wanglab/gogpt-training-data huggingface dataset:
Protein: Luminescence regulatory protein LuxO (P0C5S5)
Organism: Vibrio harveyi (Beneckea harveyi)
Function: Acts negatively to control the expression of luminescence. At low cell density, LuxO is phosphorylated, and together with sigma-54, causes repression of the luxCDABEGH operon. This repression could be indirect, LuxO could activate a negative regulator of luminescence. At high cell density, LuxO is dephosphorylated and inactive, therefore the luxCDABEGH operon is not repressed and light is emitted. LuxO and sigma-54 have also a role in activating the production of siderophore and in regulating the rugose colony morphology phenotype (By similarity).
Interaction partners:
- Phosphorelay protein LuxU
- RNA polymerase sigma-54 factor
- Regulatory protein luxO
- Autoinducer 1 sensor kinase/phosphatase LuxN
- Autoinducer 2 sensor kinase/phosphatase LuxQ
- HTH-type transcriptional regulator LuxR
- Autoinducer 2-binding periplasmic protein LuxP
- RNA-binding protein Hfq
- S-ribosylhomocysteine lyase
- CAI-1 autoinducer synthase
Sequence:
MVEDTASVAALYRSYLTPLGIDINIVGTGRDAIESLNHRIPDLILLDLRLPDMTGMDVLHAVKKSHPDVPIIFMTAHGSIDTAVEAMRHGSQDFLIKPCEADRLRVTVNNAIRKATKLKNEADNPGNQNYQGFIGSSQTMQQVYRTIDSAASSKASIFITGESGTGKEVCAEAIHAASKRGDKPFIAINCAAIPKDLIESELFGHVKGAFTGAANDRQGAAELADGGTLFLDELCEMDLDLQTKLLRFIQTGTFQKVGSSKMKSVDVRFVCATNRDPWKEVQEGRFREDLYYRLYVIPLHLPPLRERGKDVIEIAYSLLGYMSHEEGKSFVRFAQDVIERFNSYEWPGNVRQLQNVLRNIVVLNNGKEITLDMLPPPLNQPVVRQSVAKFIEPDIMTVSDIMPLWMTEKMAIEQAIQACEGNIPRAAGYLDVSPSTIYRKLQAWNSKDEKQNV
Protein: 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase (EC 2.7.7.60) (4-diphosphocytidyl-2C-methyl-D-erythritol synthase) (CDP-ME synthase) (MEP cytidylyltransferase) (MCT) (Q46893)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP).
Interaction partners:
- 4-diphosphocytidyl-2-C-methyl-D-erythritol kinase
- 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase
- 1-deoxy-D-xylulose 5-phosphate reductoisomerase
- 1-deoxy-D-xylulose-5-phosphate synthase
- 4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase
- 4-hydroxy-3-methylbut-2-enyl diphosphate reductase
- Farnesyl diphosphate synthase
- Isopentenyl-diphosphate Delta-isomerase
- tRNA pseudouridine synthase D
- 5'/3'-nucleotidase SurE
Sequence:
MATTHLDVCAVVPAAGFGRRMQTECPKQYLSIGNQTILEHSVHALLAHPRVKRVVIAISPGDSRFAQLPLANHPQITVVDGGDERADSVLAGLKAAGDAQWVLVHDAARPCLHQDDLARLLALSETSRTGGILAAPVRDTMKRAEPGKNAIAHTVDRNGLWHALTPQFFPRELLHDCLTRALNEGATITDEASALEYCGFHPQLVEGRADNIKVTRPEDLALAEFYLTRTIHQENT
Protein: Neurexophilin-1 (Q61200)
Organism: Mus musculus (Mouse)
Function: May be signaling molecules that resemble neuropeptides. Ligand for alpha-neurexins.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Neurexin-1
Sequence:
MQAACWYVLLLLQPTVYLVTCANLTNGGKSELLKSGSSKSTLKHIWTESSKDLSISRLLSQTFRGKENDTDLDLRYDTPEPYSEQDLWDWLRNSTDLQEPRPRAKRRPIVKTGKFKKMFGWGDFHSNIKTVKLNLLITGKIVDHGNGTFSVYFRHNSTGQGNVSVSLVPPTKIVEFDLAQQTVIDAKDSKSFNCRIEYEKVDKATKNTLCNYDPSKTCYQEQTQSHVSWLCSKPFKVICIYISFYSTDYKLVQKVCPDYNYHSDTPYFPSG
Protein: DnaJ homolog subfamily C member 27 (Rab and DnaJ domain-containing protein) (Q9NZQ0)
Organism: Homo sapiens (Human)
Function: GTPase which can activate the MEK/ERK pathway and induce cell transformation when overexpressed. May act as a nuclear scaffold for MAPK1, probably by association with MAPK1 nuclear export signal leading to enhanced ERK1/ERK2 signaling.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q8CFP6}.
