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FA83G_MOUSE
ID   FA83G_MOUSE             Reviewed;         812 AA.
AC   Q5SWY7; Q5U437; Q8C1B0;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Protein FAM83G;
GN   Name=Fam83g;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Skin;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryo;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Kidney, and Pancreas;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: May regulate the bone morphogenetic proteins (BMP) pathway.
CC       {ECO:0000250|UniProtKB:A6ND36}.
CC   -!- SUBUNIT: Found in a macromolecular complex with SMAD1. Interacts with
CC       SMAD1 (via MH2 domain); in a SMAD4-independent manner.
CC       {ECO:0000250|UniProtKB:A6ND36}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:A6ND36}. Nucleus {ECO:0000250|UniProtKB:A6ND36}.
CC       Note=Detected predominantly in cytosolic. Upon BMP stimulation, a small
CC       portion of PAWS1 is detected in the nucleus.
CC       {ECO:0000250|UniProtKB:A6ND36}.
CC   -!- PTM: BMP signaling induces the phosphorylation of PAWS1 through BMPR1A
CC       at Ser-609, Ser-613 and Ser-615. In response to BMP phosphorylation at
CC       Ser-609 is necessary for the activation of SMAD4-independent BMP target
CC       genes such as NEDD9 and ASNS. {ECO:0000250|UniProtKB:A6ND36}.
CC   -!- SIMILARITY: Belongs to the FAM83 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC26012.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AK028566; BAC26012.1; ALT_FRAME; mRNA.
DR   EMBL; AL596209; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC085279; AAH85279.1; -; mRNA.
DR   CCDS; CCDS36175.1; -.
DR   RefSeq; NP_848733.2; NM_178618.3.
DR   RefSeq; XP_006534182.1; XM_006534119.3.
DR   AlphaFoldDB; Q5SWY7; -.
DR   SMR; Q5SWY7; -.
DR   STRING; 10090.ENSMUSP00000090697; -.
DR   iPTMnet; Q5SWY7; -.
DR   PhosphoSitePlus; Q5SWY7; -.
DR   MaxQB; Q5SWY7; -.
DR   PaxDb; Q5SWY7; -.
DR   PRIDE; Q5SWY7; -.
DR   ProteomicsDB; 266833; -.
DR   Antibodypedia; 6816; 102 antibodies from 19 providers.
DR   Ensembl; ENSMUST00000093019; ENSMUSP00000090697; ENSMUSG00000042377.
DR   GeneID; 69640; -.
DR   KEGG; mmu:69640; -.
DR   UCSC; uc007jid.1; mouse.
DR   CTD; 644815; -.
DR   MGI; MGI:1916890; Fam83g.
DR   VEuPathDB; HostDB:ENSMUSG00000042377; -.
DR   eggNOG; ENOG502QS42; Eukaryota.
DR   GeneTree; ENSGT00940000157932; -.
DR   HOGENOM; CLU_019056_1_0_1; -.
DR   InParanoid; Q5SWY7; -.
DR   OMA; HSEQMAN; -.
DR   OrthoDB; 354494at2759; -.
DR   PhylomeDB; Q5SWY7; -.
DR   TreeFam; TF330777; -.
DR   BioGRID-ORCS; 69640; 2 hits in 71 CRISPR screens.
DR   ChiTaRS; Fam83g; mouse.
DR   PRO; PR:Q5SWY7; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   RNAct; Q5SWY7; protein.
DR   Bgee; ENSMUSG00000042377; Expressed in lip and 76 other tissues.
DR   Genevisible; Q5SWY7; MM.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0019901; F:protein kinase binding; IBA:GO_Central.
DR   GO; GO:0030509; P:BMP signaling pathway; ISS:UniProtKB.
DR   GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR   InterPro; IPR012461; FAM83_N.
DR   Pfam; PF07894; FAM83; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Nucleus; Phosphoprotein; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:A6ND36"
FT   CHAIN           2..812
FT                   /note="Protein FAM83G"
FT                   /id="PRO_0000330818"
FT   REGION          76..119
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          362..389
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          455..509
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          521..812
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        539..562
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        575..589
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:A6ND36"
FT   MOD_RES         4
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:A6ND36"
FT   MOD_RES         124
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:A6ND36"
FT   MOD_RES         127
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:A6ND36"
FT   MOD_RES         356
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:A6ND36"
FT   MOD_RES         609
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:A6ND36"
FT   MOD_RES         613
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:A6ND36"
FT   MOD_RES         615
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:A6ND36"
FT   MOD_RES         649
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:A6ND36"
FT   CONFLICT        18
FT                   /note="S -> F (in Ref. 3; AAH85279)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        747
FT                   /note="L -> V (in Ref. 1; BAC26012)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        800
FT                   /note="S -> L (in Ref. 3; AAH85279)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   812 AA;  89830 MW;  D3B9A9EBCD15DD15 CRC64;
     MAFSQVQCLD DNHVNWRSSE SKPEFFYSEE QRLALEALVA RGRDAFYEVL KRENIRDFLS
     ELELSRIVEA IEVYDPGSED PRVSGRRPEP QDNGGADASE ETSAAGGPPA TETLPSLEYW
     PQKSDRSIPQ LDLGWPDTIA YRGVTRASVY MQPPIDGQPH IKEVVRKMVS QAQKVIAVVM
     DMFTDVDIFK DLLDAGFKRK VAVYIIVDES NVKYFLHMCE RARMHLGHLK NLRVRSSGGT
     EFFTRSATKF KGVLAQKFMF VDGDRAVCGS YSFTWSAART DRNVISVLSG QVVEMFDRQF
     QELYLMSQSV SLKDIPMEKE PEPEPIVLPS VVPLVPTGTM AKKLVNPKYA LVKAKSVDEI
     AKSSSDKQEV TRPPGLRGPA VAERPGDLSE LLPPVHPGLL NLERANMFEY LPTWVEPDPE
     PGSDILGYIN IIDPNIWNPQ PNQMNRIKIR DTAHASAQHQ LWKQSQGARP CPAPCPPPAP
     RDSQGVVPAE NGFPQGNPEP QAPVPKPRTV PVASVLARDG SDIGWALDTP EKETPQNGID
     PRLPSTASES EVPQQQHSSM TQDDPDGLER GLPNGLDEDE DDDDDYVTLS DQDSLSGSSG
     PGPGHRRPSV ASSMSDEYFE VRERSVPLQR RHSEQMANGP GHPPRRQLSA PHVTRGTFGG
     PLSSPLWAQG RSREDVDASR IQGQRPMDRQ AQGQHFHRHG STTSRTPGPP RFRPAADGTQ
     SSSKKASPAA AGPHHWQPKG SPTPRMLPDP GSPRPTRNTR LRAELRATEE HASPFGIPYS
     KLSQSKHLKA RAGGSQWAPS DSKRRARDHK EP
 
 
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