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Coatomer subunit beta' (Beta'-coat protein) (Beta'-COP) (p102)

 COPB2_HUMAN             Reviewed;         906 AA.
P35606; B4DZI8;
01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
07-NOV-2018, entry version 190.
RecName: Full=Coatomer subunit beta';
AltName: Full=Beta'-coat protein;
Short=Beta'-COP;
AltName: Full=p102;
Name=COPB2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=8335000;
Harrison-Lavoie K.J., Lewis V.A., Hynes G.M., Collison K.S.,
Nutland E., Willison K.R.;
"A 102 kDa subunit of a Golgi-associated particle has homology to beta
subunits of trimeric G proteins.";
EMBO J. 12:2847-2853(1993).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Testis;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16641997; DOI=10.1038/nature04728;
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
Gibbs R.A.;
"The DNA sequence, annotation and analysis of human chromosome 3.";
Nature 440:1194-1198(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
PROTEIN SEQUENCE OF 2-9.
TISSUE=Platelet;
PubMed=12665801; DOI=10.1038/nbt810;
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
Thomas G.R., Vandekerckhove J.;
"Exploring proteomes and analyzing protein processing by mass
spectrometric identification of sorted N-terminal peptides.";
Nat. Biotechnol. 21:566-569(2003).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-859, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-859, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[12]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-627, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-859, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-859, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-859, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-859 AND THR-861, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[18]
INTERACTION WITH JAGN1.
PubMed=25129144; DOI=10.1038/ng.3069;
Boztug K., Jaervinen P.M., Salzer E., Racek T., Moench S.,
Garncarz W., Gertz E.M., Schaeffer A.A., Antonopoulos A., Haslam S.M.,
Schieck L., Puchalka J., Diestelhorst J., Appaswamy G., Lescoeur B.,
Giambruno R., Bigenzahn J.W., Elling U., Pfeifer D., Conde C.D.,
Albert M.H., Welte K., Brandes G., Sherkat R.,
van der Werff Ten Bosch J., Rezaei N., Etzioni A.,
Bellanne-Chantelot C., Superti-Furga G., Penninger J.M., Bennett K.L.,
von Blume J., Dell A., Donadieu J., Klein C.;
"JAGN1 deficiency causes aberrant myeloid cell homeostasis and
congenital neutropenia.";
Nat. Genet. 46:1021-1027(2014).
[19]
INVOLVEMENT IN MCPH19, AND VARIANT MCPH19 CYS-254.
PubMed=29036432; DOI=10.1093/hmg/ddx362;
DiStasio A., Driver A., Sund K., Donlin M., Muraleedharan R.M.,
Pooya S., Kline-Fath B., Kaufman K.M., Prows C.A., Schorry E.,
Dasgupta B., Stottmann R.W.;
"Copb2 is essential for embryogenesis and hypomorphic mutations cause
human microcephaly.";
Hum. Mol. Genet. 26:4836-4848(2017).
-!- FUNCTION: The coatomer is a cytosolic protein complex that binds
to dilysine motifs and reversibly associates with Golgi non-
clathrin-coated vesicles, which further mediate biosynthetic
protein transport from the ER, via the Golgi up to the trans Golgi
network. Coatomer complex is required for budding from Golgi
membranes, and is essential for the retrograde Golgi-to-ER
transport of dilysine-tagged proteins. In mammals, the coatomer
can only be recruited by membranes associated to ADP-ribosylation
factors (ARFs), which are small GTP-binding proteins; the complex
also influences the Golgi structural integrity, as well as the
processing, activity, and endocytic recycling of LDL receptors (By
similarity). {ECO:0000250}.
-!- FUNCTION: This coatomer complex protein, essential for Golgi
budding and vesicular trafficking, is a selective binding protein
(RACK) for protein kinase C, epsilon type. It binds to Golgi
membranes in a GTP-dependent manner (By similarity).
{ECO:0000250}.
-!- SUBUNIT: Oligomeric complex that consists of at least the alpha,
beta, beta', gamma, delta, epsilon and zeta subunits. Probably
interacts with PEX11A. Interacts with SCYL1 (By similarity).
Interacts with JAGN1 (PubMed:25129144). {ECO:0000250,
ECO:0000269|PubMed:25129144}.
