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NDRG3_HUMAN
ID   NDRG3_HUMAN             Reviewed;         375 AA.
AC   Q9UGV2; A2A2S8; E1P5U7; E1P5U8; Q5TH32; Q96PL8; Q96SM2; Q9BXY7; Q9H3N7;
AC   Q9H411; Q9H8J6;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2002, sequence version 2.
DT   03-AUG-2022, entry version 164.
DE   RecName: Full=Protein NDRG3;
DE   AltName: Full=N-myc downstream-regulated gene 3 protein;
GN   Name=NDRG3;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RX   PubMed=11352569; DOI=10.1006/geno.2000.6496;
RA   Zhou R.-H., Kokame K., Tsukamoto Y., Yutani C., Kato H., Miyata T.;
RT   "Characterization of the human NDRG gene family: a newly identified member,
RT   NDRG4, is specifically expressed in brain and heart.";
RL   Genomics 73:86-97(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA   Mao Y., Xie Y., Zhou Z., Zhao W., Zhao S., Wang W., Huang Y., Wang S.,
RA   Tang R., Chen X., Wu C.;
RL   Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Spleen;
RX   PubMed=11936845; DOI=10.1023/a:1017934810825;
RA   Qu X., Zhai Y., Wei H., Zhang C., Xing G., Yu Y., He F.;
RT   "Characterization and expression of three novel differentiation-related
RT   genes belong to the human NDRG gene family.";
RL   Mol. Cell. Biochem. 229:35-44(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC   TISSUE=Placenta, and Teratocarcinoma;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=11780052; DOI=10.1038/414865a;
RA   Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA   Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA   Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA   Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA   Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA   Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA   Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA   Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA   Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA   Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA   Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA   Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA   Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA   Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA   Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA   Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA   Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA   Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA   Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA   Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA   Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA   Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA   Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT   "The DNA sequence and comparative analysis of human chromosome 20.";
RL   Nature 414:865-871(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Testis;
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   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-322; SER-335; SER-352 AND
RP   SER-374, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [10]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT   refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-331 AND SER-335, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [12]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT   site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [13]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [14]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA   Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT   "System-wide temporal characterization of the proteome and phosphoproteome
RT   of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [15]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [16]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-329; SER-331; THR-332;
RP   SER-334; SER-335; SER-338; SER-341 AND THR-355, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [17]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-331, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q9UGV2-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9UGV2-2; Sequence=VSP_003419;
CC       Name=3;
CC         IsoId=Q9UGV2-3; Sequence=VSP_003420;
CC   -!- TISSUE SPECIFICITY: Ubiquitous. Highly expressed in brain.
CC       {ECO:0000269|PubMed:11352569}.
CC   -!- SIMILARITY: Belongs to the NDRG family. {ECO:0000305}.
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DR   EMBL; AB044943; BAB20067.1; -; mRNA.
DR   EMBL; AF251054; AAK34944.1; -; mRNA.
DR   EMBL; AF308609; AAL08807.1; -; mRNA.
DR   EMBL; AK023618; BAB14620.1; -; mRNA.
DR   EMBL; AK027665; BAB55277.1; -; mRNA.
DR   EMBL; AL031662; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL132768; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471077; EAW76112.1; -; Genomic_DNA.
DR   EMBL; CH471077; EAW76109.1; -; Genomic_DNA.
DR   EMBL; CH471077; EAW76114.1; -; Genomic_DNA.
DR   EMBL; CH471077; EAW76115.1; -; Genomic_DNA.
DR   EMBL; BC136489; AAI36490.1; -; mRNA.
DR   CCDS; CCDS13284.1; -. [Q9UGV2-2]
DR   CCDS; CCDS13285.1; -. [Q9UGV2-1]
DR   RefSeq; NP_071922.2; NM_022477.3. [Q9UGV2-2]
DR   RefSeq; NP_114402.1; NM_032013.3. [Q9UGV2-1]
DR   RefSeq; XP_016883468.1; XM_017027979.1. [Q9UGV2-1]
DR   PDB; 6L4B; X-ray; 2.20 A; A/B/C/D/E/F=1-375.
DR   PDB; 6L4G; X-ray; 3.30 A; A/B=1-375.
DR   PDB; 6L4H; X-ray; 3.40 A; A/B/C/D=1-375.
DR   PDBsum; 6L4B; -.
DR   PDBsum; 6L4G; -.
