CEP85_HUMAN
ID CEP85_HUMAN Reviewed; 762 AA.
AC Q6P2H3; B4DRL1; D3DPK4; F8W7K4; Q5VY68; Q5VY70; Q9H6Q1; Q9H828; Q9UF52;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Centrosomal protein of 85 kDa;
DE Short=Cep85;
DE AltName: Full=Coiled-coil domain-containing protein 21;
GN Name=CEP85; Synonyms=CCDC21;
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 [LARGE SCALE MRNA] (ISOFORMS 2 AND 4), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 408-762 (ISOFORM 1).
RC TISSUE=Hepatoma, Retinoblastoma, 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 [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Placenta, and 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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 328-762 (ISOFORM 2).
RC TISSUE=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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17, 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-623, AND IDENTIFICATION BY
RP 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 [8]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=21399614; DOI=10.1038/emboj.2011.63;
RA Jakobsen L., Vanselow K., Skogs M., Toyoda Y., Lundberg E., Poser I.,
RA Falkenby L.G., Bennetzen M., Westendorf J., Nigg E.A., Uhlen M.,
RA Hyman A.A., Andersen J.S.;
RT "Novel asymmetrically localizing components of human centrosomes identified
RT by complementary proteomics methods.";
RL EMBO J. 30:1520-1535(2011).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-126 AND SER-141, AND
RP IDENTIFICATION BY MASS 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 [10]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH NEK2, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RX PubMed=26220856; DOI=10.1242/jcs.171637;
RA Chen C., Tian F., Lu L., Wang Y., Xiao Z., Yu C., Yu X.;
RT "Characterization of Cep85 - a new antagonist of Nek2A that is involved in
RT the regulation of centrosome disjunction.";
RL J. Cell Sci. 128:3290-3303(2015).
RN [11]
RP ERRATUM OF PUBMED:26220856.
RX PubMed=26471995; DOI=10.1242/jcs.180463;
RA Chen C., Tian F., Lu L., Wang Y., Xiao Z., Yu C., Yu X.;
RL J. Cell Sci. 128:3837-3837(2015).
CC -!- FUNCTION: Acts as a negative regulator of NEK2 to maintain the
CC centrosome integrity in interphase. Suppresses centrosome disjunction
CC by inhibiting NEK2 kinase activity (PubMed:26220856).
CC {ECO:0000269|PubMed:26220856}.
CC -!- INTERACTION:
CC Q6P2H3; P54274: TERF1; NbExp=2; IntAct=EBI-2808308, EBI-710997;
CC Q6P2H3; PRO_0000037548 [Q9WMX2]; Xeno; NbExp=2; IntAct=EBI-2808308, EBI-6863741;
CC Q6P2H3-3; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-12368239, EBI-739832;
CC Q6P2H3-3; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-12368239, EBI-741158;
CC Q6P2H3-3; O76064: RNF8; NbExp=3; IntAct=EBI-12368239, EBI-373337;
CC Q6P2H3-3; O00560: SDCBP; NbExp=3; IntAct=EBI-12368239, EBI-727004;
CC Q6P2H3-3; Q9BUZ4: TRAF4; NbExp=3; IntAct=EBI-12368239, EBI-3650647;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000269|PubMed:21399614,
CC ECO:0000269|PubMed:26220856}. Cytoplasm, cytoskeleton, spindle pole
CC {ECO:0000269|PubMed:21399614, ECO:0000269|PubMed:26220856}. Nucleus,
CC nucleolus {ECO:0000269|PubMed:21399614}. Note=Localizes to centrosomes
CC and nucleolus in interphase. Upon entry into mitosis, relocates from
CC nucleolus and accumulates at spindle poles (PubMed:21399614).
CC Associated with the pericentriolar material. Localizes to centrosomes
CC at a low level in G1 phase and a slightly increased level in S phase,
CC with gradually elevated levels during G2 phase. The levels at
CC centrosomes further increase at G2/M, reaching a peak at spindle poles
CC at early mitotic stages and remain high until the end of anaphase
CC (PubMed:26220856). {ECO:0000269|PubMed:21399614,
CC ECO:0000269|PubMed:26220856}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q6P2H3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6P2H3-2; Sequence=VSP_018147;
CC Name=3;
CC IsoId=Q6P2H3-3; Sequence=VSP_026435;
CC Name=4;
CC IsoId=Q6P2H3-4; Sequence=VSP_055609;
CC -!- SIMILARITY: Belongs to the CEP85 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB15203.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK024038; BAB14794.1; -; mRNA.
DR EMBL; AK025653; BAB15203.1; ALT_INIT; mRNA.
DR EMBL; AK299312; BAG61323.1; -; mRNA.