Interaction partners:
- Adenylate cyclase type 3
- Adenylate cyclase type 8
- Protein FAM184A
Sequence:
MEANMPKRKEPGRSLRIKVISMGNAEVGKSCIIKRYCEKRFVSKYLATIGIDYGVTKVHVRDREIKVNIFDMAGHPFFYEVRNEFYKDTQGVILVYDVGQKDSFDALDAWLAEMKQELGPHGNMENIIFVVCANKIDCTKHRCVDESEGRLWAESKGFLYFETSAQTGEGINEMFQTFYISIVDLCENGGKRPTTNSSASFTKEQADAIRRIRNSKDSWDMLGVKPGASRDEVNKAYRKLAVLLHPDKCVAPGSEDAFKAVVNARTALLKNIK
Protein: Endophilin-A1 (Endophilin-1) (SH3 domain protein 2A) (SH3 domain-containing GRB2-like protein 2) (SH3p4) (O35179)
Organism: Rattus norvegicus (Rat)
Function: Implicated in synaptic vesicle endocytosis. May recruit other proteins to membranes with high curvature. Required for BDNF-dependent dendrite outgrowth. Cooperates with SH3GL2 to mediate BDNF-NTRK2 early endocytic trafficking and signaling from early endosomes (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:9238017, ECO:0000269|PubMed:9341169}. Membrane {ECO:0000269|PubMed:9238017}; Peripheral membrane protein {ECO:0000269|PubMed:9238017}. Early endosome {ECO:0000250|UniProtKB:Q62420}. Presynapse {ECO:0000269|PubMed:9341169}.
Interaction partners:
- Synaptojanin-1
- Dynamin-1
- E3 ubiquitin-protein ligase parkin
- Synaptojanin-2
- Dynamin-2
- Receptor protein-tyrosine kinase
- E3 ubiquitin-protein ligase CBL
- Clathrin coat assembly protein AP180
- Amphiphysin
- Endophilin-A2
Sequence:
MSVAGLKKQFHKATQKVSEKVGGAEGTKLDDDFKEMERKVDVTSRAVMEIMTKTIEYLQPNPASRAKLSMINTMSKIRGQEKGPGYPQAEALLAEAMLKFGRELGDDCNFGPALGEVGEAMRELSEVKDSLDMEVKQNFIDPLQNLHDKDLREIQHHLKKLEGRRLDFDYKKKRQGKIPDEELRQALEKFDESKEIAESSMFNLLEMDIEQVSQLSALVQAQLEYHKQAVQILQQVTVRLEERIRQASSQPRREYQPKPRMSLEFATGDGTQPNGGLSHTGTPKPAGVQMDQPCCRALYDFEPENEGELGFKEGDIITLTNQIDENWYEGMLHGQSGFFPINYVEILVALPH
Protein: RanBP2-type domain-containing protein (Q580S9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Splicing factor TSR1
- RNA-binding protein, putative
Sequence:
MEGRKGKTSQLRGGPKHGHPSGSRSNLRSRQRDGNRHWSPSHRDSRDYKKRFRSPSPNSGSVSRSSSRGSASYSGSSVSDSYSSDSSARFDFRRRRWSPSHRSGGTAGALSYSKGYDVGDSDAVLDHPTTDWVCGVCSNPNSVNREDCYRCGATFSASVNAVPSEEVKVSNIPNGVTFADIGQRLGEYFSQYGDTCRIIAHDMDNVDTDESGGSAYLLFEGVVEATKALTYARSALLLGDIRCPMEFSLQGRAKKKLNDVWERNGEGSDDRRGGVSLLPAPPPAVEGLPDDLQPAVWKPVENFPSVEAEMNYLDMLSHHWSKLSQAQKDYYDEGVRRALAAQRRKQPSQQVTETSATSRGETNTVNAPTSSGNPSPQGNGSSLESIKKRLEEKKKSMQNVTEVPKVAASLKERLAMKKAQLSSAAKPGNATESDAVGSTTAVSSTFSPPSTASVLPPSQKESAASQQHLFFGIPIPPRFPAKTDYLLNSKSLPARAGVIFRYVPPAVAERILQPPLLPHSS
Protein: Minichromosome maintenance protein 5 (EC 3.6.4.12) (Cell division control protein 46) (P29496)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Acts as component of the MCM2-7 complex (MCM complex) which is the putative replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. The active ATPase sites in the MCM2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity; specifically the MCM2-MCM5 association is proposed to be reversible and to mediate a open ring conformation which may facilitate DNA loading. Once loaded onto DNA, double hexamers can slide on dsDNA in the absence of ATPase activity.
