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Centrosomal protein of 131 kDa (5-azacytidine-induced protein 1) (Pre-acrosome localization protein 1)

 CP131_HUMAN             Reviewed;        1083 AA.
Q9UPN4; A6NHI8; B2RN11; Q96F50;
11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
30-NOV-2010, sequence version 3.
25-OCT-2017, entry version 139.
RecName: Full=Centrosomal protein of 131 kDa;
AltName: Full=5-azacytidine-induced protein 1;
AltName: Full=Pre-acrosome localization protein 1;
Name=CEP131; Synonyms=AZI1, KIAA1118;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS
ALA-272; ALA-397 AND ALA-473.
TISSUE=Brain;
PubMed=10470851; DOI=10.1093/dnares/6.3.197;
Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N.,
Tanaka A., Kotani H., Nomura N., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XIV.
The complete sequences of 100 new cDNA clones from brain which code
for large proteins in vitro.";
DNA Res. 6:197-205(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16625196; DOI=10.1038/nature04689;
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
"DNA sequence of human chromosome 17 and analysis of rearrangement in
the human lineage.";
Nature 440:1045-1049(2006).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANTS
ALA-272; ALA-397 AND ALA-473.
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).
[4]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
TISSUE=Lymphoblast;
PubMed=14654843; DOI=10.1038/nature02166;
Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A.,
Mann M.;
"Proteomic characterization of the human centrosome by protein
correlation profiling.";
Nature 426:570-574(2003).
[5]
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).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-150, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[7]
FUNCTION IN CILIOGENESIS.
PubMed=17954613; DOI=10.1083/jcb.200707181;
Graser S., Stierhof Y.-D., Lavoie S.B., Gassner O.S., Lamla S.,
Le Clech M., Nigg E.A.;
"Cep164, a novel centriole appendage protein required for primary
cilium formation.";
J. Cell Biol. 179:321-330(2007).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47; SER-105 AND SER-150,
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).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-489 (ISOFORMS 2 AND 3),
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47; SER-89; SER-105 AND
SER-798, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-489 AND SER-496
(ISOFORMS 2 AND 3), 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).
[11]
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).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47; SER-78 AND SER-453,
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).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35; SER-47; SER-114;
SER-146; SER-381; THR-383 AND SER-798, 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).
[14]
INTERACTION WITH MAP1LC3B.
PubMed=24089205; DOI=10.1038/nature12606;
Tang Z., Lin M.G., Stowe T.R., Chen S., Zhu M., Stearns T., Franco B.,
Zhong Q.;
"Autophagy promotes primary ciliogenesis by removing OFD1 from
centriolar satellites.";
Nature 502:254-257(2013).
[15]
FUNCTION IN GENOMIC STABILITY, INTERACTION WITH CEP290; DCTN1; PCM1
AND PCNT, AND SUBCELLULAR LOCATION.
PubMed=22797915; DOI=10.1242/jcs.104059;
Staples C.J., Myers K.N., Beveridge R.D., Patil A.A., Lee A.J.,
Swanton C., Howell M., Boulton S.J., Collis S.J.;
"The centriolar satellite protein Cep131 is important for genome
stability.";
J. Cell Sci. 125:4770-4779(2012).
[16]
REVIEW, AND FUNCTION.
PubMed=24185901; DOI=10.1038/emboj.2013.241;
Chavali P.L., Gergely F.;
"Cilia born out of shock and stress.";
EMBO J. 32:3011-3013(2013).
[17]
FUNCTION IN CILIOGENESIS, UBIQUITINATION BY MIB1, INTERACTION WITH
MIB1 AND PCM1, ASSOCIATION WITH MICROTUBULES, AND SUBCELLULAR
LOCATION.
PubMed=24121310; DOI=10.1038/emboj.2013.223;
Villumsen B.H., Danielsen J.R., Povlsen L., Sylvestersen K.B.,
Merdes A., Beli P., Yang Y.G., Choudhary C., Nielsen M.L., Mailand N.,
Bekker-Jensen S.;
"A new cellular stress response that triggers centriolar satellite
reorganization and ciliogenesis.";
EMBO J. 32:3029-3040(2013).
