q8NFZ5)
Organism: Homo sapiens (Human)
Function: Inhibits NF-kappa-B activation by blocking the interaction of RIPK1 with its downstream effector NEMO/IKBKG. Forms a ternary complex with NFKB1 and MAP3K8 but appears to function upstream of MAP3K8 in the TLR4 signaling pathway that regulates MAP3K8 activation. Involved in activation of the MEK/ERK signaling pathway during innate immune response; this function seems to be stimulus- and cell type specific. Required for stability of MAP3K8. Involved in regulation of apoptosis in endothelial cells; promotes TEK agonist-stimulated endothelial survival. May act as transcriptional coactivator when translocated to the nucleus. Enhances CHUK-mediated NF-kappa-B activation involving NF-kappa-B p50-p65 and p50-c-Rel complexes.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12595760}. Nucleus {ECO:0000305}.
Interaction partners:
- Tumor necrosis factor alpha-induced protein 3
- Mitogen-activated protein kinase kinase kinase 8
- Nuclear factor NF-kappa-B p105 subunit
- Tumor necrosis factor receptor superfamily member 1A
- Polyubiquitin-C
- Polyubiquitin-B
- Proto-oncogene c-Rel
- Angiopoietin-1 receptor
- Inhibitor of nuclear factor kappa-B kinase subunit beta
- Tumor necrosis factor
Sequence:
MSRDPGSGGWEEAPRAAAALCTLYHEAGQRLRRLQDQLAARDALIARLRARLAALEGDAAPSLVDALLEQVARFREQLRRQEGGAAEAQMRQEIERLTERLEEKEREMQQLLSQPQHEREKEVVLLRRSMAEGERARAASDVLCRSLANETHQLRRTLTATAHMCQHLAKCLDERQHAQRNVGERSPDQSEHTDGHTSVQSVIEKLQEENRLLKQKVTHVEDLNAKWQRYNASRDEYVRGLHAQLRGLQIPHEPELMRKEISRLNRQLEEKINDCAEVKQELAASRTARDAALERVQMLEQQILAYKDDFMSERADRERAQSRIQELEEKVASLLHQVSWRQDSREPDAGRIHAGSKTAKYLAADALELMVPGGWRPGTGSQQPEPPAEGGHPGAAQRGQGDLQCPHCLQCFSDEQGEELLRHVAECCQ
Protein: Fibroblast growth factor 9 (FGF-9) (Glia-activating factor) (GAF) (HBGF-9) (P54130)
Organism: Mus musculus (Mouse)
Function: Plays an important role in the regulation of embryonic development, cell proliferation, cell differentiation and cell migration. May have a role in glial cell growth and differentiation during development, gliosis during repair and regeneration of brain tissue after damage, differentiation and survival of neuronal cells, and growth stimulation of glial tumors.
Subcellular location: Secreted.
