wanglab/gogpt-training-data huggingface dataset:
Protein: Myotubularin-related protein 9 (Inactive phosphatidylinositol 3-phosphatase 9) (Q96QG7)
Organism: Homo sapiens (Human)
Function: Acts as an adapter for myotubularin-related phosphatases. Increases lipid phosphatase MTMR6 catalytic activity, specifically towards phosphatidylinositol 3,5-bisphosphate and MTMR6 binding affinity for phosphorylated phosphatidylinositols. Positively regulates lipid phosphatase MTMR7 catalytic activity (By similarity). Increases MTMR8 catalytic activity towards phosphatidylinositol 3-phosphate. The formation of the MTMR6-MTMR9 complex, stabilizes both MTMR6 and MTMR9 protein levels. Stabilizes MTMR8 protein levels. Plays a role in the late stages of macropinocytosis possibly by regulating MTMR6-mediated dephosphorylation of phosphatidylinositol 3-phosphate in membrane ruffles. Negatively regulates autophagy, in part via its association with MTMR8. Negatively regulates DNA damage-induced apoptosis, in part via its association with MTMR6. Does not bind mono-, di- and tri-phosphorylated phosphatidylinositols, phosphatidic acid and phosphatidylserine.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16787938, ECO:0000269|PubMed:19038970}. Cell projection, ruffle membrane {ECO:0000250|UniProtKB:Q9Z2D0}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:16787938, ECO:0000269|PubMed:19038970}. Endoplasmic reticulum {ECO:0000269|PubMed:19038970}. Note=Localizes to ruffles during EGF-induced macropinocytosis (By similarity). Colocalizes with MTMR6 to the perinuclear region (PubMed:19038970). Partially localizes to the endoplasmic reticulum (PubMed:19038970). {ECO:0000250|UniProtKB:Q9Z2D0, ECO:0000269|PubMed:19038970}.
Interaction partners:
- Phosphatidylinositol-3,5-bisphosphate 3-phosphatase MTMR6
- Phosphatidylinositol-3-phosphate phosphatase MTMR7
- Phosphatidylinositol-3,5-bisphosphate 3-phosphatase MTMR8
- Protein FAM167A
- EMILIN-1
- Tyrosine-protein kinase Blk
Sequence:
MEFAELIKTPRVDNVVLHRPFYPAVEGTLCLTGHHLILSSRQDNTEELWLLHSNIDAIDKRFVGSLGTIIIKCKDFRIIQLDIPGMEECLNIASSIEALSTLDSITLMYPFFYRPMFEVIEDGWHSFLPEQEFELYSSATSEWRLSYVNKEFAVCPSYPPIVTVPKSIDDEALRKVATFRHGGRFPVLSYYHKKNGMVIMRSGQPLTGTNGRRCKEDEKLINATLRAGKRGYIIDTRSLNVAQQTRAKGGGFEQEAHYPQWRRIHKSIERYHILQESLIKLVEACNDQTHNMDRWLSKLEASNWLTHIKEILTTACLAAQCIDREGASILIHGTEGTDSTLQVTSLAQIILEPRSRTIRGFEALIEREWLQAGHPFQQRCAQSAYCNTKQKWEAPVFLLFLDCVWQILRQFPCSFEFNENFLIMLFEHAYASQFGTFLGNNESERCKLKLQQKTMSLWSWVNQPSELSKFTNPLFEANNLVIWPSVAPQSLPLWEGIFLRWNRSSKYLDEAYEEMVNIIEYNKELQAKVNILRRQLAELETEDGMQESP
Protein: Myosin light chain 5 (Myosin regulatory light chain 5) (Superfast myosin regulatory light chain 2) (MYLC2) (MyLC-2) (Q02045)
Organism: Homo sapiens (Human)
Interaction partners:
- Myosin-6
- Actin, cytoplasmic 1
- Actin, cytoplasmic 2
- Rho-associated protein kinase 2
- Rho-associated protein kinase 1
- Myosin light chain 1/3, skeletal muscle isoform
- Myosin-2
- Myosin light chain 3
- Myosin-13
- Myosin-4
Sequence:
MASRKTKKKEGGALRAQRASSNVFSNFEQTQIQEFKEAFTLMDQNRDGFIDKEDLKDTYASLGKTNVKDDELDAMLKEASGPINFTMFLNLFGEKLSGTDAEETILNAFKMLDPDGKGKINKEYIKRLLMSQADKMTAEEVDQMFQFASIDVAGNLDYKALSYVITHGEEKEE