Subcellular location: Nucleus. Note=Mobilized from the cytoplasm to the nucleus as mitosis is completed. Remains in the nucleus until the initiation of the next round of replication.
Interaction partners:
- DNA replication licensing factor MCM6
- Origin recognition complex subunit 5
- Cell division cycle protein CDT1
- Origin recognition complex subunit 1
- Cell division control protein 7
- DNA replication licensing factor MCM7
- Chromosome segregation in meiosis protein 3
- Cell division control protein 6
- DNA replication licensing factor MCM4
- DNA replication regulator DPB11
Sequence:
MSFDRPEIYSAPVLQGESPNDDDNTEIIKSFKNFILEFRLDSQFIYRDQLRNNILVKNYSLTVNMEHLIGYNEDIYKKLSDEPSDIIPLFETAITQVAKRISILSRAQSANNNDKDPENTSMDTDSLLLNSLPTFQLILNSNANQIPLRDLDSEHVSKIVRLSGIIISTSVLSSRATYLSIMCRNCRHTTSITINNFNSITGNTVSLPRSCLSTIESESSMANESNIGDESTKKNCGPDPYIIIHESSKFIDQQFLKLQEIPELVPVGEMPRNLTMTCDRYLTNKVIPGTRVTIVGIYSIYNSKNGAGSGRSGGGNGGSGVAIRTPYIKILGIQSDVETSSIWNSVTMFTEEEEEEFLQLSRNPKLYEILTNSIAPSIFGNEDIKKAIVCLLMGGSKKILPDGMRLRGDINVLLLGDPGTAKSQLLKFVEKVSPIAVYTSGKGSSAAGLTASVQRDPMTREFYLEGGAMVLADGGVVCIDEFDKMRDEDRVAIHEAMEQQTISIAKAGITTVLNSRTSVLAAANPIYGRYDDLKSPGDNIDFQTTILSRFDMIFIVKDDHNEERDISIANHVINIHTGNANAMQNQQEENGSEISIEKMKRYITYCRLKCAPRLSPQAAEKLSSNFVTIRKQLLINELESTERSSIPITIRQLEAIIRITESLAKLELSPIAQERHVDEAIRLFQASTMDAASQDPIGGLNQASGTSLSEIRRFEQELKRRLPIGWSTSYQTLRREFVDTHRFSQLALDKALYALEKHETIQLRHQGQNIYRSGV
Protein: RE31520p (Uncharacterized protein, isoform A) (Q9VHV6)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Protein crooked neck
- Pre-mRNA-processing factor 19
- Pre-mRNA-splicing factor syf1 homolog
- Cell division cycle 5, isoform A
- Protein BUD31 homolog
- Pleiotropic regulator 1
- Pre-mRNA-splicing factor Syf2
- Puff-specific protein Bx42
- LD24318p
- Homeobox protein goosecoid
Sequence:
MARNAEKAMTTLARWRAAKEVESGEKERRPYLASECHDLPRCEKFRLEIIRDISKKVAQIQNAGLGEFRIRDLNDEINKLLREKRHWENQISSLGGPHYRRYGPKMFDAEGREVPGNRGYKYFGAAKDLPGVRELFEQDPPPPPRKSRAELMKDIDAEYYGYRDDEDGVLIPLEERIERAAIQKAVQEWREKMARDGRIIDDEEEDEIYPLSGPAREAIEDAKARAAVEDPHGLLASKFTAHVPVPTQQDVQEALLRQRKRELLEKYAGGTN
Protein: CBL-interacting serine/threonine-protein kinase 26 (EC 2.7.11.1) (SNF1-related kinase 3.26) (SOS2-like protein kinase PKS26) (Q84VQ3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: CIPK serine-threonine protein kinases interact with CBL proteins. Binding of a CBL protein to the regulatory NAF domain of CIPK protein lead to the activation of the kinase in a calcium-dependent manner. Involved in the calcium-dependent regulation of reactive oxygen species production by the NADPH oxidase RBOHF.
