wanglab/gogpt-training-data huggingface dataset:
Protein: Carotenoid-cleaving dioxygenase, mitochondrial (EC 1.13.11.-) (EC 1.13.11.71) (Beta,beta-carotene 9',10'-oxygenase) (Q6QT07)
Organism: Mustela putorius furo (European domestic ferret) (Mustela furo)
Function: Broad specificity mitochondrial dioxygenase that mediates the asymmetric oxidative cleavage of carotenoids. Cleaves carotenes (pure hydrocarbon carotenoids) such as all-trans-beta-carotene and lycopene as well as xanthophylls (oxygenated carotenoids) such as zeaxanthin, lutein and beta-cryptoxanthin at both the 9,10 and the 9',10' carbon-carbon double bond. Through its function in carotenoids metabolism regulates oxidative stress and the production of important signaling molecules (By similarity).
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:Q99NF1}.
Interaction partners:
Sequence:
MEGTDQKKAAVGTREGLPCIAPLLTTVEETPQVVSAQVRGHFPKWLSGSLLRIGPGKFEFGKDKYNHWFDGMALLHQFKMEKGMVTYRSKFLQSDTYKTNSVHDRIVISEFGTLALPDPCKNVFERFMSKFELPAITDNTSVNYVRYKGDYYVSTETNFMNKVDIETLEKTEKVDWSKFIAVNGATAHPHYDPDGTAYNMGNSYGLHGSCYNVIRVPPEKVDLGETLHGAQVICSIASTERMKPSYYHSFGMTRNYIIFIEQPLKMNLWKMITSRIRGMAFSDGISWEPQYNTRFHVVDKNTGQLLPGMYYSKPFVTFHQINAFEDQGCVVLDLCCQDDGRSLEAYRLQNLRKAGAGLDQVYNSVGRSFPRRFVLPLHVSLNDPEGENLSPLSYSSASAVKQANGKIWCSYENLHPEDLEEEGGVEFPQINYGQFSGKKYRFFYGCGFRHLVGDSLIKLDVVNKTLMIWREDGFYPSEPVFVPAPGASEEDGGVILSVVITPDQNENNFLLVLDAKNFEELGRAEVPVRMPYGFHGTFVTV
Protein: Engulfment ABC transporter in the ovary, isoform C (FI17829p1) (E1JHH7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MAGTFTPLFFVFLRKNLLYLQRNLLPLLLICSGFAGVLTAYLHWSVKPVLHQINQFEAKNEMVLRELYFPGNELDYIYYSPISPNVEDIMDLLRVDLGIIPERLRPNNNSFEMQLEMEQQCRGSCFAIDFHRVPNRGSDRKFRYSLSSNQMRISPRKRFVNDEEIYHQIDDDDYIRSGFLSLQHILDKQYMKYQELGKDFEVVVSSMPNMEVISMDSHRLTYFGTLCSILFNVVLLSSFVVPFVEEKQNGLKEFLNLVTPMSFLNGLTFFLIRFVCYTLLMIFVLVVAYLYKALGSICFAYVAVLFLLYILSTMSYAYLISICFHSVFYAKIGGLAMLIIPYAFSFVRSWATSLAFVCFSTNTFLEGLDIFQTFSNKHREFGAVDVFRVIKSNSSTMFSVYVVLVFQSFLYAMLYNYLGCVFPGPGGLKRPMFFFLDFRIGYRLHNQTGLN
Protein: Csi2p (A0A1D8PFE1)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Nucleus, nucleolus {ECO:0000256|ARBA:ARBA00004604}.
