wanglab/gogpt-training-data huggingface dataset:
Protein: Sister chromatid cohesion protein SCC2 (Protein EMBRYO DEFECTIVE 2773) (Protein SISTER-CHROMATID COHESION 2) (AtSCC2) (A5HEI1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Essential protein required for cell fate determination during embryogenesis. Involved in sister chromatid cohesion during meiosis and mitosis. Forms a complex with SCC4, which is required for the association of the cohesin complex with chromosomes. Plays a structural role in chromatin, especially in centromere organization, chromosomal axis formation, and distribution of the cohesin subunit SCC3 on chromosomes.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q04002}. Chromosome, centromere {ECO:0000250|UniProtKB:Q04002}. Note=Associates with chromatin. {ECO:0000250|UniProtKB:Q04002}.
Interaction partners:
- Sister chromatid cohesion protein SCC4
- Structural maintenance of chromosomes protein 3
- Structural maintenance of chromosomes protein 4
- Sister chromatid cohesion 1 protein 4
- Structural maintenance of chromosomes protein 1
- Sister chromatid cohesion 1 protein 1
- Structural maintenance of chromosomes protein 5
- Protein GRAVITROPIC IN THE LIGHT 1
- Sister chromatid cohesion 1 protein 3
- Structural maintenance of chromosomes protein 6A
Sequence:
MSNPSSSGLGSSSGLTHFGIGLANTVQSEVTPYLPLPSLPIFCGAAEPGEFKLFDEVGQGSGYRSLDRSEILAQSSRIANMLHETDVSYLDLRNEARAPDCNSGEHFQLYDLVLRCNPGAFEYVTPGPTCDPLFTNEGPQKIISEPSVPVKMQRQTDTHLARSIEPEPVKRVLRPNHVEDHSWQHETLTNQSPKDVTAYDSRPETITMNELSASKKPKGKKKRKDDLSSVQPDPSVLQESIVQNFCEMLEDFCGRAEVPGDDRDEAEWSSVPVDEVRVLINELMTIRSKMLLHMVPVDILSRLLRTLDHQIHRAEGLSIYSEHSDSDSVLLVLGALESIHASLAVMANSDMPKQLYKEEIIERILEFSRHQMMAVMSAYDPSYRTGSKPAENLAFEGDDDDDNPDHDMGSASKRRRIVKNSKVKKASVNRISGAVNTALQKLCTILGLLKDLLLVERLSDSCILQLLKTSITTFLVENIQILQLKAISLIGGIYNSYSQHRTYVIDEISQLLWKLPSSKRALRAYLLPDEEQRQIQMVTALLIQLVHNSTSLPETSRQAASGNSILETSVDVGYLTKCHEAATETCCLFWTRVLERFTSFKGQDASEIKLIIENLVMDLLTALNLPEYPSVSPILEVLCVILLHNAGLKSKDVSARIMAIELLGTIAARLKRDAVLCSKDRFWTLLESDSEISVDQVCTKDCTFCLGKRAGNLLVCQICQRRFHGDCLGLKELDISSRNWHCPLCVCKRQLLVLQSYCKTDTKGTGKLESEESIENPSMITKTEVVQQMLLNYLQDVGSADDVHTFICWFYLCLWYKDVPKSQNKFKYYIARLKAKSIIRNSGATTSFLTRDAIKQITLALGMNSSFSRGFDKILNMLLASLRENAPNIRAKALRAVSIIVEADPEVLCDKRVQLAVEGRFCDSAISVREAALELVGRHIASHPDVGIKYFEKVAERIKDTGVSVRKRAIKIIRDMCTSNPNFSEFTSACAEILSRISDDESSVQDLVCKTFYEFWFEEPPGHHTQFASDASSIPLELEKKTKQMVGLLSRTPNQQLLVTIIKRALALDFFPQAAKAAGINPVALASVRRRCELMCKCLLEKILQVEEMSREEGEVQVLPYVLVLHAFCLVDPGLCTPASDPTKFVITLQPYLKSQADSRTGAQLLESIIFIIDSVLPLIRKLPLSVTEDLEQDLKHMIVRHSFLTVVHACVRCLCSVSKLAGKGVSIVEHLLQFFFKRLEAQGSDNTQIAGRSLFCLGLLIRHGNSLISTSGGKNFNLSGCLNLFKRHLRTEDIALKVRSLQALGFILIARPEYMLEEDIGKIIETTLADEANGRMKMQALQNMYEYLLDAEKQLGSEKASDNTVNSVEQGGHNVPVAAGAGDTNICGGIVQLFWDKILGRCLDFDDQIRQTSLKIVEVVLRQGLVHPITCVPYLIALETDPQEANQKLAHHLLMNMHEKYPAFFESRLGDGLQMSFIFMQSISQVTSEPNQSLQQKGSTNMLGKNDHASSTLTQARLGVSRIYKLIRGNRVSRNKFMTSIVRKFDNPTWNGSVISFLKYCTETLALLPFTSPDEPLYLVYSINRVMQIRAGAVESNLKALLHKDSAKTQHGNGAYQQDPIPGHMNMMDLNTRIQEEPRHWNSYGHATLIDLNGSVYQDSRDQFTSYQVHNGKADVHKMTSSDPPELSTDDLQKIQVDCLAAIAIQLLLKLKRYLKVTYSLNDDRCQAYSPTEPLKPGDPLSRQSVAFDLSETRTDLPSTYQDLVQRYQEFKNAMREDTVDFTIYSTNVKRKRPTPRKTSRSAKKTVAYNEDDDDDDNDDRGWHGGGGRGAARRLNYSTRSSNRR
