wanglab/gogpt-training-data huggingface dataset:
Protein: Pleckstrin homology domain-containing family O member 2 (PH domain-containing family O member 2) (Pleckstrin homology domain-containing family Q member 1) (PH domain-containing family Q member 1) (Q8K124)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MEEESIKEGSEKPRGARTADKAGWIKKSSGGLLGLWKDRYLLLCQAQLLVYENEDEQKCVETVELGSYEKCQDLRTLLKRKHHRFILLRSPGNKVSDIKFQAPSGEEKESWIKALNEGINRGKNKAFDEVKVDKTCALEHVTRNRVRGGQRRRPPTRIHLKEVASAASDGLSRLDLDVPDSGPPVFAPLSDISEDQPQEPPRALMPPVKPSPGPETSAVEDSKETPAGERALTPDSASSGANPESQEDAETPAKEDSDVKSLPNSTLSEKLKVSWENPSPEKPSAPESAQLSSSETPEATPRESKKPPAPPPKILSEKMKACMSGVDASGSSQSSEAPETTSPEPTQVSVNGMDDGPESALQAMGIPGPAPEDAAASPALPFSDLPSQFHPRSSSLGDLLRESPQHPRLPKEKLYRAQLEVKVASKQTEKLLNQVLGSEPPPVCAESLLSQAVEQLRQATQVLQEMRDLGELNQETPGLVQKRKELVTLYRRSAP
Protein: Interferon gamma (Q6PVS6)
Organism: Ovis aries (Sheep)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
PDVAKGGPLFSEILKNWKEESDKKIIQSQIVSFYFKLFENLKDNQVIQRSMDIIKQDMFQKFLNGSSEKLEDFKRLIQIPVDDLQIQRKAINELIKVMNDLSPKSNLRKRKRSQNLFRGRR
Protein: Uncharacterized membrane protein C1919.04 (O94473)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein {ECO:0000269|PubMed:16823372}. Nucleus membrane {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Uncharacterized membrane protein C70.04c
- Meiotic chromosome segregation protein C17A2.07c
- Meiotic expression up-regulated protein 18
- Uncharacterized protein C18G6.13
- Uncharacterized protein C25B2.08
Sequence:
MDLSFIEGFETIWTVVRAVVLNYLLRSLKILSTILYVSAVISWNVSLKVFGNVLLPGFLTIRTVVIFILRIVSLFLWILADPAILLVQSVYWYFIRAPARFILMVGITLYPLYVLLSWAVFLGIIVGFSLNSVFTFIDSFATPSSNSTVTEAMTKMKNEKVLEYPYKDRNIMLGDLASRIPSKDSEKLDEERQPIALEKTKSLDSISHSSSSSRKSSTELKIPPVETRIVAEIPVPSSVKRRRHRPNKSMGSIKNS
Protein: Frizzled-2 (dFz2) (Q9VVX3)
Organism: Drosophila melanogaster (Fruit fly)
Function: Receptor for Wnt proteins. Most of frizzled receptors are coupled to the beta-catenin canonical signaling pathway, which leads to the activation of disheveled proteins, inhibition of GSK-3 kinase, nuclear accumulation of beta-catenin and activation of Wnt target genes. A second signaling pathway involving PKC and calcium fluxes has been seen for some family members, but it is not yet clear if it represents a distinct pathway or if it can be integrated in the canonical pathway, as PKC seems to be required for Wnt-mediated inactivation of GSK-3 kinase. Both pathways seem to involve interactions with G-proteins. Required to coordinate the cytoskeletons of epidermal cells to produce a parallel array of cuticular hairs and bristles.
Subcellular location: Cell membrane {ECO:0000269|PubMed:10097073}; Multi-pass membrane protein {ECO:0000269|PubMed:10097073}.