[18]
INDUCTION.
PubMed=23137637; DOI=10.1016/j.gene.2012.10.074;
Huong P.T., Soung N.K., Jang J.H., Cha-Molstad H.J., Sakchaisri K.,
Kim S.O., Jang J.M., Kim K.E., Lee K.S., Kwon Y.T., Erikson R.L.,
Ahn J.S., Kim B.Y.;
"Regulation of CEP131 gene expression by SP1.";
Gene 513:75-81(2013).
[19]
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).
[20]
FUNCTION IN CILIARY TRAFFICKING, SUBUNIT, INTERACTION WITH BBS4, AND
ASSOCIATION WITH THE BBSOME COMPLEX.
PubMed=24550735; DOI=10.1371/journal.pgen.1004083;
Chamling X., Seo S., Searby C.C., Kim G., Slusarski D.C.,
Sheffield V.C.;
"The centriolar satellite protein AZI1 interacts with BBS4 and
regulates ciliary trafficking of the BBSome.";
PLoS Genet. 10:E1004083-E1004083(2014).
[21]
FUNCTION, INTERACTION WITH 14-3-3, SUBCELLULAR LOCATION,
PHOSPHORYLATION AT SER-47; SER-78 AND SER-731, AND MUTAGENESIS OF
SER-47; SER-78 AND SER-731.
PubMed=26616734; DOI=10.1038/ncomms10075;
Tollenaere M.A., Villumsen B.H., Blasius M., Nielsen J.C.,
Wagner S.A., Bartek J., Beli P., Mailand N., Bekker-Jensen S.;
"p38- and MK2-dependent signalling promotes stress-induced centriolar
satellite remodelling via 14-3-3-dependent sequestration of
CEP131/AZI1.";
Nat. Commun. 6:10075-10075(2015).
[22]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CEP152 AND PCM1.
PubMed=26297806; DOI=10.7554/eLife.07519;
Kodani A., Yu T.W., Johnson J.R., Jayaraman D., Johnson T.L.,
Al-Gazali L., Sztriha L., Partlow J.N., Kim H., Krup A.L.,
Dammermann A., Krogan N., Walsh C.A., Reiter J.F.;
"Centriolar satellites assemble centrosomal microcephaly proteins to
recruit CDK2 and promote centriole duplication.";
Elife 4:0-0(2015).
-!- FUNCTION: Component of centriolar satellites contributing to the
building of a complex and dynamic network required to regulate
cilia/flagellum formation (PubMed:17954613, PubMed:24185901). In
proliferating cells, MIB1-mediated ubiquitination induces its
sequestration within centriolar satellites, precluding untimely
cilia formation initiation (PubMed:24121310). In contrast, during
normal and ultraviolet or heat shock cellular stress-induced
ciliogenesis, its non-ubiquitinated form is rapidly displaced from
centriolar satellites and recruited to centrosome/basal bodies in
a microtubule- and p38 MAPK-dependent manner (PubMed:24121310,
PubMed:26616734). Acts also as a negative regulator of BBSome
ciliary trafficking (PubMed:24550735). Plays a role in sperm
flagellar formation; may be involved in the regulation of
intraflagellar transport (IFT) and/or intramanchette (IMT)
trafficking, which are important for axoneme extension and/or
cargo delivery to the nascent sperm tail (By similarity). Required
for optimal cell proliferation and cell cycle progression; may
play a role in the regulation of genome stability in non-
ciliogenic cells (PubMed:22797915, PubMed:26297806). Involved in
centriole duplication (By similarity). Required for CEP152, WDR62
and CEP63 centrosomal localization and promotes the centrosomal
localization of CDK2 (PubMed:26297806).
{ECO:0000250|UniProtKB:Q62036, ECO:0000269|PubMed:17954613,
ECO:0000269|PubMed:22797915, ECO:0000269|PubMed:24121310,
ECO:0000269|PubMed:24185901, ECO:0000269|PubMed:24550735,
ECO:0000269|PubMed:26297806, ECO:0000269|PubMed:26616734}.