Subcellular location: Cell membrane {ECO:0000269|PubMed:23335733}.
Interaction partners:
- Calcineurin B-like protein 1
- Calcineurin B-like protein 9
- Respiratory burst oxidase homolog protein F
- Calcineurin B-like protein 3
- Calcineurin B-like protein 2
- Protein phosphatase 2C 77
- Protein phosphatase 2C 56
- Respiratory burst oxidase homolog protein D
- Calcineurin B-like protein 10
- Protein ABSCISIC ACID-INSENSITIVE 5
Sequence:
MNRPKVQRRVGKYEVGKTLGQGTFAKVRCAVNTETGERVALKILDKEKVLKHKMAEQIRREICTMKLINHPNVVRLYEVLASKTKIYIVLEFGTGGELFDKIVHDGRLKEENARKYFQQLINAVDYCHSRGVYHRDLKPENLLLDAQGNLKVSDFGLSALSRQVRGDGLLHTACGTPNYAAPEVLNDQGYDGATADLWSCGVILFVLLAGYLPFEDSNLMTLYKKIIAGEYHCPPWLSPGAKNLIVRILDPNPMTRITIPEVLGDAWFKKNYKPAVFEEKEEANLDDVDAVFKDSEEHHVTEKKEEQPTSMNAFELISMSRALDLGNLFEEEEGFKRETRFAAKGAANDLVQKIEEASKPLGFDIQKKNYKMRLENVTAGRKGNLRVATEIFQVSPSLHMIEVRKTKGDTLEFHKFYKKLSTSLNDVVWKSGESSGLSK
Protein: Homeobox protein Nkx-6.2 (NK6 homeobox 2) (A0A0R4IY89)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
Interaction partners:
- Protachykinin-1 isoform X1
Sequence:
MLAVGQMDSNRQSAFVLGSTPLAALHNMTEMKTSLFPYALQSPAGFKAPSLGNLNSQIPLGTPHGISDILGRPITTAGQLLSGFPRINGLATSAGMYFNPAAVSRYPKPLTELPGRAPIFWPGMMQGSPWRDPRVPCAAQANMMLDKDGKKKHSRPTFSGQQIFALEKTFEQTKYLAGPERARLAYSLGMTESQVKVWFQNRRTKWRKRHAAEMATAKKKHDSETEKMKESSDNDEDDEYNKPLDPNSDDEKITRLLKKHKTSNLSLLSPCSNSSDTL
Protein: Sal-like protein 1 (Spalt-like transcription factor 1) (Zinc finger protein 794) (Zinc finger protein SALL1) (Zinc finger protein Spalt-1) (HSal1) (Sal-1) (Q9NSC2)
Organism: Homo sapiens (Human)
Function: Transcriptional repressor involved in organogenesis. Plays an essential role in ureteric bud invasion during kidney development.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9ER74}.