Interaction partners:
- Protein wingless
- Segment polarity protein dishevelled
- Low-density lipoprotein receptor-related protein
- Protein Wnt-5
- Protein Wnt-4
- Axin
- Dally-like, isoform A
- Tyrosine-protein kinase transmembrane receptor Ror
- Wnt inhibitor of Dorsal protein
- Tyrosine-protein kinase Drl
Sequence:
MRHNRLKVLILGLVLLLTSCRADGPLHSADHGMGGMGMGGHGLDASPAPGYGVPVIPKDPNLRCEEITIPMCRGIGYNMTSFPNEMNHETQDEAGLEVHQFWPLVEIKCSPDLKFFLCSMYTPICLEDYHKPLPVCRSVCERARSGCAPIMQQYSFEWPERMACEHLPLHGDPDNLCMEQPSYTEAGSGGSSGGSGGSGSGSGSGGKRKQGGSGSGGSGAGGSSGSTSTKPCRGRNSKNCQNPQGEKASGKECSCSCRSPLIFLGKEQLLQQQSQMPMMHHPHHWYMNLTVQRIAGVPNCGIPCKGPFFSNDEKDFAGLWIALWSGLCFCSTLMTLTTFIIDTERFKYPERPIVFLSACYFMVAVGYLSRNFLQNEEIACDGLLLRESSTGPHSCTLVFLLTYFFGMASSIWWVILSFTWFLAAGLKWGNEAITKHSQYFHLAAWLIPTVQSVAVLLLSAVDGDPILGICYVGNLNPDHLKTFVLAPLFVYLVIGTTFLMAGFVSLFRIRSVIKQQGGVGAGVKADKLEKLMIRIGIFSVLYTVPATIVIGCYLYEAAYFEDWIKALACPCAQVKGPGKKPLYSVLMLKYFMALAVGITSGVWIWSGKTLESWRRFWRRLLGAPDRTGANQALIKQRPPIPHPYAGSGMGMPVGSAAGSLLATPYTQAGGASVASTSHHHLHHHVLKQPAASHV
Protein: NADH-quinone oxidoreductase subunit A (EC 7.1.1.-) (NADH dehydrogenase I subunit A) (NDH-1 subunit A) (NUO1) (P0AFC3)
Organism: Escherichia coli (strain K12)
Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
Subcellular location: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_01394, ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01394, ECO:0000269|PubMed:15919996}.
Interaction partners:
- NADH-quinone oxidoreductase subunit G
- NADH-quinone oxidoreductase subunit B
- NADH-quinone oxidoreductase subunit N
- NADH-quinone oxidoreductase subunit K
- NADH-quinone oxidoreductase subunit L
- NADH-quinone oxidoreductase subunit M
- NADH-quinone oxidoreductase subunit J
- NADH-quinone oxidoreductase subunit C/D
- NADH-quinone oxidoreductase subunit H
- NADH-quinone oxidoreductase subunit E
Sequence:
MSMSTSTEVIAHHWAFAIFLIVAIGLCCLMLVGGWFLGGRARARSKNVPFESGIDSVGSARLRLSAKFYLVAMFFVIFDVEALYLFAWSTSIRESGWVGFVEAAIFIFVLLAGLVYLVRIGALDWTPARSRRERMNPETNSIANRQR
Protein: Protein DENND6A (DENN domain-containing protein 6A) (Q8IWF6)
Organism: Homo sapiens (Human)
Function: Guanine nucleotide exchange factor (GEF) for RAB14. Component of an endocytic recycling pathway that is required for the control of ADAM10 transport, shedding of N-cadherin/CDH2 by ADAM9 or ADAM10 and regulation of cell-cell junctions. Required for RAB14 recruitment to recycling endosomes.
Subcellular location: Recycling endosome {ECO:0000269|PubMed:22595670}. Cytoplasm {ECO:0000269|PubMed:22595670}.
Interaction partners:
- DENN domain-containing protein 10
- DENN domain-containing protein 11
- Late secretory pathway protein AVL9 homolog
Sequence:
MALRGPAGLGPGSRRPLDEAVAGAEGREAPALVAAGGAPEDDEEDDGRGRGLLRWDSFSAWLHCVCVVGFDLELGQAVEVIYPQHSKLTDREKTNICYLSFPDSNSGCLGDTQFCFRFRQSSGRRVSLHCLLDQFDKDLPVYLKKDPAYFYGYVYFRQVRDKTLKRGYFQKSLVLISKLPYIHFFHTVLKQIAPEYFEKNEPYLEAACNDVDRWPAPVPGKTLHLPIMGVVMKVRIPTCHDKPGTTQIVQLTQQVDTNISVILPTVHEVDIFRCFCPVFLHSQMLWELVLLGEPLVVMAPSPSESSETVLALVNCISPLKYFSDFRPYFTIHDSEFKEYTTRTQAPPSVILGVTNPFFAKTLQHWPHIIRIGDLKPTGEIPKQVKVKKLKNLKTLDSKPGVYTSYKPYLNRDEEIIKQLQKGVQQKRPSEAQSVILRRYFLELTQSFIIPLERYVASLMPLQKSISPWKSPPQLRQFLPEEFMKTLEKTGPQLTSRIKGDWIGLYRHFLKSPNFDGWFKTRRKEMTQKLEALHLEALCEEDLLLWIQKHTEVETVDLVLKLKNKLLQADREHLPVKPDTMEKLRTHIDAIILALPEDLQGILLKTGMT
Protein: Dapper homolog 2 (mDpr2) (Dapper antagonist of catenin 2) (Q7TN08)
Organism: Mus musculus (Mouse)
Function: Involved in regulation of intracellular signaling pathways during development. Negatively regulates the Nodal signaling pathway, possibly by promoting the lysosomal degradation of Nodal receptors, such as TGFBR1. May be involved in control of the morphogenetic behavior of kidney ureteric bud cells by keeping cells epithelial and restraining their mesenchymal character. May play an inhibitory role in the re-epithelialization of skin wounds by attenuating TGF-beta signaling.