-!- INTERACTION:
P19838:NFKB1; NbExp=3; IntAct=EBI-1056534, EBI-300010;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Golgi
apparatus membrane {ECO:0000250}; Peripheral membrane protein
{ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasmic
vesicle, COPI-coated vesicle membrane {ECO:0000250}; Peripheral
membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
Note=The coatomer is cytoplasmic or polymerized on the cytoplasmic
side of the Golgi, as well as on the vesicles/buds originating
from it. Shows only a slight preference for the cis-Golgi
apparatus, compared with the trans-Golgi. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P35606-1; Sequence=Displayed;
Name=2;
IsoId=P35606-2; Sequence=VSP_056165;
Note=No experimental confirmation available.;
-!- DISEASE: Microcephaly 19, primary, autosomal recessive (MCPH19)
[MIM:617800]: A form of microcephaly, a disease defined as a head
circumference more than 3 standard deviations below the age, sex
and ethnically matched mean. Brain weight is markedly reduced and
the cerebral cortex is disproportionately small. MCPH19 affected
individuals manifest severe developmental delay, failure to
thrive, cortical blindness, and spasticity. Brain imaging show a
simplified gyral pattern, thin corpus callosum, slight ventricular
dilation, and delayed myelination. {ECO:0000269|PubMed:29036432}.
Note=The disease may be caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the WD repeat COPB2 family. {ECO:0000305}.
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EMBL; X70476; CAA49900.1; -; mRNA.
EMBL; AK302943; BAG64100.1; -; mRNA.
EMBL; AC024933; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471052; EAW79040.1; -; Genomic_DNA.
EMBL; BC000326; AAH00326.1; -; mRNA.
CCDS; CCDS3108.1; -. [P35606-1]
PIR; S35342; S35342.
RefSeq; NP_004757.1; NM_004766.2. [P35606-1]
RefSeq; XP_016863001.1; XM_017007512.1.
UniGene; Hs.681616; -.
ProteinModelPortal; P35606; -.
SMR; P35606; -.
BioGrid; 114693; 59.
CORUM; P35606; -.
DIP; DIP-27603N; -.
IntAct; P35606; 35.
MINT; P35606; -.
STRING; 9606.ENSP00000329419; -.
iPTMnet; P35606; -.
PhosphoSitePlus; P35606; -.
SwissPalm; P35606; -.
BioMuta; COPB2; -.
DMDM; 544076; -.
EPD; P35606; -.
MaxQB; P35606; -.
PaxDb; P35606; -.
PeptideAtlas; P35606; -.
PRIDE; P35606; -.
ProteomicsDB; 55099; -.
DNASU; 9276; -.
Ensembl; ENST00000333188; ENSP00000329419; ENSG00000184432. [P35606-1]
Ensembl; ENST00000507777; ENSP00000422295; ENSG00000184432. [P35606-2]
GeneID; 9276; -.
KEGG; hsa:9276; -.
UCSC; uc003etf.5; human. [P35606-1]
CTD; 9276; -.
DisGeNET; 9276; -.
EuPathDB; HostDB:ENSG00000184432.9; -.
GeneCards; COPB2; -.
HGNC; HGNC:2232; COPB2.
HPA; HPA036867; -.
HPA; HPA058180; -.
MalaCards; COPB2; -.
MIM; 606990; gene.
MIM; 617800; phenotype.
neXtProt; NX_P35606; -.
OpenTargets; ENSG00000184432; -.
Orphanet; 2512; Autosomal recessive primary microcephaly.
PharmGKB; PA26748; -.
eggNOG; KOG0276; Eukaryota.
eggNOG; ENOG410XNNY; LUCA.
GeneTree; ENSGT00900000141083; -.
HOGENOM; HOG000163444; -.
HOVERGEN; HBG051076; -.
KO; K17302; -.
OMA; FYDWENT; -.
OrthoDB; EOG091G0284; -.
PhylomeDB; P35606; -.
TreeFam; TF300688; -.
Reactome; R-HSA-6807878; COPI-mediated anterograde transport.
Reactome; R-HSA-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
SignaLink; P35606; -.
ChiTaRS; COPB2; human.
GeneWiki; COPB2; -.
GenomeRNAi; 9276; -.
PRO; PR:P35606; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000184432; Expressed in 234 organ(s), highest expression level in parotid gland.
CleanEx; HS_COPB2; -.
ExpressionAtlas; P35606; baseline and differential.
Genevisible; P35606; HS.
GO; GO:0030126; C:COPI vesicle coat; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
GO; GO:0030133; C:transport vesicle; TAS:Reactome.
GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
GO; GO:0006888; P:ER to Golgi vesicle-mediated transport; IBA:GO_Central.