Interaction partners:
- Homeobox protein NANOG
- Sal-like protein 4
- Transcription factor SOX-2
- Histone-lysine N-methyltransferase NSD2
- Homeobox protein SIX2
- Protein phosphatase EYA1
- Telomeric repeat-binding factor 1
- POU domain, class 5, transcription factor 1
- Cyclin-Q
- Homeobox protein SIX1
Sequence:
MSRRKQAKPQHFQSDPEVASLPRRDGDTEKGQPSRPTKSKDAHVCGRCCAEFFELSDLLLHKKNCTKNQLVLIVNENPASPPETFSPSPPPDNPDEQMNDTVNKTDQVDCSDLSEHNGLDREESMEVEAPVANKSGSGTSSGSHSSTAPSSSSSSSSSSGGGGSSSTGTSAITTSLPQLGDLTTLGNFSVINSNVIIENLQSTKVAVAQFSQEARCGGASGGKLAVPALMEQLLALQQQQIHQLQLIEQIRHQILLLASQNADLPTSSSPSQGTLRTSANPLSTLSSHLSQQLAAAAGLAQSLASQSASISGVKQLPPIQLPQSSSGNTIIPSNSGSSPNMNILAAAVTTPSSEKVASSAGASHVSNPAVSSSSSPAFAISSLLSPASNPLLPQQASANSVFPSPLPNIGTTAEDLNSLSALAQQRKSKPPNVTAFEAKSTSDEAFFKHKCRFCAKVFGSDSALQIHLRSHTGERPFKCNICGNRFSTKGNLKVHFQRHKEKYPHIQMNPYPVPEHLDNIPTSTGIPYGMSIPPEKPVTSWLDTKPVLPTLTTSVGLPLPPTLPSLIPFIKTEEPAPIPISHSATSPPGSVKSDSGGPESATRNLGGLPEEAEGSTLPPSGGKSEESGMVTNSVPTASSSVLSSPAADCGPAGSATTFTNPLLPLMSEQFKAKFPFGGLLDSAQASETSKLQQLVENIDKKATDPNECIICHRVLSCQSALKMHYRTHTGERPFKCKICGRAFTTKGNLKTHYSVHRAMPPLRVQHSCPICQKKFTNAVVLQQHIRMHMGGQIPNTPVPDSYSESMESDTGSFDEKNFDDLDNFSDENMEDCPEGSIPDTPKSADASQDSLSSSPLPLEMSSIAALENQMKMINAGLAEQLQASLKSVENGSIEGDVLTNDSSSVGGDMESQSAGSPAISESTSSMQALSPSNSTQEFHKSPSIEEKPQRAVPSEFANGLSPTPVNGGALDLTSSHAEKIIKEDSLGILFPFRDRGKFKNTACDICGKTFACQSALDIHYRSHTKERPFICTVCNRGFSTKGNLKQHMLTHQMRDLPSQLFEPSSNLGPNQNSAVIPANSLSSLIKTEVNGFVHVSPQDSKDTPTSHVPSGPLSSSATSPVLLPALPRRTPKQHYCNTCGKTFSSSSALQIHERTHTGEKPFACTICGRAFTTKGNLKVHMGTHMWNSTPARRGRRLSVDGPMTFLGGNPVKFPEMFQKDLAARSGSGDPSSFWNQYAAALSNGLAMKANEISVIQNGGIPPIPGSLGSGNSSPVSGLTGNLERLQNSEPNAPLAGLEKMASSENGTNFRFTRFVEDSKEIVTS
Protein: Retinal dehydrogenase 2 (RALDH 2) (RalDH2) (EC 1.2.1.36) (Aldehyde dehydrogenase family 1 member A2) (ALDH1A2) (Retinaldehyde-specific dehydrogenase type 2) (RALDH(II)) (O94788)
Organism: Homo sapiens (Human)
Function: Converts retinaldehyde to retinoic acid. Recognizes as substrates free retinal and cellular retinol-binding protein-bound retinal. Can metabolize octanal and decanal, but has only very low activity with benzaldehyde, acetaldehyde and propanal. Displays complete lack of activity with citral (By similarity).
Subcellular location: Cytoplasm.
Interaction partners:
- Cytochrome P450 26A1
- Cytochrome P450 26B1
- Cytochrome P450 26C1
- Retinol dehydrogenase 10
- Retinol dehydrogenase 12
- Short-chain dehydrogenase/reductase 3
- Beta,beta-carotene 15,15'-dioxygenase
- Retinol dehydrogenase 11
- Retinol dehydrogenase 5
- Retinol dehydrogenase 8
Sequence:
MTSSKIEMPGEVKADPAALMASLHLLPSPTPNLEIKYTKIFINNEWQNSESGRVFPVYNPATGEQVCEVQEADKADIDKAVQAARLAFSLGSVWRRMDASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAFYVDLQGVIKTFRYYAGWADKIHGMTIPVDGDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGIDKIAFTGSTEVGKLIQEAAGRSNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGKGLGRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTVTVKIPQKNS
Protein: B-box zinc finger protein 23 (Protein DOUBLE B-BOX 4) (Protein SALT TOLERANCE HOMOLOG 6) (O82617)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable transcription factor that may be involved in seedling photomorphogenesis.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9SJU5}.
