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SCAPE_HUMAN
ID   SCAPE_HUMAN             Reviewed;        1400 AA.
AC   Q9BY12; F5H7X8; H3BNR7; Q3B7X7; Q96BS9; Q9H3D8; Q9NT03; Q9P274;
DT   15-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2013, sequence version 2.
DT   03-AUG-2022, entry version 159.
DE   RecName: Full=S phase cyclin A-associated protein in the endoplasmic reticulum {ECO:0000305};
DE            Short=S phase cyclin A-associated protein in the ER;
DE   AltName: Full=Zinc finger protein 291;
GN   Name=SCAPER {ECO:0000312|HGNC:HGNC:13081}; Synonyms=KIAA1454, ZNF291;
GN   ORFNames=MSTP063;
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).
RA   Carim-Todd L., Sumoy L., Estivill X., Escarceller M.;
RT   "Identification and characterization of ZNF291, a novel protein on
RT   chromosome 15q24.";
RL   Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT THR-1089.
RC   TISSUE=Brain;
RX   PubMed=10819331; DOI=10.1093/dnares/7.2.143;
RA   Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. XVII. The
RT   complete sequences of 100 new cDNA clones from brain which code for large
RT   proteins in vitro.";
RL   DNA Res. 7:143-150(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE SEQUENCE
RP   [LARGE SCALE MRNA] OF 1135-1400 (ISOFORM 1).
RC   TISSUE=Retina, and Testis;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA   Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA   Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16572171; DOI=10.1038/nature04601;
RA   Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA   Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA   FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA   Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA   Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA   DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA   Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA   Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA   Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA   O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA   Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA   Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT   "Analysis of the DNA sequence and duplication history of human chromosome
RT   15.";
RL   Nature 440:671-675(2006).
RN   [5]
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   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-551 AND 1024-1340 (ISOFORM 1).
RC   TISSUE=Colon, and Prostate;
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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 246-1340 (ISOFORM 1), AND VARIANT
RP   THR-1089.
RC   TISSUE=Heart;
RA   Zhao B., Xu Y.Y., Liu Y.Q., Wang X.Y., Lui B., Ye J., Song L., Zhao Y.,
RA   Cao H.Q., Zhao X.W., Gao Y., Zhang C.L., Zhang J., Liu L.S., Ding J.F.,
RA   Gao R.L., Wu Q.Y., Qiang B.Q., Yuan J.G., Liew C.C., Zhao M.S., Hui R.T.;
RL   Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1109-1400 (ISOFORM 1).
RA   Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA   Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA   Phelan M., Farmer A.;
RT   "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL   Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   FUNCTION, INTERACTION WITH CCNA2/CDK2 COMPLEX, SUBCELLULAR LOCATION, TISSUE
RP   SPECIFICITY, DEVELOPMENTAL STAGE, AND MUTAGENESIS OF 26-ARG--LEU-28;
RP   199-ARG--LEU-201 AND 678-ARG--LEU-680.
RX   PubMed=17698606; DOI=10.1083/jcb.200701166;
RA   Tsang W.Y., Wang L., Chen Z., Sanchez I., Dynlacht B.D.;
RT   "SCAPER, a novel cyclin A-interacting protein that regulates cell cycle
RT   progression.";
RL   J. Cell Biol. 178:621-633(2007).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-832, 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   [11]
RP   INVOLVEMENT IN IDDRP, TISSUE SPECIFICITY, AND VARIANTS IDDRP GLU-620 DEL
RP   AND ASN-1219.
RX   PubMed=28794130; DOI=10.1136/jmedgenet-2017-104632;
RA   Tatour Y., Sanchez-Navarro I., Chervinsky E., Hakonarson H., Gawi H.,
RA   Tahsin-Swafiri S., Leibu R., Lopez-Molina M.I., Fernandez-Sanz G.,
RA   Ayuso C., Ben-Yosef T.;
RT   "Mutations in SCAPER cause autosomal recessive retinitis pigmentosa with
RT   intellectual disability.";
RL   J. Med. Genet. 54:698-704(2017).
CC   -!- FUNCTION: CCNA2/CDK2 regulatory protein that transiently maintains
CC       CCNA2 in the cytoplasm. {ECO:0000269|PubMed:17698606}.
