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Protein

Centrosomal protein of 131 kDa

Gene

CEP131

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity7 Publications

GO - Molecular functioni

  • protein complex binding Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB

GO - Biological processi

  • cell differentiation Source: UniProtKB-KW
  • G2/M transition of mitotic cell cycle Source: Reactome
  • intraciliary transport involved in cilium morphogenesis Source: UniProtKB
  • multicellular organism development Source: UniProtKB-KW
  • positive regulation of cell proliferation Source: UniProtKB
  • positive regulation of intracellular protein transport Source: UniProtKB
  • protein localization to centrosome Source: UniProtKB
  • regulation of centrosome duplication Source: UniProtKB
  • spermatogenesis Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Cell cycle, Cilium biogenesis/degradation, Differentiation, Spermatogenesis, Transport

Enzyme and pathway databases

ReactomeiR-HSA-2565942. Regulation of PLK1 Activity at G2/M Transition.
R-HSA-380259. Loss of Nlp from mitotic centrosomes.
R-HSA-380270. Recruitment of mitotic centrosome proteins and complexes.
R-HSA-5620912. Anchoring of the basal body to the plasma membrane.
R-HSA-8854518. AURKA Activation by TPX2.

Names & Taxonomyi

Protein namesi
Recommended name:
Centrosomal protein of 131 kDa
Alternative name(s):
5-azacytidine-induced protein 1
Pre-acrosome localization protein 1
Gene namesi
Name:CEP131
Synonyms:AZI1, KIAA1118
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:29511. CEP131.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cytoplasm, Cytoplasmic vesicle, Cytoskeleton

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi47 – 471S → 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. 1 Publication
Mutagenesisi78 – 781S → 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. 1 Publication
Mutagenesisi731 – 7311S → A: No effect on interaction with 14-3-3. 1 Publication

Organism-specific databases

PharmGKBiPA128394595.
PA134920867.

Polymorphism and mutation databases

BioMutaiAZI1.
DMDMi313104247.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10831083Centrosomal protein of 131 kDaPRO_0000064781Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei14 – 141PhosphoserineBy similarity
Modified residuei35 – 351PhosphoserineCombined sources
Modified residuei47 – 471Phosphoserine; by MAPKAPK2Combined sources
Modified residuei78 – 781Phosphoserine; by MAPKAPK2Combined sources
Modified residuei89 – 891PhosphoserineCombined sources
Modified residuei105 – 1051PhosphoserineCombined sources
Modified residuei114 – 1141PhosphoserineCombined sources
Modified residuei146 – 1461PhosphoserineCombined sources
Modified residuei150 – 1501PhosphoserineCombined sources
Modified residuei381 – 3811PhosphoserineCombined sources
Modified residuei383 – 3831PhosphothreonineCombined sources
Modified residuei453 – 4531PhosphoserineCombined sources
Modified residuei499 – 4991PhosphoserineBy similarity
Modified residuei731 – 7311Phosphoserine1 Publication
Modified residuei798 – 7981PhosphoserineCombined sources
Isoform 2 (identifier: Q9UPN4-2)
Modified residuei489 – 4891PhosphoserineCombined sources
Modified residuei496 – 4961PhosphoserineCombined sources
Isoform 3 (identifier: Q9UPN4-3)
Modified residuei489 – 4891PhosphoserineCombined sources
Modified residuei496 – 4961PhosphoserineCombined sources

Post-translational modificationi

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.1 Publication
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.1 Publication

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ9UPN4.
MaxQBiQ9UPN4.
PaxDbiQ9UPN4.
PeptideAtlasiQ9UPN4.
PRIDEiQ9UPN4.

PTM databases

iPTMnetiQ9UPN4.
PhosphoSiteiQ9UPN4.

Expressioni

Inductioni

Up-regulated by the transcription factor SP1.1 Publication

Gene expression databases

BgeeiQ9UPN4.
CleanExiHS_AZI1.
ExpressionAtlasiQ9UPN4. baseline and differential.
GenevisibleiQ9UPN4. HS.

Organism-specific databases

HPAiHPA024019.
HPA049634.

Interactioni

Subunit structurei

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).6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CEP290O150789EBI-2558372,EBI-1811944

GO - Molecular functioni

  • protein complex binding Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB

Protein-protein interaction databases

BioGridi116641. 109 interactions.
DIPiDIP-56658N.
IntActiQ9UPN4. 89 interactions.
MINTiMINT-4541849.
STRINGi9606.ENSP00000393583.