-!- SUBUNIT: Self-associates. Associates with the centriolar satellite
BBSome protein complex. Interacts with BBS4; the interaction
limits BBS4 availability for association with the BBSome complex,
and hence negatively regulates ciliary localization of the BBSome
complex (PubMed:24550735). Interacts with MIB1 (PubMed:24121310).
Interacts with PCM1; the interaction increases in response to
ultraviolet light (UV) radiation (PubMed:22797915,
PubMed:24121310). Associates with microtubules; association with
microtubules is reduced in response to cellular stress, such as UV
stimulation, in a process that requires p38 MAP kinase signaling
(PubMed:24121310). Interacts with CEP290, DCTN1, PCNT, PCM1 and
CEP152. Interacts with 14-3-3 proteins following UV-induced
phosphorylation by MAPKAPK2; this inhibits formation of novel
centriolar satellites (PubMed:26616734).
{ECO:0000269|PubMed:22797915, ECO:0000269|PubMed:24089205,
ECO:0000269|PubMed:24121310, ECO:0000269|PubMed:24550735,
ECO:0000269|PubMed:26297806, ECO:0000269|PubMed:26616734}.
-!- INTERACTION:
O94986:CEP152; NbExp=3; IntAct=EBI-2558372, EBI-311012;
O15078:CEP290; NbExp=9; IntAct=EBI-2558372, EBI-1811944;
Q15154:PCM1; NbExp=5; IntAct=EBI-2558372, EBI-741421;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule
organizing center, centrosome {ECO:0000269|PubMed:14654843}.
Cytoplasm, cytoskeleton, microtubule organizing center,
centrosome, centriolar satellite {ECO:0000269|PubMed:26297806,
ECO:0000269|PubMed:26616734}. Cytoplasm, cytoskeleton, cilium
basal body. Cytoplasmic vesicle, secretory vesicle, acrosome
{ECO:0000250|UniProtKB:Q62036}. Note=Colocalized with
pericentriolar material protein PCM1 at centriolar satellites.
During spermiogenesis, becomes enriched with nephrocystin NPHP1 at
the transition zone, a structure at the base of the ciliary
axoneme important for regulating traffic into the ciliary
compartment. Traffics towards and away from the centrosome/basal
body and the transition zone of the ciliary axoneme in a
microtubule-dependent manner. Localized at the Golgi-derived
acrosome and the centrosome-containing head-tail coupling
apparatus (HTCA) (By similarity). Ubiquitinated form is
sequestered and colocalized with BBS4, CEP290, PCM1 and PCNT at
centriolar satellites in proliferating cells. Colocalized with the
pericentriolar material protein PCM1 at centrosome. Traffics
towards and away from centriolar satellites and centrosome in a
microtubule- and dynein-dependent manner in interphase cells.
Displaced from centriolar satellites but still remains associated
with the centrosome in response to cellular stress, such as
ultraviolet light (UV) radiation or heat shock, in a process that
requires p38 MAPK signaling (PubMed:26616734). {ECO:0000250,
ECO:0000269|PubMed:26616734}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q9UPN4-1; Sequence=Displayed;
Name=2;
IsoId=Q9UPN4-2; Sequence=VSP_015823;
Note=Contains a phosphoserine at position 489. Contains a
phosphoserine at position 496. {ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:19690332};
Name=3;
IsoId=Q9UPN4-3; Sequence=VSP_015823, VSP_040204;
Note=Contains a phosphoserine at position 489. Contains a
phosphoserine at position 496. {ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:19690332};
-!- INDUCTION: Up-regulated by the transcription factor SP1.
{ECO:0000269|PubMed:23137637}.
-!- PTM: Ubiquitinated. Undergoes monoubiquitination catalyzed by the
E3 ubiquitin-protein ligase MIB1 in proliferating cells,
preventing cilia formation. Monoubiquitination by MIB1 is
inhibited in response to cellular stress, such as ultraviolet
light (UV) radiation or heat shock, resulting in cilia formation
initiation. {ECO:0000269|PubMed:24121310}.