Protein: ATP synthase subunit 9, mitochondrial (Q2F971)
Organism: Oryza sativa subsp. indica (Rice)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Mitochondrion membrane {ECO:0000256|RuleBase:RU004221}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU004221}.
Interaction partners:
Sequence:
MLEGAKSIGAGAATIALAGAAVGIGNVLSSSIHSVARNPSLAKQLFGYAILGFALTEAIALFAPMMAFLISFVFR
Protein: Disks large homolog 2 (Channel-associated protein of synapse-110) (Chapsyn-110) (Postsynaptic density protein PSD-93) (Q15700)
Organism: Homo sapiens (Human)
Function: Required for perception of chronic pain through NMDA receptor signaling. Regulates surface expression of NMDA receptors in dorsal horn neurons of the spinal cord. Interacts with the cytoplasmic tail of NMDA receptor subunits as well as inward rectifying potassium channels. Involved in regulation of synaptic stability at cholinergic synapses. Part of the postsynaptic protein scaffold of excitatory synapses (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q63622}; Lipid-anchor {ECO:0000250|UniProtKB:Q63622}. Postsynaptic density {ECO:0000250|UniProtKB:Q63622}. Synapse {ECO:0000250}. Membrane {ECO:0000250|UniProtKB:Q63622}. Cell projection, axon {ECO:0000250|UniProtKB:Q63622}. Perikaryon {ECO:0000250|UniProtKB:Q63622}. Note=Concentrated in soma and postsynaptic density of a subset of neurons. {ECO:0000250|UniProtKB:Q63622}.
Interaction partners:
- Glutamate receptor ionotropic, NMDA 2A
- Glutamate receptor ionotropic, NMDA 2B
- Disks large homolog 3
- Tight junction-associated protein 1
- Disks large homolog 4
- Disks large homolog 1
- Potassium voltage-gated channel subfamily A member 4
- SH3 and multiple ankyrin repeat domains protein 3
- Ubiquitin-protein ligase E3A
- Disintegrin and metalloproteinase domain-containing protein 22
Sequence:
MFFACYCALRTNVKKYRYQDEDAPHDHSLPRLTHEVRGPELVHVSEKNLSQIENVHGYVLQSHISPLKASPAPIIVNTDTLDTIPYVNGTEIEYEFEEITLERGNSGLGFSIAGGTDNPHIGDDPGIFITKIIPGGAAAEDGRLRVNDCILRVNEVDVSEVSHSKAVEALKEAGSIVRLYVRRRRPILETVVEIKLFKGPKGLGFSIAGGVGNQHIPGDNSIYVTKIIDGGAAQKDGRLQVGDRLLMVNNYSLEEVTHEEAVAILKNTSEVVYLKVGKPTTIYMTDPYGPPDITHSYSPPMENHLLSGNNGTLEYKTSLPPISPGRYSPIPKHMLVDDDYTRPPEPVYSTVNKLCDKPASPRHYSPVECDKSFLLSAPYSHYHLGLLPDSEMTSHSQHSTATRQPSMTLQRAVSLEGEPRKVVLHKGSTGLGFNIVGGEDGEGIFVSFILAGGPADLSGELQRGDQILSVNGIDLRGASHEQAAAALKGAGQTVTIIAQYQPEDYARFEAKIHDLREQMMNHSMSSGSGSLRTNQKRSLYVRAMFDYDKSKDSGLPSQGLSFKYGDILHVINASDDEWWQARRVMLEGDSEEMGVIPSKRRVERKERARLKTVKFNAKPGVIDSKGSFNDKRKKSFIFSRKFPFYKNKEQSEQETSDPERGQEDLILSYEPVTRQEINYTRPVIILGPMKDRINDDLISEFPDKFGSCVPHTTRPKRDYEVDGRDYHFVISREQMEKDIQEHKFIEAGQYNDNLYGTSVQSVRFVAERGKHCILDVSGNAIKRLQVAQLYPIAIFIKPRSLEPLMEMNKRLTEEQAKKTYDRAIKLEQEFGEYFTAIVQGDTLEDIYNQCKLVIEEQSGPFIWIPSKEKL