Interaction partners:
- rRNA-processing protein EBP2
- rRNA-binding ribosome biosynthesis protein
- 60S ribosome subunit biogenesis protein NIP7
- Ribosomal RNA-processing protein 1
- Nucleolar GTP-binding protein 1
- mRNA-binding ribosome synthesis protein
- rRNA-binding ribosome biosynthesis protein
- Ribosome biogenesis protein YTM1
- Ribosome biogenesis protein ERB1
- Ribosome production factor 2 homolog
Sequence:
MSAIYKALQSKSSKETSEKTKHINRQRLLVISSRGITYRHRHLIQDLLALLPHARKEPKFDSKKNLHQLNEVAELYNCNNIFFFECRKHQDLYLWISKPPNGPTLKFHIQNLHTLDELNFTGNCLKGSRPILSFDKSFLENDHYKLLKEMFLQTFGVPPNARKSKPFIDHVMTFSIVDGKIWIRNYQINETLDVKENDKIEDDEDYDVDQLNLVEIGPRLVLTLITVLEGSFSGPKIYENKQYVSPNFVRAQLKQQAADQAKSRSQAALERKIKKRNQVLKADPLSNDALFK
Protein: Chromatin assembly factor 1, p105 subunit (A1Z898)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Chromatin assembly factor 1, p180 subunit
- Chromatin assembly factor 1 p55 subunit
- Histone chaperone asf1
- Proliferating cell nuclear antigen
- Proliferating cell nuclear antigen 2
- CDC45L
- DNA replication licensing factor Mcm5
- RE32990p
- Enhanced level of genomic instability 1
- Protein lethal
Sequence:
MKCKIPEISWHNRDPVLSVDIQQNGLGLRSPTICRLASGGSDAHVLIWYVNRSDDAEGVDVELAADLSRHQRAVNAVRWSPNGELLASGDDESVVFIWKQKADHEVVNIVDADGCSEQDKEVWLTLKVLRGHREDIYDLSWAPNSQFLVSGSVDNTAMLWDVHSGKSLAILDDHKGYVQGVAWDPCNQYIATMSTDRQMRIFDANTKRVLHRVSKCVLPVKEDHEMHGKSMRLYQDGTLQTFFRRLCFTPDGKLLLTPSGITDYDGVVKPINTSYGFSRHDLSKPAFVLPFPKEYAVAVRCSPVLYRLRPYNAEKNPPIISLPYRMIYAVATKNAVFFYDTQQPVPFAIVSNIHYSRLTDLAWSSDGTVLIVSSTDGYCSLITFEPTELGDCYEDMETVLSVVLKSSENATVLKKKRQKLRKVSLDEPRKPLQEKSKPNTIRRASEAGITEVGEPELDAENDSSTHSVSSNKTNSPKTKASEEEKPTPIAIRRSPRKNSTAPMPIAIRRAPRKPEDKGNSESSKPKDEMEVTHTKTTQVQKTVASPVKRKVSTEAVPPAETSQPALAVIPVFEKEIISSDDKFESPEKKSRPATPIQVRRQPRTPGSSSQFNLTPKSQPAKQATPIAVRRTPRVLIEMPVNSPVVPMEEAMDAWPLDESITPLPATKKDSRKPLPETVKTETKPAVIEASEATCERTEDIRLVYEDTQEETPKNPTESGPSTPNNKTPRRVSLRTISTPKSKKKLLE
Protein: Candida glabrata strain CBS138 chromosome A complete sequence (Q6FXW9)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
- Small ribosomal subunit protein uS9
- 40S ribosomal protein S12
- Small ribosomal subunit protein uS10
- L37
- Large ribosomal subunit protein uL5
- 60S ribosomal protein L8
- S16a
- Ribosomal protein L37
- Large ribosomal subunit protein eL31
- 40S ribosomal protein S30
Sequence:
MAREVTDIKQFLELTRRNDVQSATVKINKKLNKNGKQFRQTKFKVRGSRHLYTLTVNDAGKAKKLIQSLPPTLKVNKL
Protein: Guanine nucleotide-binding protein G(i) subunit alpha-1 (EC 3.6.5.-) (Adenylate cyclase-inhibiting G alpha protein) (B2RSH2)
Organism: Mus musculus (Mouse)
Function: Guanine nucleotide-binding proteins (G proteins) function as transducers downstream of G protein-coupled receptors (GPCRs) in numerous signaling cascades. The alpha chain contains the guanine nucleotide binding site and alternates between an active, GTP-bound state and an inactive, GDP-bound state. Signaling by an activated GPCR promotes GDP release and GTP binding. The alpha subunit has a low GTPase activity that converts bound GTP to GDP, thereby terminating the signal. Both GDP release and GTP hydrolysis are modulated by numerous regulatory proteins (By similarity). Signaling is mediated via effector proteins, such as adenylate cyclase. Inhibits adenylate cyclase activity, leading to decreased intracellular cAMP levels (By similarity). The inactive GDP-bound form prevents the association of RGS14 with centrosomes and is required for the translocation of RGS14 from the cytoplasm to the plasma membrane. Required for normal cytokinesis during mitosis. Required for cortical dynein-dynactin complex recruitment during metaphase (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P10824}. Cytoplasm {ECO:0000250|UniProtKB:P10824}. Cell membrane {ECO:0000250|UniProtKB:P10824}; Peripheral membrane protein {ECO:0000250|UniProtKB:P10824}; Cytoplasmic side {ECO:0000250|UniProtKB:P10824}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:P10824}. Cytoplasm, cell cortex {ECO:0000250|UniProtKB:P63096}. Membrane {ECO:0000250|UniProtKB:P10824}; Lipid-anchor {ECO:0000250|UniProtKB:P10824}. Note=Localizes in the centrosomes of interphase and mitotic cells, but not in centrosomes during cytokinesis. Detected at the cleavage furrow or the midbody. Localized at the plasma membrane throughout mitosis. Colocalizes with RIC8A and RGS14 at the plasma membrane. {ECO:0000250|UniProtKB:P10824}.
