1433S_HUMAN
ID 1433S_HUMAN Reviewed; 248 AA.
AC P31947; Q6FH30; Q6FH51; Q96DH0;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 225.
DE RecName: Full=14-3-3 protein sigma;
DE AltName: Full=Epithelial cell marker protein 1;
DE AltName: Full=Stratifin;
GN Name=SFN; Synonyms=HME1;
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).
RC TISSUE=Epithelium;
RX PubMed=1390337;
RA Prasad G.L., Valverius E.M., McDuffie E., Cooper H.L.;
RT "Complementary DNA cloning of a novel epithelial cell marker protein, HME1,
RT that may be down-regulated in neoplastic mammary cells.";
RL Cell Growth Differ. 3:507-513(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PROTEIN SEQUENCE OF 19-25;
RP 42-49; 118-122; 130-139; 149-159; 161-181; 196-199; 225-229 AND 231-239.
RC TISSUE=Keratinocyte;
RX PubMed=8515476; DOI=10.1006/jmbi.1993.1346;
RA Leffers H., Madsen P., Rasmussen H.H., Honore B., Andersen A.H., Walbum E.,
RA Vandekerckhove J., Celis J.E.;
RT "Molecular cloning and expression of the transformation sensitive
RT epithelial marker stratifin. A member of a protein family that has been
RT involved in the protein kinase C signalling pathway.";
RL J. Mol. Biol. 231:982-998(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
RX PubMed=9659898; DOI=10.1016/s1097-2765(00)80002-7;
RA Hermeking H., Lengauer C., Polyak K., He T.-C., Zhang L., Thiagalingam S.,
RA Kinzler K.W., Vogelstein B.;
RT "14-3-3 sigma is a p53-regulated inhibitor of G2/M progression.";
RL Mol. Cell 1:3-11(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P.,
RA Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y.,
RA LaBaer J.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Cervix, Lung, and Placenta;
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 [7]
RP PROTEIN SEQUENCE OF 42-49 AND 118-122.
RC TISSUE=Keratinocyte;
RX PubMed=1286667; DOI=10.1002/elps.11501301199;
RA Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E.,
RA Vandekerckhove J.;
RT "Microsequences of 145 proteins recorded in the two-dimensional gel protein
RT database of normal human epidermal keratinocytes.";
RL Electrophoresis 13:960-969(1992).
RN [8]
RP IDENTIFICATION IN A COMPLEX WITH XPO7; ARHGAP1; EIF4A1; VPS26A; VPS29 AND
RP VPS35.
RX PubMed=15282546; DOI=10.1038/sj.emboj.7600338;
RA Mingot J.-M., Bohnsack M.T., Jaekle U., Goerlich D.;
RT "Exportin 7 defines a novel general nuclear export pathway.";
RL EMBO J. 23:3227-3236(2004).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-248, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [10]
RP FUNCTION IN MDM2 UBIQUITINATION, AND UBIQUITINATION BY RFFL.
RX PubMed=18382127; DOI=10.4161/cc.7.5.5701;
RA Yang W., Dicker D.T., Chen J., El-Deiry W.S.;
RT "CARPs enhance p53 turnover by degrading 14-3-3sigma and stabilizing
RT MDM2.";
RL Cell Cycle 7:670-682(2008).
RN [11]
RP INTERACTION WITH GAB2.
RX PubMed=19172738; DOI=10.1038/emboj.2008.159;
RA Brummer T., Larance M., Herrera Abreu M.T., Lyons R.J., Timpson P.,
RA Emmerich C.H., Fleuren E.D.G., Lehrbach G.M., Schramek D., Guilhaus M.,
RA James D.E., Daly R.J.;
RT "Phosphorylation-dependent binding of 14-3-3 terminates signalling by the
RT Gab2 docking protein.";
RL EMBO J. 27:2305-2316(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-248, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-248, AND IDENTIFICATION BY
RP 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 [14]
RP INTERACTION WITH SLITRK1.
RX PubMed=19640509; DOI=10.1016/j.biopsych.2009.05.033;
RA Kajiwara Y., Buxbaum J.D., Grice D.E.;
RT "SLITRK1 binds 14-3-3 and regulates neurite outgrowth in a phosphorylation-
RT dependent manner.";
RL Biol. Psychiatry 66:918-925(2009).
RN [15]
RP INTERACTION WITH SRPK2.
RX PubMed=19592491; DOI=10.1074/jbc.m109.026237;
RA Jang S.W., Liu X., Fu H., Rees H., Yepes M., Levey A., Ye K.;
RT "Interaction of Akt-phosphorylated SRPK2 with 14-3-3 mediates cell cycle
RT and cell death in neurons.";
RL J. Biol. Chem. 284:24512-24525(2009).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5 AND SER-248, AND
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 [17]
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 [18]
RP INTERACTION WITH COPS6 AND COP1.
RX PubMed=21625211; DOI=10.1038/onc.2011.192;
RA Choi H.H., Gully C., Su C.H., Velazquez-Torres G., Chou P.C., Tseng C.,
RA Zhao R., Phan L., Shaiken T., Chen J., Yeung S.C., Lee M.H.;
RT "COP9 signalosome subunit 6 stabilizes COP1, which functions as an E3
RT ubiquitin ligase for 14-3-3sigma.";
RL Oncogene 30:4791-4801(2011).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-74, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
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 [20]
RP INTERACTION WITH PI4KB, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=23572552; DOI=10.1128/mbio.00098-13;
RA Greninger A.L., Knudsen G.M., Betegon M., Burlingame A.L., DeRisi J.L.;
RT "ACBD3 interaction with TBC1 domain 22 protein is differentially affected
RT by enteroviral and kobuviral 3A protein binding.";
RL MBio 4:E00098-E00098(2013).
RN [21]
RP INTERACTION WITH DAPK2.
RX PubMed=26047703; DOI=10.1016/j.bbrc.2015.05.105;
RA Yuasa K., Ota R., Matsuda S., Isshiki K., Inoue M., Tsuji A.;
RT "Suppression of death-associated protein kinase 2 by interaction with 14-3-
RT 3 proteins.";
RL Biochem. Biophys. Res. Commun. 464:70-75(2015).
RN [22]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH PHOSPHOSERINE
RP PEPTIDE.
RX PubMed=15731107; DOI=10.1074/jbc.m500982200;
RA Wilker E.W., Grant R.A., Artim S.C., Yaffe M.B.;
RT "A structural basis for 14-3-3sigma functional specificity.";
RL J. Biol. Chem. 280:18891-18898(2005).
RN [23]
RP X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 1-231 IN COMPLEX WITH PADI6
RP PHOSPHOPEPTIDES.
RX PubMed=22634725; DOI=10.1016/j.jsb.2012.05.010;
RA Rose R., Rose M., Ottmann C.;
RT "Identification and structural characterization of two 14-3-3 binding sites
RT in the human peptidylarginine deiminase type VI.";
RL J. Struct. Biol. 180:65-72(2012).
RN [24] {ECO:0007744|PDB:5MY9, ECO:0007744|PDB:5MYC}
RP X-RAY CRYSTALLOGRAPHY (1.33 ANGSTROMS) OF 1-231 IN COMPLEX WITH LRRK2
RP PHOSPHOPEPTIDE, AND SUBUNIT.
RX PubMed=28202711; DOI=10.1042/bcj20161078;
RA Stevers L.M., de Vries R.M., Doveston R.G., Milroy L.G., Brunsveld L.,
RA Ottmann C.;
RT "Structural interface between LRRK2 and 14-3-3 protein.";
RL Biochem. J. 474:1273-1287(2017).