DR   PDBsum; 6L4H; -.
DR   AlphaFoldDB; Q9UGV2; -.
DR   SMR; Q9UGV2; -.
DR   BioGRID; 121519; 29.
DR   IntAct; Q9UGV2; 7.
DR   MINT; Q9UGV2; -.
DR   STRING; 9606.ENSP00000345292; -.
DR   ESTHER; human-NDRG3; Ndr_family.
DR   MEROPS; S33.987; -.
DR   GlyGen; Q9UGV2; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9UGV2; -.
DR   PhosphoSitePlus; Q9UGV2; -.
DR   BioMuta; NDRG3; -.
DR   DMDM; 20141613; -.
DR   EPD; Q9UGV2; -.
DR   jPOST; Q9UGV2; -.
DR   MassIVE; Q9UGV2; -.
DR   MaxQB; Q9UGV2; -.
DR   PaxDb; Q9UGV2; -.
DR   PeptideAtlas; Q9UGV2; -.
DR   PRIDE; Q9UGV2; -.
DR   ProteomicsDB; 84267; -. [Q9UGV2-1]
DR   ProteomicsDB; 84268; -. [Q9UGV2-2]
DR   ProteomicsDB; 84269; -. [Q9UGV2-3]
DR   Antibodypedia; 11784; 144 antibodies from 29 providers.
DR   DNASU; 57446; -.
DR   Ensembl; ENST00000349004.6; ENSP00000345292.1; ENSG00000101079.21. [Q9UGV2-1]
DR   Ensembl; ENST00000359675.6; ENSP00000352703.2; ENSG00000101079.21. [Q9UGV2-2]
DR   GeneID; 57446; -.
DR   KEGG; hsa:57446; -.
DR   MANE-Select; ENST00000349004.6; ENSP00000345292.1; NM_032013.4; NP_114402.1.
DR   UCSC; uc002xfw.4; human. [Q9UGV2-1]
DR   CTD; 57446; -.
DR   DisGeNET; 57446; -.
DR   GeneCards; NDRG3; -.
DR   HGNC; HGNC:14462; NDRG3.
DR   HPA; ENSG00000101079; Tissue enhanced (retina).
DR   MIM; 605273; gene.
DR   neXtProt; NX_Q9UGV2; -.
DR   OpenTargets; ENSG00000101079; -.
DR   PharmGKB; PA31484; -.
DR   VEuPathDB; HostDB:ENSG00000101079; -.
DR   eggNOG; KOG2931; Eukaryota.
DR   GeneTree; ENSGT00950000182872; -.
DR   HOGENOM; CLU_035361_1_0_1; -.
DR   InParanoid; Q9UGV2; -.
DR   PhylomeDB; Q9UGV2; -.
DR   TreeFam; TF313168; -.
DR   PathwayCommons; Q9UGV2; -.
DR   SignaLink; Q9UGV2; -.
DR   BioGRID-ORCS; 57446; 46 hits in 1080 CRISPR screens.
DR   ChiTaRS; NDRG3; human.
DR   GenomeRNAi; 57446; -.
DR   Pharos; Q9UGV2; Tbio.
DR   PRO; PR:Q9UGV2; -.
DR   Proteomes; UP000005640; Chromosome 20.
DR   RNAct; Q9UGV2; protein.
DR   Bgee; ENSG00000101079; Expressed in cerebellar vermis and 205 other tissues.
DR   ExpressionAtlas; Q9UGV2; baseline and differential.
DR   Genevisible; Q9UGV2; HS.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0030154; P:cell differentiation; NAS:UniProtKB.
DR   GO; GO:0030308; P:negative regulation of cell growth; NAS:UniProtKB.
DR   GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR   GO; GO:0007283; P:spermatogenesis; NAS:UniProtKB.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR004142; NDRG.
DR   InterPro; IPR030692; NDRG3.
DR   PANTHER; PTHR11034; PTHR11034; 1.
DR   PANTHER; PTHR11034:SF20; PTHR11034:SF20; 1.