Interaction partners:
- Fibroblast growth factor receptor 1
- Fibroblast growth factor receptor 2
- Fibroblast growth factor receptor 3
- Fibroblast growth factor receptor 4
- Klotho
- Pro-epidermal growth factor
- Vascular endothelial growth factor receptor 2
- Transcription factor SOX-9
- Beta-klotho
- Vascular endothelial growth factor receptor 3
Sequence:
MAPLGEVGSYFGVQDAVPFGNVPVLPVDSPVLLSDHLGQSEAGGLPRGPAVTDLDHLKGILRRRQLYCRTGFHLEIFPNGTIQGTRKDHSRFGILEFISIAVGLVSIRGVDSGLYLGMNEKGELYGSEKLTQECVFREQFEENWYNTYSSNLYKHVDTGRRYYVALNKDGTPREGTRTKRHQKFTHFLPRPVDPDKVPELYKDILSQS
Protein: Epididymis secretory sperm binding protein (GNB2 protein) (Guanine nucleotide binding protein (G protein), beta polypeptide 2, isoform CRA_a) (cDNA FLJ77321, highly similar to Homo sapiens guanine nucleotide binding protein (G protein), beta polypeptide 2 (GNB2), mRNA) (Q6FHM2)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSELEQLRQEAEQLRNQIRDARKACGDSTLTQITAGLDPVGRIQMRTRRTLRGHLAKIYAMHWGTDSRLLVSASQDGKLIIWDSYTTNKVHAIPLRSSWVMTCAYAPSGNFVACGGLDNICSIYSLKTREGNVRVSRELPGHTGYLSCCRFLDDNQIITSSGDTTCALWDIETGQQTVGFAGHSGDVMSLSLAPDGRTFVSGACDASIKLWDVRDSMCRQTFIGHESDINAVAFFPNGYAFTTGSDDATCRLFDLRADQELLMYSHDNIICGITSVAFSRSGRLLLAGYDDFNCNIWDAMKGDRAGVLAGHDNRVSCLGVTDDGMAVATGSWDSFLKIWN
Protein: PLC-like phosphodiesterases superfamily protein (F4JQJ7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Early nodulin-like protein 1
- Germin-like protein subfamily 1 member 13
- Cysteine protease-like protein
- Peroxidase 58
- Lectin-like protein At3g16530
- Metalloendoproteinase 3-MMP
- Peroxidase 54
- Probable LRR receptor-like protein kinase At1g51890
- Endochitinase At2g43580
- Lectin-like protein LEC
Sequence:
MERFNFFNLMIIALCLSSFVHSLEMGETCSSTSECDAGLSCQSCPANGNTGSTCTRIQPLNPTSKVNGLPFNKYSWLTTHNSYAITGANSATGSFLVSPKNQEDSITNQLKNGVRGIMLDTYDFQNDIWLCHSTGGTCFNFTAFQPAINALKEINDFLESNLSEIVTIILEDYVKSQMGLTNVFNASGLSKFLLPISRMPKDGTDWPTVDDMVKQNQRLVVFTSKKDKEASEGLAYQWNYMVENQYGNDGMKDGSCSSRSESSSLDTMSRSLVFQNYFETSPNSTQACADNSSPLIEMMRTCHEAAGKRWPNFIAVDFYQRSDSGGAAEAVDEANGRLTCGCDSLVYCKSNAPFGTCDAPPPKSSPSPVSGGKDTSRKPRNLPAGNADSTAIGLSSLVLISAATLLLW
Protein: Type VI secretion protein (D3GUX1)
Organism: Escherichia coli O44:H18 (strain 042 / EAEC)
Interaction partners:
Sequence:
MASIHSLLSACQTTPRDVAEPAQVRIALWDKWLAPVTPDNPAGDDAGYDDDFQQMREEVNKLSGADAGIVSQLAEKLLTTRTKDIRVATWYIWARLRQDGEKGLADGLELLTGLLQRFGEHLHPQRSRARKAALEWLCSARILDSLSLYPEVVKADTLRIAGALWLAEQTFTDEASAPVLNGLYQALENRLMKAGGVDAVVPQEAAAPAPTVTSGSVMALSAITSGQELLSQARVLAKYLRDQPEGWLAAHRLMKSVRHDTLHQLPPLSADGRTRIAPPGPDRRASLKRLYLQQNWLSLLEQCDDMFARGASHLWLDLQWYIHQALLQTGKENYAAIIQYDLKGLLLRLPGLETLAFNDGMPFADDVTLSWIQQQVMECGERWAEEPSVTITAAPGDNDILSLEPEALQIADNEGTEAALSWLQARPGIQSDRSNWLLRLLMARVAEQTGKNDLALHLLAELDERATRLTLSQWEPELVFEVKARRLKLLRMKSAKTESDRVRLQPDMEHLLAGLIAIDAARAAVLCNSGSS
Protein: SD07723p (Straightjacket, isoform B) (Q7K0H4)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MAWSRLLAWWRLCLGLLSVLVCLAPCVNLQPAENINYNLVHSWADKLGMELFHLGDFITRRKEVQESFKDAKVVSRNGASIVDSMAKEIEMMMDLKVSAVRRIMDTAENTALSHQNDMADKMFSYYSAKEMLEPGDPVPPIPTPAPDMDKDIGEPLIYVQPKVVVLEPRPEFHNTPVNFSVSSVHVPVNVFDRAPDVIKAIQWSENLDQIFRDNYKNDPTLSWQFFGSSTGFMRQFPASKWRKDVPVDLYDCRLRSWYMEAATSPKDIVILMDGSGSMLGQRLDIAKHVVNTILDTLGTNDFVNIFTFDKEVSPVVPCFEDTLIQANLGNIRELKEGIELFRPKSIANYTAALTKAFELLEETKLSSRGAQCNQAIMIIGDGAPENNREVFELHNWRDPPYKPVRVFTYLIGKEVANWDDIRWMACENQGYYVHLSDTAEVREMVLNYIPVMARPLVLGRHDHPVIWSQVYADIEDTKLSDYLWDINQCEYQKADVLEYWQVHDRMLEPSEMHRRKYRRMKETWNQPVDSNVYQFMTTVSMPIYDRRENATRIANILGVAGTDVPINEIKKLLSPFTLGVNGYAFIVTNNGYVLFHPDFRPIFQGYILKPAYNSVDMIEVELLDDDRPARDFNPVLMTIRDSIINQSTGSKWMLVKNHFDEMKRVARVKRQYYWTAIKKTPFTLVISYPEQYGVSHMDIRADQEIHRISIKGTNLRSVFSGKRWKIHPDWLFCKHSNRTFKTPEIELLYFLERMSEPGWRWPGSRSAMPPEHAAAMFCDRQLMQALVFDARVTGWFSNNTSFNSKDDKGNEFKQRFGVTVAFLATHSGLTRWHEFHSNAAEESGVGETFSQNNTRAIDEIWYKRAVDQHFVREESFVYSVPFDAGESNSEILVTASHAVFHNEGGKTAPAAVVGFQFQHSALYKLFHNITGNACAVDDKDCYILDNNGYVIISTRVHETGRFFGEVNGAIMKRLLEENVYRQVTVYDYQAVCFESKNDNNASSMLLSPLFHLLRVGKWLLHTALWYIVQLLQWAPGVSSHYADMYGDSNDTEPPPPEPHPDHHARNGNGHGKKDDDHWLRYLTLHRTRLKPCDMKRDLYTLFNEKDNVVYNMTAHACERPFVVLPIPFSNLILLVIDQLCPRDGSVVLTVNPQPIDYHLSVNDSLACYKQAREFNRMRPHSCISRHANESGIKLCGKACSVYANLGLLLLCHILSRWL
Protein: Riboflavin transporter RibU (Riboflavin ECF transporter S component RibU) (P0CI36)
Organism: Lactococcus lactis subsp. cremoris (strain MG1363)
Function: Mediates riboflavin uptake, may also transport FMN and roseoflavin (By similarity). Probably a riboflavin-binding protein that interacts with the energy-coupling factor (ECF) ABC-transporter complex. Unlike classic ABC transporters this ECF transporter provides the energy necessary to transport a number of different substrates. The substrates themselves are bound by transmembrane, not extracytoplasmic soluble proteins. Uptake of riboflavin into proteosomes containing EcfA1A2T and RibU has been demonstrated. Uptake requires hydrolyzable Mg-ATP.
Subcellular location: Cell membrane {ECO:0000305|PubMed:21135102}; Multi-pass membrane protein {ECO:0000305|PubMed:21135102}.
