wanglab/gogpt-training-data huggingface dataset:
Protein: Protein GIGANTEA (Q9SQI2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in regulation of circadian rhythm and photoperiodic flowering. May play a role in maintenance of circadian amplitude and period length. Is involved in phytochrome B signaling. Stabilizes ADO3 and the circadian photoreceptor ADO1/ZTL. Regulates 'CONSTANS' (CO) in the long-day flowering pathway by modulating the ADO3-dependent protein stability of CDF1 and CDF2, but is not essential to activate CO transcription. Regulates, via the microRNA miR172, a CO-independent pathway that promotes photoperiodic flowering by inducing 'FLOWERING LOCUS T'.
Subcellular location: Nucleus. Cytoplasm.
Interaction partners:
- Adagio protein 1
- Adagio protein 3
- Two-component response regulator-like APRR1
- Cyclic dof factor 1
- Protein EARLY FLOWERING 3
- Adagio protein 2
- E3 ubiquitin-protein ligase COP1
- Two-component response regulator-like APRR3
- Protein LHY
- Protein CCA1
Sequence:
MASSSSSERWIDGLQFSSLLWPPPRDPQQHKDQVVAYVEYFGQFTSEQFPDDIAELVRHQYPSTEKRLLDDVLAMFVLHHPEHGHAVILPIISCLIDGSLVYSKEAHPFASFISLVCPSSENDYSEQWALACGEILRILTHYNRPIYKTEQQNGDTERNCLSKATTSGSPTSEPKAGSPTQHERKPLRPLSPWISDILLAAPLGIRSDYFRWCSGVMGKYAAGELKPPTIASRGSGKHPQLMPSTPRWAVANGAGVILSVCDDEVARYETATLTAVAVPALLLPPPTTSLDEHLVAGLPALEPYARLFHRYYAIATPSATQRLLLGLLEAPPSWAPDALDAAVQLVELLRAAEDYASGVRLPRNWMHLHFLRAIGIAMSMRAGVAADAAAALLFRILSQPALLFPPLSQVEGVEIQHAPIGGYSSNYRKQIEVPAAEATIEATAQGIASMLCAHGPEVEWRICTIWEAAYGLIPLNSSAVDLPEIIVATPLQPPILSWNLYIPLLKVLEYLPRGSPSEACLMKIFVATVETILSRTFPPESSRELTRKARSSFTTRSATKNLAMSELRAMVHALFLESCAGVELASRLLFVVLTVCVSHEAQSSGSKRPRSEYASTTENIEANQPVSNNQTANRKSRNVKGQGPVAAFDSYVLAAVCALACEVQLYPMISGGGNFSNSAVAGTITKPVKINGSSKEYGAGIDSAISHTRRILAILEALFSLKPSSVGTPWSYSSSEIVAAAMVAAHISELFRRSKALTHALSGLMRCKWDKEIHKRASSLYNLIDVHSKVVASIVDKAEPLEAYLKNTPVQKDSVTCLNWKQENTCASTTCFDTAVTSASRTEMNPRGNHKYARHSDEGSGRPSEKGIKDFLLDASDLANFLTADRLAGFYCGTQKLLRSVLAEKPELSFSVVSLLWHKLIAAPEIQPTAESTSAQQGWRQVVDALCNVVSATPAKAAAAVVLQAERELQPWIAKDDEEGQKMWKINQRIVKVLVELMRNHDRPESLVILASASDLLLRATDGMLVDGEACTLPQLELLEATARAIQPVLAWGPSGLAVVDGLSNLLKCRLPATIRCLSHPSAHVRALSTSVLRDIMNQSSIPIKVTPKLPTTEKNGMNSPSYRFFNAASIDWKADIQNCLNWEAHSLLSTTMPTQFLDTAARELGCTISLSQ
Protein: Small ribosomal subunit protein eS25B (40S ribosomal protein S25-B) (RP45) (S31) (YS23) (P0C0T4)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:22096102}.