Protein: Envelope glycoprotein K (Syncytial protein) (P68331)
Organism: Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1)
Function: Glycoprotein that probably modulates membrane fusion events during secondary envelopment of cytoplasmic capsids that bud into specific trans-Golgi network (TGN)-derived membranes. Also plays a role, together with gB, in virus-induced cell-to-cell fusion (syncytia formation). Seems to block fusion of virions with infected-cell membranes.
Subcellular location: Host cell membrane; Multi-pass membrane protein. Host endosome membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Host Golgi apparatus membrane; Multi-pass membrane protein. Note=During virion morphogenesis, this protein probably accumulates in the endosomes and trans-Golgi where secondary envelopment occurs. It is probably transported with UL20 to the cell surface from where it is endocytosed and directed to the trans-Golgi network (TGN). Cell surface expression of gK is required for virus-induced cell-to-cell fusion. Likely not present in extracellular virions.
Interaction partners:
Sequence:
MLAVRSLQHLSTVVLITAYGLVLVWYTVFGASPLHRCIYAVRPTGTNNDTALVWMKMNQTLLFLGAPTHPPNGGWRNHAHICYANLIAGRVVPFQVPPDAMNRRIMNVHEAVNCLETLWYTRVRLVVVGWFLYLAFVALHQRRCMFGVVSPAHKMVAPATYLLNYAGRIVSSVFLQYPYTKITRLLCELSVQRQNLVQLFETDPVTFLYHRPAIGVIVGCELMLRFVAVGLIVGTAFISRGACAITYPLFLTITTWCFVSTIGLTELYCILRRGPAPKNADKAAAPGRSKGLSGVCGRCCSIILSGIAVRLCYIAVVAGVVLVALHYEQEIQRRLFDV
Protein: Lactoylglutathione lyase (EC 4.4.1.5) (Aldoketomutase) (Glyoxalase I) (Glx I) (Ketone-aldehyde mutase) (Methylglyoxalase) (S-D-lactoylglutathione methylglyoxal lyase) (Q9HU72)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione.
Interaction partners:
- Hydroxyacylglutathione hydrolase
- Metallo-beta-lactamase domain-containing protein
- Glyoxalase
- Aldoketomutase
- Lactoylglutathione lyase
- Probable 2-hydroxyacid dehydrogenase
- Protein/nucleic acid deglycase HchA
- Tryptophan 2-monooxygenase
- Tryptophan synthase beta chain
- Tryptophan synthase beta chain-like PALP domain-containing protein
Sequence:
MSFNTEVQPGICMEPDAITQEYVFNHTMLRVKDPKRSLDFYSRVLGMRLLRRLDFEEGRFSLYFLAMTRGEEVPDAVDERQRYTFGRQSVLELTHNWGSESDDSQYHNGNQDPRGFGHICFSVPDLVAACERFETLGVNFVKPLDRGMKNVAFISDPDGYWVEIVQASLNGEMGRG
Protein: Kinesin-associated protein 3 (SpKAP115) (Q26626)
Organism: Strongylocentrotus purpuratus (Purple sea urchin)
Function: Binds to the tail domain of the KRP85/KRP95 heterodimer to form a heterotrimeric kinesin-II complex and may regulate the spindle vesicle targeting of this complex.