Interaction partners:
- Guanine nucleotide-binding protein G
- Regulator of G-protein signaling 4
- Chaperone Ric-8A
- Guanine nucleotide-binding protein G
- Lysophosphatidic acid receptor 1
- Guanine nucleotide-binding protein G
- Mitogen-activated protein kinase 3
- D
- Gamma-aminobutyric acid type B receptor subunit 2
- Sphingosine 1-phosphate receptor 1
Sequence:
MGCTLSAEDKAAVERSKMIDRNLREDGEKAAREVKLLLLGAGESGKSTIVKQMKIIHEAGYSEEECKQYKAVVYSNTIQSIIAIIRAMGRLKIDFGDSARADDARQLFVLAGAAEEGFMTAELAGVIKRLWKDSGVQACFNRSREYQLNDSAAYYLNDLDRIAQPNYIPTQQDVLRTRVKTTGIVETHFTFKDLHFKMFDVGGQRSERKKWIHCFEGVTAIIFCVALSDYDLVLAEDEEMNRMHESMKLFDSICNNKWFTDTSIILFLNKKDLFEEKIKKSPLTICYPEYAGSNTYEEAAAYIQCQFEDLNKRKDTKEIYTHFTCATDTKNVQFVFDAVTDVIIKNNLKDCGLF
Protein: RE44043p (Synaptotagmin 7, isoform B) (Q6NNV2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MASIVLIACLAILGLIITIALFLAGGYLWWRHKRSQLQFIEPNEDEESSSYSLRAAQDIVDSGNPPTKPQVPVAHAITTPLQNNINRKLNGFLSLRTPLIGGSGASQTKPQIISSVGNPGDGTTKDSANKSISMTDMYLDSTDPSENVGQIHFSLEYDFQNTTLILKVLQGKELPAKDLSGTSDPYVRVTLLPDKKHRLETKIKRRTLNPRWNETFYFEGFPIQKLQSRVLHLHVFDYDRFSRDDSIGEVFLPLCQVDFAGKQSFWKALKPPAKDKCGELLSSLCYHPSNSILTLTLIKARNLKAKDINGKSDPYVKVWLQFGDKRF
Protein: Casein kinase 1-like protein 2 (EC 2.7.11.1) (Protein CASEIN KINASE I-LIKE 2) (Q9CAI5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates. It can phosphorylate a large number of proteins.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16126836}. Nucleus {ECO:0000269|PubMed:16126836}.