Protein: Putative formamidase C869.04 (EC 3.5.1.49) (Formamide amidohydrolase) (Q9URY7)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Hydrolyzes formamide with the production of ammonia which can be used as a source of nitrogen for growth. May also act on acetamide, propanamide and butanamide (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Glutamine synthetase
- Probable NAD-specific glutamate dehydrogenase
- NADP-specific glutamate dehydrogenase
- Probable 1-aminocyclopropane-1-carboxylate deaminase
- Malate dehydrogenase, mitochondrial
- NAD-dependent malic enzyme
- NAD-dependent malic enzyme
- Pyruvate carboxylase
- Fumarate hydratase, mitochondrial
- Putative serine acetyltransferase
Sequence:
MAPRTIVKVDLNKPAWEQPNLHNRWHPDIPFAESIDEGETVKIECLDWTGGQIKNDDSAEDIKNVDLTRIHYLSGPFEIKGAEPGDVLVVEIQDVQPLENQPWGYSGIFAKENGGGFLDEHYPKAAKAVFDFEGIFCSSRHIPGVRFPGLIHPGIIGTAPSKEILAEWNRREGALVAENPHSTHVMAQLPNASYAFAGILADEKLSATVASEGARTIPGRPENGGNCDIKNLSRGSKVFLPVHVPGAKLSIGDLHFSQGDGEISFCGAIEMAGSITIKCKILKNGISDLAMKSPMYLPGPVEPHFSPSRYLTFEGFSVDESGKQHYLCTTTAYRQTCLRVIEYFRRFGYNDYQLYLLLSCAPIQGHVAGIVDIPNSCTTIGVPMDIFEFDVSPNGKAKIIDLGSCAFANS
Protein: RNA-binding protein rsd1 (O13845)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
- Pre-mRNA-splicing factor cdc5
- Protein kinase dsk1
- U1 small nuclear ribonucleoprotein 70 kDa homolog
- Ceramide very long chain fatty acid hydroxylase scs7
- Splicing factor U2AF 59 kDa subunit
- U2 snRNP component prp10
Sequence:
MQLDAEALAEAPFRKQEVPQNQENQQKASSSFHESSLTSSTHSHPSNPPPPPTRLHDRSFKPVSKNYESEGRLTPPPVSMGYRYARSSKQSFQREDSGYNDDVVTNSSSHRTPRHHRRSYSPRSDYGSRSPSPHSSVDSHQSRSPVRSRDRDRSSRSSRSRHPSSRSRHRYDDYSRSPPYSSRHSRSRRRYEERSSRSSRAHDYDYEDLRDDDRSHERKRSRSRPRERSSKLSEEERDRRTVFVSQLANRLTSRELYDFFEQAGPVRDAQIVRDKISGRSKGVAYVEFCHEDSVQAAIALSGKRLLGLPVIVQLTEAEKNRKAREAAELARAASAEIPFHRLCVSNIHFNLTDEDVKAIFEPFGDIEFVHLQRDDQNRSKGFGYIQYRNPISARNALEKMNGFDLAGRNMRVCLGNDKFTTETTSSMLKRFDETLARQERSQPSQRNGGSSTYESQDYREAAPLSPTEEESRPITRDELMKKLARSEDISDNSKLVSEPEPPIRSRCALLENMFNPAEETSPNWVQELEQDVKEECDEKYGKVVHIAVVPNELGQIFVKFENADFAEKAITGLHQRWFGGRTIKASILPETDYYFKFPNAKTA
Protein: Protein-glutamine deamidase Cif (EC 3.5.1.44) (Cycle-inhibiting factor homolog) (CHPL) (Q7N439)
Organism: Photorhabdus laumondii subsp. laumondii (strain DSM 15139 / CIP 105565 / TT01) (Photorhabdus luminescens subsp. laumondii)
Function: Protein-glutamine deamidase effector that inhibits the host cell cycle and other key cellular processes such as the actin network and programmed-cell death. Acts by mediating the side chain deamidation of 'Gln-40' of host NEDD8, converting it to glutamate, thereby abolishing the activity of cullin-RING-based E3 ubiquitin-protein ligase complexes (CRL complexes) (By similarity). Inactivation of CRL complexes prevents ubiquitination and subsequent degradation of the cyclin-dependent kinase inhibitors CDKN1A/p21 and CDKN1B/p27, leading to G1 and G2 cell cycle arrests in host cells. Deamidation of 'Gln-40' of host NEDD8 also triggers macrophage-specific programmed cell death (By similarity). Also able to catalyze deamidation of 'Gln-40' of host ubiquitin in vitro; however, NEDD8 constitutes the preferred substrate in vivo (By similarity).