Interaction partners:
- Kinesin-II 85 kDa subunit
- Kinesin-II 95 kDa subunit
- Kinesin-like protein KIF15
- Kinesin motor domain-containing protein
- Kinesin-like protein
- Uncharacterized protein.
- Uncharacterized protein.
- Kinesin motor domain-containing protein
- ABC_transp_aux domain-containing protein.
- Kinesin heavy chain
Sequence:
MQAEDARYLKRKVKGGSIDVHPTEKALVVNYELEATILGEMGDPMLGERKECQKIIRLRSLNSTTDIAALAREVVEKCKLIHPSKLPEVEQLLYYLQNRKETTQKAGAKKGELTGKLKDPPPYEGTELNEVANINDIEDYIELLYEDNPEKVRGTALILQLARNPDNLEELQSNETVLGALARVLREEWKHSVELATNIVYIFFCFSSFSQFHSIVAHFKIGALVMGVVEHELKKHLSWNEELLKKKKTAEENPASKRDFEKSTKKYHGLLKKQEQLLRVSFYLLLNLSEDPKVELKMKNKNIIRLLIKTLERDNAELLILVVSFLKKLGIYVENKNEMAEQQIIERLAKLVPCDHEDLLNITLRLLLNLSFDTDLRGKMIKLGMLPKFVELLANDNHRLVVLCVLYHVSQDDKAKSMFTYTDCIPMIMKMMLESPTERLEIELVALGINLACNKHNAQLICEGNGLRLLMRRALKFRDPLLLKMIRNISQHDGPSKAQFIEYISDVARIIKESNDEELVVEALGIMANLTIPDLDYEMIINEFGLVPWIKEKLEPGAAEDDLVLEVVMLVGTVATDDSCAAMLAKSGIIQSLIELLNAKQEDDEIVCQIVYVFYQMVFHEATREVIIKLTQAPAYLIDLMHDKNSEIRKVCDNTLDIISEFDEEWARKIKLEKFRWHNSQWLEMVESQQIDDGEGGLMYGDESYSPYIQESDILDRPDLFYGQTGYEDGEMYDGQVTPEYVDEYGNVQNGEYLGRPASAMYGNRYQSEYESLRPGSRVAYLTEDGQPLDEYGNPIEVYAESVDQYGRPVTPTYQYGSQAQQGPGYPY
Protein: UPF0056 inner membrane protein (Q9HUV6)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Subcellular location: Cell inner membrane {ECO:0000256|RuleBase:RU362048}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU362048}. Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
- Secreted protein
- Transmembrane protein
- Probable acyl-CoA dehydrogenase
- Probable transcriptional regulator
Sequence:
MHLLFSVYLKMLVLYSPFFVLSCFISLSRGFGPRDRKRMAWRVALAALIASVALYLFGRYIFILFGITADAFRIGAGSVLFISALGMAQGRAAVQSDNVQQDVTIVPLTIPLTVGPGTIGALLVMGVGQGWEAKLISLVAIFLACLTLGTTLYLSDRIERLLGDQGLQIVSRLMGLFVCALAAQIIVTGLKGSLFPG
Protein: Cytoplasmic tRNA 2-thiolation protein 1 (EC 2.7.7.-) (Cytoplasmic tRNA adenylyltransferase 1) (O94282)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of tRNA(Lys), tRNA(Glu) and tRNA(Gln). Directly binds tRNAs and probably acts by catalyzing adenylation of tRNAs, an intermediate required for 2-thiolation. It is unclear whether it acts as a sulfurtransferase that transfers sulfur from thiocarboxylated urm1 onto the uridine of tRNAs at wobble position. Prior mcm(5) tRNA modification by the elongator complex is required for 2-thiolation. May also be involved in protein urmylation.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03053, ECO:0000269|PubMed:16823372}.