Interaction partners:
- Dapper homolog 3
- Segment polarity protein dishevelled homolog DVL-1
Sequence:
MWAPSGQGPAGWDRRRVGARLRAALAGLQELQGLRATQQARVRGALGLHPAPGPRGQELRLEAALTALREQLSRLRRQDAGLKTHLDQLDQQISELQLDVSRSSCEALDSDSRPSSGFYELSDAGSCSLSTSCASVCSDRLSPSLGSWLPVFQPSKSRSGIGDWRPRSADETTVPAWSPQLTEDSRLLHGAEGTGRLTGMFRPRPVSTGDLERVLPADVGLQRAGTDAAHLLGQGIEIPAHALDPTYQRDLVARGGQEVYPYPSPLHAVALQSPLFALPKEAPCFDICSPPQEPPLVPVDENRTQPEPIRELGSAEAYIHRLLHLRGQELPLRDVGQEQGGDTAAFPPKPCGQRSESTCQLEKQACGADRGGLKLGRGAAKDSLKQHGPVSLVGAEPLSSPLKEETIPWNPCVHGDNTVGSSPCSQAQQPLNDCGQGPVLSPSRVLGTESPPLAPEPFAYTSCTTGETSPVKLRMGFSQNKAVKVRRRVSEKVPRLGKQLPPQPERQRVTERDPSRPHQGGLSRRPTLAREPPGRSCSESTLYPVPFLVPVVVAQRESYPTSPQAFFPMEAALLSSAARRKQRRWQSTMEISAKAGSVSQPGPSMGLPRSPAKRGSGPRAQSRPTLARQDACARCESDPSEHSADCTSLYHSTIAETSEDEEASDHTANRFGDESSSNDSEGCFRGSRRRLAIGSAEAGQGGWAWPRVPPQQPSRAPGNTRPPLPPVPKLCRIKASKALKKKIRRFQPAALKVMTMV
Protein: Diphosphomevalonate decarboxylase (EC 4.1.1.33) (Mevalonate (diphospho)decarboxylase) (MDDase) (Mevalonate pyrophosphate decarboxylase) (P53602)
Organism: Homo sapiens (Human)
Function: Catalyzes the ATP dependent decarboxylation of (R)-5-diphosphomevalonate to form isopentenyl diphosphate (IPP). Functions in the mevalonate (MVA) pathway leading to isopentenyl diphosphate (IPP), a key precursor for the biosynthesis of isoprenoids and sterol synthesis.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14972328}.
Interaction partners:
- Mevalonate kinase
- Isopentenyl-diphosphate Delta-isomerase 1
- Isopentenyl-diphosphate delta-isomerase 2
- Farnesyl pyrophosphate synthase
- Phosphomevalonate kinase
- Geranylgeranyl pyrophosphate synthase
- Hydroxymethylglutaryl-CoA synthase, cytoplasmic
- Lanosterol synthase
- Squalene monooxygenase
- 3-hydroxy-3-methylglutaryl-coenzyme A reductase
Sequence:
MASEKPLAAVTCTAPVNIAVIKYWGKRDEELVLPINSSLSVTLHQDQLKTTTTAVISKDFTEDRIWLNGREEDVGQPRLQACLREIRCLARKRRNSRDGDPLPSSLSCKVHVASVNNFPTAAGLASSAAGYACLAYTLARVYGVESDLSEVARRGSGSACRSLYGGFVEWQMGEQADGKDSIARQVAPESHWPELRVLILVVSAEKKLTGSTVGMRASVETSPLLRFRAESVVPARMAEMARCIRERDFPSFAQLTMKDSNQFHATCLDTFPPISYLNAISWRIIHLVHRFNAHHGDTKVAYTFDAGPNAVIFTLDDTVAEFVAAVWHGFPPGSNGDTFLKGLQVRPAPLSAELQAALAMEPTPGGVKYIIVTQVGPGPQILDDPCAHLLGPDGLPKPAA
Protein: Teratocarcinoma-derived growth factor (Cripto growth factor) (Epidermal growth factor-like Cripto protein) (P51865)
Organism: Mus musculus (Mouse)
Function: GPI-anchored cell membrane protein involved in Nodal signaling. Cell-associated Tdgf1 acts as a Nodal coreceptor in cis. Shedding of Tdgf1 by Tmem8a modulates Nodal signaling by allowing soluble Tdgf1 to act as a Nodal coreceptor on other cells. Could play a role in the determination of the epiblastic cells that subsequently give rise to the mesoderm.