Interaction partners:
- Thiamine transporter ThiT
- Biotin transporter BioY
- Energy-coupling factor transporter ATP-binding protein EcfA2
- Energy-coupling factor transporter ATP-binding protein EcfA1
- 6,7-dimethyl-8-ribityllumazine synthase
- Energy-coupling factor transporter transmembrane protein EcfT
- Niacin transporter NiaX
- Riboflavin biosynthesis protein RibBA
- Cof-type HAD-IIB family hydrolase
Sequence:
MSKTRRMVLIAMLAALSTILLLPILQFPLLPGIDFMKVELSIIPVLIGVFTLGLGDGFIILFIRSVLWYLLFNQGPSTWIGVPMNFVALGIFMAIVWFFTKKKFSIKNYTVGIVLATIASVLVMMVLNVFYALPLYRLAAGFDVDKIFAGATHLFNMGSLSVTLNPTYLLTVVLPFNALQYIIFALVFGLIVTVFKKNKVVKFYNA
Protein: Histone H1.0 (Histone H1') (Histone H1(0)) (MyD196) [Cleaved into: Histone H1.0, N-terminally processed] (P10922)
Organism: Mus musculus (Mouse)
Function: Histones H1 are necessary for the condensation of nucleosome chains into higher-order structures. The histones H1.0 are found in cells that are in terminal stages of differentiation or that have low rates of cell division.
Subcellular location: Nucleus. Chromosome.
Interaction partners:
- Prothymosin alpha
- Cyclin-dependent kinase 2
- E3 ubiquitin-protein ligase RNF168
- Importin subunit beta-1
- Histone H4
- Cyclin-dependent kinase 1
- Cyclin-dependent kinase 5
- Histone H3.3
- High mobility group protein B1
- Histone H3.2
Sequence:
MTENSTSAPAAKPKRAKASKKSTDHPKYSDMIVAAIQAEKNRAGSSRQSIQKYIKSHYKVGENADSQIKLSIKRLVTTGVLKQTKGVGASGSFRLAKGDEPKRSVAFKKTKKEVKKVATPKKAAKPKKAASKAPSKKPKATPVKKAKKKPAATPKKAKKPKVVKVKPVKASKPKKAKTVKPKAKSSAKRASKKK
Protein: Myeloma-overexpressed gene protein (Oncogene in multiple myeloma) (Q96EZ4)
Organism: Homo sapiens (Human)
Interaction partners:
- Src substrate cortactin
- G1/S-specific cyclin-D1
Sequence:
MALRICVTYTPALPIGLCTRCCLCLEQSPSWCHCLRGVSFLTFHLHQSVPLGDRDSLLMFTRQAGHFVEGSKAGRSRGRLCLSQALRVAVRGAFVSLWFAAGAGDRERNKGDKGAQTGAGLSQEAEDVDVSRARRVTDAPQGTLCGTGNRNSGSQSARVVGVAHLGEAFRVGVEQAISSCPEEVHGRHGLSMEIMWARMDVALRSPGRGLLAGAGALCMTLAESSCPDYERGRRACLTLHRHPTPHCSTWGLPLRVAGSWLTVVTVEALGGWRMGVRRTGQVGPTMHPPPVSGASPLLLHHLLLLLLIIILTC
Protein: Isovaleryl-CoA dehydrogenase, mitochondrial (EC 1.3.8.4) (G5EEH6)
Organism: Caenorhabditis elegans
Subcellular location: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
Interaction partners:
- Probable methylcrotonoyl-CoA carboxylase beta chain, mitochondrial
- Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial
- Methylcrotonoyl-CoA carboxylase subunit alpha
- 2-oxoisovalerate dehydrogenase subunit alpha
- Probable enoyl-CoA hydratase, mitochondrial
- Probable enoyl-CoA hydratase, mitochondrial
- Trifunctional enzyme subunit alpha, mitochondrial
- Trifunctional enzyme subunit alpha, mitochondrial
- 2-oxoisovalerate dehydrogenase subunit beta, mitochondrial
- Enoyl-CoA hydratase
Sequence:
MSALASKLFAKCAAGGRALQSQAVRQFSAYPIDDSMFGLNDEEIALRQSIRQFADKELAPYADKIDKDNGWDQLRPFWKKLGDQGLLGITAPAEYGGSGMNYFSHVIAMEELSRAAGGIALSYGAHSNLCINQIVRNGSEEQRKKYLPKLISGEHMGALAMSEAQAGSDVVSMKLRAEKKGDKYVLNGTKFWITNGPDADVLVVYAKTDPSKHQHGITCFLVEKNTPGFSQSPKLDKLGMRGSNTCELVFDNCEIHESQIMGGKGKGVYVLMTGLDYERLVLSGGPLGLMQAACDIAFDYAHQRTAFGQKIGSFQLLQGKLADMYTTLNASRSYLYMVAKAADKGNVSNKDCAGVILYVAEKCTQVCLDAIQILGGNGYINDYPAGRLLRDAKLYEIGAGTSEVRRLIIGRALNKEYSN
Protein: L-arginine-binding protein (G3XD47)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Binds L-arginine with high affinity. Shows no measurable affinity for L-ornithine.