Subcellular location: Secreted {ECO:0000250|UniProtKB:P0DUW5}. Host nucleus {ECO:0000250|UniProtKB:P0DUW5}. Note=Secreted via the type III secretion system (T3SS). {ECO:0000250|UniProtKB:P0DUW5}.
Interaction partners:
Sequence:
MGDDIMPISNLAKESEVRAVKDIPCKNIETDNHLEIGLSSGLSRSKDTSKFKKNSINTIKLIDDIIALHNDPKGNKLLWNDNWQDKIINRDLANIFEKIDESVSELGGLEMYQEMVGVNPYDPTEPVCGLSAQNIFKLMTEGEHAVDPVEMAQTGKIDGNEFAESVDQLSSAKNYVALVNDRRLGHMFLIDIPSNDQETVGYIYQSDLGQGALPPLKIADWLNSRGKDAVSLNKLKKLLSREFNLLSDDEKRALISETLDIHKDVSNVELDRIKRDRGVDIYLTEYDVNNFYENIETLKSKLSNYDKKLSKPK
Protein: DNA damage-inducible transcript 4 protein (HIF-1 responsive protein RTP801) (Protein regulated in development and DNA damage response 1) (REDD-1) (Q9NX09)
Organism: Homo sapiens (Human)
Function: Regulates cell growth, proliferation and survival via inhibition of the activity of the mammalian target of rapamycin complex 1 (mTORC1). Inhibition of mTORC1 is mediated by a pathway that involves DDIT4/REDD1, AKT1, the TSC1-TSC2 complex and the GTPase RHEB. Plays an important role in responses to cellular energy levels and cellular stress, including responses to hypoxia and DNA damage. Regulates p53/TP53-mediated apoptosis in response to DNA damage via its effect on mTORC1 activity. Its role in the response to hypoxia depends on the cell type; it mediates mTORC1 inhibition in fibroblasts and thymocytes, but not in hepatocytes (By similarity). Required for mTORC1-mediated defense against viral protein synthesis and virus replication (By similarity). Inhibits neuronal differentiation and neurite outgrowth mediated by NGF via its effect on mTORC1 activity. Required for normal neuron migration during embryonic brain development. Plays a role in neuronal cell death.
Subcellular location: Mitochondrion {ECO:0000250}. Cytoplasm, cytosol {ECO:0000269|PubMed:12453409}.
Interaction partners:
- Thioredoxin-interacting protein
- Tuberin
- Hamartin
- E3 ubiquitin-protein ligase HUWE1
- TBC1 domain family member 7
- Cellular tumor antigen p53
- Tumor protein 63
- Regulatory-associated protein of mTOR
- Serine/threonine-protein kinase mTOR
- 14-3-3 protein beta/alpha
Sequence:
MPSLWDRFSSSSTSSSPSSLPRTPTPDRPPRSAWGSATREEGFDRSTSLESSDCESLDSSNSGFGPEEDTAYLDGVSLPDFELLSDPEDEHLCANLMQLLQESLAQARLGSRRPARLLMPSQLVSQVGKELLRLAYSEPCGLRGALLDVCVEQGKSCHSVGQLALDPSLVPTFQLTLVLRLDSRLWPKIQGLFSSANSPFLPGFSQSLTLSTGFRVIKKKLYSSEQLLIEEC
Protein: Arginase (EC 3.5.3.1) (P37818)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
- Ornithine aminotransferase car2
- Ornithine decarboxylase
- Ornithine carbamoyltransferase, mitochondrial
- Arginase
- Arginine biosynthesis bifunctional protein ArgJ