Interaction partners:
- B-box type zinc finger family protein
- B-box domain protein 30
- At5g54470
- B-box zinc finger protein 32
- Transcription factor HY5
- B-box domain protein 31
- E3 ubiquitin-protein ligase COP1
- B-box zinc finger family protein
- Zinc finger protein CONSTANS-LIKE 12
- Transcription factor HY5-like
Sequence:
MKIQCEVCEKAEAEVLCCSDEAVLCKPCDIKVHEANKLFQRHHRVALQKDAASATTASGAPLCDICQERKGYFFCLEDRAMLCNDCDEAIHTCNSHQRFLLSGVQVSDQSLTENSECSTSFSSETYQIQSKVSLNSQYSSEETEAGNSGEIVHKNPSVILSP
Protein: Exonuclease domain-containing protein (Q54RJ2)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
Sequence:
MSTTTTSTSSSTPTTSVKQKFKYLIVLDFEATCEKDVKFPNQEIIEFPSVIINTETLETVSTFREYVKPIINPNLSKFCTELTGIKQETVENAALFPDVLKSHCDWFFESLPKDIQSDEYCFVCCGDWDLLQCLPKQLKLCNNLSKPSYLSKWINIKKQYTLFYNRPSFGMTNMLRELNIPLEGRHHCGLSDSLNISKILKRMIEEGCNFDLVSTMKSVK
Protein: Transmembrane protein 128 (Q5BJH2)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MDSSRARQQLRRRFLLLPDAEAQLDREGDAGPETSTAVEKKEKPLPRLNIHSGFWILASIVVTYYVDFFKTLKENFHTSSWFLCGSALLLVSLSIAFYCIVYLEWYCGIGEYDVKYPALIPITTASFIAAGICFNIALWHVWSFFTPLLLFTQFMGVVMFITLLG
Protein: Methylmalonyl-CoA mutase, mitochondrial (MCM) (EC 5.4.99.2) (Methylmalonyl-CoA isomerase) (P16332)
Organism: Mus musculus (Mouse)
Function: Catalyzes the reversible isomerization of methylmalonyl-CoA (MMCoA) (generated from branched-chain amino acid metabolism and degradation of dietary odd chain fatty acids and cholesterol) to succinyl-CoA (3-carboxypropionyl-CoA), a key intermediate of the tricarboxylic acid cycle.
Subcellular location: Mitochondrion matrix {ECO:0000250|UniProtKB:P22033}. Mitochondrion {ECO:0000250|UniProtKB:P22033}. Cytoplasm {ECO:0000250|UniProtKB:P22033}.