-!- PTM: MAPKAPK2-dependent phosphorylation at Ser-47 and Ser-78
occurs in response to cellular stress such as exposure to
ultraviolet irradiation and promotes binding to 14-3-3 proteins
which leads to cytoplasmic sequestration of CEP131 and blocks
formation of new centriolar satellites.
{ECO:0000269|PubMed:26616734}.
-!- MISCELLANEOUS: Transient cell cultured-based knock-down (by RNAi)
of CEP131 leads to a reduction in ciliogenesis (PubMed:17954613,
PubMed:24121310). However, analysis of mice with chronic absence
of CEP131 following genetic deletion (knockout) shows that cilia
develop and function normally in vivo. This suggests that CEP131
is not essential for ciliogenesis, except for the modified cilia
of the developing sperm flagella, and that there is an alternative
mechanism to compensate for the lack of CEP131.
{ECO:0000305|PubMed:17954613, ECO:0000305|PubMed:24121310}.
-!- SIMILARITY: Belongs to the CEP131 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAA83070.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; AB029041; BAA83070.1; ALT_INIT; mRNA.
EMBL; AC027601; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC011615; AAH11615.2; -; mRNA.
EMBL; BC136580; AAI36581.1; -; mRNA.
CCDS; CCDS32764.1; -. [Q9UPN4-3]
CCDS; CCDS45808.1; -. [Q9UPN4-2]
CCDS; CCDS82215.1; -. [Q9UPN4-1]
RefSeq; NP_001009811.2; NM_001009811.3. [Q9UPN4-3]
RefSeq; NP_001306157.1; NM_001319228.1. [Q9UPN4-1]
RefSeq; NP_055799.2; NM_014984.3. [Q9UPN4-2]
UniGene; Hs.514578; -.
ProteinModelPortal; Q9UPN4; -.
SMR; Q9UPN4; -.
BioGrid; 116641; 119.
CORUM; Q9UPN4; -.
DIP; DIP-56658N; -.
IntAct; Q9UPN4; 92.
MINT; MINT-4541849; -.
STRING; 9606.ENSP00000393583; -.
iPTMnet; Q9UPN4; -.
PhosphoSitePlus; Q9UPN4; -.
BioMuta; AZI1; -.
DMDM; 313104247; -.
EPD; Q9UPN4; -.
PaxDb; Q9UPN4; -.
PeptideAtlas; Q9UPN4; -.
PRIDE; Q9UPN4; -.
Ensembl; ENST00000269392; ENSP00000269392; ENSG00000141577. [Q9UPN4-1]
Ensembl; ENST00000374782; ENSP00000363914; ENSG00000141577. [Q9UPN4-3]
Ensembl; ENST00000450824; ENSP00000393583; ENSG00000141577. [Q9UPN4-2]
GeneID; 22994; -.
KEGG; hsa:22994; -.
UCSC; uc002jzn.2; human. [Q9UPN4-1]
CTD; 22994; -.
DisGeNET; 22994; -.
EuPathDB; HostDB:ENSG00000141577.13; -.
GeneCards; CEP131; -.
H-InvDB; HIX0014243; -.
HGNC; HGNC:29511; CEP131.
HPA; HPA024019; -.
MIM; 613479; gene.
neXtProt; NX_Q9UPN4; -.
OpenTargets; ENSG00000141577; -.
PharmGKB; PA128394595; -.
PharmGKB; PA134920867; -.
eggNOG; ENOG410IEUN; Eukaryota.
eggNOG; ENOG410YVPU; LUCA.
GeneTree; ENSGT00390000001758; -.
HOGENOM; HOG000293266; -.
HOVERGEN; HBG024371; -.
InParanoid; Q9UPN4; -.
KO; K16540; -.
OMA; EVHRRVK; -.
OrthoDB; EOG091G0C9E; -.
PhylomeDB; Q9UPN4; -.
TreeFam; TF328914; -.
Reactome; R-HSA-2565942; Regulation of PLK1 Activity at G2/M Transition.