Interaction partners:
- Cryptochrome-2
- At3g49990
- Stomatal closure-related actin-binding protein 1
- Cytochrome P450, family 705, subfamily A, polypeptide 25
- Actin-depolymerizing factor 4
- Peroxidase 13
- Serine/threonine-protein kinase MPS1
- Cryptochrome-1
- Shaggy-related protein kinase delta
- Bystin
Sequence:
MEPRVGNKFRLGRKIGGGSFGEIYLGTNIQTNEEVAIKLENVKTKHPQLLYESKLYKVLQGGTGVPNVKWYGVEGDYNVLVIDLLGPSLEDLFNFCSRKLSLKTVLMLADQMINRIEFVHQKSFLHRDIKPDNFLMGLGRRANQVYVIDFGLAKKYRDSNHQHIPYRENKNLTGTARYASMNTHLGIEQSRRDDLESLGFVLMYFLKGSLPWQGLKAGNKKQKYEKISEKKVSTSIEALCRGYPSEFASYFHYCRSLRFDDKPDYAYLKRLFRDLFIREGFQFDYVFDWTILKYQQSQISTPPPRHHGPVVGPSSALPPAITSAERPSGGDEARPSGWSSGIPRRNSGQIFNSGSLAKQKAPVSSDPAISKDVVLSSSSFLRATGSSRRAAVSSSREAAVLGTDSEPSNPQIVEAGSGSNSKIPVSRNSPIVSSEINKLSSPSRATTSVMKNYEANLKGIESLHF
Protein: NADH-ubiquinone oxidoreductase chain 4 (EC 7.1.1.2) (Q35300)
Organism: Oryza sativa subsp. japonica (Rice)
Subcellular location: Mitochondrion membrane {ECO:0000256|RuleBase:RU003297}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU003297}.
Interaction partners:
Sequence:
MLEHFCECYFDLSGPILCPVLGSITLLFIPNSSIRLIRLIGLCVSLITFLYPLVPRIQFDPSTAKSQFVESLRWLPYENIHLYMGIDGLSLFFVILTTFLIPICISVGWSGMRSFGKEYITAFLIREFLMIAVSCMLDPLLFYVLSESVPIPMFIIIGVWGSRQRKIKAAYQFFLYTLLGSVFMLLAILLILLQTGTTDLQILLTTEFSERRQILLWIAFFASFAVKVPMVPVHIWLPEAHVEAPTAGS
Protein: Flavohemoglobin expression-modulating QEGLA motif protein (Q9HXU3)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- Lipoprotein
Sequence:
MSQRKAQNDYQKIIRSLSDRIVEAQTPIRVLDAIKWDDGIRQDFLKGRGKHAPKVDRGYYDSRPLAFDASAKKQEFQNIERDITRQLGQFNPVGQIMRRMCKEYRMVIRMLEARGTPDLGLISQELYGSASDAFHAGDPTLADLGLMLSDYLNNIADRGDLKDEPKTLTAKEVVPILQARLNTVFGEEEGTIRVFESDGIVADAAAGADYIKVRADALFNERDVRALEVHEGLVHVGTTLNGLSQPICTFLAKGPPSSTVTQEGLAILMEVIAFASYPTRLRKLTNRTRAIHMAEEGADFLDVFHFYREQGYSLEDSYQNASRVFRGSTPDGLPFTKDLSYLKGFILIYNYIQLAVRKGKLEQIPLLFCGKTTLEDMRTLRQLVDEGLVAPPKYLPPQFRDLNALSAWMCFSNFLNHLSLDRIEADYANIL
Protein: Glutathione S-transferase P (EC 2.5.1.18) (Chain 7) (GST 7-7) (GST class-pi) (P04906)
Organism: Rattus norvegicus (Rat)
Function: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Involved in the formation of glutathione conjugates of both prostaglandin A2 (PGA2) and prostaglandin J2 (PGJ2). Participates in the formation of novel hepoxilin regioisomers. Regulates negatively CDK5 activity via p25/p35 translocation to prevent neurodegeneration.
Subcellular location: Cytoplasm {ECO:0000250}. Mitochondrion {ECO:0000250}. Nucleus {ECO:0000250}. Note=The 83 N-terminal amino acids function as un uncleaved transit peptide, and arginine residues within it are crucial for mitochondrial localization. {ECO:0000250}.