DR EMBL; AL355877; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL451139; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471059; EAX07834.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX07835.1; -; Genomic_DNA.
DR EMBL; BC019902; AAH19902.1; -; mRNA.
DR EMBL; BC064528; AAH64528.1; -; mRNA.
DR EMBL; AL133609; CAB63740.1; -; mRNA.
DR CCDS; CCDS277.1; -. [Q6P2H3-1]
DR CCDS; CCDS60038.1; -. [Q6P2H3-4]
DR CCDS; CCDS81285.1; -. [Q6P2H3-2]
DR PIR; T43448; T43448.
DR RefSeq; NP_001268446.1; NM_001281517.2. [Q6P2H3-4]
DR RefSeq; NP_001268447.1; NM_001281518.2. [Q6P2H3-3]
DR RefSeq; NP_001306873.1; NM_001319944.1. [Q6P2H3-2]
DR RefSeq; NP_073615.2; NM_022778.4. [Q6P2H3-1]
DR PDB; 5OI7; X-ray; 1.67 A; A/B=570-656.
DR PDB; 5OID; X-ray; 4.60 A; B=570-656.
DR PDBsum; 5OI7; -.
DR PDBsum; 5OID; -.
DR AlphaFoldDB; Q6P2H3; -.
DR SMR; Q6P2H3; -.
DR BioGRID; 122301; 152.
DR IntAct; Q6P2H3; 59.
DR MINT; Q6P2H3; -.
DR STRING; 9606.ENSP00000252992; -.
DR GlyGen; Q6P2H3; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q6P2H3; -.
DR MetOSite; Q6P2H3; -.
DR PhosphoSitePlus; Q6P2H3; -.
DR BioMuta; CEP85; -.
DR DMDM; 74737212; -.
DR EPD; Q6P2H3; -.
DR jPOST; Q6P2H3; -.
DR MassIVE; Q6P2H3; -.
DR MaxQB; Q6P2H3; -.
DR PaxDb; Q6P2H3; -.
DR PeptideAtlas; Q6P2H3; -.
DR PRIDE; Q6P2H3; -.
DR ProteomicsDB; 29962; -.
DR ProteomicsDB; 66901; -. [Q6P2H3-1]
DR ProteomicsDB; 66902; -. [Q6P2H3-2]
DR ProteomicsDB; 66903; -. [Q6P2H3-3]
DR Antibodypedia; 16049; 71 antibodies from 15 providers.
DR DNASU; 64793; -.
DR Ensembl; ENST00000252992.8; ENSP00000252992.4; ENSG00000130695.16. [Q6P2H3-1]
DR Ensembl; ENST00000451429.8; ENSP00000417002.3; ENSG00000130695.16. [Q6P2H3-2]
DR Ensembl; ENST00000640292.2; ENSP00000492362.2; ENSG00000130695.16. [Q6P2H3-4]
DR GeneID; 64793; -.
DR KEGG; hsa:64793; -.
DR MANE-Select; ENST00000451429.8; ENSP00000417002.3; NM_001319944.2; NP_001306873.1. [Q6P2H3-2]
DR UCSC; uc001bls.3; human. [Q6P2H3-1]
DR CTD; 64793; -.
DR GeneCards; CEP85; -.
DR HGNC; HGNC:25309; CEP85.
DR HPA; ENSG00000130695; Tissue enhanced (skeletal muscle, tongue).
DR MIM; 618898; gene.
DR neXtProt; NX_Q6P2H3; -.
DR OpenTargets; ENSG00000130695; -.
DR PharmGKB; PA142672180; -.
DR VEuPathDB; HostDB:ENSG00000130695; -.
DR eggNOG; ENOG502QR5U; Eukaryota.
DR GeneTree; ENSGT00620000087993; -.
DR HOGENOM; CLU_020103_0_0_1; -.
DR InParanoid; Q6P2H3; -.
DR OMA; DWKTPML; -.
DR OrthoDB; 489645at2759; -.
DR PhylomeDB; Q6P2H3; -.
DR TreeFam; TF331041; -.
DR PathwayCommons; Q6P2H3; -.
DR SignaLink; Q6P2H3; -.
DR BioGRID-ORCS; 64793; 275 hits in 1081 CRISPR screens.
DR ChiTaRS; CEP85; human.
DR GenomeRNAi; 64793; -.
DR Pharos; Q6P2H3; Tdark.
DR PRO; PR:Q6P2H3; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q6P2H3; protein.
DR Bgee; ENSG00000130695; Expressed in oocyte and 183 other tissues.
DR ExpressionAtlas; Q6P2H3; baseline and differential.
DR Genevisible; Q6P2H3; HS.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0000242; C:pericentriolar material; IDA:UniProtKB.