Interaction partners:
- Methylmalonyl-CoA epimerase, mitochondrial
- Succinate--CoA ligase [GDP-forming] subunit beta, mitochondrial
- Methylmalonic aciduria type A homolog, mitochondrial
- Succinate--CoA ligase subunit beta, mitochondrial
- Succinate--CoA ligase subunit alpha, mitochondrial
- Malonate--CoA ligase ACSF3, mitochondrial
- Protein argonaute-2
- ATP-citrate synthase
- Phosphoenolpyruvate carboxykinase, cytosolic
- Pyruvate carboxylase, mitochondrial
Sequence:
MLRAKNQLFLLSPHYLKQLNIPSASRWKRLLHQQQPLHPEWAVLAKKQLKGKNPEDLIWHTPEGISIKPLYSRADTLDLPEELPGVKPFTRGPYPTMYTYRPWTIRQYAGFSTVEESNKFYKDNIKAGQQGLSVAFDLATHRGYDSDNPRVRGDVGMAGVAIDTVEDTKILFDGIPLEKMSVSMTMNGAVIPVLATFIVTGEEQGVPKEKLTGTIQNDILKEFMVRNTYIFPPEPSMKIIADIFQYTAQHMPKFNSISISGYHMQEAGADAILELAYTIADGLEYCRTGLQAGLTIDEFAPRLSFFWGIGMNFYMEIAKMRAGRRLWAHLIEKMFQPKNSKSLLLRAHCQTSGWSLTEQDPYNNIVRTAIEAMAAVFGGTQSLHTNSFDEALGLPTVKSARIARNTQIIIQEESGIPKVADPWGGSYMMESLTNDVYEAALKLIYEVEEMGGMAKAVAEGIPKLRIEECAARRQARIDSGSEVIVGVNKYQLEKEDSVEVLAIDNTSVRKKQIEKLKKIKSSRDQALAEQCLSALTQCAASGDGNILALAVDAARARCTVGEITDALKKVFGEHKANDRMVSGAYRQEFGESKEITSAIKRVNKFMEREGRRPRLLVAKMGQDGHDRGAKVIATGFADLGFDVDIGPLFQTPREVAQQAVDADVHAVGVSTLAAGHKTLVPELIKELTALGRPDILVMCGGVIPPQDYEFLYEVGVSNVFGPGTRIPRAAVQVLDDIEKCLAEKQQSV
Protein: Mitochondrial uncoupling protein 4 (AtPUMP4) (Mitochondrial dicarboxylate carrier 2) (Q9SB52)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: PUMPS are mitochondrial transporter proteins that create proton leaks across the inner mitochondrial membrane, thus uncoupling oxidative phosphorylation. This leads to a decrease in the efficiency of oxidative phosphorylation and an increase in heat production. May be involved in protecting plant cells against oxidative stress damage (By similarity). Recombinant PUMP4, reconstituted into liposomes, transports a wide range of dicarboxylic acids including malate, oxaloacetate and succinate as well as phosphate, sulfate and thiosulfate. However, it is unknown if these transports are of any biological significance in vivo.
Subcellular location: Mitochondrion inner membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Probable CCR4-associated factor 1 homolog 11
- Mitochondrial substrate carrier family protein
- Avr9/Cf-9 rapidly elicited protein
- At1g72820/F3N23_2
- Nematode resistance protein-like HSPRO2
- Uncharacterized protein F12A4.5
- Probable CCR4-associated factor 1 homolog 9
- Tetraspanin-8
- Transducin/WD40 repeat-like superfamily protein
- Ras guanine nucleotide exchange factor Q-like protein
Sequence:
MGVKSFVEGGIASVIAGCSTHPLDLIKVRLQLHGEAPSTTTVTLLRPALAFPNSSPAAFLETTSSVPKVGPISLGINIVKSEGAAALFSGVSATLLRQTLYSTTRMGLYEVLKNKWTDPESGKLNLSRKIGAGLVAGGIGAAVGNPADVAMVRMQADGRLPLAQRRNYAGVGDAIRSMVKGEGVTSLWRGSALTINRAMIVTAAQLASYDQFKEGILENGVMNDGLGTHVVASFAAGFVASVASNPVDVIKTRVMNMKVGAYDGAWDCAVKTVKAEGAMALYKGFVPTVCRQGPFTVVLFVTLEQVRKLLRDF
Protein: Tubulin-specific chaperone A (B5G0E7)
Organism: Taeniopygia guttata (Zebra finch) (Poephila guttata)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|RuleBase:RU364030}.
Interaction partners:
Sequence:
MADPRLRQIKIKTGVVRRLAKEKIMYEKEAKQQEEKIEKMKAEACDDYGIKKQIEILQESRMMIPDCQRRLEVAHAELTQLLENEKELEEAEEYKEARSILESVKLEA
Protein: NAD(P)H-hydrate epimerase (EC 5.1.99.6) (Apolipoprotein A-I-binding protein) (AI-BP) (NAD(P)HX epimerase) (Q6DHK1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of both epimers of NAD(P)HX.
Subcellular location: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03159}. Secreted {ECO:0000255|HAMAP-Rule:MF_03159}.
Interaction partners:
- ATP-dependent
- Pyridoxamine 5'-phosphate oxidase.
- m7GpppN-mRNA hydrolase
- RNA helicase
- RNA helicase
- Decapping mRNA 1A.
- Decapping mRNA 1B.