CC -!- FUNCTION: Adapter protein implicated in the regulation of a large
CC spectrum of both general and specialized signaling pathways. Binds to a
CC large number of partners, usually by recognition of a phosphoserine or
CC phosphothreonine motif. Binding generally results in the modulation of
CC the activity of the binding partner. When bound to KRT17, regulates
CC protein synthesis and epithelial cell growth by stimulating Akt/mTOR
CC pathway. May also regulate MDM2 autoubiquitination and degradation and
CC thereby activate p53/TP53. {ECO:0000269|PubMed:18382127}.
CC -!- FUNCTION: p53-regulated inhibitor of G2/M progression.
CC {ECO:0000269|PubMed:18382127}.
CC -!- SUBUNIT: Homodimer (PubMed:28202711). Interacts with KRT17 and SAMSN1
CC (By similarity). Found in a complex with XPO7, EIF4A1, ARHGAP1, VPS26A,
CC VPS29 and VPS35. Interacts with GAB2. Interacts with SRPK2. Interacts
CC with COPS6. Interacts with COP1; this interaction leads to proteasomal
CC degradation. Interacts with the 'Thr-369' phosphorylated form of DAPK2
CC (PubMed:26047703). Interacts with PI4KB (PubMed:23572552). Interacts
CC with SLITRK1 (PubMed:19640509). Interacts with LRRK2; this interaction
CC is dependent on LRRK2 phosphorylation (PubMed:28202711). {ECO:0000250,
CC ECO:0000250|UniProtKB:O70456, ECO:0000269|PubMed:15282546,
CC ECO:0000269|PubMed:15731107, ECO:0000269|PubMed:19172738,
CC ECO:0000269|PubMed:19592491, ECO:0000269|PubMed:19640509,
CC ECO:0000269|PubMed:21625211, ECO:0000269|PubMed:22634725,
CC ECO:0000269|PubMed:23572552, ECO:0000269|PubMed:26047703,
CC ECO:0000269|PubMed:28202711}.
CC -!- INTERACTION:
CC P31947; P00519: ABL1; NbExp=2; IntAct=EBI-476295, EBI-375543;
CC P31947; Q96IF1: AJUBA; NbExp=2; IntAct=EBI-476295, EBI-949782;
CC P31947; P10398: ARAF; NbExp=3; IntAct=EBI-476295, EBI-365961;
CC P31947; Q92934: BAD; NbExp=6; IntAct=EBI-476295, EBI-700771;
CC P31947; P15056: BRAF; NbExp=3; IntAct=EBI-476295, EBI-365980;
CC P31947; Q68D86: CCDC102B; NbExp=3; IntAct=EBI-476295, EBI-10171570;
CC P31947; Q86Z20: CCDC125; NbExp=3; IntAct=EBI-476295, EBI-11977221;
CC P31947; P51946: CCNH; NbExp=4; IntAct=EBI-476295, EBI-741406;
CC P31947; Q8NHY2: COP1; NbExp=6; IntAct=EBI-476295, EBI-1176214;
CC P31947; Q7L5N1: COPS6; NbExp=7; IntAct=EBI-476295, EBI-486838;
CC P31947; P00533: EGFR; NbExp=9; IntAct=EBI-476295, EBI-297353;
CC P31947; Q9UJM3: ERRFI1; NbExp=3; IntAct=EBI-476295, EBI-2941912;
CC P31947; Q9NYF3: FAM53C; NbExp=3; IntAct=EBI-476295, EBI-1644252;
CC P31947; Q8IZU0: FAM9B; NbExp=3; IntAct=EBI-476295, EBI-10175124;
CC P31947; P98177: FOXO4; NbExp=3; IntAct=EBI-476295, EBI-4481939;
CC P31947; O60269: GPRIN2; NbExp=2; IntAct=EBI-476295, EBI-740397;
CC P31947; P56524: HDAC4; NbExp=4; IntAct=EBI-476295, EBI-308629;
CC P31947; Q9UQL6: HDAC5; NbExp=3; IntAct=EBI-476295, EBI-715576;
CC P31947; Q8WUI4: HDAC7; NbExp=3; IntAct=EBI-476295, EBI-1048378;
CC P31947; Q5T1R4: HIVEP3; NbExp=5; IntAct=EBI-476295, EBI-28989979;
CC P31947; Q14103-4: HNRNPD; NbExp=7; IntAct=EBI-476295, EBI-432545;
CC P31947; Q17RB8: LONRF1; NbExp=3; IntAct=EBI-476295, EBI-2341787;
CC P31947; Q5S007: LRRK2; NbExp=5; IntAct=EBI-476295, EBI-5323863;
CC P31947; P43355: MAGEA1; NbExp=3; IntAct=EBI-476295, EBI-740978;
CC P31947; P78559: MAP1A; NbExp=3; IntAct=EBI-476295, EBI-929047;
CC P31947; Q9Y2U5: MAP3K2; NbExp=2; IntAct=EBI-476295, EBI-357393;
CC P31947; P10636-2: MAPT; NbExp=2; IntAct=EBI-476295, EBI-7796412;
CC P31947; P27448: MARK3; NbExp=2; IntAct=EBI-476295, EBI-707595;
CC P31947; Q13064: MKRN3; NbExp=3; IntAct=EBI-476295, EBI-2340269;
CC P31947; Q96HA8: NTAQ1; NbExp=4; IntAct=EBI-476295, EBI-741158;
CC P31947; P55771: PAX9; NbExp=3; IntAct=EBI-476295, EBI-12111000;
CC P31947; O00444: PLK4; NbExp=2; IntAct=EBI-476295, EBI-746202;
CC P31947; Q96QF0: RAB3IP; NbExp=3; IntAct=EBI-476295, EBI-747844;
CC P31947; P04049: RAF1; NbExp=6; IntAct=EBI-476295, EBI-365996;
CC P31947; Q8NFH8: REPS2; NbExp=2; IntAct=EBI-476295, EBI-7067016;
CC P31947; P31947: SFN; NbExp=4; IntAct=EBI-476295, EBI-476295;
CC P31947; Q13470: TNK1; NbExp=2; IntAct=EBI-476295, EBI-1383444;
CC P31947; P04637: TP53; NbExp=4; IntAct=EBI-476295, EBI-366083;
CC P31947; P61981: YWHAG; NbExp=2; IntAct=EBI-476295, EBI-359832;
CC P31947; P63104: YWHAZ; NbExp=3; IntAct=EBI-476295, EBI-347088;
CC P31947; Q53FD0: ZC2HC1C; NbExp=3; IntAct=EBI-476295, EBI-740767;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus {ECO:0000250}. Secreted.
CC Note=May be secreted by a non-classical secretory pathway.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P31947-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P31947-2; Sequence=VSP_021768;
CC -!- TISSUE SPECIFICITY: Present mainly in tissues enriched in stratified
CC squamous keratinizing epithelium.
CC -!- PTM: Ubiquitinated. Ubiquitination by RFFL induces proteasomal
CC degradation and indirectly regulates p53/TP53 activation.
CC {ECO:0000269|PubMed:18382127}.
CC -!- SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}.
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DR EMBL; M93010; AAA59546.1; -; mRNA.
DR EMBL; X57348; CAA40623.1; -; mRNA.
DR EMBL; AF029081; AAC52029.1; -; Genomic_DNA.
DR EMBL; AF029082; AAC52030.1; -; mRNA.
DR EMBL; CR541905; CAG46703.1; -; mRNA.
DR EMBL; CR541926; CAG46724.1; -; mRNA.
DR EMBL; AL034380; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC000329; AAH00329.1; -; mRNA.
DR EMBL; BC000995; AAH00995.1; -; mRNA.
DR EMBL; BC001550; AAH01550.1; -; mRNA.