Structurei

3D structure databases

ProteinModelPortaliQ9UPN4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini269 – 28921IQAdd
BLAST

Sequence similaritiesi

Belongs to the CEP131 family.Curated
Contains 1 IQ domain.Curated

Phylogenomic databases

eggNOGiENOG410IEUN. Eukaryota.
ENOG410YVPU. LUCA.
GeneTreeiENSGT00390000001758.
HOGENOMiHOG000293266.
HOVERGENiHBG024371.
InParanoidiQ9UPN4.
KOiK16540.
OMAiEKGATWN.
OrthoDBiEOG7CNZF5.
PhylomeDBiQ9UPN4.
TreeFamiTF328914.

Family and domain databases

InterProiIPR030465. CEP131.
[Graphical view]
PANTHERiPTHR31540:SF1. PTHR31540:SF1. 1 hit.

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9UPN4-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MKGTRAIGSV PERSPAGVDL SLTGLPPPVS RRPGSAATTK PIVRSVSVVT
60 70 80 90 100
GSEQKRKVLE ATGPGGSQAI NNLRRSNSTT QVSQPRSGSP RPTEPTDFLM
110 120 130 140 150
LFEGSPSGKK RPASLSTAPS EKGATWNVLD DQPRGFTLPS NARSSSALDS
160 170 180 190 200
PAGPRRKECT VALAPNFTAN NRSNKGAVGN CVTTMVHNRY TPSERAPPLK
210 220 230 240 250
SSNQTAPSLN NIIKAATCEG SESSGFGKLP KNVSSATHSA RNNTGGSTGL
260 270 280 290 300
PRRKEVTEEE AERFIHQVNQ ATVTIQRWYR HQVQRRGAGA ARLEHLLQAK
310 320 330 340 350
REEQRQRSGE GTLLDLHQQK EAARRKAREE KARQARRAAI QELQQKRALR
360 370 380 390 400
AQKASTAERG PPENPRETRV PGMRQPAQEL SPTPGGTAHQ ALKANNTGGG
410 420 430 440 450
LPAAGPGDRC LPTSDSSPEP QQPPEDRTQD VLAQDAAGDN LEMMAPSRGS
460 470 480 490 500
AKSRGPLEEL LHTLQLLEKE PDVLPRPRTH HRGRYAWASE VTTEDDASSL
510 520 530 540 550
TADNLEKFGK LSAFPEPPED GTLLSEAKLQ SIMSFLDEME KSGQDQLDSQ
560 570 580 590 600
QEGWVPEAGP GPLELGSEVS TSVMRLKLEV EEKKQAMLLL QRALAQQRDL
610 620 630 640 650
TARRVKETEK ALSRQLQRQR EHYEATIQRH LAFIDQLIED KKVLSEKCEA
660 670 680 690 700
VVAELKQEDQ RCTERVAQAQ AQHELEIKKL KELMSATEKA RREKWISEKT
710 720 730 740 750
KKIKEVTVRG LEPEIQKLIA RHKQEVRRLK SLHEAELLQS DERASQRCLR
760 770 780 790 800
QAEELREQLE REKEALGQQE RERARQRFQQ HLEQEQWALQ QQRQRLYSEV
810 820 830 840 850
AEERERLGQQ AARQRAELEE LRQQLEESSS ALTRALRAEF EKGREEQERR
860 870 880 890 900
HQMELNTLKQ QLELERQAWE AGRTRKEEAW LLNREQELRE EIRKGRDKEI
910 920 930 940 950
ELVIHRLEAD MALAKEESEK AAESRIKRLR DKYEAELSEL EQSERKLQER
960 970 980 990 1000
CSELKGQLGE AEGENLRLQG LVRQKERALE DAQAVNEQLS SERSNLAQVI
1010 1020 1030 1040 1050
RQEFEDRLAA SEEETRQAKA ELATLQARQQ LELEEVHRRV KTALARKEEA
1060 1070 1080
VSSLRTQHEA AVKRADHLEE LLEQHRRPTP STK
Length:1,083
Mass (Da):122,149
Last modified:November 30, 2010 - v3
Checksum:i31C8CA426569CCAC
GO
Isoform 2 (identifier: Q9UPN4-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     491-493: Missing.

Show »
Length:1,080
Mass (Da):121,847
Checksum:i87E96867F87F0FC3
GO
Isoform 3 (identifier: Q9UPN4-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     491-493: Missing.
     777-812: Missing.