Interaction partners:
- Cytoplasmic tRNA 2-thiolation protein 2
- Adenylyltransferase and sulfurtransferase uba4
- Elongator complex protein 3
- Ubiquitin-related modifier 1
- Probable 3-mercaptopyruvate sulfurtransferase
- Elongator complex protein 4
- Elongator complex protein 1
- Elongator complex protein 5
- DNA replication licensing factor mcm5
- tRNA
Sequence:
MSNKLCQLCNERRPALVRPKTGQKICKECFYYVFETEIHNVIIENKLFVRGERVGIGASGGKDSTVLAYVMKLLNERYDYGLELYLISVDEGIRGYRDDSLDTVKRNQQQYGLPMKIVSYADLYDGWTMDNVVARIGTKNNCTYCGVFRRQALDRAALSLDIHHLVTGHNADDIAETILMNLLRGDVARLPRSTEITTQSDSSPTKRSKPFKYSYEKEIVLYAHYKKLDYFSTECTYSPEAFRGTARAMIKQLENIRPSSILDIIYSGESMQLASSVQEQLPQQTTCERCGFISSNRICKACMLLEGLNKGITGLGLGSDRKTKKLQSQIPACAE
Protein: Intelectin-1 (ITLN-1) (Endothelial lectin HL-1) (Galactofuranose-binding lectin) (Intestinal lactoferrin receptor) (Omentin) (Q8WWA0)
Organism: Homo sapiens (Human)
Function: Lectin that specifically recognizes microbial carbohydrate chains in a calcium-dependent manner. Binds to microbial glycans that contain a terminal acyclic 1,2-diol moiety, including beta-linked D-galactofuranose (beta-Galf), D-phosphoglycerol-modified glycans, D-glycero-D-talo-oct-2-ulosonic acid (KO) and 3-deoxy-D-manno-oct-2-ulosonic acid (KDO). Binds to glycans from Gram-positive and Gram-negative bacteria, including K.pneumoniae, S.pneumoniae, Y.pestis, P.mirabilis and P.vulgaris. Does not bind human glycans. Probably plays a role in the defense system against microorganisms (Probable). May function as adipokine that has no effect on basal glucose uptake but enhances insulin-stimulated glucose uptake in adipocytes. Increases AKT phosphorylation in the absence and presence of insulin. May interact with lactoferrin/LTF and increase its uptake, and may thereby play a role in iron absorption.
Subcellular location: Cell membrane {ECO:0000305|PubMed:11747454}; Lipid-anchor, GPI-anchor {ECO:0000305|PubMed:11747454}. Secreted {ECO:0000269|PubMed:11313366, ECO:0000269|PubMed:16531507, ECO:0000305|PubMed:11747454}. Note=Enriched in lipid rafts. {ECO:0000250|UniProtKB:O88310}.
Interaction partners:
- Lactotransferrin
- Serpin A12
- Intelectin-2
- Resistin-like beta
- Retinoic acid receptor responder protein 2
- Resistin
- Nicotinamide phosphoribosyltransferase
- Adiponectin
- Leptin
Sequence:
MNQLSFLLFLIATTRGWSTDEANTYFKEWTCSSSPSLPRSCKEIKDECPSAFDGLYFLRTENGVIYQTFCDMTSGGGGWTLVASVHENDMRGKCTVGDRWSSQQGSKAVYPEGDGNWANYNTFGSAEAATSDDYKNPGYYDIQAKDLGIWHVPNKSPMQHWRNSSLLRYRTDTGFLQTLGHNLFGIYQKYPVKYGEGKCWTDNGPVIPVVYDFGDAQKTASYYSPYGQREFTAGFVQFRVFNNERAANALCAGMRVTGCNTEHHCIGGGGYFPEASPQQCGDFSGFDWSGYGTHVGYSSSREITEAAVLLFYR
Protein: Dihydroneopterin aldolase (DHNA) (EC 4.1.2.25) (7,8-dihydroneopterin 2'-epimerase) (7,8-dihydroneopterin aldolase) (7,8-dihydroneopterin epimerase) (EC 5.1.99.8) (Dihydroneopterin epimerase) (P0AC16)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the conversion of 7,8-dihydroneopterin to 6-hydroxymethyl-7,8-dihydropterin. Can use L-threo-dihydroneopterin and D-erythro-dihydroneopterin as substrates for the formation of 6-hydroxymethyldihydropterin, but it can also catalyze the epimerization of carbon 2' of dihydroneopterin to dihydromonapterin at appreciable velocity.