DR EMBL; BC002995; AAH02995.1; -; mRNA.
DR EMBL; BC023552; AAH23552.1; -; mRNA.
DR CCDS; CCDS288.1; -. [P31947-1]
DR PIR; S34753; S34753.
DR PIR; S38956; S38956.
DR RefSeq; NP_006133.1; NM_006142.3. [P31947-1]
DR PDB; 1YWT; X-ray; 2.40 A; A/B=1-248.
DR PDB; 1YZ5; X-ray; 2.80 A; A/B=1-248.
DR PDB; 3IQJ; X-ray; 1.15 A; A=1-231.
DR PDB; 3IQU; X-ray; 1.05 A; A=1-231.
DR PDB; 3IQV; X-ray; 1.20 A; A=1-231.
DR PDB; 3LW1; X-ray; 1.28 A; A=1-248.
DR PDB; 3MHR; X-ray; 1.15 A; A=1-231.
DR PDB; 3O8I; X-ray; 2.00 A; A=1-231.
DR PDB; 3P1N; X-ray; 1.40 A; A=1-231.
DR PDB; 3P1O; X-ray; 1.90 A; A=1-231.
DR PDB; 3P1P; X-ray; 1.95 A; A=1-231.
DR PDB; 3P1Q; X-ray; 1.70 A; A=1-231.
DR PDB; 3P1R; X-ray; 1.70 A; A=1-231.
DR PDB; 3P1S; X-ray; 1.65 A; A=1-231.
DR PDB; 3SMK; X-ray; 2.10 A; A=1-231.
DR PDB; 3SML; X-ray; 1.90 A; A=1-231.
DR PDB; 3SMM; X-ray; 2.00 A; A=1-231.
DR PDB; 3SMN; X-ray; 2.00 A; A=1-231.
DR PDB; 3SMO; X-ray; 1.80 A; A=1-231.
DR PDB; 3SP5; X-ray; 1.80 A; A=1-231.
DR PDB; 3SPR; X-ray; 1.99 A; A=1-231.
DR PDB; 3T0L; X-ray; 1.60 A; A=1-231.
DR PDB; 3T0M; X-ray; 1.62 A; A=1-231.
DR PDB; 3U9X; X-ray; 1.80 A; A=1-231.
DR PDB; 3UX0; X-ray; 1.75 A; A=1-231.
DR PDB; 4DAT; X-ray; 1.40 A; A=1-231.
DR PDB; 4DAU; X-ray; 2.00 A; A=1-231.
DR PDB; 4DHM; X-ray; 1.70 A; A=1-231.
DR PDB; 4DHN; X-ray; 1.80 A; A=1-231.
DR PDB; 4DHO; X-ray; 1.70 A; A=1-231.
DR PDB; 4DHP; X-ray; 1.75 A; A=1-231.
DR PDB; 4DHQ; X-ray; 1.75 A; A=1-231.
DR PDB; 4DHR; X-ray; 1.40 A; A=1-231.
DR PDB; 4DHS; X-ray; 1.74 A; A=1-231.
DR PDB; 4DHT; X-ray; 1.80 A; A=1-231.
DR PDB; 4DHU; X-ray; 1.67 A; A=1-231.
DR PDB; 4FL5; X-ray; 1.90 A; A/B=1-231.
DR PDB; 4FR3; X-ray; 1.90 A; A=1-231.
DR PDB; 4IEA; X-ray; 1.70 A; A=1-231.
DR PDB; 4JC3; X-ray; 2.05 A; A=1-231.
DR PDB; 4JDD; X-ray; 2.10 A; A=1-231.
DR PDB; 4QLI; X-ray; 1.45 A; A=1-231.
DR PDB; 4Y32; X-ray; 1.70 A; A/B=1-231.
DR PDB; 4Y3B; X-ray; 1.80 A; A/B=1-231.
DR PDB; 4Y5I; X-ray; 1.40 A; A/B=1-231.
DR PDB; 5BTV; X-ray; 1.70 A; A=1-231.
DR PDB; 5HF3; X-ray; 1.80 A; A=1-231.
DR PDB; 5LTW; X-ray; 4.50 A; A/B/E/F/I/J=1-231.
DR PDB; 5LU1; X-ray; 2.40 A; A/B/E/F=1-231.
DR PDB; 5LU2; X-ray; 2.50 A; A/B=1-231.
DR PDB; 5MHC; X-ray; 1.20 A; A=1-231.
DR PDB; 5MOC; X-ray; 1.80 A; A=1-231.
DR PDB; 5MXO; X-ray; 1.20 A; A=1-231.
DR PDB; 5MY9; X-ray; 1.33 A; A=1-231.
DR PDB; 5MYC; X-ray; 1.46 A; A=1-231.
DR PDB; 5N5R; X-ray; 1.80 A; A=1-231.
DR PDB; 5N5T; X-ray; 1.80 A; A=1-231.
DR PDB; 5N5W; X-ray; 1.37 A; A=1-231.
DR PDB; 5N75; X-ray; 1.80 A; A=1-231.
DR PDB; 5OEG; X-ray; 3.15 A; A=1-231.
DR PDB; 5OEH; X-ray; 2.35 A; A=1-231.
DR PDB; 5OK9; X-ray; 2.35 A; A/B/E/F=1-231.
DR PDB; 5OKF; X-ray; 3.20 A; A/B/C/D=1-231.
DR PDB; 5OM0; X-ray; 3.20 A; A/B=1-231.
DR PDB; 5OMA; X-ray; 3.90 A; A/B/C/D=1-231.
DR PDB; 6FAU; X-ray; 1.25 A; A/C=1-231.
DR PDB; 6FAV; X-ray; 1.40 A; A/C=1-231.
DR PDB; 6FAW; X-ray; 1.40 A; A/C=1-231.
DR PDB; 6FBB; X-ray; 1.30 A; A=1-231.
DR PDB; 6FBW; X-ray; 1.45 A; A/C=1-231.
DR PDB; 6FBY; X-ray; 1.50 A; A/C=1-231.
DR PDB; 6FCP; X-ray; 1.45 A; A=1-231.
DR PDB; 6FI4; X-ray; 2.00 A; A=1-231.
DR PDB; 6FI5; X-ray; 1.70 A; A=1-231.
DR PDB; 6G6X; X-ray; 1.13 A; A=1-231.
DR PDB; 6G8I; X-ray; 1.60 A; A=1-231.
DR PDB; 6G8J; X-ray; 1.47 A; A=1-231.
DR PDB; 6G8K; X-ray; 1.25 A; A=1-231.
DR PDB; 6G8L; X-ray; 1.37 A; A=1-231.
DR PDB; 6G8P; X-ray; 1.90 A; A=1-231.
DR PDB; 6G8Q; X-ray; 1.85 A; A=1-231.
DR PDB; 6GHP; X-ray; 1.95 A; A=1-231.
DR PDB; 6HHP; X-ray; 1.80 A; A=1-231.
DR PDB; 6HKB; X-ray; 1.70 A; A=1-231.
DR PDB; 6HKF; X-ray; 1.80 A; A=1-231.
DR PDB; 6HMT; X-ray; 1.10 A; A=1-231.
DR PDB; 6HMU; X-ray; 1.20 A; A=1-231.
DR PDB; 6HN2; X-ray; 1.70 A; A=1-231.
DR PDB; 6NV2; X-ray; 1.13 A; A=1-231.
DR PDB; 6QDR; X-ray; 1.61 A; A=1-231.
DR PDB; 6QDS; X-ray; 1.72 A; A=1-231.
DR PDB; 6QDT; X-ray; 1.70 A; A=1-231.