Interaction partners:
- Small ribosomal subunit protein RACK1
- Small ribosomal subunit protein eS8A
- Small ribosomal subunit protein eS21B
- Small ribosomal subunit protein eS6A
- Small ribosomal subunit protein eS28A
- Small ribosomal subunit protein eS28B
- Small ribosomal subunit protein eS17B
- Small ribosomal subunit protein uS10
- Small ribosomal subunit protein uS8A
- Small ribosomal subunit protein eS7A
Sequence:
MPPKQQLSKAAKAAAALAGGKKSKKKWSKKSMKDRAQHAVILDQEKYDRILKEVPTYRYVSVSVLVDRLKIGGSLARIALRHLEKEGIIKPISKHSKQAIYTRAAASE
Protein: Negative elongation factor B (NELF-B) (Cofactor of BRCA1) (Q8C4Y3)
Organism: Mus musculus (Mouse)
Function: Essential component of the NELF complex, a complex that negatively regulates the elongation of transcription by RNA polymerase II (Pol II). The NELF complex, which acts via an association with the DSIF complex and causes transcriptional pausing, is counteracted by the P-TEFb kinase complex (By similarity). May be able to induce chromatin unfolding (By similarity). Essential for early embryogenesis; plays an important role in maintaining the undifferentiated state of embryonic stem cells (ESCs) by preventing unscheduled expression of developmental genes. Plays a key role in establishing the responsiveness of stem cells to developmental cues; facilitates plasticity and cell fate commitment in ESCs by establishing the appropriate expression level of signaling molecules. Supports the transcription of genes involved in energy metabolism in cardiomyocytes; facilitates the association of transcription initiation factors with the promoters of the metabolism-related genes.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q8WX92}.
Interaction partners:
- Negative elongation factor A
- Negative elongation factor D
- Negative elongation factor E
- Transcription elongation factor SPT5
- Transcription elongation factor SPT4-A
- DNA-directed RNA polymerases I, II, and III subunit RPABC1
- DNA-directed RNA polymerase II subunit RPB3
- DNA-directed RNA polymerase II subunit RPB1
- DNA-directed RNA polymerases I, II, and III subunit RPABC2
- DNA-directed RNA polymerase II subunit RPB9
Sequence:
MFAGLQDLGVANGEDLKETLTNCTEPLKAIEQFQTENGVLLPSLQSALPFLDLHGTPRLEFHQSVFDELRDKLLERVSAIASEGKAEERYKKLEDLLEKSFSLVKMPSLQPVVMCVMKHLPKVPEKKLKLVMADKELYRACAVEVKRQIWQDNQALFGDEVSPLLKQYILEKESALFSTELSVLHNFFSPSPKTRRQGEVVQKLTQMVGKNVKLYDMVLQFLRTLFLRTRNVHYCTLRAELLMSLHDLDVSDICTVDPCHKFTWCLDACIRERFVDSKRARELQGFLDGVKKGQEQVLGDLSMILCDPFAINTLSLSTIRHLQELVSQETLPRDSPDLLLLLRLLALGQGAWDLIDSQVFKEPKMEAELITKFLPMLMSLVVDDFTFNVDQKLPAEEKASVTYPNTLPESFTKFLQEQRMACEVGLYYVLHITKQRNKNALLRLLPGLVETFGDLAFSDIFLHLLTGSLVLLADEFALEDFCSSLFDGFFLTASPRKENVHRHVLRLLLHLHARVAPSKLEALQKALEPTGQSGEAVKELYSQLGEKLEQLDHRKPSPTQAAETPALDLPLPSVPAPATL
Protein: Aurora kinase (EC 2.7.11.1) (Q27393)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSHPSDHVLRPKENAPHRMPEKSAAVLNMQKNLLLGKKPNSENMAPDSKPLPGSSGALIRSAATTVRPATKPGLGGSNSIASSEGNNFQKPMVPSVKKTTSEFAAPAPVAPIKKPESLSKQKPTAASSESSKELGAASSSAEKEKTKTETQPQKPKKTWELNNFDIGRLLGRGKFGNVYLAREKESQFVVALKVLFKRQIGESNVEHQVRREIEIQSHLRHPHILRLYAYFHDDVRIYLILEYAPQGTLFNALQAQPMKRFDERQSATYIQALCSALLYLHERDIIHRDIKPENLLLGHKGVLKIADFGWSVHEPNSMRMTLCGTVDYLPPEMVQGKPHTKNVDLWSLGVLCFELLVGHAPFYSKNYDETYKKILKVDYKLPEHISKAASHLISKLLVLNPQHRLPLDQVMVHPWILAHTQ
Protein: Bublin coiled-coil protein (Q18012)
Organism: Caenorhabditis elegans
Function: Dynamic component of the endotube in intestinal cells, interacts with intermediate filament and regulates intestinal lumen morphology.