CC   -!- SUBUNIT: Interacts with CCNA2/CDK2 complex, but not with CCNA2/CDC2,
CC       CCNB1/CDC2 or CCNE1/CDK2 complexes, at multiple phases of the cell
CC       cycle, including S and G2/M. {ECO:0000269|PubMed:17698606}.
CC   -!- INTERACTION:
CC       Q9BY12; P24941: CDK2; NbExp=3; IntAct=EBI-308519, EBI-375096;
CC       Q9BY12-3; Q9Y5Z0: BACE2; NbExp=3; IntAct=EBI-25837959, EBI-11282723;
CC       Q9BY12-3; P46379-2: BAG6; NbExp=3; IntAct=EBI-25837959, EBI-10988864;
CC       Q9BY12-3; P28329-3: CHAT; NbExp=3; IntAct=EBI-25837959, EBI-25837549;
CC       Q9BY12-3; P02489: CRYAA; NbExp=3; IntAct=EBI-25837959, EBI-6875961;
CC       Q9BY12-3; O75190-2: DNAJB6; NbExp=3; IntAct=EBI-25837959, EBI-12593112;
CC       Q9BY12-3; P50570-2: DNM2; NbExp=3; IntAct=EBI-25837959, EBI-10968534;
CC       Q9BY12-3; Q14204: DYNC1H1; NbExp=3; IntAct=EBI-25837959, EBI-356015;
CC       Q9BY12-3; P22607: FGFR3; NbExp=3; IntAct=EBI-25837959, EBI-348399;
CC       Q9BY12-3; Q8TB36: GDAP1; NbExp=3; IntAct=EBI-25837959, EBI-11110431;
CC       Q9BY12-3; P14136: GFAP; NbExp=3; IntAct=EBI-25837959, EBI-744302;
CC       Q9BY12-3; O14908-2: GIPC1; NbExp=3; IntAct=EBI-25837959, EBI-25913156;
CC       Q9BY12-3; P01112: HRAS; NbExp=3; IntAct=EBI-25837959, EBI-350145;
CC       Q9BY12-3; P42858: HTT; NbExp=6; IntAct=EBI-25837959, EBI-466029;
CC       Q9BY12-3; O14901: KLF11; NbExp=3; IntAct=EBI-25837959, EBI-948266;
CC       Q9BY12-3; Q92876: KLK6; NbExp=3; IntAct=EBI-25837959, EBI-2432309;
CC       Q9BY12-3; P35240: NF2; NbExp=3; IntAct=EBI-25837959, EBI-1014472;
CC       Q9BY12-3; Q9BVL2: NUP58; NbExp=3; IntAct=EBI-25837959, EBI-2811583;
CC       Q9BY12-3; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-25837959, EBI-5235340;
CC       Q9BY12-3; O14656-2: TOR1A; NbExp=3; IntAct=EBI-25837959, EBI-25847109;
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC       {ECO:0000269|PubMed:17698606}. Nucleus {ECO:0000269|PubMed:17698606}.
CC       Note=Predominantly located in the endoplasmic reticulum, only a small
CC       portion is detected in the nucleus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9BY12-1; Sequence=Displayed;
CC       Name=3;
CC         IsoId=Q9BY12-3; Sequence=VSP_046503;
CC   -!- TISSUE SPECIFICITY: Widely expressed with high expression in testis.
CC       Isoform 1 is detected in various tissues, including retina, fetal and
CC       adult brain. Isoform 2 is expressed in the retina at high levels, and
CC       in the brain at very low levels (PubMed:28794130).
CC       {ECO:0000269|PubMed:17698606, ECO:0000269|PubMed:28794130}.
CC   -!- DEVELOPMENTAL STAGE: Expressed at each stage of the cell cycle,
CC       including G0, although the expression is somewhat higher in late G1 and
CC       S phases. {ECO:0000269|PubMed:17698606}.
CC   -!- PTM: Phosphorylated in vitro by the CCNA2/CDK2 complex.
CC   -!- DISEASE: Intellectual developmental disorder and retinitis pigmentosa
CC       (IDDRP) [MIM:618195]: An autosomal recessive disease characterized by
CC       mild to moderate intellectual disability, retinitis pigmentosa, and
CC       attention-deficit hyperactivity disorder observed in some patients.