Interaction partners:
- Peroxiredoxin-6
- Glutathione S-transferase theta-1
- Cytochrome P450 2E1
- Epoxide hydrolase 1
- Cytochrome P450 1A1
- Cytochrome P450 1B1
- Glutathione S-transferase omega-1
- Glutathione S-transferase kappa 1
- glutathione transferase
- Glutathione S-transferase theta-2
Sequence:
MPPYTIVYFPVRGRCEATRMLLADQGQSWKEEVVTIDVWLQGSLKSTCLYGQLPKFEDGDLTLYQSNAILRHLGRSLGLYGKDQKEAALVDMVNDGVEDLRCKYGTLIYTNYENGKDDYVKALPGHLKPFETLLSQNQGGKAFIVGNQISFADYNLLDLLLVHQVLAPGCLDNFPLLSAYVARLSARPKIKAFLSSPDHLNRPINGNGKQ
Protein: Small nuclear ribonucleoprotein F (snRNP-F) (Sm protein F) (Sm-F) (SmF) (O59734)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Plays a role in pre-mRNA splicing as a core component of the spliceosomal U1, U2, U4 and U5 small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:16823372}. Cytoplasm {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Pre-mRNA-splicing factor cwf4
- Small nuclear ribonucleoprotein Sm D1
- Pre-mRNA-splicing factor brr2
- Small nuclear ribonucleoprotein-associated protein B
- Small nuclear ribonucleoprotein G
- Small nuclear ribonucleoprotein Sm D2
- Small nuclear ribonucleoprotein E
- Pre-mRNA-splicing factor prp1
- Pre-mRNA-splicing factor cwf10
- Pre-mRNA-processing factor 19
Sequence:
MSFVPVNPKPFLQGLIGKPVLVRLKWGQEYKGTLQSVDSYMNLQLLNAEELVDGVKTGDLGEILIRCNNVLWVGESTV
Protein: Small ribosomal subunit protein uS9 (40S ribosomal protein S16) (Q29201)
Organism: Sus scrofa (Pig)
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P62249}. Nucleus, nucleolus {ECO:0000250|UniProtKB:P62249}.
Interaction partners:
- 40S ribosomal protein S4
- 40S ribosomal protein S30
- Small ribosomal subunit protein uS12
- Small ribosomal subunit protein uS13
- Small ribosomal subunit protein eS21
- Large ribosomal subunit protein uL4
- Small ribosomal subunit protein uS2
- Small ribosomal subunit protein uS19
- Large ribosomal subunit protein uL29
- Small ribosomal subunit protein uS7
Sequence:
MPSKGPLQSVQVFGRKKTATAVAHCKRGNGLIKVNGRPLEMIEPRTLQYKLLEPVLLLGKERFAGVDIRVRVKGGGHVAQIYAIRQSISKALVAYYQKYVDEASKKEIKDILIQYDRTLLVADPRRCESKKFGGPGARARYQKSYR
Protein: Calcium uptake protein 2, mitochondrial (hMICU3) (EF-hand domain-containing family member A1) (Q8IYU8)
Organism: Homo sapiens (Human)
Function: Key regulator of mitochondrial calcium uniporter (MCU) required to limit calcium uptake by MCU when cytoplasmic calcium is low. MICU1 and MICU2 form a disulfide-linked heterodimer that stimulate and inhibit MCU activity, depending on the concentration of calcium. MICU2 acts as a gatekeeper of MCU that senses calcium level via its EF-hand domains: prevents channel opening at resting calcium, avoiding energy dissipation and cell-death triggering.
Subcellular location: Mitochondrion intermembrane space {ECO:0000269|PubMed:24231807, ECO:0000269|PubMed:24560927, ECO:0000269|PubMed:26774479, ECO:0000269|PubMed:27099988}. Mitochondrion inner membrane {ECO:0000269|PubMed:24231807, ECO:0000269|PubMed:27099988, ECO:0000269|PubMed:28615291}. Note=Recruited to the mitochondrial inner membrane via its association with the uniplex complex. {ECO:0000269|PubMed:24231807}.