DR PDB; 6QDU; X-ray; 1.63 A; A=1-231.
DR PDB; 6QHL; X-ray; 1.20 A; A=1-248.
DR PDB; 6QHM; X-ray; 1.25 A; A=1-248.
DR PDB; 6QIU; X-ray; 1.80 A; A=1-231.
DR PDB; 6QZR; X-ray; 2.30 A; A/B/C/D/E/F/G/H=1-248.
DR PDB; 6QZS; X-ray; 1.90 A; A/B=1-248.
DR PDB; 6R5L; X-ray; 1.88 A; A=1-231.
DR PDB; 6RHC; X-ray; 1.20 A; A=1-231.
DR PDB; 6RJL; X-ray; 1.28 A; A=1-248.
DR PDB; 6RJQ; X-ray; 1.89 A; A=1-248.
DR PDB; 6RJZ; X-ray; 1.58 A; A=1-248.
DR PDB; 6RK8; X-ray; 1.60 A; A=1-248.
DR PDB; 6RKI; X-ray; 1.88 A; A=1-248.
DR PDB; 6RKK; X-ray; 1.88 A; A=1-248.
DR PDB; 6RKM; X-ray; 1.88 A; A=1-248.
DR PDB; 6RL3; X-ray; 1.30 A; A=1-248.
DR PDB; 6RL4; X-ray; 1.60 A; A=1-248.
DR PDB; 6RL6; X-ray; 1.60 A; A=1-248.
DR PDB; 6RM5; X-ray; 1.88 A; A=1-248.
DR PDB; 6RM7; X-ray; 1.60 A; A=1-248.
DR PDB; 6RP6; X-ray; 1.89 A; A=1-231.
DR PDB; 6RWH; X-ray; 1.68 A; A=1-248.
DR PDB; 6RWI; X-ray; 1.65 A; A=1-248.
DR PDB; 6RWS; X-ray; 1.53 A; A=1-248.
DR PDB; 6RWU; X-ray; 1.46 A; A=1-248.
DR PDB; 6RX2; X-ray; 1.82 A; A=1-248.
DR PDB; 6S39; X-ray; 1.88 A; A=1-248.
DR PDB; 6S3C; X-ray; 2.00 A; A=1-248.
DR PDB; 6S40; X-ray; 1.90 A; A=1-248.
DR PDB; 6S9Q; X-ray; 1.69 A; A=1-248.
DR PDB; 6SIN; X-ray; 1.64 A; A=1-231.
DR PDB; 6SIO; X-ray; 1.60 A; A=1-231.
DR PDB; 6SIP; X-ray; 1.60 A; A=1-231.
DR PDB; 6SIQ; X-ray; 1.60 A; A=1-231.
DR PDB; 6SLV; X-ray; 1.90 A; A=1-231.
DR PDB; 6SLW; X-ray; 2.00 A; A=1-248.
DR PDB; 6SLX; X-ray; 1.80 A; A=1-248.
DR PDB; 6T5F; X-ray; 2.63 A; A/B/C/D=1-231.
DR PDB; 6T5H; X-ray; 2.04 A; A/B=1-231.
DR PDB; 6T80; X-ray; 2.99 A; A/B/C/D=1-231.
DR PDB; 6TCH; X-ray; 1.80 A; B=1-231.
DR PDB; 6TJM; X-ray; 1.85 A; A=1-231.
DR PDB; 6TL3; X-ray; 2.46 A; A=1-231.
DR PDB; 6TLF; X-ray; 2.90 A; A=1-248.
DR PDB; 6TLG; X-ray; 2.40 A; A=1-248.
DR PDB; 6TM7; X-ray; 3.00 A; A/B=1-248.
DR PDB; 6TWZ; X-ray; 2.80 A; A/B/C/D=1-231.
DR PDB; 6W0L; X-ray; 2.30 A; A=1-231.
DR PDB; 6XWD; X-ray; 1.60 A; A=1-231.
DR PDB; 6XXC; X-ray; 1.30 A; A=1-231.
DR PDB; 6XY5; X-ray; 1.30 A; A=1-231.
DR PDB; 6Y18; X-ray; 1.30 A; A=1-231.
DR PDB; 6Y1D; X-ray; 1.38 A; A=1-231.
DR PDB; 6Y1J; X-ray; 1.13 A; A=1-248.
DR PDB; 6Y3M; X-ray; 1.50 A; A=1-248.
DR PDB; 6Y3O; X-ray; 1.50 A; A=1-248.
DR PDB; 6Y3R; X-ray; 1.50 A; A=1-248.
DR PDB; 6Y3S; X-ray; 1.95 A; A=1-248.
DR PDB; 6Y3V; X-ray; 1.50 A; A=1-248.
DR PDB; 6Y3W; X-ray; 1.34 A; A=1-231.
DR PDB; 6Y40; X-ray; 1.75 A; A=1-248.
DR PDB; 6Y44; X-ray; 1.71 A; A=1-248.
DR PDB; 6Y58; X-ray; 1.90 A; A=1-231.
DR PDB; 6Y7T; X-ray; 2.50 A; A/F/K/P=1-248.
DR PDB; 6Y8A; X-ray; 1.50 A; A=1-248.
DR PDB; 6Y8B; X-ray; 1.54 A; A=1-248.
DR PDB; 6Y8D; X-ray; 1.51 A; A=1-248.
DR PDB; 6Y8E; X-ray; 1.42 A; A=1-248.
DR PDB; 6YE9; X-ray; 1.80 A; A=1-231.
DR PDB; 6YIA; X-ray; 1.30 A; A=1-231.
DR PDB; 6YIB; X-ray; 1.70 A; A=1-231.
DR PDB; 6YIC; X-ray; 1.60 A; A=1-231.
DR PDB; 6YLU; X-ray; 1.88 A; A=1-231.
DR PDB; 6YOW; X-ray; 1.23 A; A=1-231.
DR PDB; 6YOX; X-ray; 2.05 A; A=1-248.
DR PDB; 6YOY; X-ray; 1.80 A; A=1-231.
DR PDB; 6YP2; X-ray; 1.80 A; A=1-231.
DR PDB; 6YP3; X-ray; 1.80 A; A=1-231.
DR PDB; 6YP8; X-ray; 1.80 A; A=1-231.
DR PDB; 6YPL; X-ray; 1.80 A; A=1-231.
DR PDB; 6YPY; X-ray; 1.40 A; A=1-231.
DR PDB; 6YQ2; X-ray; 1.40 A; A=1-231.
DR PDB; 6YR5; X-ray; 2.25 A; A/B/C/D=1-231.
DR PDB; 6YR6; X-ray; 1.75 A; A/C/E/G=1-231.
DR PDB; 6YR7; X-ray; 2.10 A; A/B=1-231.
DR PDB; 6ZCJ; X-ray; 1.53 A; A=1-231.
DR PDB; 6ZVB; X-ray; 2.51 A; A=1-248.
DR PDB; 6ZVC; X-ray; 2.51 A; A=1-248.
DR PDB; 6ZVD; X-ray; 2.50 A; A=1-248.
DR PDB; 6ZVE; X-ray; 2.51 A; A=1-248.
DR PDB; 7AEW; X-ray; 1.20 A; AAA=1-231.
DR PDB; 7AOG; X-ray; 1.50 A; A=1-248.
DR PDB; 7AXN; X-ray; 1.40 A; A=1-248.
DR PDB; 7AYF; X-ray; 1.75 A; A=1-248.
DR PDB; 7AZ1; X-ray; 1.15 A; A=1-248.
DR PDB; 7AZ2; X-ray; 1.08 A; A=1-248.
DR PDB; 7B13; X-ray; 1.37 A; A=1-231.