DR   Pfam; PF03096; Ndr; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..375
FT                   /note="Protein NDRG3"
FT                   /id="PRO_0000159577"
FT   REGION          326..375
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        326..359
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0007744|PubMed:19413330,
FT                   ECO:0007744|PubMed:22814378"
FT   MOD_RES         322
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         329
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         331
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19690332,
FT                   ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT   MOD_RES         332
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         334
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         335
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT   MOD_RES         338
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         341
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         352
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         355
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         361
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9QYF9"
FT   MOD_RES         374
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   VAR_SEQ         20..31
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039,
FT                   ECO:0000303|PubMed:15489334, ECO:0000303|Ref.2"
FT                   /id="VSP_003419"
FT   VAR_SEQ         47..135
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_003420"
FT   CONFLICT        32
FT                   /note="E -> G (in Ref. 3; AAL08807)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        71
FT                   /note="F -> S (in Ref. 4; BAB55277)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        122
FT                   /note="P -> S (in Ref. 2; AAK34944)"
FT                   /evidence="ECO:0000305"
FT   STRAND          31..37
FT                   /evidence="ECO:0007829|PDB:6L4B"
FT   STRAND          40..48
FT                   /evidence="ECO:0007829|PDB:6L4B"
FT   STRAND          52..54
FT                   /evidence="ECO:0007829|PDB:6L4B"
FT   STRAND          56..60
FT                   /evidence="ECO:0007829|PDB:6L4B"
FT   HELIX           67..75
FT                   /evidence="ECO:0007829|PDB:6L4B"
FT   HELIX           78..84
FT                   /evidence="ECO:0007829|PDB:6L4B"
FT   STRAND          89..93
FT                   /evidence="ECO:0007829|PDB:6L4B"
FT   TURN            95..97
FT                   /evidence="ECO:0007829|PDB:6L4B"
FT   HELIX           113..118
FT                   /evidence="ECO:0007829|PDB:6L4B"
FT   HELIX           120..126
FT                   /evidence="ECO:0007829|PDB:6L4B"
FT   STRAND          132..137
FT                   /evidence="ECO:0007829|PDB:6L4B"
FT   HELIX           139..150
FT                   /evidence="ECO:0007829|PDB:6L4B"
FT   TURN            152..154
FT                   /evidence="ECO:0007829|PDB:6L4B"
FT   STRAND          155..162
FT                   /evidence="ECO:0007829|PDB:6L4B"
FT   STRAND          173..176
FT                   /evidence="ECO:0007829|PDB:6L4H"
FT   HELIX           185..193
FT                   /evidence="ECO:0007829|PDB:6L4B"
FT   HELIX           196..201
FT                   /evidence="ECO:0007829|PDB:6L4B"
FT   HELIX           204..215
FT                   /evidence="ECO:0007829|PDB:6L4B"
FT   HELIX           219..230
FT                   /evidence="ECO:0007829|PDB:6L4B"
FT   STRAND          254..261
FT                   /evidence="ECO:0007829|PDB:6L4B"
FT   HELIX           267..275
FT                   /evidence="ECO:0007829|PDB:6L4B"
FT   TURN            279..281
FT                   /evidence="ECO:0007829|PDB:6L4B"
FT   STRAND          282..289
FT                   /evidence="ECO:0007829|PDB:6L4B"
FT   HELIX           294..297
FT                   /evidence="ECO:0007829|PDB:6L4B"
FT   HELIX           299..312
FT                   /evidence="ECO:0007829|PDB:6L4B"
FT   STRAND          315..318
FT                   /evidence="ECO:0007829|PDB:6L4G"
SQ   SEQUENCE   375 AA;  41409 MW;  237B6DF43AAB7F1E CRC64;
     MDELQDVQLT EIKPLLNDKN GTRNFQDFDC QEHDIETTHG VVHVTIRGLP KGNRPVILTY
     HDIGLNHKSC FNAFFNFEDM QEITQHFAVC HVDAPGQQEG APSFPTGYQY PTMDELAEML
     PPVLTHLSLK SIIGIGVGAG AYILSRFALN HPELVEGLVL INVDPCAKGW IDWAASKLSG
     LTTNVVDIIL AHHFGQEELQ ANLDLIQTYR MHIAQDINQD NLQLFLNSYN GRRDLEIERP
     ILGQNDNKSK TLKCSTLLVV GDNSPAVEAV VECNSRLNPI NTTLLKMADC GGLPQVVQPG
     KLTEAFKYFL QGMGYIPSAS MTRLARSRTH STSSSLGSGE SPFSRSVTSN QSDGTQESCE
     SPDVLDRHQT MEVSC
 
 
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