- Peptidase M20 domain-containing protein C757.05c
- Urease
- Spermidine synthase
- Argininosuccinate lyase
- Probable argininosuccinate lyase
Sequence:
MSPHKIPEVHRHIMSSRYMEGNAVSIINMPFSGGQPKDGAELAPEMIEAAGLPEDLERLGYSVNVVQNPKFKSRPLKEGPNQALMKNPLYVSNVTRQVRNIVQQELEKQRIAVNIGGDHSLAIGTVEGVQAVYDDACVLWIDAHADINTPDSSPSKNLHGCPLSFSLGYAEPLPEEFAWTRRVIEERRLAFIGLRDLDPMERAFLRERSITAYTMHDVDKYGIARVVEMALEHINPGRRRPIHLSFDVDACDPIVAPATGTRVPGGLTFREAMYICESVAETGSLVAVDVMEVNPLLGNKEEAKTTVDLARSIVRTCLGQTLL
Protein: Deoxyribodipyrimidine photolyase (Q9HVD2)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- DUF1722 domain-containing protein
- Probable transcriptional regulator
Sequence:
MNGLPMNLIWFRCDLRTTDNSALLAAADGRPCLALYLLSPAQWREHDDAPCKVDFWLRNLGELQRQLAALNIPLLVRDCGHWRQAPEVIGRLCRELGVGAVHVNQEYGVNEERRDQAVGQRLREQGVAFHSHLDQLFFAPGSVLTRTGGYFQVFSQFRKVCHERLYQALPGVRPRPQPQPPHALASDPLPDAVPAFPRPADSLRRLWPAGEEVAQERLRDFADQHLADYHERRDFPALPGTSQLSPYLAAGVLSPRQCLDAALVANRGEFSGGQQGAATWINELLWREFYKHILVGYPRVSRHRPFREETEALRWRQAPAELEAWQQGRTGIPIIDAAMRQLLATGWMHNRLRMVVAMFLSKNLLIDWREGERWFMRHLIDGDLAANNGGWQWSASTGTDAVPYFRLFNPLSQSERFDPRGEFIRHWLPELAGLERKAIHDPSSLGLFAGVDYPRPMVDLKASRERALAAFRNLPPRDGRA
Protein: Renalase (EC 1.6.3.5) (Monoamine oxidase-C) (MAO-C) (alpha-NAD(P)H oxidase/anomerase) (Q5U2W9)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the oxidation of the less abundant 1,2-dihydro-beta-NAD(P) and 1,6-dihydro-beta-NAD(P) to form beta-NAD(P)(+) (By similarity). The enzyme hormone is secreted by the kidney, and circulates in blood and modulates cardiac function and systemic blood pressure. Lowers blood pressure in vivo by decreasing cardiac contractility and heart rate and preventing a compensatory increase in peripheral vascular tone, suggesting a causal link to the increased plasma catecholamine and heightened cardiovascular risk. High concentrations of catecholamines activate plasma renalase and promotes its secretion and synthesis.
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
- Amine oxidase [flavin-containing] B
- Amine oxidase [flavin-containing] A
Sequence:
MFRVLVVGAGLTGSLCAALLRKEITAPLYLALWDKAGDIGGRMTTANSPHNPRCTADLGAQYITCTPHYAKKHQNFYEELLAHGILEPLTSPIKGMEVKEGESNFVAPHGVSSIIKYYLKESGAEVFLRQCVTQINLRDNKWEVSEDTGSTQQFDLVILTMPAPQILGLQGDIVNLISERQRQQLASVSYSSRYALGLFYEAGMKIDVPWAGQYITSNPCIRFISIDSKKRNTESSECGPLLVVHTTVPFGVTHLEHSEEDVQELITQQLETILPGLPPPVATKCWKWRYSQVTNSAANSPGQMTLHLNPFLIYI
Protein: Putative endopeptidase RzpR (EC 3.4.-.-) (Putative Rz endopeptidase from lambdoid prophage Rac) (P77551)
Organism: Escherichia coli (strain K12)
Interaction partners:
Sequence:
MRQRDVAALDAKYTKELADAKAENDALRDDVAAGRRRLHIKAVCQSVREATTASGVDNAASPRLADTAERDYFTLRERLVMMQAQLEGAQQYITEQCLK