Subcellular location: Periplasm {ECO:0000305}.
Interaction partners:
- Histidine/lysine/arginine/ornithine transport system permease protein HisM
- Histidine/lysine/arginine/ornithine transport system permease protein HisQ
- Arginine/ornithine transport ATP-binding protein AotP
- Glutamate/aspartate import permease protein GltK
- Putative glutamine transport system permease protein GlnP
- Glutamate/aspartate import permease protein GltK
- Putative glutamine transport system permease protein GlnP
- Arginine ABC transporter permease protein ArtM
- Probable amino acid binding protein
- Glutamate/aspartate import permease protein GltK
Sequence:
MKKLALLGALALSVLSLPTFAADKPVRIGIEAAYPPFSLKTPDGQLAGFDVDIGNALCEEMKVQCKWVEQEFDGLIPALKVRKIDAILSSMTITDERKRSVDFTNKYYNTPARFVMKEGASLNDPKADLKGKKAGVLRGSTADRYASAELTPAGVEVVRYNSQQEANMDLVAGRLDAVVADSVNLEDGFLKTDAGKGYAFVGPQLTDAKYFGEGVGIAVRKGDSELAGKFNAAIDALRANGKYKQIQDKYFSFDVYGSN
Protein: NADH-ubiquinone oxidoreductase chain 4L (EC 7.1.1.2) (NADH dehydrogenase subunit 4L) (P03902)
Organism: Bos taurus (Bovine)
Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:17060615, ECO:0000269|PubMed:18721790, ECO:0000269|PubMed:25209663}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- NADH-ubiquinone oxidoreductase chain 5
- NADH-ubiquinone oxidoreductase chain 4
- NADH dehydrogenase iron-sulfur protein 3, mitochondrial
- NADH-ubiquinone oxidoreductase chain 2
- NADH dehydrogenase iron-sulfur protein 2, mitochondrial
- NADH-ubiquinone oxidoreductase chain 3
- NADH dehydrogenase flavoprotein 1, mitochondrial
- NADH dehydrogenase iron-sulfur protein 8, mitochondrial
- NADH-ubiquinone oxidoreductase chain 1
- NADH-ubiquinone oxidoreductase chain 6
Sequence:
MSMVYMNIMMAFTVSLVGLLMYRSHLMSSLLCLEGMMLSLFVMAALTILNSHFTLASMMPIILLVFAACEAALGLSLLVMVSNTYGTDYVQNLNLLQC
Protein: Large subunit GTPase 1 homolog (EC 3.6.1.-) (Nucleostemin-3) (Q9W590)
Organism: Drosophila melanogaster (Fruit fly)
Function: GTPase required for the nuclear export of the 60S ribosomal subunit. Probably acts by mediating the release of Nmd3 from the 60S ribosomal subunit after export into the cytoplasm. Regulator of body size; acts in serotonergic neurons to regulate insulin signaling and thus exerts global growth control.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:18628395}. Note=Punctate distribution.