Subcellular location: Cell membrane {ECO:0000269|PubMed:10640699}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:10640699}. Secreted {ECO:0000250|UniProtKB:P13385}. Note=Released from the cell membrane by GPI cleavage. {ECO:0000250|UniProtKB:P13385}.
Interaction partners:
- Activin receptor type-1B
- Left-right determination factor 1
- Activin receptor type-2B
- Nodal
- Activin receptor type-1C
- Endoplasmic reticulum chaperone BiP
- Left-right determination factor 2
- Activin receptor type-2A
- Growth/differentiation factor 3
- Pro-epidermal growth factor
Sequence:
MGYFSSSVVLLVAISSAFEFGPVAGRDLAIRDNSIWDQKEPAVRDRSFQFVPSVGIQNSKSLNKTCCLNGGTCILGSFCACPPSFYGRNCEHDVRKEHCGSILHGTWLPKKCSLCRCWHGQLHCLPQTFLPGCDGHVMDQDLKASGTPCQTPSVTTTFMLAGACLFLDMKV
Protein: Protocadherin-18 (Q9HCL0)
Organism: Homo sapiens (Human)
Function: Potential calcium-dependent cell-adhesion protein.
Subcellular location: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
Interaction partners:
- Divergent protein kinase domain 2A
Sequence:
MHQMNAKMHFRFVFALLIVSFNHDVLGKNLKYRIYEEQRVGSVIARLSEDVADVLLKLPNPSTVRFRAMQRGNSPLLVVNEDNGEISIGATIDREQLCQKNLNCSIEFDVITLPTEHLQLFHIEVEVLDINDNSPQFSRSLIPIEISESAAVGTRIPLDSAFDPDVGENSLHTYSLSANDFFNIEVRTRTDGAKYAELIVVRELDRELKSSYELQLTASDMGVPQRSGSSILKISISDSNDNSPAFEQQSYIIQLLENSPVGTLLLDLNATDPDEGANGKIVYSFSSHVSPKIMETFKIDSERGHLTLFKQVDYEITKSYEIDVQAQDLGPNSIPAHCKIIIKVVDVNDNKPEININLMSPGKEEISYIFEGDPIDTFVALVRVQDKDSGLNGEIVCKLHGHGHFKLQKTYENNYLILTNATLDREKRSEYSLTVIAEDRGTPSLSTVKHFTVQINDINDNPPHFQRSRYEFVISENNSPGAYITTVTATDPDLGENGQVTYTILESFILGSSITTYVTIDPSNGAIYALRIFDHEEVSQITFVVEARDGGSPKQLVSNTTVVLTIIDENDNVPVVIGPALRNNTAEITIPKGAESGFHVTRIRAIDRDSGVNAELSCAIVAGNEENIFIIDPRSCDIHTNVSMDSVPYTEWELSVIIQDKGNPQLHTKVLLKCMIFEYAESVTSTAMTSVSQASLDVSMIIIISLGAICAVLLVIMVLFATRCNREKKDTRSYNCRVAESTYQHHPKRPSRQIHKGDITLVPTINGTLPIRSHHRSSPSSSPTLERGQMGSRQSHNSHQSLNSLVTISSNHVPENFSLELTHATPAVEQVSQLLSMLHQGQYQPRPSFRGNKYSRSYRYALQDMDKFSLKDSGRGDSEAGDSDYDLGRDSPIDRLLGEGFSDLFLTDGRIPAAMRLCTEECRVLGHSDQCWMPPLPSPSSDYRSNMFIPGEEFPTQPQQQHPHQSLEDDAQPADSGEKKKSFSTFGKDSPNDEDTGDTSTSSLLSEMSSVFQRLLPPSLDTYSECSEVDRSNSLERRKGPLPAKTVGYPQGVAAWAASTHFQNPTTNCGPPLGTHSSVQPSSKWLPAMEEIPENYEEDDFDNVLNHLNDGKHELMDASELVAEINKLLQDVRQS
Protein: Cytochrome P450 4A14 (CYPIVA14) (Cytochrome P450-LA-omega 3) (Lauric acid omega-hydroxylase) (Long-chain fatty acid omega-monooxygenase) (EC 1.14.14.80) (P20817)
Organism: Rattus norvegicus (Rat)
Function: A cytochrome P450 monooxygenase that catalyzes omega and omega-1 hydroxylation of saturated fatty acids. Exhibits preferential omega versus omega-1 regioselectivity and (R) versus (S) stereoselectivity for hydroxylation of dodecanoic (lauric) acid. Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (CPR; NADPH-ferrihemoprotein reductase).