Reactome; R-HSA-380259; Loss of Nlp from mitotic centrosomes.
Reactome; R-HSA-380270; Recruitment of mitotic centrosome proteins and complexes.
Reactome; R-HSA-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
Reactome; R-HSA-380320; Recruitment of NuMA to mitotic centrosomes.
Reactome; R-HSA-5620912; Anchoring of the basal body to the plasma membrane.
Reactome; R-HSA-8854518; AURKA Activation by TPX2.
GeneWiki; AZI1; -.
GenomeRNAi; 22994; -.
PRO; PR:Q9UPN4; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000141577; -.
CleanEx; HS_AZI1; -.
ExpressionAtlas; Q9UPN4; baseline and differential.
Genevisible; Q9UPN4; HS.
GO; GO:0001669; C:acrosomal vesicle; IEA:UniProtKB-SubCell.
GO; GO:0034451; C:centriolar satellite; IDA:UniProtKB.
GO; GO:0005813; C:centrosome; IDA:UniProtKB.
GO; GO:0035869; C:ciliary transition zone; IDA:GO_Central.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0045171; C:intercellular bridge; IDA:HPA.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0015630; C:microtubule cytoskeleton; IDA:HPA.
GO; GO:0005815; C:microtubule organizing center; IDA:HPA.
GO; GO:0032403; F:protein complex binding; IDA:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
GO; GO:0097711; P:ciliary basal body-plasma membrane docking; TAS:Reactome.
GO; GO:0000086; P:G2/M transition of mitotic cell cycle; TAS:Reactome.
GO; GO:0035735; P:intraciliary transport involved in cilium assembly; IMP:UniProtKB.
GO; GO:0007275; P:multicellular organism development; IEA:UniProtKB-KW.
GO; GO:0008284; P:positive regulation of cell proliferation; IMP:UniProtKB.
GO; GO:0090316; P:positive regulation of intracellular protein transport; IMP:UniProtKB.
GO; GO:0071539; P:protein localization to centrosome; IMP:UniProtKB.
GO; GO:0010824; P:regulation of centrosome duplication; IMP:UniProtKB.
GO; GO:0010389; P:regulation of G2/M transition of mitotic cell cycle; TAS:Reactome.
GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
InterPro; IPR030465; CEP131.
PANTHER; PTHR31540; PTHR31540; 1.
1: Evidence at protein level;
Alternative splicing; Cell cycle; Cell projection;
Cilium biogenesis/degradation; Complete proteome; Cytoplasm;
Cytoplasmic vesicle; Cytoskeleton; Developmental protein;
Differentiation; Phosphoprotein; Polymorphism; Reference proteome;
Spermatogenesis; Transport; Ubl conjugation.
CHAIN 1 1083 Centrosomal protein of 131 kDa.
/FTId=PRO_0000064781.
DOMAIN 269 289 IQ.
MOD_RES 14 14 Phosphoserine.
{ECO:0000250|UniProtKB:Q62036}.
MOD_RES 35 35 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 47 47 Phosphoserine; by MAPKAPK2.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 78 78 Phosphoserine; by MAPKAPK2.
{ECO:0000244|PubMed:21406692}.
MOD_RES 89 89 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 105 105 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332}.
MOD_RES 114 114 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 146 146 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 150 150 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18669648}.
MOD_RES 381 381 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 383 383 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 453 453 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 499 499 Phosphoserine.
{ECO:0000250|UniProtKB:Q62036}.
MOD_RES 731 731 Phosphoserine.
{ECO:0000269|PubMed:26616734}.
MOD_RES 798 798 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
VAR_SEQ 491 493 Missing (in isoform 2 and isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_015823.
VAR_SEQ 777 812 Missing (in isoform 3). {ECO:0000305}.
/FTId=VSP_040204.
VARIANT 43 43 V -> I (in dbSNP:rs8067409).
/FTId=VAR_056740.
VARIANT 70 70 I -> V (in dbSNP:rs8067409).
/FTId=VAR_060226.
VARIANT 272 272 T -> A (in dbSNP:rs2466773).