DR PDB; 7B15; X-ray; 1.59 A; A=1-231.
DR PDB; 7B9M; X-ray; 1.70 A; A=1-231.
DR PDB; 7B9R; X-ray; 1.15 A; A=1-231.
DR PDB; 7B9T; X-ray; 1.15 A; A=1-231.
DR PDB; 7BA3; X-ray; 1.40 A; A=1-231.
DR PDB; 7BA5; X-ray; 1.45 A; A=1-231.
DR PDB; 7BA6; X-ray; 1.40 A; A=1-231.
DR PDB; 7BA7; X-ray; 1.45 A; A=1-231.
DR PDB; 7BA8; X-ray; 1.20 A; A=1-231.
DR PDB; 7BA9; X-ray; 1.48 A; A=1-231.
DR PDB; 7BAA; X-ray; 1.10 A; A=1-231.
DR PDB; 7BAB; X-ray; 1.30 A; A=1-231.
DR PDB; 7BDP; X-ray; 1.75 A; A=1-248.
DR PDB; 7BDT; X-ray; 1.75 A; A=1-248.
DR PDB; 7BDY; X-ray; 1.80 A; A=1-248.
DR PDB; 7BFW; X-ray; 1.80 A; A=1-248.
DR PDB; 7BG3; X-ray; 1.40 A; A=1-248.
DR PDB; 7BGQ; X-ray; 1.75 A; A=1-248.
DR PDB; 7BGR; X-ray; 1.80 A; A=1-248.
DR PDB; 7BGV; X-ray; 1.68 A; A=1-248.
DR PDB; 7BGW; X-ray; 1.90 A; A=1-248.
DR PDB; 7BI3; X-ray; 1.20 A; A=1-248.
DR PDB; 7BIQ; X-ray; 1.20 A; A=1-248.
DR PDB; 7BIW; X-ray; 1.20 A; A=1-248.
DR PDB; 7BIY; X-ray; 1.80 A; A=1-248.
DR PDB; 7BJB; X-ray; 1.80 A; A=1-248.
DR PDB; 7BJF; X-ray; 1.40 A; A=1-248.
DR PDB; 7BJL; X-ray; 1.40 A; A=1-248.
DR PDB; 7BJW; X-ray; 1.40 A; A=1-248.
DR PDB; 7BKH; X-ray; 1.40 A; A=1-248.
DR PDB; 7BM9; X-ray; 1.80 A; A=1-248.
DR PDB; 7BMC; X-ray; 2.00 A; A=1-248.
DR PDB; 7NFW; X-ray; 1.19 A; A=1-248.
DR PDB; 7NIF; X-ray; 1.71 A; A=1-248.
DR PDB; 7NIG; X-ray; 1.90 A; A=1-248.
DR PDB; 7NIX; X-ray; 1.90 A; A=1-248.
DR PDB; 7NIZ; X-ray; 1.48 A; A=1-248.
DR PDB; 7NJ6; X-ray; 1.59 A; A=1-248.
DR PDB; 7NJ8; X-ray; 1.80 A; A=1-248.
DR PDB; 7NJ9; X-ray; 1.40 A; A=1-248.
DR PDB; 7NJA; X-ray; 1.75 A; A=1-248.
DR PDB; 7NJB; X-ray; 1.40 A; A=1-248.
DR PDB; 7NK3; X-ray; 1.40 A; A=1-248.
DR PDB; 7NK5; X-ray; 1.40 A; A=1-248.
DR PDB; 7NLA; X-ray; 1.40 A; A=1-248.
DR PDB; 7NLE; X-ray; 1.40 A; A=1-248.
DR PDB; 7NM1; X-ray; 1.40 A; A=1-248.
DR PDB; 7NM3; X-ray; 1.40 A; A=1-248.
DR PDB; 7NM9; X-ray; 1.70 A; A=1-248.
DR PDB; 7NMA; X-ray; 1.75 A; A=1-248.
DR PDB; 7NMH; X-ray; 1.40 A; A=1-248.
DR PDB; 7NMW; X-ray; 1.50 A; A=1-248.
DR PDB; 7NMX; X-ray; 2.30 A; A=1-248.
DR PDB; 7NN2; X-ray; 1.80 A; A=1-248.
DR PDB; 7NND; X-ray; 1.40 A; A=1-248.
DR PDB; 7NNE; X-ray; 1.96 A; A=1-248.
DR PDB; 7NP2; X-ray; 1.27 A; A=1-248.
DR PDB; 7NPB; X-ray; 1.37 A; A=1-248.
DR PDB; 7NPG; X-ray; 1.37 A; A=1-248.
DR PDB; 7NQP; X-ray; 1.24 A; A=1-248.
DR PDB; 7NR7; X-ray; 1.40 A; A=1-248.
DR PDB; 7NRK; X-ray; 1.75 A; A=1-248.
DR PDB; 7NRL; X-ray; 1.80 A; A=1-248.
DR PDB; 7NSV; X-ray; 1.33 A; A=1-248.
DR PDB; 7NV4; X-ray; 1.20 A; A=1-231.
DR PDB; 7NVI; X-ray; 1.20 A; A=1-231.
DR PDB; 7NWS; X-ray; 1.20 A; A=1-231.
DR PDB; 7NXS; X-ray; 1.20 A; A=1-231.
DR PDB; 7NXT; X-ray; 1.20 A; A=1-231.
DR PDB; 7NXW; X-ray; 1.20 A; A=1-231.
DR PDB; 7NXY; X-ray; 1.20 A; A=1-231.
DR PDB; 7NY4; X-ray; 1.40 A; A=1-231.
DR PDB; 7NYE; X-ray; 1.40 A; A=1-231.
DR PDB; 7NYF; X-ray; 1.40 A; A=1-231.
DR PDB; 7NYG; X-ray; 1.40 A; A=1-231.
DR PDB; 7NZ6; X-ray; 1.40 A; A=1-231.
DR PDB; 7NZG; X-ray; 1.40 A; A=1-231.
DR PDB; 7NZK; X-ray; 1.40 A; A=1-231.
DR PDB; 7NZV; X-ray; 1.40 A; A=1-231.
DR PDB; 7O07; X-ray; 1.20 A; A=1-231.
DR PDB; 7O34; X-ray; 1.20 A; A=1-231.
DR PDB; 7O3A; X-ray; 1.20 A; A=1-231.
DR PDB; 7O3F; X-ray; 1.40 A; A=1-231.
DR PDB; 7O3P; X-ray; 1.40 A; A=1-231.
DR PDB; 7O3Q; X-ray; 1.80 A; A=1-231.
DR PDB; 7O3R; X-ray; 1.80 A; A=1-231.
DR PDB; 7O3S; X-ray; 2.00 A; A=1-231.
DR PDB; 7O57; X-ray; 1.40 A; A=1-231.
DR PDB; 7O59; X-ray; 1.20 A; A=1-231.
DR PDB; 7O5A; X-ray; 1.80 A; A=1-231.
DR PDB; 7O5C; X-ray; 1.80 A; A=1-231.
DR PDB; 7O5D; X-ray; 1.80 A; A=1-231.
DR PDB; 7O5F; X-ray; 1.80 A; A=1-231.
DR PDB; 7O5G; X-ray; 1.80 A; A=1-231.
DR PDB; 7O5O; X-ray; 1.80 A; A=1-231.
DR PDB; 7O5P; X-ray; 1.80 A; A=1-231.
DR PDB; 7O5S; X-ray; 1.80 A; A=1-231.
DR PDB; 7O5U; X-ray; 1.80 A; A=1-231.
DR PDB; 7O5X; X-ray; 1.80 A; A=1-231.