CC       {ECO:0000269|PubMed:28794130}. Note=The disease may be caused by
CC       variants affecting the gene represented in this entry.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAG47945.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=AAH15212.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=AAI07416.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC       Sequence=AAK29205.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAA95978.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
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DR   EMBL; AF242528; AAK29205.1; ALT_INIT; mRNA.
DR   EMBL; AB040887; BAA95978.1; ALT_SEQ; mRNA.
DR   EMBL; AL137612; CAB70841.1; -; mRNA.
DR   EMBL; BX647285; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AC015798; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC016343; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC027243; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC051643; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC090179; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC090751; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471136; EAW99218.1; -; Genomic_DNA.
DR   EMBL; BC015212; AAH15212.1; ALT_INIT; mRNA.
DR   EMBL; BC107415; AAI07416.1; ALT_SEQ; mRNA.
DR   EMBL; AF119814; AAG47945.1; ALT_INIT; mRNA.
DR   EMBL; BT006762; AAP35408.1; -; mRNA.
DR   CCDS; CCDS53961.1; -. [Q9BY12-3]
DR   CCDS; CCDS53962.1; -. [Q9BY12-1]
DR   PIR; T46314; T46314.
DR   RefSeq; NP_001139395.1; NM_001145923.1. [Q9BY12-3]
DR   RefSeq; NP_065894.2; NM_020843.2. [Q9BY12-1]
DR   RefSeq; XP_005254476.1; XM_005254419.2.
DR   RefSeq; XP_016877758.1; XM_017022269.1. [Q9BY12-1]
DR   RefSeq; XP_016877759.1; XM_017022270.1. [Q9BY12-1]
DR   AlphaFoldDB; Q9BY12; -.
DR   SMR; Q9BY12; -.
DR   BioGRID; 119067; 22.
DR   IntAct; Q9BY12; 35.
DR   STRING; 9606.ENSP00000454973; -.
DR   iPTMnet; Q9BY12; -.
DR   PhosphoSitePlus; Q9BY12; -.
DR   BioMuta; SCAPER; -.
DR   DMDM; 510120715; -.
DR   EPD; Q9BY12; -.
DR   jPOST; Q9BY12; -.
DR   MassIVE; Q9BY12; -.
DR   MaxQB; Q9BY12; -.
DR   PaxDb; Q9BY12; -.
DR   PeptideAtlas; Q9BY12; -.
DR   PRIDE; Q9BY12; -.
DR   ProteomicsDB; 27620; -.
DR   ProteomicsDB; 41275; -.
DR   ProteomicsDB; 79561; -. [Q9BY12-1]
DR   Antibodypedia; 27436; 70 antibodies from 17 providers.
DR   DNASU; 49855; -.
DR   Ensembl; ENST00000324767.11; ENSP00000326924.7; ENSG00000140386.13. [Q9BY12-1]
DR   Ensembl; ENST00000538941.6; ENSP00000442190.2; ENSG00000140386.13. [Q9BY12-3]
DR   Ensembl; ENST00000563290.6; ENSP00000454973.1; ENSG00000140386.13. [Q9BY12-1]
DR   GeneID; 49855; -.
DR   KEGG; hsa:49855; -.
DR   MANE-Select; ENST00000563290.6; ENSP00000454973.1; NM_020843.4; NP_065894.2.
DR   UCSC; uc002bbx.4; human. [Q9BY12-1]
DR   CTD; 49855; -.
DR   DisGeNET; 49855; -.
DR   GeneCards; SCAPER; -.
DR   HGNC; HGNC:13081; SCAPER.
DR   HPA; ENSG00000140386; Tissue enhanced (retina).
DR   MalaCards; SCAPER; -.
DR   MIM; 611611; gene.
DR   MIM; 618195; phenotype.
DR   neXtProt; NX_Q9BY12; -.
DR   OpenTargets; ENSG00000140386; -.
DR   Orphanet; 110; Bardet-Biedl syndrome.
DR   Orphanet; 791; Retinitis pigmentosa.
DR   PharmGKB; PA162402512; -.
DR   VEuPathDB; HostDB:ENSG00000140386; -.
DR   eggNOG; KOG4722; Eukaryota.
DR   GeneTree; ENSGT00390000011159; -.