Interaction partners:
- 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase
- Dihydropteroate synthase
- GTP cyclohydrolase 1
- Dihydrofolate synthase/folylpolyglutamate synthase
- Dihydromonapterin reductase
- Alkaline phosphatase
- Riboflavin biosynthesis protein RibD
Sequence:
MDIVFIEQLSVITTIGVYDWEQTIEQKLVFDIEMAWDNRKAAKSDDVADCLSYADIAETVVSHVEGARFALVERVAEEVAELLLARFNSPWVRIKLSKPGAVARAANVGVIIERGNNLKENN
Protein: E3 ubiquitin-protein ligase Os03g0188200 (EC 2.3.2.27) (RING-H2 finger protein Os03g0188200) (RING-type E3 ubiquitin transferase Os03g0188200) (Q8H7N9)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Possesses E3 ubiquitin-protein ligase in vitro.
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MAHRRIALAVLVTLLLSAFRPCLAQQSNDDTSKHHRSATAGGFTPTTVVVLVALITAFVLLTVFSVLINRCAQARAPPRRAFRSTASHQPVGGAAAASRASRGLDKEVVEAFPTAVYGDVKARMAAKSGPLECAVCLAEFADSDELRVLPACCHVFHPDCIDPWLAAAVTCPLCRANLTAPPVSLAAAESSDLTAPEEAVQEEESEELDEASLMATFTPESVIDFGATHDHEFDRAGYPHYRRTQSAMDAAPDRHTLRLPEHVMKELAADRRHRRAASLAGYPDSVERTPRWLTSLWRSVSWQRQSRADWDAGEEHGGSKRVHPVAGAQDETPSGSGSDGSKENSDSDALNRV
Protein: RNA helicase (EC 3.6.4.13) (F6TRA5)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAENDVDNELLDYEDDEVETAAGGDGAEAPAKKDVKGSYVSIHSSGFRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLATLQQLEPVTGQVSVLVMCHTRELAFQISKEYERFSKYMPNVKVAVFFGGLSIKKDEEVLKKNCPHIVVGTPGRILALARNKSLNLKHIKHFILDECDKMLEQLDMRRDVQEIFRMTPHEKQVMMFSATLSKEIRPV
Protein: Suppressor of cytokine signaling 7 (SOCS-7) (Q8VHQ2)
Organism: Mus musculus (Mouse)
Function: Regulates signaling cascades probably through protein ubiquitination and/or sequestration. Functions in insulin signaling and glucose homeostasis through IRS1 ubiquitination and subsequent proteasomal degradation. Inhibits also prolactin, growth hormone and leptin signaling by preventing STAT3 and STAT5 activation, sequestering them in the cytoplasm and reducing their binding to DNA. May be a substrate recognition component of a SCF-like E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15242778}. Nucleus {ECO:0000269|PubMed:15242778}. Cell membrane {ECO:0000269|PubMed:15242778}; Peripheral membrane protein {ECO:0000269|PubMed:15242778}; Cytoplasmic side {ECO:0000269|PubMed:15242778}. Note=Mostly cytoplasmic, but shuttles between the cytoplasm and the nucleus. Rapidly relocalizes to the nucleus after UV irradiation. Cytoplasmic location depends upon SEPT7 presence. {ECO:0000250|UniProtKB:O14512}.
Interaction partners:
- Tyrosine-protein kinase JAK2
- Cullin-5
- Signal transducer and activator of transcription 3
- Elongin-C
- Signal transducer and activator of transcription
- Non-receptor tyrosine-protein kinase TYK2
- Signal transducer and activator of transcription 1
- Tyrosine-protein kinase JAK3
- Signal transducer and activator of transcription 5B
- RING-box protein 2
Sequence:
MVFRNVGRPPEEEDAEAAREPGPSELLCPRHRCALDPKALPPGLALERTWGPVAGLEAQLAALGLGQPAGPGIKTAGGGCCPCPCPPQPPPPQPPPPAAAPQAGEDPTETSDALLVLEGLESEAESLETNSCSEEELSSPGRGGGGVGGRLLLQPPGPELPPVPFPLQDLVPPGRLSRGEQQQQQPPPPPPPPGPLRPLAGPSRKGSFKIRLSRLFRTKSCNGGSGGGDGTGKRPSGDLAASAASLTDMGGSAVRELDTGRKPRLTRTQSAFSPVSFSPLFTGETVSLVDVDISQRGLTSPHPPTPPPPPRRSLSLLDDISGTLPTSVLVAPMGSSLQSFPLPPPPPPHAPDAFPRIAPIRASESLHSQPPQHLQCPLYRPDSSSFAASLRELEKCGWYWGPMNWEDAEMKLKGKPDGSFLVRDSSDPRYILSLSFRSQGITHHTRMEHYRGTFSLWCHPKFEDRCQSVVEFIKRAIMHSKNGKFLYFLRSRVPGLPPTPVQLLYPVSRFSNVKSLQHLCRFRIRQLVRIDHIPDLPLPKPLISYIRKFYYYDPQEEVYLSLKEAQLISKQKQEVEPST
Protein: Putative short-chain fatty acid transporter (P76460)
Organism: Escherichia coli (strain K12)
Function: May be responsible for the uptake of short-chain fatty acids.