Subcellular location: Cell junction {ECO:0000269|PubMed:33857431}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:33857431}. Note=In the intestine, localizes subapically and at cell junctions, indicating localization to the endotube. Interacts with intermediate filament (IF) proteins and localizes to the IF network in an IF-dependent manner. {ECO:0000269|PubMed:33857431}.
Interaction partners:
- FIP
- SNU homolog
- Intermediate filament protein ifd-2
- Histidine ammonia-lyase
Sequence:
MVVEQKEQEPIVKMRDRNVNAAAHSALARGIEALNEGEVTEETEEIRKLDTQLDHLNDYMSKMEERLKAHNDRMMETLKQQKEEREKRRRSFHERMSQNQSEDEEFKKQMSSILKRVQSVKRTEK
Protein: Asporin (A0A1W2Q6A1)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MKEYMMLLLLAVCSAKPFFSPSHTALKTMMLKDMEDTDDEDNDDDDDDNSLFPTKEPVNPFFPFDLFPTCPFGCQCYSRVVHCSDLEMSANPLDNNGIEPGAFEGVTVFHIRIAEAKLTSIPKGLPPTLL
Protein: S-phase kinase associated protein 2 (D6RAG5)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MHRKHLQEIPDLSSNVATSFTWGWDSSKTSELLSGMGVSALEKEEPDSENIPQELLSNLGHPESPPRKRLKSKGSDKDFVIVRRPKLNRENFPDLSTLVRRCPNLVHLDLSDSVMLKNDCFQEFFQLNYLQHLSLSRCYDIIPETLLELGEIPTLKTLQVFGIVPDGTLQLLKEALPHLQINCSHFTTIARPTIGNKKNQEIWGIKCRLTLQKPSCL
Protein: Protein Wnt-10b (Q801F7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Member of the Wnt ligand gene family that encodes for secreted proteins, which activate the Wnt signaling cascade. Involved in neurogenesis. Performs a partially redundant function with wnt1 in the formation of the midbrain-hindbrain boundary (MHB) organizer.
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:O00744}. Secreted {ECO:0000250|UniProtKB:O00744}.
Interaction partners:
- Low density lipoprotein receptor-related protein 5
- Frizzled class receptor 2
- Secreted frizzled-related protein 5.
- Frizzled-5
- Wnt inhibitory factor 1
- Protein wntless homolog
- Porcupine O-acyltransferase
- Secreted frizzled-related protein 1
- Secreted frizzled-related protein 2
- Frizzled class receptor 1
Sequence:
MELPHRQCLGRVLIVTAALLSPAFTVLGNDILGLKVAGEPVLTPNAVCLRLAGLTKKQMRLCVRSPDVTASALQGIQVAIHECQHQLRDQRWNCSSLENHGKLPHQSAILNRGFRESAFSLSLLAAGVVHSVASACSLGKLRGCGCEAKRRLDDDKIRLKLTQLQLQTFQRSGVSLAGAGENTPELSSLHGSLPANLHSSHPMSLLKPLPDEVTMLQDTWEWGGCSHDIRFGVRFSRDWLDSRGSPRDIHARTRIHNNRVGRQVVTDNMRRKCKCHGTSGSCQFKTCWYVSPEFRLVGSLLREKFLTAIFINSQNKNNGVFNSRTGGSTGSDPLRGQRRRSISRELVYFEKSPDFCDREPAVDSLGTQGRICNKSSPGMDGCGSLCCGRGHNILKQARSERCHCRFHWCCYVLCEECKVTEWVNVCK
Protein: ethanolamine-phosphate cytidylyltransferase (EC 2.7.7.14) (CTP:phosphoethanolamine cytidylyltransferase) (A9D2X7)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MSGLAPDGLPKGNRVWADGCYDMVHFGHANQLRQAKQFGQKLIVGVHNDEEIRLHKGPPVFNEQERYRMVAGIKWVDEVVENAPYATTVETLDKYDCDFCVHGDDITLTADGKDTYQEVKDHQRYRECKRTCGVSTTDLVGRMLLLTKNHHTQDEHIEQHVERARSLSTAILEYSKDNVAMSPWTRVSRFIPTTTTILEFAEGRPPKPTDKVVYVTGSFDLFHIGHLAFLEKAKEFGDYLIVGILSDQTVNQYKGSNHPIMSIHERVLSVLAYKPVNEVVFGAPYEITSDILDQFNVQAVINGFRDNNSSVVNSSLASIDPFAEAKRRGIYHEVDSGSDMTTDLIIDRIIHHRLEYETRNKKKEKKEADVAKAMNLI
Protein: Oocyte maturation, alpha (G5E8X8)
Organism: Mus musculus (Mouse)
Interaction partners:
- Oogenesin-3
- Oocyte maturation, beta
- Protein TCL1B1
- Protein TCL1B3
- Protein TCL1B5
Sequence:
MDTLVFTKVHLESWVYKGLRGQHDSILELLKENLHHYLCIEFDEGLNDTVVYIIGFKFFAMFAMFVIVSLACNLRTKRNRARAWARGLQSPVWWNRRYFI