DR PDB; 7O6F; X-ray; 2.00 A; A=1-231.
DR PDB; 7O6G; X-ray; 1.80 A; A=1-231.
DR PDB; 7O6I; X-ray; 1.80 A; A=1-231.
DR PDB; 7O6J; X-ray; 1.40 A; A=1-231.
DR PDB; 7O6K; X-ray; 1.40 A; A=1-231.
DR PDB; 7O6M; X-ray; 1.40 A; A=1-231.
DR PDB; 7O6O; X-ray; 1.40 A; A=1-231.
DR PDB; 7QIK; X-ray; 2.01 A; A/B=1-231.
DR PDB; 7QIP; X-ray; 2.65 A; A/B=1-231.
DR PDBsum; 1YWT; -.
DR PDBsum; 1YZ5; -.
DR PDBsum; 3IQJ; -.
DR PDBsum; 3IQU; -.
DR PDBsum; 3IQV; -.
DR PDBsum; 3LW1; -.
DR PDBsum; 3MHR; -.
DR PDBsum; 3O8I; -.
DR PDBsum; 3P1N; -.
DR PDBsum; 3P1O; -.
DR PDBsum; 3P1P; -.
DR PDBsum; 3P1Q; -.
DR PDBsum; 3P1R; -.
DR PDBsum; 3P1S; -.
DR PDBsum; 3SMK; -.
DR PDBsum; 3SML; -.
DR PDBsum; 3SMM; -.
DR PDBsum; 3SMN; -.
DR PDBsum; 3SMO; -.
DR PDBsum; 3SP5; -.
DR PDBsum; 3SPR; -.
DR PDBsum; 3T0L; -.
DR PDBsum; 3T0M; -.
DR PDBsum; 3U9X; -.
DR PDBsum; 3UX0; -.
DR PDBsum; 4DAT; -.
DR PDBsum; 4DAU; -.
DR PDBsum; 4DHM; -.
DR PDBsum; 4DHN; -.
DR PDBsum; 4DHO; -.
DR PDBsum; 4DHP; -.
DR PDBsum; 4DHQ; -.
DR PDBsum; 4DHR; -.
DR PDBsum; 4DHS; -.
DR PDBsum; 4DHT; -.
DR PDBsum; 4DHU; -.
DR PDBsum; 4FL5; -.
DR PDBsum; 4FR3; -.
DR PDBsum; 4IEA; -.
DR PDBsum; 4JC3; -.
DR PDBsum; 4JDD; -.
DR PDBsum; 4QLI; -.
DR PDBsum; 4Y32; -.
DR PDBsum; 4Y3B; -.
DR PDBsum; 4Y5I; -.
DR PDBsum; 5BTV; -.
DR PDBsum; 5HF3; -.
DR PDBsum; 5LTW; -.
DR PDBsum; 5LU1; -.
DR PDBsum; 5LU2; -.
DR PDBsum; 5MHC; -.
DR PDBsum; 5MOC; -.
DR PDBsum; 5MXO; -.
DR PDBsum; 5MY9; -.
DR PDBsum; 5MYC; -.
DR PDBsum; 5N5R; -.
DR PDBsum; 5N5T; -.
DR PDBsum; 5N5W; -.
DR PDBsum; 5N75; -.
DR PDBsum; 5OEG; -.
DR PDBsum; 5OEH; -.
DR PDBsum; 5OK9; -.
DR PDBsum; 5OKF; -.
DR PDBsum; 5OM0; -.
DR PDBsum; 5OMA; -.
DR PDBsum; 6FAU; -.
DR PDBsum; 6FAV; -.
DR PDBsum; 6FAW; -.
DR PDBsum; 6FBB; -.
DR PDBsum; 6FBW; -.
DR PDBsum; 6FBY; -.
DR PDBsum; 6FCP; -.
DR PDBsum; 6FI4; -.
DR PDBsum; 6FI5; -.
DR PDBsum; 6G6X; -.
DR PDBsum; 6G8I; -.
DR PDBsum; 6G8J; -.
DR PDBsum; 6G8K; -.
DR PDBsum; 6G8L; -.
DR PDBsum; 6G8P; -.
DR PDBsum; 6G8Q; -.
DR PDBsum; 6GHP; -.
DR PDBsum; 6HHP; -.
DR PDBsum; 6HKB; -.
DR PDBsum; 6HKF; -.
DR PDBsum; 6HMT; -.
DR PDBsum; 6HMU; -.
DR PDBsum; 6HN2; -.
DR PDBsum; 6NV2; -.
DR PDBsum; 6QDR; -.
DR PDBsum; 6QDS; -.
DR PDBsum; 6QDT; -.
DR PDBsum; 6QDU; -.
DR PDBsum; 6QHL; -.
DR PDBsum; 6QHM; -.
DR PDBsum; 6QIU; -.
DR PDBsum; 6QZR; -.
DR PDBsum; 6QZS; -.
DR PDBsum; 6R5L; -.
DR PDBsum; 6RHC; -.
DR PDBsum; 6RJL; -.
DR PDBsum; 6RJQ; -.
DR PDBsum; 6RJZ; -.
DR PDBsum; 6RK8; -.
DR PDBsum; 6RKI; -.
DR PDBsum; 6RKK; -.
DR PDBsum; 6RKM; -.
DR PDBsum; 6RL3; -.
DR PDBsum; 6RL4; -.
DR PDBsum; 6RL6; -.
DR PDBsum; 6RM5; -.
DR PDBsum; 6RM7; -.
DR PDBsum; 6RP6; -.
DR PDBsum; 6RWH; -.
DR PDBsum; 6RWI; -.
DR PDBsum; 6RWS; -.
DR PDBsum; 6RWU; -.
DR PDBsum; 6RX2; -.
DR PDBsum; 6S39; -.
DR PDBsum; 6S3C; -.
DR PDBsum; 6S40; -.
DR PDBsum; 6S9Q; -.
DR PDBsum; 6SIN; -.
DR PDBsum; 6SIO; -.
DR PDBsum; 6SIP; -.
DR PDBsum; 6SIQ; -.
DR PDBsum; 6SLV; -.
DR PDBsum; 6SLW; -.
DR PDBsum; 6SLX; -.
DR PDBsum; 6T5F; -.
DR PDBsum; 6T5H; -.
DR PDBsum; 6T80; -.
DR PDBsum; 6TCH; -.
DR PDBsum; 6TJM; -.
DR PDBsum; 6TL3; -.
DR PDBsum; 6TLF; -.
DR PDBsum; 6TLG; -.
DR PDBsum; 6TM7; -.
DR PDBsum; 6TWZ; -.
DR PDBsum; 6W0L; -.
DR PDBsum; 6XWD; -.
DR PDBsum; 6XXC; -.
DR PDBsum; 6XY5; -.
DR PDBsum; 6Y18; -.
DR PDBsum; 6Y1D; -.
DR PDBsum; 6Y1J; -.
DR PDBsum; 6Y3M; -.
DR PDBsum; 6Y3O; -.
DR PDBsum; 6Y3R; -.
DR PDBsum; 6Y3S; -.
DR PDBsum; 6Y3V; -.
DR PDBsum; 6Y3W; -.
DR PDBsum; 6Y40; -.
DR PDBsum; 6Y44; -.
DR PDBsum; 6Y58; -.
DR PDBsum; 6Y7T; -.
DR PDBsum; 6Y8A; -.
DR PDBsum; 6Y8B; -.
DR PDBsum; 6Y8D; -.
DR PDBsum; 6Y8E; -.
DR PDBsum; 6YE9; -.
DR PDBsum; 6YIA; -.
DR PDBsum; 6YIB; -.