Protein: Uncharacterized protein (Q383N0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MFSESLYSFHTVSADKNQSNNQKGLLEDEPCQYSNGNNEPGSKAKGNRDHELVGRWGSPRHGGGVGVRISTSVSGKFDKRCPKPSEGYVPPHYVGLPKYWLPNETFHPEINPRSQRITKWENYVGNSERYHAICELVKELWLANAPVNGNEMGIDGVNGALRQLGIEVWSPLAENFFSELSLNETNGQRLVGYSAFKRVFVRELQALLTPSSGTNRLDGEGVPRGDTCGVRLCDPNTICSSIQTLRRHQSTQGASSKNTVSSAAASSSFRRTAAGEPSVGWPGISDICSALSGHDLLGVTAADVYLSPDSRRRSSILGSSSTGTDALQRVMGRGNQGLYPLPIGANGKTLDGVSVVSRMSIANSCEGDSCTPVARSRRSSSHRSALAVVTSPNKCEGRKLRRADEGSPEAAGAQRRGRSTTKTKGGKQKTRQKSRGSSATPRRPSRKSSSKRRNRSGSKRRNRSGSKRRNRSSSSRGRLPQECEGRDDSSTSLSSVRIVKNPTGTQRDGSVVEDESHYGPCDAAGRGSYRSRVMTLHRWRRTSPPVLCVDVRMPDDKRGTFDVYRGDTVEGLVGDFASAYNLSDRLSKRLERLLARKLEYYKWKL
Protein: FI01015p (Klumpfuss, isoform A) (Klumpfuss, isoform C) (Klumpfuss, isoform D) (Q9VTD3)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MTMAEGTDPMGHGHHTNPHNPPQQPPQHHPHHLPLPHPPPAPPPQLLNFNHHQQQYLPHMYPAAAAAAQSHSHYGGLQYPHPHALQHQHHPHQHQHHLPLALSLHQQAAAAAAVAAAVATNHSNNNNQASVANNNIVVPWKQRKRKRLSAVLDKLHHNNNNNNNNNNETHSNGMACKAEPMEMKGDLAEDAEQDEDHDGSVPDEEDDSVDQDGDAGKYIKSEQPVSEDEENEQEMDQDIEDISGEDLELSHSDDNDQDDSPRISMSPLQLQAAQSNLPQDQNQPMNKENPLHVDIKTEIPSPYDRYFPIPSPLFGYYLHTKYLNEVFRRRHDLYPSPLQHTPSSIASETETSPNAQERKSSSNHVLPHALLANNSPPPSLPSPPRSESSVTNNVATTTTSSTTKKRSSPKPKGKKGEKKPMPPPQERPLDLCMRNEVEPKKYKKSGSKSSLESRSAGMMPPPPALSAASSLESMSALSPASSSHSGHMPITSAATPNHQPPPNSPYANAMNAAHAAAAAAAAAMIKMEMPLHPLHHQQMHHSQVPTTTVGVPVIKGDVASPTTKETVAWRYNLDVSPVVEEMPPGSDVAYVCPTCGQMFSLHDRLAKHMASRHKSRNPANDIAKAYSCDVCRRSFARSDMLTRHMRLHTGVKPYTCKVCGQVFSRSDHLSTHQRTHTGEKPYKCPQCPYAACRRDMITRHMRTHTRYDSRGGSREGREGREGREGKESRDSRRSNERIEEPNSPGSHSLLDMKMNMNMGMGMGLNMGLPMNPMSLLQEELLQKSQPGLTLGGPMPLVVKTESA
Protein: Glutathione S-transferase Mu 2 (EC 2.5.1.18) (GST 4-4) (GSTM2-2) (Glutathione S-transferase Yb-2) (GST Yb2) (P08010)
Organism: Rattus norvegicus (Rat)
Function: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Participates in the formation of novel hepoxilin regioisomers.
Subcellular location: Cytoplasm.
Interaction partners:
Sequence:
MPMTLGYWDIRGLAHAIRLFLEYTDTSYEDKKYSMGDAPDYDRSQWLSEKFKLGLDFPNLPYLIDGSHKITQSNAILRYLGRKHNLCGETEEERIRVDVLENQAMDTRLQLAMVCYSPDFERKKPEYLEGLPEKMKLYSEFLGKQPWFAGNKITYVDFLVYDVLDQHRIFEPKCLDAFPNLKDFVARFEGLKKISDYMKSGRFLSKPIFAKMAFWNPK
Protein: Calcium-binding and coiled-coil domain-containing protein 2 (Nuclear domain 10 protein NDP52) (D6REB0)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}. Cytoplasm, perinuclear region {ECO:0000256|ARBA:ARBA00004556}. Cytoplasmic vesicle, autophagosome membrane {ECO:0000256|ARBA:ARBA00037854}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00037854}.