Subcellular location: Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein.
Interaction partners:
Sequence:
MGFSVFTPTRSLDGVSGFFQGAFLLSLFLVLFKAVQFYLRRQWLLKALEKFPSTPSHWLWGHDLKDREFQQVLTWVEKFPGACLQWLSGSKTRVLLYDPDYVKVVLGRSDPKASGIYQFLAPWIGYGLLLLNGKKWFQHRRMLTPAFHYGILKPYVKIMADSVNIMLDKWEKLDDQDHPLEIFHYVSLMTLDTVMKCAFSHQGSVQLDVNSRSYTKAVEDLNNLTFFRVRSAFYGNSIIYNMSSDGRLSRRACQIAHEHTDGVIKMRKAQLQNEEELQKARKKRHLDFLDILLFAKMEDGKSLSDEDLRAEVDTFMFEGHDTTASGISWVFYALATHPEHQERCREEVQSILGDGTSVTWDHLDQIPYTTMCIKEALRLYPPVPSVSRELSSPVTFPDGRSIPKGITTTILIYGLHHNPSYWPNPKVFDPSRFSPDSPRHSHAYLPFSGGARNCIGKQFAMNELKVAVALTLLRFELLPDPTRIPVPMARLVLKSKNGIHLRLKKLR
Protein: Cysteine--tRNA ligase, cytoplasmic (EC 6.1.1.16) (Cysteinyl-tRNA synthetase) (CysRS) (P49589)
Organism: Homo sapiens (Human)
Function: Catalyzes the ATP-dependent ligation of cysteine to tRNA(Cys).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:30824121}.
Interaction partners:
- Leucine--tRNA ligase, cytoplasmic
- Elongation factor 1-gamma
- Leucine--tRNA ligase, mitochondrial
- Probable cysteine--tRNA ligase, mitochondrial
- Serine--tRNA ligase, cytoplasmic
- Isoleucine--tRNA ligase, cytoplasmic
- Isoleucine--tRNA ligase, mitochondrial
- Probable proline--tRNA ligase, mitochondrial
- Tyrosine--tRNA ligase, cytoplasmic
- Glycine--tRNA ligase
Sequence:
MADSSGQQGKGRRVQPQWSPPAGTQPCRLHLYNSLTRNKEVFIPQDGKKVTWYCCGPTVYDASHMGHARSYISFDILRRVLKDYFKFDVFYCMNITDIDDKIIKRARQNHLFEQYREKRPEAAQLLEDVQAALKPFSVKLNETTDPDKKQMLERIQHAVQLATEPLEKAVQSRLTGEEVNSCVEVLLEEAKDLLSDWLDSTLGCDVTDNSIFSKLPKFWEGDFHRDMEALNVLPPDVLTRVSEYVPEIVNFVQKIVDNGYGYVSNGSVYFDTAKFASSEKHSYGKLVPEAVGDQKALQEGEGDLSISADRLSEKRSPNDFALWKASKPGEPSWPCPWGKGRPGWHIECSAMAGTLLGASMDIHGGGFDLRFPHHDNELAQSEAYFENDCWVRYFLHTGHLTIAGCKMSKSLKNFITIKDALKKHSARQLRLAFLMHSWKDTLDYSSNTMESALQYEKFLNEFFLNVKDILRAPVDITGQFEKWGEEEAELNKNFYDKKTAIHKALCDNVDTRTVMEEMRALVSQCNLYMAARKAVRKRPNQALLENIALYLTHMLKIFGAVEEDSSLGFPVGGPGTSLSLEATVMPYLQVLSEFREGVRKIAREQKVPEILQLSDALRDNILPELGVRFEDHEGLPTVVKLVDRNTLLKEREEKRRVEEEKRKKKEEAARRKQEQEAAKLAKMKIPPSEMFLSETDKYSKFDENGLPTHDMEGKELSKGQAKKLKKLFEAQEKLYKEYLQMAQNGSFQ
Protein: B-box zinc finger protein 20 (Protein BZR1 SUPPRESSOR 1) (Protein DOUBLE B-BOX 2) (Protein SALT TOLERANCE HOMOLOG 7) (Q0IGM7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Acts as positive regulator of seedling photomorphogenesis. Plays a negative role in brassinosteroid responses.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- F-box/kelch-repeat protein SKIP25