Subcellular location: Cell inner membrane; Multi-pass membrane protein.
Interaction partners:
- Acetate CoA-transferase subunit beta
- Acetate CoA-transferase subunit alpha
- Acetyl-CoA acetyltransferase
Sequence:
MIGRISRFMTRFVSRWLPDPLIFAMLLTLLTFVIALWLTPQTPISMVKMWGDGFWNLLAFGMQMALIIVTGHALASSAPVKSLLRTAASAAKTPVQGVMLVTFFGSVACVINWGFGLVVGAMFAREVARRVPGSDYPLLIACAYIGFLTWGGGFSGSMPLLAATPGNPVEHIAGLIPVGDTLFSGFNIFITVALIVVMPFITRMMMPKPSDVVSIDPKLLMEEADFQKQLPKDAPPSERLEESRILTLIIGALGIAYLAMYFSEHGFNITINTVNLMFMIAGLLLHKTPMAYMRAISAAARSTAGILVQFPFYAGIQLMMEHSGLGGLITEFFINVANKDTFPVMTFFSSALINFAVPSGGGHWVIQGPFVIPAAQALGADLGKSVMAIAYGEQWMNMAQPFWALPALAIAGLGVRDIMGYCITALLFSGVIFVIGLTLF
Protein: Serine/threonine-protein kinase GRIK1 (EC 2.7.11.1) (Protein GEMINIVIRUS REP INTERACTING KINASE 1) (Protein GRIK1) (SnRK1-activating protein kinase 2) (AtSnAK2) (Q93V58)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Activates SnRK1.1/KIN10 and SnRK1.2/KIN11 by phosphorylation of their activation-loop 'Thr-198' and 'Thr-176', respectively. Required for the regulation by SnRK1 kinases of the transcription of a large set of genes, the modification the activity of metabolic enzymes, and the control of various nutrient-responsive cellular developmental processes.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12172024}. Nucleus {ECO:0000269|PubMed:12172024}. Note=Restricted to the nucleus in cells infected by geminivirus.
Interaction partners:
- PHD finger protein ALFIN-LIKE 1
- SNF1-related protein kinase catalytic subunit alpha KIN10
- At5g06430
- SNF1-related protein kinase regulatory subunit beta-2
- Protein EMSY-LIKE 1
- SNF1-related protein kinase catalytic subunit alpha KIN11
- Mitochondrial fission protein ELM1
- At1g10140
- Sucrose nonfermenting 4-like protein
- SNF1-related protein kinase regulatory subunit beta-1
Sequence:
MFCDSFAFAQVMSCFGCFGGSERSRHSPNPYDDDTYSHDSGETSNPGGDDEEGEEEEEVEELSRSKRSEEILKCKLQNGLVCRQFPVKETNKLTRGEDEDGNKTINEFVRERKIGSGSYGKVVLYRSTVDDKHYAIKAFHKSHLSRLRVAPSETAMGDVLREVMIMKTLEHPNIVNLIEVIDDPEFDDFYMVLEYVDGKWAYDDSGPPGALGEITARKYLRDVVAGLMYLHAHNVIHGDIKPDNLLVTSTGRVKIGDFSVSQVFKDDDDQLRRSPGTPVFTAPECCLGITYSGRSADTWAVGVTLYCMILGQYPFLGDTLQDTYDKIVHNPLIIPEGLNPRLRDLIEGLLCKDPNQRMTLKAVAEHPWITGEDGAISEYCCWCKRKAEEEEDQNHS
Protein: Transaldolase (EC 2.2.1.2) (P15019)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway.