Interaction partners:
Sequence:
MWVTLPIDLNNKSAKQQEVQFKAYYLPKDDEYYQFCYVDEDGVVRGASIPFQFRPENEEDILVVTTQGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKDYWETELLQLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMKKQQELMDENFDLSKRLSENEIICNALQRQKERL
Protein: Kinesin-like protein KIF13B (Kinesin-like protein GAKIN) (Q9NQT8)
Organism: Homo sapiens (Human)
Function: Involved in reorganization of the cortical cytoskeleton. Regulates axon formation by promoting the formation of extra axons. May be functionally important for the intracellular trafficking of MAGUKs and associated protein complexes.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:20194617}. Cell projection, axon {ECO:0000269|PubMed:20194617}. Note=accumulates at the distal part of the microtubules in the tips of axons, but not of dendrites.
Interaction partners:
- Arf-GAP with dual PH domain-containing protein 1
- Disks large homolog 4
- Guanylate kinase
- Kinesin-like protein KIF1C
- 55 kDa erythrocyte membrane protein
- Disks large homolog 1
- Kinesin-like protein KIF1B
- Kinesin-like protein KIF23
- 14-3-3 protein beta/alpha
Sequence:
MGDSKVKVAVRIRPMNRRETDLHTKCVVDVDANKVILNPVNTNLSKGDARGQPKVFAYDHCFWSMDESVKEKYAGQDIVFKCLGENILQNAFDGYNACIFAYGQTGSGKSYTMMGTADQPGLIPRLCSGLFERTQKEENEEQSFKVEVSYMEIYNEKVRDLLDPKGSRQTLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFKITLTHTLYDVKSGTSGEKVGKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISALADQSAGKNKNKFVPYRDSVLTWLLKDSLGGNSKTAMVATVSPAADNYDETLSTLRYADRAKHIVNHAVVNEDPNARIIRDLREEVEKLREQLTKAEAMKSPELKDRLEESEKLIQEMTVTWEEKLRKTEEIAQERQKQLESLGISLQSSGIKVGDDKCFLVNLNADPALNELLVYYLKEHTLIGSANSQDIQLCGMGILPEHCIIDITSEGQVMLTPQKNTRTFVNGSSVSSPIQLHHGDRILWGNNHFFRLNLPKKKKKAEREDEDQDPSMKNENSSEQLDVDGDSSSEVSSEVNFNYEYAQMEVTMKALGSNDPMQSILNSLEQQHEEEKRSALERQRLMYEHELEQLRRRLSPEKQNCRSMDRFSFHSPSAQQRLRQWAEEREATLNNSLMRLREQIVKANLLVREANYIAEELDKRTEYKVTLQIPASSLDANRKRGSLLSEPAIQVRRKGKGKQIWSLEKLDNRLLDMRDLYQEWKECEEDNPVIRSYFKRADPFYDEQENHSLIGVANVFLESLFYDVKLQYAVPIINQKGEVAGRLHVEVMRLSGDVGERIAGGDEVAEVSFEKETQENKLVCMVKILQATGLPQHLSHFVFCKYSFWDQQEPVIVAPEVDTSSSSVSKEPHCMVVFDHCNEFSVNITEDFIEHLSEGALAIEVYGHKINDPRKNPALWDLGIIQAKTRSLRDRWSEVTRKLEFWVQILEQNENGEYCPVEVISAKDVPTGGIFQLRQGQSRRVQVEVKSVQESGTLPLMEECILSVGIGCVKVRPLRAPRTHETFHEEEEDMDSYQDRDLERLRRKWLNALTKRQEYLDQQLQKLVSKRDKTEDDADREAQLLEMRLTLTEERNAVMVPSAGSGIPGAPAEWTPVPGMETHIPVIFLDLNADDFSSQDNLDDPEAGGWDATLTGEEEEEFFELQIVKQHDGEVKAEASWDSAVHGCPQLSRGTPVDERLFLIVRVTVQLSHPADMQLVLRKRICVNVHGRQGFAQSLLKKMSHRSSIPGCGVTFEIVSNIPEDAQGVEEREALARMAANVENPASADSEAYIEKYLRSVLAVENLLTLDRLRQEVAVKEQLTGKGKLSRRSISSPNVNRLSGSRQDLIPSYSLGSNKGRWESQQDVSQTTVSRGIAPAPALSVSPQNNHSPDPGLSNLAASYLNPVKSFVPQMPKLLKSLFPVRDEKRGKRPSPLAHQPVPRIMVQSASPDIRVTRMEEAQPEMGPDVLVQTMGAPALKICDKPAKVPSPPPVIAVTAVTPAPEAQDGPPSPLSEASSGYFSHSVSTATLSDALGPGLDAAAPPGSMPTAPEAEPEAPISHPPPPTAVPAEEPPGPQQLVSPGRERPDLEAPAPGSPFRVRRVRASELRSFSRMLAGDPGCSPGAEGNAPAPGAGGQALASDSEEADEVPEWLREGEFVTVGAHKTGVVRYVGPADFQEGTWVGVELDLPSGKNDGSIGGKQYFRCNPGYGLLVRPSRVRRATGPVRRRSTGLRLGAPEARRSATLSGSATNLASLTAALAKADRSHKNPENRKSWAS
Protein: ATP synthase subunit a, chloroplastic (ATP synthase F0 sector subunit a) (F-ATPase subunit IV) (P56758)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000255|HAMAP-Rule:MF_01393}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01393}.