Protein: Uncharacterized protein (Q38CX2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- NADH-ubiquinone oxidoreductase 20 kDa subunit, mitochondrial
- Electron transfer protein, putative
- NADH-ubiquinone oxidoreductase, mitochondrial, putative
- NADH dehydrogenase flavoprotein 1, mitochondrial
- Acyl carrier protein
- Reiske iron-sulfur protein, mitochondrial
- Cytochrome c1, heme protein, mitochondrial
- Mitochondrial processing peptidase, beta subunit, putative
- Mitochondrial processing peptidase alpha subunit, putative
- NADH dehydrogenase
Sequence:
MSRRVFARNMNGEISSTWRGGGSEANAMGVNVATFGATGVLGTHIHHLCCYHGFTSIVPFRFRAGMASGVRHLRMAGDGTVGQNFDTDYEIDKEFVVKSILEKVDNVINAVGAWQEPAVYENSQSWFSMEAINVEWPRMLARWCREMGILRLTHMSMVGADLHSPSKLLRQKRAAEIAVLEEFPTATIIRGTDIFAENDYSYSRYLMAQRKYKIVPMPNRGQRIHQPVFAGDLAEATCRSILLDHTEGRIAELGGPVRFTTADYLRWCADCNGVLNLTWHMPKWMWRVGCTLNERLPIKQGILLGTKAPSWNTDWLERQFIDNCATPERDPELLDWEDFGIPREDLYRMEEKYFITSAMWSQDSPYLDLAPRM
Protein: Coiled-coil domain-containing protein 57 (Q2TAC2)
Organism: Homo sapiens (Human)
Function: Pleiotropic regulator of centriole duplication, mitosis, and ciliogenesis. Critical interface between centrosome and microtubule-mediated cellular processes. Centriole duplication protein required for recruitment of CEP63, CEP152, and PLK4 to the centrosome. Independent of its centrosomal targeting, localizes to and interacts with microtubules and regulates microtubule nucleation, stability, and mitotic progression.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:32402286}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriolar satellite {ECO:0000269|PubMed:32402286}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:32402286}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:32402286}. Note=Localizes to resolvable rings at the proximal end of centrioles (PubMed:32402286). In mitotic cells, localizes to spindle microtubules during metaphase (PubMed:32402286). {ECO:0000269|PubMed:32402286}.
Interaction partners:
Sequence:
MLPLGSEPALNELLLRKEEEWRALQAHRTQLQEAALQDTRSQLEEAQGKLRCLQEDFVYNLQVLEERDLELERYDAAFAQAREWEEARRAEVSELKIEAAKLRQALAREARKVEELQQQQQLAFQEHRLELERVHSDKNGEIDHHREQYENLKWTLERKLEELDGELALQRQELLLEFESKMRKREHEFRLQADNMSNTALSRELKVKLLHKELEALKEAGAKAAESLQRAEATNAELERKLQSRAGELQDLEAMSRARVKDLEDKLHSVQLTRKKEEETFKRKHEELDRLAREKDAVLVAVKGAHVEQLQELQTRVLELQAHCETLEAQLRRAEWRQADTAKEKDAAIDQLREDASTVKSAWDAQIAQLSKEMVSRDLQIQTLQEEEVKLKAQVARSQQDIERYKQQLSLAVERERSLERDQVQLGLDWQRRCDDIERDQIQKSEALIQGLSMAKSQVAAKLQETEQALQEQEVVLKAVTLERDQAVQALRMHGLPRPGAQMLLRQHEEEISKDFPSSEIQRLREQNTSLRNAIAQMRKEMEALSHQIPPPIQTAAESTDANQPDPEAGGDAATPDYVLALEAEIRTLKHKFKTLEKHLEDVLDPLKMSSPHAESQPSVRTSTETTGGSAQAGQAGGSVQAGQAGGSVQAGPVSSGLALRKLGDRVQLLNLLVTRLRQKVLREPLEPAALQRELPREVDQVHLEVLELRKQVAELGKHLRIAQHGGAEPSGRKQPPASDAVALGREDAKSAEDEAPSRHLGKHQPRSAQVGSRLDALQGPKTQHSIHTVTCKSPRQKEDRSPKPPQAPQHPEEHGRQSHSSSSFASGTLQDMWRLLDLGSSPSGVTSQGDSTPELPAPPAADRRPVKMQAGIATPGMKTAAQAKAKTTGASRSHPAKAKGCQRPPKIRNYNIMD
Protein: Histone-lysine N-methyltransferase, H3 lysine-4 specific (EC 2.1.1.354) (COMPASS component SET1) (Lysine N-methyltransferase 2) (SET domain-containing protein 1) (P38827)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalytic component of the COMPASS (Set1C) complex that specifically mono-, di- and trimethylates histone H3 to form H3K4me1/2/3, which subsequently plays a role in telomere length maintenance and transcription elongation regulation.