Interaction partners:
- Transketolase 2
- Transketolase 1
- Glucose-6-phosphate isomerase
- Fructose-bisphosphate aldolase
- Triosephosphate isomerase
- Ribulose-phosphate 3-epimerase
- Fructose-1,6-bisphosphatase
- Glyceraldehyde-3-phosphate dehydrogenase 3
- Transaldolase NQM1
- Glyceraldehyde-3-phosphate dehydrogenase 1
Sequence:
MSEPAQKKQKVANNSLEQLKASGTVVVADTGDFGSIAKFQPQDSTTNPSLILAAAKQPTYAKLIDVAVEYGKKHGKTTEEQVENAVDRLLVEFGKEILKIVPGRVSTEVDARLSFDTQATIEKARHIIKLFEQEGVSKERVLIKIASTWEGIQAAKELEEKDGIHCNLTLLFSFVQAVACAEAQVTLISPFVGRILDWYKSSTGKDYKGEADPGVISVKKIYNYYKKYGYKTIVMGASFRSTDEIKNLAGVDYLTISPALLDKLMNSTEPFPRVLDPVSAKKEAGDKISYISDESKFRFDLNEDAMATEKLSEGIRKFSADIVTLFDLIEKKVTA
Protein: Holliday junction branch migration complex subunit RuvB (EC 3.6.4.-) (Q9AE09)
Organism: Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / BCRC 11384 / CCUG 27702 / LMG 3730 / NBRC 12168 / NCIMB 10025 / NRRL B-2784 / 534)
Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an open structure. The RuvB hexamer acts as an ATP-dependent pump, pulling dsDNA into and through the RuvAB complex. RuvB forms 2 homohexamers on either side of HJ DNA bound by 1 or 2 RuvA tetramers; 4 subunits per hexamer contact DNA at a time. Coordinated motions by a converter formed by DNA-disengaged RuvB subunits stimulates ATP hydrolysis and nucleotide exchange. Immobilization of the converter enables RuvB to convert the ATP-contained energy into a lever motion, pulling 2 nucleotides of DNA out of the RuvA tetramer per ATP hydrolyzed, thus driving DNA branch migration. The RuvB motors rotate together with the DNA substrate, which together with the progressing nucleotide cycle form the mechanistic basis for DNA recombination by continuous HJ branch migration. Branch migration allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves cruciform DNA.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00016}.
Interaction partners:
- Holliday junction branch migration complex subunit RuvA
- Crossover junction endodeoxyribonuclease RuvC
- DNA repair protein RecN
- Protein RecA
- DNA polymerase I
- Single-stranded DNA-specific exonuclease
- UvrABC system protein C
- DNA repair protein RecO
- Regulatory protein RecX
- Putative pre-16S rRNA nuclease
Sequence:
MERTEFEIPGGIPPRRNGGQGRAADTNVDANLKPDEYDAEVTLRPKSLTEFIGQPKVRDQLSLVLTGAKNRGVVPDHVLLSGPPGLGKTTMAMIIAQELGTSLRMTSGPALERAGDLAAMLSNLMEGDVLFIDEIHRIARPAEEMLYMAMEDFRIDVIVGKGPGATSIPLEIPPFTLVGATTRSGMLTGPLRDRFGFTAQMEFYDVPDLTKVVKRTAKILDVGIDNDAAVEIASRSRGTPRIANRLLRRVRDFAEVHADGHITMGAANAALIVFDVDEVGLDRLDRAVLDALIRGHGGGPVGVNTLAVAVGEEPGTVEEVCEPYLVRAGMIARTGRGRVATAAAWRHLGLEPPEGTIGDY
Protein: Aleurain-like protease (A8MQZ1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MSAKTILSSVVLVVLVAASAAANIGFDESNPIRMVSDGLREVEESVSQILGQSRHVLSFARFTHRYGKKYQNVEEMKLRFSIFKENLDLIRSTNKKGLSYKLGVNQFADLTWQEFQRTKLGAAQNCSATLKGSHKVTEAALPETKDWREDGIVSPVKDQGGCGSCWTFSTTGALEAAYHQAFGKGISLSEQQLVDCAGAFNNYGCNGGLPSQAFEYIKSNGGLDTEKAYPYTGKDETCKFSAENVGVQVLNSVNITLGAEDELKHAVGLVRPVSIAFEVIHSFRLYKSGVYTDSHCGSTPMDVNHAVLAVGYGVEDGVPYWLIKNSWGADWGDKGYFKMEMGKNMCGKYCYMCIIPRCGLR