Show »
Length:1,044
Mass (Da):117,397
Checksum:iE8307197B6D9111E
GO

Sequence cautioni

The sequence BAA83070.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti43 – 431V → I.
Corresponds to variant rs8067409 [ dbSNP | Ensembl ].
VAR_056740
Natural varianti70 – 701I → V.
Corresponds to variant rs8067409 [ dbSNP | Ensembl ].
VAR_060226
Natural varianti272 – 2721T → A.2 Publications
Corresponds to variant rs2466773 [ dbSNP | Ensembl ].
VAR_060227
Natural varianti397 – 3971T → A.2 Publications
Corresponds to variant rs2659015 [ dbSNP | Ensembl ].
VAR_060228
Natural varianti473 – 4731V → A.2 Publications
Corresponds to variant rs2659016 [ dbSNP | Ensembl ].
VAR_060229

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei491 – 4933Missing in isoform 2 and isoform 3. 1 PublicationVSP_015823
Alternative sequencei777 – 81236Missing in isoform 3. CuratedVSP_040204Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB029041 mRNA. Translation: BAA83070.1. Different initiation.
AC027601 Genomic DNA. No translation available.
BC011615 mRNA. Translation: AAH11615.2.
BC136580 mRNA. Translation: AAI36581.1.
CCDSiCCDS32764.1. [Q9UPN4-3]
CCDS45808.1. [Q9UPN4-2]
RefSeqiNP_001009811.2. NM_001009811.3. [Q9UPN4-3]
NP_001306157.1. NM_001319228.1. [Q9UPN4-1]
NP_055799.2. NM_014984.3. [Q9UPN4-2]
UniGeneiHs.514578.

Genome annotation databases

EnsembliENST00000269392; ENSP00000269392; ENSG00000141577. [Q9UPN4-1]
ENST00000374782; ENSP00000363914; ENSG00000141577. [Q9UPN4-3]
ENST00000450824; ENSP00000393583; ENSG00000141577. [Q9UPN4-2]
GeneIDi22994.
KEGGihsa:22994.
UCSCiuc002jzn.2. human. [Q9UPN4-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB029041 mRNA. Translation: BAA83070.1. Different initiation.
AC027601 Genomic DNA. No translation available.
BC011615 mRNA. Translation: AAH11615.2.
BC136580 mRNA. Translation: AAI36581.1.
CCDSiCCDS32764.1. [Q9UPN4-3]
CCDS45808.1. [Q9UPN4-2]
RefSeqiNP_001009811.2. NM_001009811.3. [Q9UPN4-3]
NP_001306157.1. NM_001319228.1. [Q9UPN4-1]
NP_055799.2. NM_014984.3. [Q9UPN4-2]
UniGeneiHs.514578.

3D structure databases

ProteinModelPortaliQ9UPN4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116641. 109 interactions.
DIPiDIP-56658N.
IntActiQ9UPN4. 89 interactions.
MINTiMINT-4541849.
STRINGi9606.ENSP00000393583.

PTM databases

iPTMnetiQ9UPN4.
PhosphoSiteiQ9UPN4.

Polymorphism and mutation databases

BioMutaiAZI1.
DMDMi313104247.

Proteomic databases

EPDiQ9UPN4.
MaxQBiQ9UPN4.
PaxDbiQ9UPN4.
PeptideAtlasiQ9UPN4.
PRIDEiQ9UPN4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000269392; ENSP00000269392; ENSG00000141577. [Q9UPN4-1]
ENST00000374782; ENSP00000363914; ENSG00000141577. [Q9UPN4-3]
ENST00000450824; ENSP00000393583; ENSG00000141577. [Q9UPN4-2]
GeneIDi22994.
KEGGihsa:22994.
UCSCiuc002jzn.2. human. [Q9UPN4-1]

Organism-specific databases

CTDi22994.
GeneCardsiCEP131.
H-InvDBHIX0014243.
HGNCiHGNC:29511. CEP131.
HPAiHPA024019.
HPA049634.
MIMi613479. gene.
neXtProtiNX_Q9UPN4.
PharmGKBiPA128394595.
PA134920867.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IEUN. Eukaryota.
ENOG410YVPU. LUCA.
GeneTreeiENSGT00390000001758.
HOGENOMiHOG000293266.
HOVERGENiHBG024371.
InParanoidiQ9UPN4.
KOiK16540.
OMAiEKGATWN.
OrthoDBiEOG7CNZF5.
PhylomeDBiQ9UPN4.
TreeFamiTF328914.