- Transcription factor HY5
- B-box zinc finger protein 32
- Protein BRASSINAZOLE-RESISTANT 1
- GATA transcription factor 2
- B-box type zinc finger family protein
- At5g54470
- B-box domain protein 30
- B-box domain protein 31
- 2-oxoglutarate
Sequence:
MKIWCAVCDKEEASVFCCADEAALCNGCDRHVHFANKLAGKHLRFSLTSPTFKDAPLCDICGERRALLFCQEDRAILCRECDIPIHQANEHTKKHNRFLLTGVKISASPSAYPRASNSNSAAAFGRAKTRPKSVSSEVPSSASNEVFTSSSSTTTSNCYYGIEENYHHVSDSGSGSGCTGSISEYLMETLPGWRVEDLLEHPSCVSYEDNIITNNNNSESYRVYDGSSQFHHQGFWDHKPFS
Protein: MAP kinase-activated protein kinase 5 (MAPK-activated protein kinase 5) (MAPKAP kinase 5) (MAPKAPK-5) (EC 2.7.11.1) (O54992)
Organism: Mus musculus (Mouse)
Function: Tumor suppressor serine/threonine-protein kinase involved in mTORC1 signaling and post-transcriptional regulation. Phosphorylates FOXO3, ERK3/MAPK6, ERK4/MAPK4, HSP27/HSPB1, p53/TP53 and RHEB. Acts as a tumor suppressor by mediating Ras-induced senescence and phosphorylating p53/TP53. Involved in post-transcriptional regulation of MYC by mediating phosphorylation of FOXO3: phosphorylation of FOXO3 leads to promote nuclear localization of FOXO3, enabling expression of miR-34b and miR-34c, 2 post-transcriptional regulators of MYC that bind to the 3'UTR of MYC transcript and prevent MYC translation. Acts as a negative regulator of mTORC1 signaling by mediating phosphorylation and inhibition of RHEB. Part of the atypical MAPK signaling via its interaction with ERK3/MAPK6 or ERK4/MAPK4: the precise role of the complex formed with ERK3/MAPK6 or ERK4/MAPK4 is still unclear, but the complex follows a complex set of phosphorylation events: upon interaction with atypical MAPK (ERK3/MAPK6 or ERK4/MAPK4), ERK3/MAPK6 (or ERK4/MAPK4) is phosphorylated and then mediates phosphorylation and activation of MAPKAPK5, which in turn phosphorylates ERK3/MAPK6 (or ERK4/MAPK4). Mediates phosphorylation of HSP27/HSPB1 in response to PKA/PRKACA stimulation, inducing F-actin rearrangement.
Subcellular location: Cytoplasm. Nucleus. Note=Translocates to the cytoplasm following phosphorylation and activation. Interaction with ERK3/MAPK6 or ERK4/MAPK4 and phosphorylation at Thr-182, activates the protein kinase activity, followed by translocation to the cytoplasm. Phosphorylation by PKA/PRKACA at Ser-115 also induces nuclear export.