GO; GO:0006891; P:intra-Golgi vesicle-mediated transport; IDA:UniProtKB.
GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to ER; IBA:GO_Central.
GO; GO:1901998; P:toxin transport; IEA:Ensembl.
Gene3D; 2.130.10.10; -; 1.
InterPro; IPR006692; Coatomer_WD-assoc_reg.
InterPro; IPR016453; COPB2.
InterPro; IPR020472; G-protein_beta_WD-40_rep.
InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
InterPro; IPR001680; WD40_repeat.
InterPro; IPR017986; WD40_repeat_dom.
InterPro; IPR036322; WD40_repeat_dom_sf.
Pfam; PF04053; Coatomer_WDAD; 1.
Pfam; PF00400; WD40; 4.
PIRSF; PIRSF005567; Coatomer_beta'_subunit; 1.
PRINTS; PR00320; GPROTEINBRPT.
SMART; SM00320; WD40; 6.
SUPFAM; SSF50978; SSF50978; 2.
PROSITE; PS50082; WD_REPEATS_2; 5.
PROSITE; PS50294; WD_REPEATS_REGION; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; Coiled coil; Complete proteome;
Cytoplasm; Cytoplasmic vesicle; Direct protein sequencing;
Disease mutation; ER-Golgi transport; Golgi apparatus; Membrane;
Phosphoprotein; Primary microcephaly; Protein transport;
Reference proteome; Repeat; Transport; WD repeat.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:12665801}.
CHAIN 2 906 Coatomer subunit beta'.
/FTId=PRO_0000050912.
REPEAT 13 52 WD 1.
REPEAT 55 94 WD 2.
REPEAT 97 136 WD 3.
REPEAT 140 180 WD 4.
REPEAT 183 224 WD 5.
REPEAT 227 266 WD 6.
COILED 866 891 {ECO:0000255}.
MOD_RES 627 627 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 859 859 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 861 861 Phosphothreonine.
{ECO:0000244|PubMed:24275569}.
VAR_SEQ 1 29 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_056165.
VARIANT 254 254 R -> C (in MCPH19; unknown pathological
significance; dbSNP:rs1229568621).
{ECO:0000269|PubMed:29036432}.
/FTId=VAR_080601.
SEQUENCE 906 AA; 102487 MW; 824BB63BEFAA53F6 CRC64;
MPLRLDIKRK LTARSDRVKS VDLHPTEPWM LASLYNGSVC VWNHETQTLV KTFEVCDLPV
RAAKFVARKN WVVTGADDMQ IRVFNYNTLE RVHMFEAHSD YIRCIAVHPT QPFILTSSDD
MLIKLWDWDK KWSCSQVFEG HTHYVMQIVI NPKDNNQFAS ASLDRTIKVW QLGSSSPNFT
LEGHEKGVNC IDYYSGGDKP YLISGADDRL VKIWDYQNKT CVQTLEGHAQ NVSCASFHPE
LPIIITGSED GTVRIWHSST YRLESTLNYG MERVWCVASL RGSNNVALGY DEGSIIVKLG
REEPAMSMDA NGKIIWAKHS EVQQANLKAM GDAEIKDGER LPLAVKDMGS CEIYPQTIQH
NPNGRFVVVC GDGEYIIYTA MALRNKSFGS AQEFAWAHDS SEYAIRESNS IVKIFKNFKE
KKSFKPDFGA ESIYGGFLLG VRSVNGLAFY DWDNTELIRR IEIQPKHIFW SDSGELVCIA
TEESFFILKY LSEKVLAAQE THEGVTEDGI EDAFEVLGEI QEIVKTGLWV GDCFIYTSSV
NRLNYYVGGE IVTIAHLDRT MYLLGYIPKD NRLYLGDKEL NIISYSLLVS VLEYQTAVMR
RDFSMADKVL PTIPKEQRTR VAHFLEKQGF KQQALTVSTD PEHRFELALQ LGELKIAYQL
AVEAESEQKW KQLAELAISK CQFGLAQECL HHAQDYGGLL LLATASGNAN MVNKLAEGAE
RDGKNNVAFM SYFLQGKVDA CLELLIRTGR LPEAAFLART YLPSQVSRVV KLWRENLSKV
NQKAAESLAD PTEYENLFPG LKEAFVVEEW VKETHADLWP AKQYPLVTPN EERNVMEEGK
DFQPSRSTAQ QELDGKPASP TPVIVASHTA NKEEKSLLEL EVDLDNLELE DIDTTDINLD
EDILDD


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