Interaction partners:
- ATP synthase subunit c, chloroplastic
- ATP synthase subunit b, chloroplastic
- ATP synthase subunit alpha, chloroplastic
- ATP synthase subunit beta, chloroplastic
- ATP synthase subunit alpha
- ATP synthase epsilon chain, chloroplastic
- ATP synthase subunit alpha
- ATP synthase subunit 9
- ATP synthase subunit d, mitochondrial
- ATP synthase subunit delta, chloroplastic
Sequence:
MNVLSCSINTLIKEGLYEISGVEVGQHFYWQIGGFQVHAQVLITSWVVIAILLGSAVLAIRNPQTIPTDGQNFFEFVLEFIRDVSKTQIGEEYGPWVPFIGTLFLFIFVSNWSGALLPWKIIQLPQGELAAPTNDINTTVALALLTSVAYFYAGLSKKGLGYFSKYIQPTPILLPINILEDFTKPLSLSFRLFGNILADELVVVVLVSLVPLVVPIPVMFLGLFTSGIQALIFATLAAAYIGESMEGHH
Protein: Cytochrome P450 2D10 (EC 1.14.14.1) (CYPIID10) (Cytochrome P450-CMF1B) (Cytochrome P450-DB5) (Debrisoquine 4-hydroxylase) (P12939)
Organism: Rattus norvegicus (Rat)
Function: Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics.
Subcellular location: Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein.
Interaction partners:
- Cytochrome P450 7A1
- NADPH-dependent 3-keto-steroid reductase Hsd3b5
- 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 4
- Steroid 17-alpha-hydroxylase/17,20 lyase
Sequence:
MELLNGTGLWPMAIFTVIFILLVDLMHRHQRWTSRYPPGPVPWPVLGNLLQVDPSNMPYSMYKLQHRYGDVFSLQMGWKPMVIVNRLKAVQEVLVTHGEDTADRPPVPIFKCLGVKPRSQGVVFASYGPEWREQRRFSVSTLRTFGMGKKSLEEWVTKEAGHLCDAFTAQNGRSINPKAMLNKALCNVIASLIFARRFEYEDPYLIRMLTLVEESLIEVSGFIPEVLNTFPALLRIPGLADKVFQGQKTFMAFLDNLLAENRTTWDPAQPPRNLTDAFLAEVEKAKGNPESSFNDENLRMVVVDLFTAGMVTTATTLTWALLLMILYPDVQRRVQQEIDEVIGQVRCPEMTDQAHMPYTNAVIHEVQRFGDIAPLNLPRITSCDIEVQDFVIPKGTTLIINLSSVLKDETVWEKPLRFHPEHFLDAQGNFVKHEAFMPFSAGRRACLGEPLARMELFLFFTCLLQHFSFSVPAGQPRPSTLGNFAISVAPLPYQLCAAVREQGH
Protein: NAP1-binding protein 2 (Q12163)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Negatively regulates the high-osmolarity glycerol (HOG) pathway through its negative regulation of the HOG1 kinase activity. Mediates the binding between the PTC1 phosphatase and the PBS2 MAP/ERK kinase (MEK). With PTC1, regulates endoplasmic reticulum inheritance through the cell wall integrity (CWI) MAPK pathway by modulating the MAPK, SLT2.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14573466}.