Interaction partners:
- Mitogen-activated protein kinase 6
- Heat shock protein beta-1
- Mitogen-activated protein kinase 11
- Mitogen-activated protein kinase 14
- Mitogen-activated protein kinase 12
- Mitogen-activated protein kinase 13
- DnaJ homolog subfamily B member 1
- Mitogen-activated protein kinase 4
- Kalirin
- Septin-7
Sequence:
MSEDSDMEKAIKETSILEEYSINWTQKLGAGISGPVRVCVKKSTQERFALKILLDRPKARNEVRLHMMCATHPNIVQIIEVFANSVQFPHESSPRARLLIVMEMMEGGELFHRISQHRHFTEKQASQVTKQIALALQHCHLLNIAHRDLKPENLLFKDNSLDAPVKLCDFGFAKVDQGDLMTPQFTPYYVAPQVLEAQRRHQKEKSGIIPTSPTPYTYNKSCDLWSLGVIIYVMLCGYPPFYSKHHSRTIPKDMRKKIMTGSFEFPEEEWSQISEMAKDVVRKLLKVKPEERLTIEGVLDHPWLNSTEALDNVLPSAQLMMDKAVVAGIQQAHAEQLANMRIQDLKVSLKPLHSVNNPILRKRKLLGTKPKDGIYIHDHENGTEDSNVALEKLRDVIAQCILPQAGKGENEDEKLNEVMQEAWKYNRECKLLRDALQSFSWNGRGFTDKVDRLKLAEVVKQVIEEQTLPHEPQ
Protein: Gap junction protein (F1SDC3)
Organism: Sus scrofa (Pig)
Subcellular location: Cell junction, gap junction {ECO:0000256|ARBA:ARBA00004610}. Cell membrane {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU000630}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU000630}.
Interaction partners:
- Sodium channel protein
Sequence:
MGDWSFLGEFLEEVHKHSTVIGKVWLTVLFIFRMLVLGTAAESSWGDEQADFQCDTMQPGCENVCYDQAFPISHIRYWVLQIIFVSTPSLVYMGHAMHTVRVQEKRKLREAERAKEVRGAGSYEYPVAEKTELSCWEEVNGRIVLQGTLLNTYVFSILIRTTMEVAFIVGQYLLYGIFLDTLHVCRRSPCPHPVNCYVSRPTEKNVFIVFMLAVAGLSLFLSLAELYHLGWKKIRQRFVKSQQGLAECQLPSPSAGMVQSCTPPPDFSQCLENGPGEKFFSPFSNKVASQQNTDNLATEQVRGQEQIPGEGFIHIRYAQKSEVPNESAPGHRLPHGYQSDKRRLSKASSKARSDDLSV
Protein: Desiccation-related protein PCC3-06 (P23283)
Organism: Craterostigma plantagineum (Blue gem) (Torenia plantagineum)
Interaction partners:
Sequence:
MEAMSFAARSTVLSISKSFPKNNSPTYLTLRPKFSRVRFTTVASQSQGRQQVSENAEDAKKKFSETTDSLKHKTSEATDSASHKANGAARETNDKAKETYNAASGKAGELKDKTQEGAENVREKAMDAGNDAMEKTRNAGERVADGVSNVGQNVKENVMGAGEKVKEFAEDVKDTVMGKSEEVKNQAEHETKKRSTSTNYF
Protein: CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 4 (Alpha 2,3-ST 4) (Beta-galactoside alpha-2,3-sialyltransferase 4) (EC 2.4.3.2) (EC 2.4.3.4) (Alpha 2,3-sialyltransferase IV) (Gal-beta-1,3-GalNAc-alpha-2,3-sialyltransferase) (Gal-beta-1,4-GlcNAc-alpha-2,3-sialyltransferase) (N-acetyllactosaminide alpha-2,3-sialyltransferase) (EC 2.4.3.6) (ST3Gal IV) (ST3GalIV) (Sialyltransferase 4C) (SIAT4-C) (P61131)
Organism: Rattus norvegicus (Rat)
Function: A beta-galactoside alpha2-3 sialyltransferase involved in terminal sialylation of glycoproteins and glycolipids. Catalyzes the transfer of sialic acid (N-acetyl-neuraminic acid; Neu5Ac) from the nucleotide sugar donor CMP-Neu5Ac onto acceptor Galbeta-(1->3)-GalNAc- and Galbeta-(1->4)-GlcNAc-terminated glycoconjugates through an alpha2-3 linkage (By similarity). Plays a major role in hemostasis. Responsible for sialylation of plasma VWF/von Willebrand factor, preventing its recognition by asialoglycoprotein receptors (ASGPR) and subsequent clearance. Regulates ASGPR-mediated clearance of platelets (By similarity). Participates in the biosynthesis of the sialyl Lewis X epitopes, both on O- and N-glycans, which are recognized by SELE/E-selectin, SELP/P-selectin and SELL/L-selectin. Essential for selectin-mediated rolling and adhesion of leukocytes during extravasation (By similarity). Contributes to adhesion and transendothelial migration of neutrophils likely through terminal sialylation of CXCR2 (By similarity). In glycosphingolipid biosynthesis, sialylates GM1 and GA1 gangliosides to form GD1a and GM1b, respectively (By similarity). Metabolizes brain c-series ganglioside GT1c forming GQ1c (Probable). Synthesizes ganglioside LM1 (IV3Neu5Ac-nLc4Cer), a major structural component of peripheral nerve myelin (By similarity).