Subcellular location: Nucleus {ECO:0000269|PubMed:29071121}. Chromosome {ECO:0000269|PubMed:29071121}. Note=Localizes to the 5' region of active genes transcribed by RNAPII. {ECO:0000269|PubMed:29071121}.
Interaction partners:
- COMPASS component SWD1
- COMPASS component SWD2
- COMPASS component SWD3
- Histone H3
- Histone-lysine N-methyltransferase, H3 lysine-79 specific
- COMPASS component BRE2
- COMPASS component SDC1
- COMPASS component SPP1
- COMPASS component SHG1
- Histone-lysine N-methyltransferase, H3 lysine-36 specific
Sequence:
MSNYYRRAHASSGSYRQPQEQPQYSRSGHYQYSNGHSHQQYSSQYNQRRRYNHNDGTRRRYNDDRPHSSNNASTRQYYATNNSQSGPYVNKKSDISSRRGMSQSRYSNSNVHNTLASSSGSLPTESALLLQQRPPSVLRYNTDNLKSKFHYFDPIKGEFFNKDKMLSWKATDKEFSETGYYVVKELQDGQFKFKIKHRHPEIKASDPRNENGIMTSGKVATHRKCRNSLILLPRISYDRYSLGPPPSCEIVVYPAQDSTTTNIQDISIKNYFKKYGEISHFEAFNDPNSALPLHVYLIKYASSDGKINDAAKAAFSAVRKHESSGCFIMGFKFEVILNKHSILNNIISKFVEINVKKLQKLQENLKKAKEKEAENEKAKELQGKDITLPKEPKVDTLSHSSGSEKRIPYDLLGVVNNRPVLHVSKIFVAKHRFCVEDFKYKLRGYRCAKFIDHPTGIYIIFNDIAHAQTCSNAESGNLTIMSRSRRIPILIKFHLILPRFQNRTRFNKSSSSSNSTNVPIKYESKEEFIEATAKQILKDLEKTLHVDIKKRLIGPTVFDALDHANFPELLAKRELKEKEKRQQIASKIAEDELKRKEEAKRDFDLFGLYGGYAKSNKRNLKRHNSLALDHTSLKRKKLSNGIKPMAHLLNEETDSKETTPLNDEGITRVSKEHDEEDENMTSSSSEEEEEEAPDKKFKSESEPTTPESDHLHGIKPLVPDQNGSSDVLDASSMYKPTATEIPEPVYPPEEYDLKYSQTLSSMDLQNAIKDEEDMLILKQLLSTYTPTVTPETSAALEYKIWQSRRKVLEEEKASDWQIELNGTLFDSELQPGSSFKAEGFRKIADKLKINYLPHRRRVHQPLNTVNIHNERNEYTPELCQREESSNKEPSDSVPQEVSSSRDNRASNRRFQQDIEAQKAAIGTESELLSLNQLNKRKKPVMFARSAIHNWGLYALDSIAAKEMIIEYVGERIRQPVAEMREKRYLKNGIGSSYLFRVDENTVIDATKKGGIARFINHCCDPNCTAKIIKVGGRRRIVIYALRDIAASEELTYDYKFEREKDDEERLPCLCGAPNCKGFLN
Protein: Type 1 fimbriae regulatory protein FimB (P0ADH5)
Organism: Escherichia coli (strain K12)
Function: FimB is one of the 2 regulatory proteins which control the phase variation of type 1 fimbriae in E.coli. These proteins mediate the periodic inversion of a 300bp DNA segment that harbors the promoter for the fimbrial structural gene, FimA. FimB switches FimA on.