Interaction partners:
- Calcium uptake protein 1, mitochondrial
- Calcium uniporter protein, mitochondrial
- Calcium uniporter regulatory subunit MCUb, mitochondrial
- Essential MCU regulator, mitochondrial
- Mitochondrial calcium uniporter regulator 1
- Calcium uptake protein 3, mitochondrial
- Mitochondrial adenyl nucleotide antiporter SLC25A23
- Prohibitin-2
- Non-selective voltage-gated ion channel VDAC1
- Mitochondrial sodium/calcium exchanger protein
Sequence:
MAAAAGSCARVAAWGGKLRRGLAVSRQAVRSPGPLAAAVAGAALAGAGAAWHHSRVSVAARDGSFTVSAQKNVEHGIIYIGKPSLRKQRFMQFSSLEHEGEYYMTPRDFLFSVMFEQMERKTSVKKLTKKDIEDTLSGIQTAGCGSTFFRDLGDKGLISYTEYLFLLTILTKPHSGFHVAFKMLDTDGNEMIEKREFFKLQKIISKQDDLMTVKTNETGYQEAIVKEPEINTTLQMRFFGKRGQRKLHYKEFRRFMENLQTEIQEMEFLQFSKGLSFMRKEDFAEWLLFFTNTENKDIYWKNVREKLSAGESISLDEFKSFCHFTTHLEDFAIAMQMFSLAHRPVRLAEFKRAVKVATGQELSNNILDTVFKIFDLDGDECLSHEEFLGVLKNRMHRGLWVPQHQSIQEYWKCVKKESIKGVKEVWKQAGKGLF
Protein: Chemokine interleukin-8-like domain-containing protein (A0A060YQJ4)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
- Chemokine interleukin-8-like domain-containing protein
- Chemokine interleukin-8-like domain-containing protein
- Chemokine interleukin-8-like domain-containing protein
- Chemokine
- Chemokine interleukin-8-like domain-containing protein
- C-C motif chemokine
Sequence:
MISCRVCVLAALFSLLIITLIPTTQSADCCLKFTRRPVHCRWLKGYTFQDITSSCDLNAVIFQNLRNKFVCADPSQDWTKRVQRCLR
Protein: Nucleoporin p58/p45 (58 kDa nucleoporin) (Nucleoporin-like protein 1) (Q8R332)
Organism: Mus musculus (Mouse)
Function: Component of the nuclear pore complex, a complex required for the trafficking across the nuclear membrane.
Subcellular location: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:P70581}. Nucleus membrane {ECO:0000250|UniProtKB:P70581}; Peripheral membrane protein {ECO:0000250|UniProtKB:P70581}; Cytoplasmic side {ECO:0000250|UniProtKB:P70581}. Nucleus membrane {ECO:0000250|UniProtKB:P70581}; Peripheral membrane protein {ECO:0000250|UniProtKB:P70581}; Nucleoplasmic side {ECO:0000250|UniProtKB:P70581}. Note=Biased towards cytoplasmic side. Central region of the nuclear pore complex, within the transporter. {ECO:0000250|UniProtKB:P70581}.
Interaction partners:
- Nuclear pore complex protein Nup54
- Nuclear pore glycoprotein p62
- Nuclear pore complex protein Nup93
- Nucleoporin NUP35
- Nuclear pore complex protein Nup107
- Nuclear pore complex protein Nup214
- E3 SUMO-protein ligase RanBP2
- Nuclear pore complex protein Nup155
- Nucleoporin 205
- Nucleoporin NUP188
Sequence:
MATGFSFGSGTLGSTTVAPGGTGAGSGFSFGTVASSTPSVGLNFGSLGSSVTPASTSASAGGFGTGLFGSKPATGFTLGGTSAGTAATTSASTTGFSLGFSKPAASATPFALPVTSTSASGLTLSSALTSTPAASTGFTLNNLGATPATTTTASTGLSLGGALAGLGGSLFQSGNTATSGLGQNALSLSLGTTAPTSAASNEGLGGIDFSTSSDKKSDKTGTRPEDSKALKDENLPPVICQDVENLQKFVKEQKQVQEEISRMSSKAMLKVQEDIKALKQLLSLAASGLQRNTLNIDKLKLETAQELKNAEIALRTQKTPPGLQHENTAPADYFRILVQQFEVQLQQYRQQIEELENHLATQASNSHITPQDLSMAMQKIYQTFVALAAQLQSIHENVKVLKEQYLGYRKMFLGDAVDVFEARRTEAKKWQNAPRVTTGPTPFSTMPNAAAVAMAATLTQQQQPATGPQPSLGVSFGTPFGSGIGTGLQSSGLGSSNLGGFGTSSGFGCGTTGASTFGFGTTDKPSGSLSAGFGSSSTSGFNFSNPGITASAGLTFGVSNPASAGFGTGGQLLQLKRPPAGNKRGKR