DR   HOGENOM; CLU_005178_0_0_1; -.
DR   InParanoid; Q9BY12; -.
DR   OMA; CEHPLAE; -.
DR   OrthoDB; 82115at2759; -.
DR   PhylomeDB; Q9BY12; -.
DR   TreeFam; TF324831; -.
DR   PathwayCommons; Q9BY12; -.
DR   SignaLink; Q9BY12; -.
DR   BioGRID-ORCS; 49855; 15 hits in 1078 CRISPR screens.
DR   ChiTaRS; SCAPER; human.
DR   GenomeRNAi; 49855; -.
DR   Pharos; Q9BY12; Tbio.
DR   PRO; PR:Q9BY12; -.
DR   Proteomes; UP000005640; Chromosome 15.
DR   RNAct; Q9BY12; protein.
DR   Bgee; ENSG00000140386; Expressed in cortical plate and 189 other tissues.
DR   ExpressionAtlas; Q9BY12; baseline and differential.
DR   Genevisible; Q9BY12; HS.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR   GO; GO:0016607; C:nuclear speck; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:1990917; C:ooplasm; IEA:Ensembl.
DR   GO; GO:0061827; C:sperm head; IEA:Ensembl.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0001547; P:antral ovarian follicle growth; IEA:Ensembl.
DR   GO; GO:0060041; P:retina development in camera-type eye; IMP:MGI.
DR   GO; GO:0072520; P:seminiferous tubule development; IEA:Ensembl.
DR   GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
DR   InterPro; IPR003604; Matrin/U1-like-C_Znf_C2H2.
DR   InterPro; IPR032446; SCAPER_N.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   Pfam; PF16501; SCAPER_N; 1.
DR   SMART; SM00451; ZnF_U1; 1.
DR   SUPFAM; SSF57667; SSF57667; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Disease variant; Endoplasmic reticulum;
KW   Intellectual disability; Metal-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Retinitis pigmentosa; Zinc; Zinc-finger.
FT   CHAIN           1..1400
FT                   /note="S phase cyclin A-associated protein in the
FT                   endoplasmic reticulum"
FT                   /id="PRO_0000047513"
FT   ZN_FING         792..816
FT                   /note="C2H2-type"
FT   REGION          36..61
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          226..277
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          517..550
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          701..723
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        230..251
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        253..270
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         832
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   VAR_SEQ         1..257
FT                   /note="MMASFQRSNSHDKVRRIVAEEGRTARNLIAWSVPLESKDDDGKPKCQTGGKS
FT                   KRTIQGTHKTTKQSTAVDCKITSSTTGDKHFDKSPTKTRHPRKIDLRARYWAFLFDNLR
FT                   RAVDEIYVTCESDQSVVECKEVLMMLDNYVRDFKALIDWIQLQEKLEKTDAQSRPTSLA
FT                   WEVKKMSPGRHVIPSPSTDRINVTSNARRSLNFGGSTGTVPAPRLAPTGVSWADKVKAH
FT                   HTGSTASSEITPAQSCPPMTVQKASRKN -> MKTKYIFCNIT (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:17974005"
FT                   /id="VSP_046503"
FT   VARIANT         620
FT                   /note="Missing (in IDDRP; unknown pathological
FT                   significance)"
FT                   /evidence="ECO:0000269|PubMed:28794130"
FT                   /id="VAR_081681"
FT   VARIANT         1089
FT                   /note="P -> T (in dbSNP:rs1607017)"
FT                   /evidence="ECO:0000269|PubMed:10819331, ECO:0000269|Ref.7"
FT                   /id="VAR_019978"
FT   VARIANT         1139
FT                   /note="A -> T (in dbSNP:rs3743176)"
FT                   /id="VAR_059910"
FT   VARIANT         1140
FT                   /note="A -> T (in dbSNP:rs3743176)"
FT                   /id="VAR_052806"
FT   VARIANT         1219
FT                   /note="S -> N (in IDDRP; unknown pathological significance;
FT                   dbSNP:rs1305542291)"
FT                   /evidence="ECO:0000269|PubMed:28794130"
FT                   /id="VAR_081682"
FT   MUTAGEN         26..28
FT                   /note="RNL->AAA: No effect on CCNA2/CDK2 complex-binding."