Interaction partners:
- Type-1 fimbrial protein, A chain
- Uncharacterized fimbrial-like protein SfmA
- Zinc chaperone YeiR
- Chaperone protein FimC
- Probable fimbrial chaperone SfmC
- Type 1 fimbrin D-mannose specific adhesin
- Fimbrin-like protein FimI
- Uncharacterized fimbrial-like protein SfmH
- Protein FimF
- 1-phosphofructokinase
Sequence:
MKNKADNKKRNFLTHSEIESLLKAANTGPHAARNYCLTLLCFIHGFRASEICRLRISDIDLKAKCIYIHRLKKGFSTTHPLLNKEVQALKNWLSIRTSYPHAESEWVFLSRKGNPLSRQQFYHIISTSGGNAGLSLEIHPHMLRHSCGFALANMGIDTRLIQDYLGHRNIRHTVWYTASNAGRFYGIWDRARGRQRHAVL
Protein: A disintegrin and metalloproteinase with thrombospondin motifs 12 (ADAM-TS 12) (ADAM-TS12) (ADAMTS-12) (EC 3.4.24.-) (P58397)
Organism: Homo sapiens (Human)
Function: Metalloprotease that may play a role in the degradation of COMP. Cleaves also alpha-2 macroglobulin and aggregan. Has anti-tumorigenic properties.
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000250}.
Interaction partners:
- Cartilage oligomeric matrix protein
- Upstream stimulatory factor 2
- Upstream stimulatory factor 1
- SNF-related serine/threonine-protein kinase
- Furin
Sequence:
MPCAQRSWLANLSVVAQLLNFGALCYGRQPQPGPVRFPDRRQEHFIKGLPEYHVVGPVRVDASGHFLSYGLHYPITSSRRKRDLDGSEDWVYYRISHEEKDLFFNLTVNQGFLSNSYIMEKRYGNLSHVKMMASSAPLCHLSGTVLQQGTRVGTAALSACHGLTGFFQLPHGDFFIEPVKKHPLVEGGYHPHIVYRRQKVPETKEPTCGLKDSVNISQKQELWREKWERHNLPSRSLSRRSISKERWVETLVVADTKMIEYHGSENVESYILTIMNMVTGLFHNPSIGNAIHIVVVRLILLEEEEQGLKIVHHAEKTLSSFCKWQKSINPKSDLNPVHHDVAVLLTRKDICAGFNRPCETLGLSHLSGMCQPHRSCNINEDSGLPLAFTIAHELGHSFGIQHDGKENDCEPVGRHPYIMSRQLQYDPTPLTWSKCSEEYITRFLDRGWGFCLDDIPKKKGLKSKVIAPGVIYDVHHQCQLQYGPNATFCQEVENVCQTLWCSVKGFCRSKLDAAADGTQCGEKKWCMAGKCITVGKKPESIPGGWGRWSPWSHCSRTCGAGVQSAERLCNNPEPKFGGKYCTGERKRYRLCNVHPCRSEAPTFRQMQCSEFDTVPYKNELYHWFPIFNPAHPCELYCRPIDGQFSEKMLDAVIDGTPCFEGGNSRNVCINGICKMVGCDYEIDSNATEDRCGVCLGDGSSCQTVRKMFKQKEGSGYVDIGLIPKGARDIRVMEIEGAGNFLAIRSEDPEKYYLNGGFIIQWNGNYKLAGTVFQYDRKGDLEKLMATGPTNESVWIQLLFQVTNPGIKYEYTIQKDGLDNDVEQQMYFWQYGHWTECSVTCGTGIRRQTAHCIKKGRGMVKATFCDPETQPNGRQKKCHEKACPPRWWAGEWEACSATCGPHGEKKRTVLCIQTMVSDEQALPPTDCQHLLKPKTLLSCNRDILCPSDWTVGNWSECSVSCGGGVRIRSVTCAKNHDEPCDVTRKPNSRALCGLQQCPSSRRVLKPNKGTISNGKNPPTLKPVPPPTSRPRMLTTPTGPESMSTSTPAISSPSPTTASKEGDLGGKQWQDSSTQPELSSRYLISTGSTSQPILTSQSLSIQPSEENVSSSDTGPTSEGGLVATTTSGSGLSSSRNPITWPVTPFYNTLTKGPEMEIHSGSGEEREQPEDKDESNPVIWTKIRVPGNDAPVESTEMPLAPPLTPDLSRESWWPPFSTVMEGLLPSQRPTTSETGTPRVEGMVTEKPANTLLPLGGDHQPEPSGKTANRNHLKLPNNMNQTKSSEPVLTEEDATSLITEGFLLNASNYKQLTNGHGSAHWIVGNWSECSTTCGLGAYWRRVECSTQMDSDCAAIQRPDPAKRCHLRPCAGWKVGNWSKCSRNCSGGFKIREIQCVDSRDHRNLRPFHCQFLAGIPPPLSMSCNPEPCEAWQVEPWSQCSRSCGGGVQERGVFCPGGLCDWTKRPTSTMSCNEHLCCHWATGNWDLCSTSCGGGFQKRTVQCVPSEGNKTEDQDQCLCDHKPRPPEFKKCNQQACKKSADLLCTKDKLSASFCQTLKAMKKCSVPTVRAECCFSCPQTHITHTQRQRRQRLLQKSKEL
Protein: AT4g33380/F17M5_140 (Dimethylallyl, adenosine tRNA methylthiotransferase) (Q8VZI6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Vacuolar fusion protein MON1 homolog
- TIP41-like protein
- AP-2 complex subunit mu
- RGS1-HXK1-interacting protein 1
- 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase
- Uncharacterized protein At5g48340
- Pentatricopeptide repeat-containing protein At5g55840
- Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A gamma isoform
- At1g31300/T19E23_12
- Serine/threonine-protein phosphatase PP2A-1 catalytic subunit
Sequence:
MARGGGEWTGGIAGTGVLSFKRITLLVCFFNILIALFVLRFLYASSLHIYSNNDNVVKYTADEIRKMEESIRIRRSKEPTLILQLVKKLKHEVSTAESSTELSPNVKHKLVDEILQRLKSFEDKSNVTQLREVVETWRNEKLEEAKELIQGQNGVNSTLIVEEAGMLVRALELEWDVLSEEIGFWLPAEVTNVEHDDKPEGEEEPEEILAGRPVPAVCNAELHTDYGGAAVRWGLTHHKESAADCCQACLDQAKRAKPGETRCNIWVYCPSEFGCFSPDIYEHKHQECWLKYAEKPKQNFKDRYSETYRNNHPKAPSIVPWVSGVVTA
Protein: BCL2 interacting protein 3 like (A0A8I6ACG8)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}. Mitochondrion membrane {ECO:0000256|ARBA:ARBA00004325}.
Interaction partners:
Sequence:
MSHLVEPPPPLHNNNNNCEEGEQSLPPPAGLNSSWVELPMNSSNGNGNGNGKNGGLEHVPSSSSIHNGDMEKILLDAQHESGQSSSRGSSHCDSPSPQEDGQIMFDVEMHTSRDHSSQSEEEVVDGEKEVEALKKSADWVSDWSSRPENIPPKEFLFRHPKRAASLSMRKSGAMKKGGIFSAEFLKVFIPSLFLSHVLALGLGW
Protein: ABC transporter arginine-binding protein 1 (P30860)
Organism: Escherichia coli (strain K12)
Function: Part of the ABC transporter complex ArtPIQMJ involved in arginine transport. Binds L-arginine with high affinity.
Subcellular location: Periplasm {ECO:0000269|PubMed:8801422}.