Subcellular location: Golgi apparatus, Golgi stack membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Note=Membrane-bound form in trans cisternae of Golgi. {ECO:0000250}.
Interaction partners:
- Galactoside alpha-
- Galactoside alpha-
- Hexosyltransferase
- Hexosyltransferase
- Hexosyltransferase
- CMP-N-acetylneuraminate-beta-1,4-galactoside alpha-2,3-sialyltransferase
- L-Fucosyltransferase
- Signal peptide peptidase like 3
- Alpha-
Sequence:
MTSKSHWKLLALALVLVVVMVWYSISREDRYIEFFYFPVSEKKEPCFQGEAERQASKIFGNHSREQPIFLQLKDYFWVKTPSAYELPFGTKGSEDLLLRVLAITSYSIPESIQSLECRRCVVVGNGHRLKNSSLGGVINKYDVVIRLNNAPVAGYEGDVGSKTTIRLFYPESAHFDPKIENNPDTLLVLVAFKAMDFHWIETILSDKKRVRKGFWKQPPLIWDVNPKQIRILNPFFMEIAADKLLSLPIQQPRKIKQKPTTGLLAITLALHLCDLVHIAGFGYPDAYNKKQTIHYYEQITLKSMAGSGHNVSQEAVAIKRMLEMGAVKNLTYF
Protein: B-box zinc finger protein 25 (Protein SALT TOLERANCE HOMOLOG 1) (Salt tolerance-like protein) (Q9SID1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Acts as negative regulator of seedling photomorphogenesis. BBX25/STH and BBX24/STO function as transcriptional corepressors of HY5 activity, leading to the down-regulation of BBX22 expression. BBX25/STH acts additively with BBX24/STO during de-etiolation and the hypocotyl shade avoidance response.
Subcellular location: Nucleus {ECO:0000269|PubMed:23624715}.
Interaction partners:
- Transcription factor HY5
- B-box zinc finger protein 32
- E3 ubiquitin-protein ligase COP1
- B-box type zinc finger family protein
- B-box domain protein 31
- Transcription factor HY5-like
- At5g54470
- B-box domain protein 30
- B-box zinc finger family protein
- Protein CCA1
Sequence:
MKIQCDVCEKAPATLICCADEAALCAKCDVEVHAANKLASKHQRLFLDSLSTKFPPCDICLEKAAFIFCVEDRALLCRDCDEATHAPNTRSANHQRFLATGIRVALSSTSCNQEVEKNHFDPSNQQSLSKPPTQQPAAPSPLWATDEFFSYSDLDCSNKEKEQLDLGELDWLAEMGLFGDQPDQEALPVAEVPELSFSHLAHAHSYNRPMKSNVPNKKQRLEYRYDDEEEHFLVPDLG
Protein: FI17537p1 (Q9VPU4)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- U4/U6 small nuclear ribonucleoprotein Prp31
- U5 small nuclear ribonucleoprotein 200 kDa helicase
- U6 snRNA-associated Sm-like protein LSm6
- Peptidyl-prolyl cis-trans isomerase
- RE11167p
- SD09427p
- Splicing factor 3B subunit 1
- LD24714p
- Putative RNA-binding protein Alsin2
- U6 snRNA-associated Sm-like protein LSm4
Sequence:
MTEYWKSNERKFCDFCKCWLSDNKASVAFHESGKRHKMNVAKRITDISRNSEKSERERQKMDAEIRKMEEAAMKSYAQDVHSRGDMTARSINTVMRATATAAASGGAHSFAGRSRQVDPMRLEGLSDEEEDQRRVAPGKVTSDAAVPEASLWVEGKSDEGHTYYWNVKTNESVWKPPKEGYLSYEEYERINQLAIDQQQISQAEESLKFRANVDEEVARVNREKMKAFRRTDNPKEKKQKEERRQTFKTEEEAATKEIGQWQTVEVKAPEQPIDWQLPKTDYYSAAPVVSASSEPEPPVKKFKEKTIGGLDEEIAATAPATFKRKFIRKGNSRQRAED