Interaction partners:
- 60S ribosomal export protein NMD3
- 60S ribosomal protein L27
- Uncharacterized protein, isoform A
- Eukaryotic translation initiation factor 6
- Nucleolar GTP-binding protein 1
- LD10434p
- Protein SDA1 homolog
- Probable ribosome biogenesis protein RLP24
- Large ribosomal subunit protein eL24
- Large ribosomal subunit protein uL18
Sequence:
MGKKNKGGAPNLGRQLIKDRFGHTQRRKVDNDTMLHTTELQDGYDWGRLNLSSVTEESSFQAFLRTAELAGTEFQAEKLNITFVNPKQRVGLLSKTQEQRMHQKHDEHRDQLKIPRRPKWTKETSAEELVRAENEAFLDWRRDLALLQEDEEILMTPYEKNLEFWRQLWRVVERSDVVVQIVDARNPLLFRSADLERYVKEVEPSKMNMILVNKSDLLTEEQRRHWAEYFDSEGIRTAFYSATLVEEELKREAEECLDSFPEVQQLRRAVEEIKQSLDSVEDALNVIEQKYKTIPETQNDELPRLPGDKNSPRLLSRLELIEFLRNIYTGPRHTEQHVTVGMVGYPNVGKSSTINSLMTVKKVSVSATPGKTKRFQTLFLDKDILLCDCPGLVMPSFVLTKADMLLNGILPIDQMRDHVPAVNLLCERIPRHVLEDKYGIVIAKPLEGEDMERPPHSEELLLAYGYNRGFMTSNGQPDQARSARYVLKDYVNGRLLYAMSPPSVPQTEYHTFPERQRRVIEESQLPGQQQRAMRINKSTSKELDNQFFSDKPTHAHVKGRTNFPNVRLANDGSLVAGNDPAAKPWRHVKKERREKLRKKFSHLDEH
Protein: NAD-dependent protein lipoamidase sirtuin-4, mitochondrial (EC 2.3.1.-) (NAD-dependent ADP-ribosyltransferase sirtuin-4) (EC 2.4.2.-) (NAD-dependent protein biotinylase sirtuin-4) (EC 2.3.1.-) (NAD-dependent protein deacetylase sirtuin-4) (EC 2.3.1.286) (Regulatory protein SIR2 homolog 4) (SIR2-like protein 4) (Q8R216)
Organism: Mus musculus (Mouse)
Function: Acts as NAD-dependent protein lipoamidase, biotinylase, deacetylase and ADP-ribosyl transferase. Catalyzes more efficiently removal of lipoyl- and biotinyl- than acetyl-lysine modifications. Inhibits the pyruvate dehydrogenase complex (PDH) activity via the enzymatic hydrolysis of the lipoamide cofactor from the E2 component, DLAT, in a phosphorylation-independent manner. Catalyzes the transfer of ADP-ribosyl groups onto target proteins, including mitochondrial GLUD1, inhibiting GLUD1 enzyme activity. Acts as a negative regulator of mitochondrial glutamine metabolism by mediating mono ADP-ribosylation of GLUD1: expressed in response to DNA damage and negatively regulates anaplerosis by inhibiting GLUD1, leading to block metabolism of glutamine into tricarboxylic acid cycle and promoting cell cycle arrest. In response to mTORC1 signal, SIRT4 expression is repressed, promoting anaplerosis and cell proliferation. Acts as a tumor suppressor. Also acts as a NAD-dependent protein deacetylase: mediates deacetylation of 'Lys-471' of MLYCD, inhibiting its activity, thereby acting as a regulator of lipid homeostasis. Does not seem to deacetylate PC. Controls fatty acid oxidation by inhibiting PPARA transcriptional activation. Impairs SIRT1-PPARA interaction probably through the regulation of NAD(+) levels. Down-regulates insulin secretion (By similarity).
Subcellular location: Mitochondrion matrix {ECO:0000255|HAMAP-Rule:MF_03161, ECO:0000269|PubMed:16959573, ECO:0000269|PubMed:23746352}.