Interaction partners:
- Arginine ABC transporter permease protein ArtQ
- Arginine ABC transporter permease protein ArtM
- Arginine transport ATP-binding protein ArtP
- Histidine/lysine/arginine/ornithine transport system permease protein HisM
- Histidine/lysine/arginine/ornithine transport system permease protein HisQ
- Glutamate/aspartate import permease protein GltK
- Glutamine transport system permease protein GlnP
- L-cystine transport system permease protein TcyL
- Glutamate/aspartate import permease protein GltJ
- Inner membrane amino-acid ABC transporter permease protein YhdY
Sequence:
MKKLVLAALLASFTFGASAAEKINFGVSATYPPFESIGANNEIVGFDIDLAKALCKQMQAECTFTNHAFDSLIPSLKFRKYDAVISGMDITPERSKQVSFTTPYYENSAVVIAKKDTYKTFADLKGKRIGMENGTTHQKYIQDQHPEVKTVSYDSYQNAFIDLKNGRIDGVFGDTAVVNEWLKTNPQLGVATEKVTDPQYFGTGLGIAVRPDNKALLEKLNNALAAIKADGTYQKISDQWFPQ
Protein: ARM repeat superfamily protein (Q0WML1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- Snurportin-1
- Importin subunit beta-1
- ARM repeat superfamily protein
- ARM repeat superfamily protein
- At3g02460
- At3g08890
- Protein RMD5 homolog
- Protein MAEA homolog
- Ribosomal RNA-processing protein 8
- GTP-binding nuclear protein Ran-1
Sequence:
MERNYIMKMVCETACSKEAEIRQAAFECLVSIASTYYEVLEHYIQTLFELTSNAVKGDEESVSLQAIEFWSSICDEEIDRQEYDSPASGDSSPPHSSFIEKALPHLVQMLLETLLKQEEDQDHDDDVWNISMAGGTCLGLVARTVGDHVVPLVMPFVEKNISSPDWRCREAATYAFGSILEGPTIDKLAPMVAAGLEFLLNATKDQNNHVRDTTAWTLSRIFEFLHSPDSGFSVISPENLPRIVSVLLESIKDVPNVAEKVCGAIYNLAQGYEDSGASSSLLSPYLTEIITHLLAAAERTDGAESKLRGAAYETLNEVVRCSNLSEASSIIAHLLPAIMKKLAETMDLPIISTDDREKQAEVQASLCGVLQVIIQKLSGREDTKPIIMQSADDIMRLFLRVFGCHSSSVHEEAMLAIGALAYATGAEFVKYMPELFKYLQMGLQNFEEYQVCSITVGVLGDICRALDEKILPFCDQIMGLLIQNLQSGALHRSVKPPIFSCFGDIALAIGAHFERYVAPAVQIMQGAAQVCAQMDTLDEELMDYANQLRRSIFEAYSGILQGFKDTKAELMMPYAQHLLQFVELVSKDPLRDESVTKAAVAAMGDLADVVGENTKQLFQNFTFFGEFLNECLESEDEDLKVTARWTQGMIARLMHPS
Protein: CDKN1A interacting zinc finger protein 1 (Q8VEH2)
Organism: Mus musculus (Mouse)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Cyclin-dependent kinase inhibitor 1
- Msx2-interacting protein
Sequence:
MFNPQLQQQQQLQQQQQQLQQQLQQQQLQQQQQQILQLQQLLQQSPPQASLSIPVSRGLPQQSSPQQLLSLQGLHSTSLLNGPMLQRALLLQQLQGLDQFAMPPATYDGASLTMPTATLGNLRAFNVTAPSLAAPSLTPPQMVTPNLQQFFPQATRQSLLGPPPVGVPINPSQLNHSGRNTQKQARTPSSTTPNRKDSSSQTVPLEDREDPTEGSEEATELQMDTCEDQDSLVGPDSMLSEPQVPEPEPFETLEPPAKRCRSSEESTEKGPTGQPQARVQPQTQMTAPKQTQTPDRLPEPPEVQMLPRIQPQALQIQTQPKLLRQAQTQTSPEHLAPQQDQVEPQVPSQPPWQLQPRETDPPNQAQAQTQPQPLWQAQSQKQAQTQAHPQVPTQAQSQEQTSEKTQDQPQTWPQGSVPPPEQASGPACATEPQLSSHAAEAGSDPDKALPEPVSAQSSEDRSREASAGGLDLGECEKRAGEMLGMWGAGSSLKVTILQSSNSRAFNTTPLTSGPRPGDSTSATPAIASTPSKQSLQFFCYICKASSSSQQEFQDHMSEAQHQQRLGEIQHSSQTCLLSLLPMPRDILEKEAEDPPPKRWCNTCQVYYVGDLIQHRRTQEHKVAKQSLRPFCTICNRYFKTPRKFVEHVKSQGHKDKAQELKTLEKETGSPDEDHFITVDAVGCFESGQEEDEDDDEEEEEEGEIEAEEEFCKQVKPRETSSEQGKGSETYNPNTAYGEDFLVPVMGYVCQICHKFYDSNSELRLSHCKSLAHFENLQKYKAKNPSPPPTRPVSRKCAINARNALTALFTSSHQPSPQDTVKMPSKVKPGSPGLPPPLRRSTRLKT