Protein: Polyadenylate-binding protein-interacting protein 7 (PABP-interacting protein 7) (Poly(A)-binding protein-interacting protein 7) (PAM2-containing protein CID7) (Protein CTC-INTERACTING DOMAIN 7) (O64843)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Polyadenylate-binding protein-interacting protein 5
- Polyadenylate-binding protein-interacting protein 8
- Polyadenylate-binding protein-interacting protein 10
- Polyadenylate-binding protein-interacting protein 13
- Polyadenylate-binding protein-interacting protein 11
- Polyadenylate-binding protein-interacting protein 2
- Polyadenylate-binding protein-interacting protein 9
- Polyadenylate-binding protein-interacting protein 12
- Polyadenylate-binding protein-interacting protein 4
- Protein EARLY RESPONSIVE TO DEHYDRATION 15
Sequence:
MSLTKKASEPKLSGTSIKPTTLNPHAAEFVPFTLRSPSSGGTSTLDTRLLASSSSVGKAVLDRTESSASHHSDEEARQFWSHQLPDDITPDFGLMTQDDNSYGSGSLSLANLSLFDGNEAEKFPSASGGYGFSDQTGLASHNANGNSLADKSRYPISSFGEDPQRQSFMQLSPKPWDKQIMNAEQLLGNDRERNPFSGKSRHGFVNDMITESPGDMEVNPVDFLASQFPGFAAESLAEVYFANGCDLQLTIEMLTQLELQVDGGLNQNISPKTYAPPSLTPMDFPALSISNSHGIPAQFGGDDLQQTGNHYQSPEKDNMFFFKSGPSVSQPGAIDYVSAVRKLASQDSGMWKYERNDSADSSIGSSRNSGAYKSGRGRSIYSDKLQSRAQTRPAPVWVETGDAVGNMYSELREEARDYARLRNVYFEQARQAYLVGNKALAKELSVKGQLHNMQMKAAHGKAQEAIYRQRNPVGQGNSRGNERMIDLHGLHVSEALQVLKHELSVLRSTARATQERLQIYICVGTGHHTRGSRTPARLPVAVQRYLLEEEGLDYSEPQAGLLRVIIY
Protein: NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial (NDUFV2) (EC 7.1.1.2) (NADH-ubiquinone oxidoreductase 24 kDa subunit) (P19404)
Organism: Homo sapiens (Human)
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:0000250|UniProtKB:P04394}; Peripheral membrane protein {ECO:0000250|UniProtKB:P04394}; Matrix side {ECO:0000250|UniProtKB:P04394}.
Interaction partners:
- NADH dehydrogenase iron-sulfur protein 7, mitochondrial
- NADH dehydrogenase 1 beta subcomplex subunit 4
- NADH dehydrogenase 1 beta subcomplex subunit 6
- NADH dehydrogenase 1 alpha subcomplex subunit 10, mitochondrial
- NADH dehydrogenase iron-sulfur protein 8, mitochondrial
- NADH dehydrogenase 1 alpha subcomplex subunit 8
- NADH dehydrogenase 1 alpha subcomplex subunit 2
- NADH dehydrogenase iron-sulfur protein 5
- NADH dehydrogenase iron-sulfur protein 2, mitochondrial
- NADH dehydrogenase 1 beta subcomplex subunit 10
Sequence:
MFFSAALRARAAGLTAHWGRHVRNLHKTVMQNGAGGALFVHRDTPENNPDTPFDFTPENYKRIEAIVKNYPEGHKAAAVLPVLDLAQRQNGWLPISAMNKVAEVLQVPPMRVYEVATFYTMYNRKPVGKYHIQVCTTTPCMLRNSDSILEAIQKKLGIKVGETTPDKLFTLIEVECLGACVNAPMVQINDNYYEDLTAKDIEEIIDELKAGKIPKPGPRSGRFSCEPAGGLTSLTEPPKGPGFGVQAGL
Protein: Transcriptional regulatory protein CpxR (P0AE88)
Organism: Escherichia coli (strain K12)