{ECO:0000269|PubMed:10470851,
ECO:0000269|PubMed:15489334}.
/FTId=VAR_060227.
VARIANT 397 397 T -> A (in dbSNP:rs2659015).
{ECO:0000269|PubMed:10470851,
ECO:0000269|PubMed:15489334}.
/FTId=VAR_060228.
VARIANT 473 473 V -> A (in dbSNP:rs2659016).
{ECO:0000269|PubMed:10470851,
ECO:0000269|PubMed:15489334}.
/FTId=VAR_060229.
MUTAGEN 47 47 S->A: Partially reduces in vitro
phosphorylation by MAPKAPK2 and decreases
binding to 14-3-3. Abolishes in vitro
phosphorylation by MAPKAPK2, interaction
with 14-3-3 and stress-induced centriolar
satellite remodeling; when associated
with A-78. {ECO:0000269|PubMed:26616734}.
MUTAGEN 78 78 S->A: Partially reduces in vitro
phosphorylation by MAPKAPK2 and decreases
binding to 14-3-3. Abolishes in vitro
phosphorylation by MAPKAPK2, interaction
with 14-3-3 and stress-induced centriolar
satellite remodeling; when associated
with A-47. {ECO:0000269|PubMed:26616734}.
MUTAGEN 731 731 S->A: No effect on interaction with 14-3-
3. {ECO:0000269|PubMed:26616734}.
SEQUENCE 1083 AA; 122149 MW; 31C8CA426569CCAC CRC64;
MKGTRAIGSV PERSPAGVDL SLTGLPPPVS RRPGSAATTK PIVRSVSVVT GSEQKRKVLE
ATGPGGSQAI NNLRRSNSTT QVSQPRSGSP RPTEPTDFLM LFEGSPSGKK RPASLSTAPS
EKGATWNVLD DQPRGFTLPS NARSSSALDS PAGPRRKECT VALAPNFTAN NRSNKGAVGN
CVTTMVHNRY TPSERAPPLK SSNQTAPSLN NIIKAATCEG SESSGFGKLP KNVSSATHSA
RNNTGGSTGL PRRKEVTEEE AERFIHQVNQ ATVTIQRWYR HQVQRRGAGA ARLEHLLQAK
REEQRQRSGE GTLLDLHQQK EAARRKAREE KARQARRAAI QELQQKRALR AQKASTAERG
PPENPRETRV PGMRQPAQEL SPTPGGTAHQ ALKANNTGGG LPAAGPGDRC LPTSDSSPEP
QQPPEDRTQD VLAQDAAGDN LEMMAPSRGS AKSRGPLEEL LHTLQLLEKE PDVLPRPRTH
HRGRYAWASE VTTEDDASSL TADNLEKFGK LSAFPEPPED GTLLSEAKLQ SIMSFLDEME
KSGQDQLDSQ QEGWVPEAGP GPLELGSEVS TSVMRLKLEV EEKKQAMLLL QRALAQQRDL
TARRVKETEK ALSRQLQRQR EHYEATIQRH LAFIDQLIED KKVLSEKCEA VVAELKQEDQ
RCTERVAQAQ AQHELEIKKL KELMSATEKA RREKWISEKT KKIKEVTVRG LEPEIQKLIA
RHKQEVRRLK SLHEAELLQS DERASQRCLR QAEELREQLE REKEALGQQE RERARQRFQQ
HLEQEQWALQ QQRQRLYSEV AEERERLGQQ AARQRAELEE LRQQLEESSS ALTRALRAEF
EKGREEQERR HQMELNTLKQ QLELERQAWE AGRTRKEEAW LLNREQELRE EIRKGRDKEI
ELVIHRLEAD MALAKEESEK AAESRIKRLR DKYEAELSEL EQSERKLQER CSELKGQLGE
AEGENLRLQG LVRQKERALE DAQAVNEQLS SERSNLAQVI RQEFEDRLAA SEEETRQAKA
ELATLQARQQ LELEEVHRRV KTALARKEEA VSSLRTQHEA AVKRADHLEE LLEQHRRPTP
STK


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