Interaction partners:
- Serine/threonine-protein kinase STE20
- Protein phosphatase 2C homolog 1
- MAP kinase kinase PBS2
- Serine/threonine-protein kinase CLA4
- Serine/threonine-protein kinase BCK1/SLK1/SSP31
- Nucleosome assembly protein
- Protein phosphatase 2C homolog 2
- Mitogen-activated protein kinase HOG1
- Rho-type GTPase-activating protein 1
- Tyrosine-protein phosphatase 2
Sequence:
MATMETTTQKDTNILKSGLKKTIGVLNEAVLQNGREVEAVQAGNSDTMEDTETTTIGYISIKDYAYADSNPLHYGYFDGDNEEDEMVSDSSNGEDTYNKRQSITLPDDYIVNQRAVALYDFEPENDNELRLAEGDIVFISYKHGQGWLVAENESGSKTGLVPEEFVSYIQPEDGENEVENKARPFYLTHLITQSVSPKNNIDNTNEDEYDDNDEWEDIDDVAEVEADMKTKLDISD
Protein: Leucine-rich repeat and calponin homology domain-containing protein (dLRCH) (Q960C5)
Organism: Drosophila melanogaster (Fruit fly)
Function: May play a role in the stabilization of the actin-rich cell cortex during cell division.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:20805893}. Cytoplasm, cell cortex {ECO:0000269|PubMed:20805893}. Cleavage furrow {ECO:0000269|PubMed:20805893}. Note=Associated with the actin network at the onset of mitosis (PubMed:20805893). Associated with spindle microtubules in metaphase (PubMed:20805893). {ECO:0000269|PubMed:20805893}.
Interaction partners:
- Uncharacterized protein
- Uncharacterized protein
- Serine/threonine-protein kinase ATM
Sequence:
MAATVYQRLHSVAVGVGSAAGSAIGSGSASLPGSGTGSGSGIGHAGNTSSSTSSALLSHSQLTRSLERILEEAHFSGELILTNRKLKDFPRTGTKYSLTDTVIADLSRNRFAELPEEVTTFAFLETLLLYHNTIRSIPESVKQLSSLTYLDLRSNQLSSLPREICFLPLQVLLVSNNRLTSLPDELGRLDQTLTDLDASYNQLANLPARLGELRSLRSLSLRSNHLLYLPRELTCLSLISLDVSNNKIASLPLEIRHMSTLVELQLENNPLTSPPASLCMRGLVHVFKFLETQATKDEKGSRSGGNYDGYTTLRRAPRHNSSGNVLEASTTGSTNNQRRHQVDSGYNTSDGLDKRWSHDAPTKSKTDSPLHCVSNSTAATLPRTLPSAVHSQADLMDASLTSSTSTIVDESLTLSPTASPCKLSYAHSNSSSNGSSPDQDDDIMLDHQERTVHHANGRSGKGLGNIQTYKEYKEALKQQRNQEISVYKQKHPNANHSPNDDEDLSPSPPSISNGSSSNTLPKSIMKQNSNQIGHNGNGNGSANGNGVDDVVIPKKPIQKVIPSRITEIKPASTSDIRSANSSDCLGYVKPQSPMKNGTSKFNTSNGGGVQTTVGIVSSTTIKSPVSSTTKLGTVKTHRSVTWNHDIPAEKLSFTMRREFDRQREETELMSQLRTIIETRLKMTLPVDIASALTDGVILCHLANYVRPRSVASIHVPSPGVNKLTMARCRRNVDNFLEACRRIGVDENLICCAADVLEGKGAVQVAITVGELFRLHGNGGCGSGNSSGAATPTKSPTRTTRATMSPTPLA
Protein: ubiquitinyl hydrolase 1 (EC 3.4.19.12) (Q96B65)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MTVEQNVLQQSAAQKHQQTFLNQLREITGINDTQILQQALKDSNGNLELAVAFLTAKNAKTPQQEETTYYQTALPGNDRYISVGSQADTNVIDLTGDDKDDLQRAIALSLAESNRAFRETGITDEEQAISRVLEASIAENKACLKRTPTEVWRDSRNPYDRKRQDKAPVGLKNVGNTCWFSAVIQSLFNLLEFRRLVLNYKPPSNAQDLPRNQKEHRNLPFMRELRYLFALLVGTKRKYVDPSRAVEILKDAFKSNDSQQEWHQDYRKFRETTMYLIIGLENFQRESYIDSLLFLICAYQNNKELLSKGLYRGHDEELISHYRRECLLKLNEQAAELFESGEDREVNNGLIIMNEFIVPFLPLLLVDEMEEKDILAVEDMRNRWCSYLGQEMEPHLQEKLTDFLPKLLDCSMEIKSFHEPPKLPSYSTHELCERFARIMLSLSRTPADGR