DR PDBsum; 6YIC; -.
DR PDBsum; 6YLU; -.
DR PDBsum; 6YOW; -.
DR PDBsum; 6YOX; -.
DR PDBsum; 6YOY; -.
DR PDBsum; 6YP2; -.
DR PDBsum; 6YP3; -.
DR PDBsum; 6YP8; -.
DR PDBsum; 6YPL; -.
DR PDBsum; 6YPY; -.
DR PDBsum; 6YQ2; -.
DR PDBsum; 6YR5; -.
DR PDBsum; 6YR6; -.
DR PDBsum; 6YR7; -.
DR PDBsum; 6ZCJ; -.
DR PDBsum; 6ZVB; -.
DR PDBsum; 6ZVC; -.
DR PDBsum; 6ZVD; -.
DR PDBsum; 6ZVE; -.
DR PDBsum; 7AEW; -.
DR PDBsum; 7AOG; -.
DR PDBsum; 7AXN; -.
DR PDBsum; 7AYF; -.
DR PDBsum; 7AZ1; -.
DR PDBsum; 7AZ2; -.
DR PDBsum; 7B13; -.
DR PDBsum; 7B15; -.
DR PDBsum; 7B9M; -.
DR PDBsum; 7B9R; -.
DR PDBsum; 7B9T; -.
DR PDBsum; 7BA3; -.
DR PDBsum; 7BA5; -.
DR PDBsum; 7BA6; -.
DR PDBsum; 7BA7; -.
DR PDBsum; 7BA8; -.
DR PDBsum; 7BA9; -.
DR PDBsum; 7BAA; -.
DR PDBsum; 7BAB; -.
DR PDBsum; 7BDP; -.
DR PDBsum; 7BDT; -.
DR PDBsum; 7BDY; -.
DR PDBsum; 7BFW; -.
DR PDBsum; 7BG3; -.
DR PDBsum; 7BGQ; -.
DR PDBsum; 7BGR; -.
DR PDBsum; 7BGV; -.
DR PDBsum; 7BGW; -.
DR PDBsum; 7BI3; -.
DR PDBsum; 7BIQ; -.
DR PDBsum; 7BIW; -.
DR PDBsum; 7BIY; -.
DR PDBsum; 7BJB; -.
DR PDBsum; 7BJF; -.
DR PDBsum; 7BJL; -.
DR PDBsum; 7BJW; -.
DR PDBsum; 7BKH; -.
DR PDBsum; 7BM9; -.
DR PDBsum; 7BMC; -.
DR PDBsum; 7NFW; -.
DR PDBsum; 7NIF; -.
DR PDBsum; 7NIG; -.
DR PDBsum; 7NIX; -.
DR PDBsum; 7NIZ; -.
DR PDBsum; 7NJ6; -.
DR PDBsum; 7NJ8; -.
DR PDBsum; 7NJ9; -.
DR PDBsum; 7NJA; -.
DR PDBsum; 7NJB; -.
DR PDBsum; 7NK3; -.
DR PDBsum; 7NK5; -.
DR PDBsum; 7NLA; -.
DR PDBsum; 7NLE; -.
DR PDBsum; 7NM1; -.
DR PDBsum; 7NM3; -.
DR PDBsum; 7NM9; -.
DR PDBsum; 7NMA; -.
DR PDBsum; 7NMH; -.
DR PDBsum; 7NMW; -.
DR PDBsum; 7NMX; -.
DR PDBsum; 7NN2; -.
DR PDBsum; 7NND; -.
DR PDBsum; 7NNE; -.
DR PDBsum; 7NP2; -.
DR PDBsum; 7NPB; -.
DR PDBsum; 7NPG; -.
DR PDBsum; 7NQP; -.
DR PDBsum; 7NR7; -.
DR PDBsum; 7NRK; -.
DR PDBsum; 7NRL; -.
DR PDBsum; 7NSV; -.
DR PDBsum; 7NV4; -.
DR PDBsum; 7NVI; -.
DR PDBsum; 7NWS; -.
DR PDBsum; 7NXS; -.
DR PDBsum; 7NXT; -.
DR PDBsum; 7NXW; -.
DR PDBsum; 7NXY; -.
DR PDBsum; 7NY4; -.
DR PDBsum; 7NYE; -.
DR PDBsum; 7NYF; -.
DR PDBsum; 7NYG; -.
DR PDBsum; 7NZ6; -.
DR PDBsum; 7NZG; -.
DR PDBsum; 7NZK; -.
DR PDBsum; 7NZV; -.
DR PDBsum; 7O07; -.
DR PDBsum; 7O34; -.
DR PDBsum; 7O3A; -.
DR PDBsum; 7O3F; -.
DR PDBsum; 7O3P; -.
DR PDBsum; 7O3Q; -.
DR PDBsum; 7O3R; -.
DR PDBsum; 7O3S; -.
DR PDBsum; 7O57; -.
DR PDBsum; 7O59; -.
DR PDBsum; 7O5A; -.
DR PDBsum; 7O5C; -.
DR PDBsum; 7O5D; -.
DR PDBsum; 7O5F; -.
DR PDBsum; 7O5G; -.
DR PDBsum; 7O5O; -.
DR PDBsum; 7O5P; -.
DR PDBsum; 7O5S; -.
DR PDBsum; 7O5U; -.
DR PDBsum; 7O5X; -.
DR PDBsum; 7O6F; -.
DR PDBsum; 7O6G; -.
DR PDBsum; 7O6I; -.
DR PDBsum; 7O6J; -.
DR PDBsum; 7O6K; -.
DR PDBsum; 7O6M; -.
DR PDBsum; 7O6O; -.
DR PDBsum; 7QIK; -.
DR PDBsum; 7QIP; -.
DR AlphaFoldDB; P31947; -.
DR SMR; P31947; -.
DR BioGRID; 109072; 357.
DR DIP; DIP-29861N; -.
DR ELM; P31947; -.
DR IntAct; P31947; 214.
DR MINT; P31947; -.
DR STRING; 9606.ENSP00000340989; -.
DR BindingDB; P31947; -.
DR ChEMBL; CHEMBL1909482; -.
DR GlyGen; P31947; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P31947; -.
DR MetOSite; P31947; -.
DR PhosphoSitePlus; P31947; -.
DR SwissPalm; P31947; -.
DR BioMuta; SFN; -.
DR DMDM; 398953; -.
DR OGP; P31947; -.
DR SWISS-2DPAGE; P31947; -.
DR EPD; P31947; -.
DR jPOST; P31947; -.
DR MassIVE; P31947; -.
DR MaxQB; P31947; -.
DR PaxDb; P31947; -.
DR PeptideAtlas; P31947; -.
DR PRIDE; P31947; -.
DR ProteomicsDB; 54818; -.
DR ProteomicsDB; 54819; -. [P31947-2]
DR TopDownProteomics; P31947-1; -. [P31947-1]
DR TopDownProteomics; P31947-2; -. [P31947-2]
DR Antibodypedia; 1907; 779 antibodies from 45 providers.
DR CPTC; P31947; 3 antibodies.
DR DNASU; 2810; -.
DR Ensembl; ENST00000339276.6; ENSP00000340989.4; ENSG00000175793.12. [P31947-1]
DR GeneID; 2810; -.
DR KEGG; hsa:2810; -.
DR MANE-Select; ENST00000339276.6; ENSP00000340989.4; NM_006142.5; NP_006133.1.
DR UCSC; uc001bnc.2; human. [P31947-1]
DR CTD; 2810; -.
DR DisGeNET; 2810; -.
DR GeneCards; SFN; -.
DR HGNC; HGNC:10773; SFN.