DR GO; GO:0000922; C:spindle pole; IDA:UniProtKB.
DR GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-KW.
DR GO; GO:0006469; P:negative regulation of protein kinase activity; IMP:UniProtKB.
DR GO; GO:0046602; P:regulation of mitotic centrosome separation; IMP:UniProtKB.
DR InterPro; IPR029777; Cep85.
DR InterPro; IPR040210; Cep85/Cep85L.
DR PANTHER; PTHR31075; PTHR31075; 1.
DR PANTHER; PTHR31075:SF3; PTHR31075:SF3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Chromosome partition; Coiled coil;
KW Cytoplasm; Cytoskeleton; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..762
FT /note="Centrosomal protein of 85 kDa"
FT /id="PRO_0000233660"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 94..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 257..433
FT /note="Mediates interaction with NEK2 and is required for
FT its function in the suppression of centrosome disjunction"
FT /evidence="ECO:0000269|PubMed:26220856"
FT REGION 434..476
FT /note="Required for centrosome localization and for its
FT function in the suppression of centrosome disjunction"
FT /evidence="ECO:0000269|PubMed:26220856"
FT REGION 443..474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 541..570
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 334..657
FT /evidence="ECO:0000255"
FT COILED 723..750
FT /evidence="ECO:0000255"
FT COMPBIAS 10..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 541..558
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 17
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 126
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 141
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 623
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT VAR_SEQ 1..568
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_026435"
FT VAR_SEQ 19..70
FT /note="SSDVIQKGSSLGTEWQTPVISEPFRSRFSRCSSVADSGDTAIGTSCSDIAED
FT -> N (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055609"
FT VAR_SEQ 710..711
FT /note="SA -> S (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_018147"
FT VARIANT 48
FT /note="R -> H (in dbSNP:rs35831900)"
FT /id="VAR_053938"
FT VARIANT 213
FT /note="S -> N (in dbSNP:rs3795686)"
FT /id="VAR_053939"
FT VARIANT 542
FT /note="A -> T (in dbSNP:rs7550997)"
FT /id="VAR_033665"
FT VARIANT 668
FT /note="Q -> H (in dbSNP:rs36013141)"
FT /id="VAR_053940"
FT CONFLICT 258..260
FT /note="LSK -> HSSQ (in Ref. 1; BAB14794)"
FT /evidence="ECO:0000305"
FT CONFLICT 517
FT /note="E -> G (in Ref. 1; BAG61323)"
FT /evidence="ECO:0000305"
FT CONFLICT 561
FT /note="S -> G (in Ref. 1; BAB15203)"
FT /evidence="ECO:0000305"
FT HELIX 572..652
FT /evidence="ECO:0007829|PDB:5OI7"
SQ SEQUENCE 762 AA; 85639 MW; E6003FD530D8ACA8 CRC64;
MAMQEKYPTE GISHVTSPSS DVIQKGSSLG TEWQTPVISE PFRSRFSRCS SVADSGDTAI
GTSCSDIAED FCSSSGSPPF QPIKSHVTIP TAHVMPSTLG TSPAKPNSTP VGPSSSKLPL
SGLAESVGMT RNGDLGAMKH SPGLSRDLMY FSGATGENGI EQSWFPAVGH ERQEEARKFD
IPSMESTLNQ SAMMETLYSD PHHRVRFHNP RTSTSKELYR VLPEAKKAPG SGAVFERNGP
HSNSSGVLPL GLQPAPGLSK PLPSQVWQPS PDTWHPREQS CELSTCRQQL ELIRLQMEQM
QLQNGAICHH PAAFGPSLPI LEPAQWISIL NSNEHLLKEK ELLIDKQRKH ISQLEQKVRE
SELQVHSALL GRPAPFGDVC LLRLQELQRE NTFLRAQFAQ KTEALSREKI DLEKKLSASE
VEVQLIRESL KVALQKHSEE VKKQEERVKG RDKHINNLKK KCQKESEQNR EKQQRIETLE
RYLADLPTLE DHQKQSQQLK DSELKSTELQ EKVTELESLL EETQAICREK EIQLESLRQR
EAEFSSAGHS LQDKQSVEET SGEGPEVEME SWQKRYDSLQ KIVEKQQQKM DQLRSQVQSL
EQEVAQEEGT SQALREEAQR RDSALQQLRT AVKELSVQNQ DLIEKNLTLQ EHLRQAQPGS
PPSPDTAQLA LELHQELASC LQDLQAVCSI VTQRAQGHDP NLSLLLGIHS AQHPETQLDL
QKPDVIKRKL EEVQQLRRDI EDLRTTMSDR YAQDMGENCV TQ