Enzyme and pathway databases

ReactomeiR-HSA-2565942. Regulation of PLK1 Activity at G2/M Transition.
R-HSA-380259. Loss of Nlp from mitotic centrosomes.
R-HSA-380270. Recruitment of mitotic centrosome proteins and complexes.
R-HSA-5620912. Anchoring of the basal body to the plasma membrane.
R-HSA-8854518. AURKA Activation by TPX2.

Miscellaneous databases

GeneWikiiAZI1.
GenomeRNAii22994.
PROiQ9UPN4.
SOURCEiSearch...

Gene expression databases

BgeeiQ9UPN4.
CleanExiHS_AZI1.
ExpressionAtlasiQ9UPN4. baseline and differential.
GenevisibleiQ9UPN4. HS.

Family and domain databases

InterProiIPR030465. CEP131.
[Graphical view]
PANTHERiPTHR31540:SF1. PTHR31540:SF1. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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."
    Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    DNA Res. 6:197-205(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANTS ALA-272; ALA-397 AND ALA-473.
    Tissue: Brain.
  2. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
    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.
    Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANTS ALA-272; ALA-397 AND ALA-473.
    Tissue: Lung.
  4. "Proteomic characterization of the human centrosome by protein correlation profiling."
    Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.
    Nature 426:570-574(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Tissue: Lymphoblast.
  5. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  6. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-150, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. "Cep164, a novel centriole appendage protein required for primary cilium formation."
    Graser S., Stierhof Y.-D., Lavoie S.B., Gassner O.S., Lamla S., Le Clech M., Nigg E.A.
    J. Cell Biol. 179:321-330(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN CILIOGENESIS.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47; SER-105 AND SER-150, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-489 (ISOFORMS 2 AND 3), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: 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), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  11. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    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.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47; SER-78 AND SER-453, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35; SER-47; SER-114; SER-146; SER-381; THR-383 AND SER-798, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma and Erythroleukemia.
  14. "Autophagy promotes primary ciliogenesis by removing OFD1 from centriolar satellites."
    Tang Z., Lin M.G., Stowe T.R., Chen S., Zhu M., Stearns T., Franco B., Zhong Q.
    Nature 502:254-257(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MAP1LC3B.
  15. Cited for: FUNCTION IN GENOMIC STABILITY, INTERACTION WITH CEP290; DCTN1; PCM1 AND PCNT, SUBCELLULAR LOCATION.
  16. "Cilia born out of shock and stress."
    Chavali P.L., Gergely F.
    EMBO J. 32:3011-3013(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW, FUNCTION.
  17. "A new cellular stress response that triggers centriolar satellite reorganization and ciliogenesis."
    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.
    EMBO J. 32:3029-3040(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN CILIOGENESIS, UBIQUITINATION BY MIB1, INTERACTION WITH MIB1 AND PCM1, ASSOCIATION WITH MICROTUBULES, SUBCELLULAR LOCATION.
  18. Cited for: INDUCTION.
  19. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  20. "The centriolar satellite protein AZI1 interacts with BBS4 and regulates ciliary trafficking of the BBSome."
    Chamling X., Seo S., Searby C.C., Kim G., Slusarski D.C., Sheffield V.C.
    PLoS Genet. 10:E1004083-E1004083(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN CILIARY TRAFFICKING, SUBUNIT, INTERACTION WITH BBS4, ASSOCIATION WITH THE BBSOME COMPLEX.
  21. "p38- and MK2-dependent signalling promotes stress-induced centriolar satellite remodelling via 14-3-3-dependent sequestration of CEP131/AZI1."
    Tollenaere M.A., Villumsen B.H., Blasius M., Nielsen J.C., Wagner S.A., Bartek J., Beli P., Mailand N., Bekker-Jensen S.
    Nat. Commun. 6:10075-10075(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH 14-3-3, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-47; SER-78 AND SER-731, MUTAGENESIS OF SER-47; SER-78 AND SER-731.
  22. "Centriolar satellites assemble centrosomal microcephaly proteins to recruit CDK2 and promote centriole duplication."
    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.
    Elife 4:0-0(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CEP152 AND PCM1.

Entry informationi

Entry nameiCP131_HUMAN
AccessioniPrimary (citable) accession number: Q9UPN4
Secondary accession number(s): A6NHI8, B2RN11, Q96F50
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 11, 2005
Last sequence update: November 30, 2010
Last modified: July 6, 2016
This is version 128 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

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 CEP131.2 Publications

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.