DR HPA; ENSG00000175793; Group enriched (esophagus, skin, vagina).
DR MIM; 601290; gene.
DR neXtProt; NX_P31947; -.
DR OpenTargets; ENSG00000175793; -.
DR PharmGKB; PA177; -.
DR VEuPathDB; HostDB:ENSG00000175793; -.
DR eggNOG; KOG0841; Eukaryota.
DR GeneTree; ENSGT01050000244964; -.
DR HOGENOM; CLU_058290_1_0_1; -.
DR InParanoid; P31947; -.
DR OMA; ECRVFYL; -.
DR OrthoDB; 1176818at2759; -.
DR PhylomeDB; P31947; -.
DR TreeFam; TF102003; -.
DR PathwayCommons; P31947; -.
DR Reactome; R-HSA-111447; Activation of BAD and translocation to mitochondria.
DR Reactome; R-HSA-1445148; Translocation of SLC2A4 (GLUT4) to the plasma membrane.
DR Reactome; R-HSA-5625740; RHO GTPases activate PKNs.
DR Reactome; R-HSA-5628897; TP53 Regulates Metabolic Genes.
DR Reactome; R-HSA-6804114; TP53 Regulates Transcription of Genes Involved in G2 Cell Cycle Arrest.
DR Reactome; R-HSA-75035; Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex.
DR Reactome; R-HSA-9614399; Regulation of localization of FOXO transcription factors.
DR Reactome; R-HSA-9755779; SARS-CoV-2 targets host intracellular signalling and regulatory pathways.
DR SignaLink; P31947; -.
DR SIGNOR; P31947; -.
DR BioGRID-ORCS; 2810; 17 hits in 1082 CRISPR screens.
DR ChiTaRS; SFN; human.
DR EvolutionaryTrace; P31947; -.
DR GeneWiki; Stratifin; -.
DR GenomeRNAi; 2810; -.
DR Pharos; P31947; Tbio.
DR PRO; PR:P31947; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P31947; protein.
DR Bgee; ENSG00000175793; Expressed in cervix squamous epithelium and 195 other tissues.
DR Genevisible; P31947; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; TAS:ProtInc.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0051219; F:phosphoprotein binding; IEA:Ensembl.
DR GO; GO:0019901; F:protein kinase binding; IBA:GO_Central.
DR GO; GO:0008426; F:protein kinase C inhibitor activity; TAS:ProtInc.
DR GO; GO:0061436; P:establishment of skin barrier; ISS:UniProtKB.
DR GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IDA:HGNC-UCL.
DR GO; GO:0031424; P:keratinization; IEA:Ensembl.
DR GO; GO:0003334; P:keratinocyte development; IEA:Ensembl.
DR GO; GO:0043616; P:keratinocyte proliferation; IEA:Ensembl.
DR GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:HGNC-UCL.
DR GO; GO:0010839; P:negative regulation of keratinocyte proliferation; IEA:Ensembl.
DR GO; GO:0006469; P:negative regulation of protein kinase activity; TAS:ProtInc.
DR GO; GO:2000647; P:negative regulation of stem cell proliferation; IEA:Ensembl.
DR GO; GO:0030307; P:positive regulation of cell growth; IEA:Ensembl.
DR GO; GO:0045606; P:positive regulation of epidermal cell differentiation; ISS:UniProtKB.
DR GO; GO:0046827; P:positive regulation of protein export from nucleus; IEA:Ensembl.
DR GO; GO:0008104; P:protein localization; IBA:GO_Central.
DR GO; GO:0000079; P:regulation of cyclin-dependent protein serine/threonine kinase activity; IEA:Ensembl.
DR GO; GO:0010482; P:regulation of epidermal cell division; ISS:UniProtKB.
DR GO; GO:0001836; P:release of cytochrome c from mitochondria; IDA:HGNC-UCL.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0072089; P:stem cell proliferation; IEA:Ensembl.
DR CDD; cd10019; 14-3-3_sigma; 1.
DR Gene3D; 1.20.190.20; -; 1.
DR IDEAL; IID00301; -.
DR InterPro; IPR000308; 14-3-3.
DR InterPro; IPR023409; 14-3-3_CS.
DR InterPro; IPR036815; 14-3-3_dom_sf.
DR InterPro; IPR023410; 14-3-3_domain.
DR InterPro; IPR037435; 14-3-3_sigma.
DR PANTHER; PTHR18860; PTHR18860; 1.
DR Pfam; PF00244; 14-3-3; 1.
DR PIRSF; PIRSF000868; 14-3-3; 1.
DR PRINTS; PR00305; 1433ZETA.
DR SMART; SM00101; 14_3_3; 1.
DR SUPFAM; SSF48445; SSF48445; 1.
DR PROSITE; PS00796; 1433_1; 1.
DR PROSITE; PS00797; 1433_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Direct protein sequencing;
KW Nucleus; Phosphoprotein; Reference proteome; Secreted; Ubl conjugation.
FT CHAIN 1..248
FT /note="14-3-3 protein sigma"
FT /id="PRO_0000058643"
FT SITE 56
FT /note="Interaction with phosphoserine on interacting
FT protein"
FT SITE 129
FT /note="Interaction with phosphoserine on interacting
FT protein"
FT MOD_RES 5
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 74
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 248
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:20068231"
FT VAR_SEQ 85..116
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_021768"
FT VARIANT 155
FT /note="M -> I (in dbSNP:rs11542705)"
FT /id="VAR_048095"
FT CONFLICT 77
FT /note="K -> M (in Ref. 4; CAG46703)"
FT /evidence="ECO:0000305"
FT CONFLICT 120
FT /note="Y -> H (in Ref. 2; AAA59546)"
FT /evidence="ECO:0000305"
FT CONFLICT 242
FT /note="A -> V (in Ref. 2; AAA59546)"
FT /evidence="ECO:0000305"
FT HELIX 3..15
FT /evidence="ECO:0007829|PDB:3IQU"
FT HELIX 19..31
FT /evidence="ECO:0007829|PDB:3IQU"
FT HELIX 38..69
FT /evidence="ECO:0007829|PDB:3IQU"
FT STRAND 72..75
FT /evidence="ECO:0007829|PDB:6T5H"
FT HELIX 80..104
FT /evidence="ECO:0007829|PDB:3IQU"
FT HELIX 107..110
FT /evidence="ECO:0007829|PDB:3IQU"
FT HELIX 114..134
FT /evidence="ECO:0007829|PDB:3IQU"
FT HELIX 137..139
FT /evidence="ECO:0007829|PDB:6RJL"
FT HELIX 140..161
FT /evidence="ECO:0007829|PDB:3IQU"
FT HELIX 167..182
FT /evidence="ECO:0007829|PDB:3IQU"
FT HELIX 187..204
FT /evidence="ECO:0007829|PDB:3IQU"
FT HELIX 205..207
FT /evidence="ECO:0007829|PDB:3IQU"
FT HELIX 210..230
FT /evidence="ECO:0007829|PDB:3IQU"
SQ SEQUENCE 248 AA; 27774 MW; 7F4B44E3AA59ECE6 CRC64;
MERASLIQKA KLAEQAERYE DMAAFMKGAV EKGEELSCEE RNLLSVAYKN VVGGQRAAWR
VLSSIEQKSN EEGSEEKGPE VREYREKVET ELQGVCDTVL GLLDSHLIKE AGDAESRVFY
LKMKGDYYRY LAEVATGDDK KRIIDSARSA YQEAMDISKK EMPPTNPIRL GLALNFSVFH
YEIANSPEEA ISLAKTTFDE AMADLHTLSE DSYKDSTLIM QLLRDNLTLW TADNAGEEGG
EAPQEPQS