Sequence:
MLGVRALFGIGLLVTSRGGFVLTHTRACSSAASNIYSKHLTHRPTCTMANTGVKYLGQEEAQQIDEELFSDFSFSVDQLMELAGLSCATAVAKGYPVTSLLKSPARVLVICGPGNNGGDGLVCARHLKLFGYEPSVLYPKRPNKQLFQNLSIQCQKMEIPFLTEMPEADLIDEAYSLVVDAIFGFSFKGAVREPFGEILSQLKKITVPIASVDIPSGWDVEKGCPDGIQPDMLISLTAPKKSAALFKGRFHFLGGRFVPPVLEQKYQLNLPQYPGTECVFQLN
Protein: Embryonic polyadenylate-binding protein 2 (Embryonic poly(A)-binding protein 2) (ePABP-2) (ePABP2) (Embryonic poly(A)-binding protein type II) (Poly(A)-binding protein nuclear-like 1) (Q5XFR0)
Organism: Mus musculus (Mouse)
Function: Binds the poly(A) tail of mRNA.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q6TY21}.
Interaction partners:
- Polyadenylate-binding protein 2
- Protein BTG4
Sequence:
MEPYLSNELFPPPTEAWLQTVSSDPEAQGWGAWGRTEKTSLVPRAGSRAGSDKEAEENEDASFLLSLLEPENLAKSPVFNQELEAIKLKLWAMEHAEAQPEPPCVQRKATEEERAEVRQLLSPETVDCFFSRTSKENVEADHRSVFVGNVDYGGSAAELEAYFSPCGEIHRVTILCDKFSGHPKGYAYIEFASHRSVKAAVGLDESTFRGRVIKVLPKRTNFPGISSTDRGGLRTHSGNRAAFLHGSLHRKARLRAHGRSRGHGGAPQWFSPY
Protein: Uncharacterized membrane protein C14C4.07 (O13714)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MSSHDDDHTPLLISDPSVNKPFRSRTPSPEREYCSDCPLQAKGSACNGNSHSLKHETNGASSSNNNVAKSSSHDSFKAKPKNYDSTSNSNEPISFNEPDSSNSHHNNESICNNDNCCREIARRRSLSPLLILPLNFINAFSWGMIEIPLLFLLRQELCAIHYNLDPTQLSPDDPICRLAEITTGVSKVRAAFGSLAAFLGLFSTAYYGTMGDIYGRRLVLFITVSFLLLGDLWLLYQSYAPKHPYFVLFAAALKGLGGYISTVVASQNSFVADCSKTEFRAWYLGLNFAAYHLGTALGPSLSGFIVQYTPHMYYVFYITSTFWIIYLLYVWLILPESLDVSESKEQQNKISGFSSIWRSCLEPLIILWPRSLCTEESCEFHQYDINADTHAGRRHWDVLLAAILISLTLLGAGSMGLLPLYTDYKFGWGPMKASLILSTDSFASSITLVALFPLLSKVIEKIIEKLYSSEGLFEDPSRADNTSSLQGIRNVFSYLVRPGYSRSSILRGRTADEKYTIVKRDVWNAQLGYAIALSAAVLLAVAKSDVALFTAVIIQAISNMVVPCVQSIALNGVQSEYNGRVLAAFAVFEAVALIIRGPIYAFVYTESMKVSYPNMIFFLSAVIYGCCFIIIFFMRLYRPLNRKR
Protein: Protein PLANT CADMIUM RESISTANCE 8 (AtPCR8) (Q9M815)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May be involved in heavy metals transport.
Subcellular location: Cell membrane {ECO:0000269|PubMed:19334764}; Single-pass membrane protein {ECO:0000269|PubMed:19334764}.
Interaction partners:
- Putative F-box/kelch-repeat protein At3g27910
Sequence:
MGRVTTPSEEDSNNGLPVQQPGTPNQRTRVPVSQFAPPNYQQANVNLSVGRPWSTGLFDCQADQANAVLTTIVPCVTFGQIAEVMDEGEMTCPLGTFMYLLMMPALCSHWVMGSKYREKMRRKFNLVEAPYSDCASHVLCPCCSLCQEYRELKIRNLDPSLGWNGILAQGQGQYEREAPSFAPTNQYMSK