Interaction partners:
- NAD-dependent protein deacetylase sirtuin-3
- NAD-dependent protein deacylase sirtuin-6
- NAD-dependent protein deacetylase sirtuin-2
- NAD-dependent protein deacylase sirtuin-5, mitochondrial
- NAD-dependent protein deacetylase sirtuin-7
- Nicotinamide phosphoribosyltransferase
- NAD-dependent protein deacetylase sirtuin-1
- NAD kinase
- Glutamine-dependent NAD
- ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 2
Sequence:
MSGLTFRPTKGRWITHLSRPRSCGPSGLFVPPSPPLDPEKIKELQRFISLSKKLLVMTGAGISTESGIPDYRSEKVGLYARTDRRPIQHIDFVRSAPVRQRYWARNFVGWPQFSSHQPNPAHWALSNWERLGKLHWLVTQNVDALHSKAGSQRLTELHGCMHRVLCLNCGEQTARRVLQERFQALNPSWSAEAQGVAPDGDVFLTEEQVRSFQVPCCDRCGGPLKPDVVFFGDTVNPDKVDFVHRRVKEADSLLVVGSSLQVYSGYRFILTAREQKLPIAILNIGPTRSDDLACLKLDSRCGELLPLIDPRRQHSDVQRLEMNFPLSSAAQDP
Protein: Tensin-1 (EC 3.1.3.-) (E9Q0S6)
Organism: Mus musculus (Mouse)
Function: May act as a protein phosphatase and/or a lipid phosphatase (By similarity). Involved in fibrillar adhesion formation (By similarity). Essential for myofibroblast differentiation and myofibroblast-mediated extracellular matrix deposition (By similarity). Enhances RHOA activation in the presence of DLC1. Plays a role in cell polarization and migration (By similarity). May be involved in cartilage development and in linking signal transduction pathways to the cytoskeleton (By similarity).
Subcellular location: Cell surface {ECO:0000250|UniProtKB:Q9HBL0}. Cell junction, focal adhesion {ECO:0000250|UniProtKB:Q9HBL0}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q9HBL0}. Note=Localizes to both focal adhesions and fibrillar adhesions. Localized at the cell periphery preferentially to fibrillar adhesions rather than to focal adhesions. Translocates from the cell edge to the cell center in an ITGB1BP1-dependent manner. {ECO:0000250|UniProtKB:Q9HBL0}.
Interaction partners:
- Integrin beta-1
- Vinculin
- Paxillin
Sequence:
MGCTVSLVCCEALEPLPSCGPQPPGTPPGPARPERCEPGGAAPDPRRRLLLQPEDLEAPKTHHFKVKAFKKVKPCGICRQAITREGCVCKVCSFSCHRKCQAKVAAPCVPPSSHELVPITTETVPKNVVDVGEGDCRVGSSPKNLEEGGSMRVSPSIQPQPQSQPTSLSRNTSVSRAMEDSCELDLVYVTERIIAVSFPSTANEENFRSNLREVAQMLKSKHGGNYLLFNLSEQRPDITKLHAKVLEFGWPDLHTPALEKICSVCKAMDTWLNADPHNVVVLHNKGNRGRIGVVIAAYLHYSNISASADQALDRFAMKRFYEDKIVPIGQPSQRRYVHYFSGLLSGSIKMNNKPLFLHHVIMHGIPNFESKGGCRPFLRIYQAMQPVYTSGIYNIPGDSQASICITIEPGLLLKGDILLKCYHKKFRSPARDVIFRVQFHTCAIHDLGVVFGKEDLDEAFKDDRFPDYGKVEFVFSYGPEKIQGMEHLENGPSVSVDYNTSDPLIRWDSYDNFSGHREDGMEEVVGHTQGPLDGSLYAKVKKKDSLNGSSGPVTTARPALSATPNHVEHTLSVSSDSGNSTASTKTDKTDEPVSGATTAPAALSPQEKKELDRLLSGFGVDREKQGAMYRAQQLRSHPGGGPTVPSPGRHIVPAQVHVNGGALASERETDILDDELPIQDGQSGGSMGTLSSLDGVTNTSESGYPETLSPLTNGLDKPYSTEPVLNGGGYPYEAANRVIPVHSSHSAPIRPSYSAQEGLAGYQREGPHPAWSQQVTSAHCGCDPSGLFRSQSFPDVEPQLPQAPTRGGSSREAVQRGLNSWQQQQPHPPPRQQERSPLQSLARSKPSPQLSAETPVAALPEFPRAASQQEIEQSIETLNMLMLDLEPASAAAPLHKSQSVPGAWPGASPLSSQPLLGSSRQSHPLTQSRSGYIPSGHSLGTPELVSSGRPYSPYDYQLHPAGSNQSFHPKSPASSTFLPSPHSSAGPQEPPASLPGLIAQPQLPPKETTSDPSRTPEEEPLNLEGLVAHRVAGVQARERQPAEPPGPLRRRAASDGQYENQSPEATSPRSPGVRSPVQCVSPELALTIALNPGGRPKEPHLHSYKEAFEEMEGTSPSSPPHSVARSPPGLAKTPLSALGLKPHNPADILLHPTGVARRLIQPEEDEGEEVTKPPEEPRSYVESVARTAVAGPRAQDVEPKSFSAPAAHAYGHETPLRNGTPGGSFVSPSPLSTSSPILSADSTSVGSFPSVVSSDQGPRTPFQPMLDSSIRSGSLGQPSPAALSYQSSSPVPVGGSSYNSPDYSLQPFSSSPESQGQPQYSAASVHMVPGSPQARHRTVGTNTPPSPGFGRRAVNPTMAAPGSPSLSHRQVMGPSGPGFHGNVVSGHPASAATTPGSPSLGRHPVGSHQVPGLHSSVVTTPGSPSLGRHPGAHQGNLASSLHSNAVISPGSPSLGRHLGGSGSVVPGSPSLDRHAAYGGYSTPEDRRPTLSRQSSASGYQAPSTPSFPVSPAYYPGLSSPATSPSPDSAAFRQGSPTPALPEKRRMSVGDRAGSLPNYATINGKVSSSPVANGMASGSSTVSFSHTLPDFSKYSMPDNSPETRAKVKFVQDTSKYWYKPEISREQAIALLKDQEPGAFIIRDSHSFRGAYGLAMKVSSPPPTITQQGKKGDMTHELVRHFLIETGPRGVKLKGCPNEPNFGSLSALVYQHSVIPLALPCKLVIPSRDPTDESKDSSGPANSTTDLLKQGAACNVLFVNSVDMESLTGPQAISKATSETLAADPTPAATIVHFKVSAQGITLTDNQRKLFFRRHYPLNTVTFCDLDPQERKWMKTEGGAPAKLFGFVARKQGSTTDNACHLFAELDPNQPASAIVNFVSKVMLSAGQKR
Protein: Dual specificity protein phosphatase 23 (EC 3.1.3.16) (EC 3.1.3.48) (Low molecular mass dual specificity phosphatase 3) (LDP-3) (VH1-like phosphatase Z) (Q9BVJ7)
Organism: Homo sapiens (Human)
Function: Protein phosphatase that mediates dephosphorylation of proteins phosphorylated on Tyr and Ser/Thr residues. In vitro, it can dephosphorylate p44-ERK1 (MAPK3) but not p54 SAPK-beta (MAPK10) in vitro. Able to enhance activation of JNK and p38 (MAPK14).
Subcellular location: Cytoplasm, cytosol. Nucleus. Note=Mainly cytosolic. Also nuclear.
Interaction partners:
- Dual specificity protein phosphatase 15
Sequence:
MGVQPPNFSWVLPGRLAGLALPRLPAHYQFLLDLGVRHLVSLTERGPPHSDSCPGLTLHRLRIPDFCPPAPDQIDRFVQIVDEANARGEAVGVHCALGFGRTGTMLACYLVKERGLAAGDAIAEIRRLRPGSIETYEQEKAVFQFYQRTK