FT                   /evidence="ECO:0000269|PubMed:17698606"
FT   MUTAGEN         199..201
FT                   /note="RSL->AAA: Loss of CCNA2/CDK2 complex-binding."
FT                   /evidence="ECO:0000269|PubMed:17698606"
FT   MUTAGEN         678..680
FT                   /note="RAL->AAA: No effect on CCNA2/CDK2 complex-binding."
FT                   /evidence="ECO:0000269|PubMed:17698606"
FT   CONFLICT        1
FT                   /note="M -> V (in Ref. 1; AAK29205)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1262
FT                   /note="S -> F (in Ref. 7; AAG47945)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1400 AA;  158287 MW;  9DBAF02F75CB1AA7 CRC64;
     MMASFQRSNS HDKVRRIVAE EGRTARNLIA WSVPLESKDD DGKPKCQTGG KSKRTIQGTH
     KTTKQSTAVD CKITSSTTGD KHFDKSPTKT RHPRKIDLRA RYWAFLFDNL RRAVDEIYVT
     CESDQSVVEC KEVLMMLDNY VRDFKALIDW IQLQEKLEKT DAQSRPTSLA WEVKKMSPGR
     HVIPSPSTDR INVTSNARRS LNFGGSTGTV PAPRLAPTGV SWADKVKAHH TGSTASSEIT
     PAQSCPPMTV QKASRKNERK DAEGWETVQR GRPIRSRSTA VMPKVSLATE ATRSKDDSDK
     ENVCLLPDES IQKGQFVGDG TSNTIESHPK DSLHSCDHPL AEKTQFTVST LDDVKNSGSI
     RDNYVRTSEI SAVHIDTECV SVMLQAGTPP LQVNEEKFPA EKARIENEMD PSDISNSMAE
     VLAKKEELAD RLEKANEEAI ASAIAEEEQL TREIEAEENN DINIETDNDS DFSASMGSGS
     VSFCGMSMDW NDVLADYEAR ESWRQNTSWG DIVEEEPARP PGHGIHMHEK LSSPSRKRTI
     AESKKKHEEK QMKAQQLREK LREEKTLKLQ KLLEREKDVR KWKEELLDQR RRMMEEKLLH
     AEFKREVQLQ AIVKKAQEEE AKVNEIAFIN TLEAQNKRHD VLSKLKEYEQ RLNELQEERQ
     RRQEEKQARD EAVQERKRAL EAERQARVEE LLMKRKEQEA RIEQQRQEKE KAREDAARER
     ARDREERLAA LTAAQQEAME ELQKKIQLKH DESIRRHMEQ IEQRKEKAAE LSSGRHANTD
     YAPKLTPYER KKQCSLCNVL ISSEVYLFSH VKGRKHQQAV RENTSIQGRE LSDEEVEHLS
     LKKYIIDIVV ESTAPAEALK DGEERQKNKK KAKKIKARMN FRAKEYESLM ETKNSGSDSP
     YKAKLQRLAK DLLKQVQVQD SGSWANNKVS ALDRTLGEIT RILEKENVAD QIAFQAAGGL
     TALEHILQAV VPATNVNTVL RIPPKSLCNA INVYNLTCNN CSENCSDVLF SNKITFLMDL
     LIHQLTVYVP DENNTILGRN TNKQVFEGLT TGLLKVSAVV LGCLIANRPD GNCQPATPKI
     PTQEMKNKPS QGDPFNNRVQ DLISYVVNMG LIDKLCACFL SVQGPVDENP KMAIFLQHAA
     GLLHAMCTLC FAVTGRSYSI FDNNRQDPTG LTAALQATDL AGVLHMLYCV LFHGTILDPS
     TASPKENYTQ NTIQVAIQSL RFFNSFAALH LPAFQSIVGA EGLSLAFRHM ASSLLGHCSQ
     VSCESLLHEV IVCVGYFTVN HPDNQVIVQS GRHPTVLQKL CQLPFQYFSD PRLIKVLFPS
     LIAACYNNHQ NKIILEQEMS CVLLATFIQD LAQTPGQAEN QPYQPKGKCL GSQDYLELAN
     RFPQQAWEEA RQFFLKKEKK
 
 
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