Function: Response regulator member of the two-component regulatory system CpxA/CpxR which responds to envelope stress response by activating expression of downstream genes including cpxP, degP, dsbA and ppiA. Required for efficient binding of stationary phase cells to hydrophobic surfaces, part of the process of biofilm formation. Induced upon cell surface binding, subsequently induces genes it controls (cpxP, dsbA and spy, degP is only partially induced). Binds and activates transcription from the degP promoter; binding is enhanced by phosphorylation. This system combats a variety of extracytoplasmic protein-mediated toxicities by increasing the transcription of the periplasmic protease, DegP in concert with sigma factor E, as well as that of CpxP protein. Other downstream effectors may include SrkA.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Sensor histidine kinase CpxA
- Sensor histidine kinase EnvZ
- Periplasmic protein CpxP
- Lipoprotein NlpE
- Periplasmic serine endoprotease DegP
- Sensor protein BasS
- Signal transduction histidine-protein kinase BaeS
- Phosphate regulon sensor protein PhoR
- Transcriptional regulatory protein RcsB
- Sensor histidine kinase CusS
Sequence:
MNKILLVDDDRELTSLLKELLEMEGFNVIVAHDGEQALDLLDDSIDLLLLDVMMPKKNGIDTLKALRQTHQTPVIMLTARGSELDRVLGLELGADDYLPKPFNDRELVARIRAILRRSHWSEQQQNNDNGSPTLEVDALVLNPGRQEASFDGQTLELTGTEFTLLYLLAQHLGQVVSREHLSQEVLGKRLTPFDRAIDMHISNLRRKLPDRKDGHPWFKTLRGRGYLMVSAS
Protein: Peroxisome proliferation transcriptional regulator (Oleate-activated transcription factor 2) (P52960)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: The PIP2-OAF1 heterodimer acts as a transcriptional activator to induce the transcription of genes encoding proteins involved in fatty acid beta-oxidation, a response called oleic acid induction, when cells grow on fatty acids as sole carbon source. Recognizes and binds to the oleate response element (ORE) (or peroxisome box), two inverted CGG triplets spaced by 14 to 18 intervening nucleotides, in the promoter region of a number of genes (such as CTA1, FOX1 to FOX3, FAA2, PAS8, PAS10, etc.) for peroxisomal proteins. Activity is inhibited by OAF1 under non-inducing conditions. Activity is repressed by glucose.
Subcellular location: Nucleus.
Interaction partners:
- Oleate-activated transcription factor 1
- Cytochrome B pre-mRNA-processing protein 1
Sequence:
MYFTDESSPAMNRVGKKRNRLSFVCQACRKAKTKCDQEKPRCGRCTKQNLFCIYDVARQAAPRNPNKDATIARLKKEIRYWRNKTVDLTQEKKDFYTALKRPTEELAARRTCKSLQENSFPISLYKTHPRLIMTKVMKREINPLSEKYLIFQDTFLKTLIASVLLSCSRNSMIPALNADISRSRTQPCVKNNVVKMREVLLKNSKYESQRKSINEFTDRLLQRKNPEEQIAVNKVISLLYSNRESSYLEDTCPTENDYSDLLKGYINEIEKTLPPKAIIEQYLSHFFEHIFHLIPFASKEMLEESIHTTVQYNELGEVRLSMGTTLIRNKMENLCILLLILRIAYISLTFIEDKIEDYSPYITKEMLEQYPIQSEVIFLAQQILASENWCACANENTISCLLYIWCAFVFSPTEGDFLLEQPSDVIINLVILIGTSIGLHRDPSDFPALNHPEASDKRLLNLRRIQWLSIISMATLESSLKGRLLVSPLSMIDLFIDVRDPNCVEIYKKRVKKDLTGSESDEQLLEIHEIFFHRAQLALFLSDLNNITISYSGSVPMDTLETLRVKANELLKNKFQLRSVDINIYDEEKTFQKLTFNSILNSISLSGQILGKLMMLRASIALMLYFETLAMERSECLSFFYKYFFQCCADTISLIRFFFLYFNGSYEKVLSSLVCFITTKVIQLAVPTTMFTLLVIIMRVELAKNMLLVKCNECNARGDISDLPEIKEKIKSLDTIKENFERLLLEVYLLASQNLRFKYFYIFKMLTLFDVFIQRLRKGQLFSGLFVKVDKDLTTKKIATMLELTLGINLDKSDHLIDRLKGKNLTVNFTLDQLYQIIKEFDRIKNIGVADPQNSLNPSKPNMKDNTPTIELLLNSSVENESVPPYSSSNDPTNVGNASTYSLAHNISNQNNEENMPPSIGSSESNRAAPNLNFMPINNNYNNSGSNINNNDNVKLPSNFKNYYDPPMSSLDISMDVPDIFGSLDFFDYDLLFQND