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Q9HC77

- CENPJ_HUMAN

UniProt

Q9HC77 - CENPJ_HUMAN

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Protein
Centromere protein J
Gene
CENPJ, CPAP, LAP, LIP1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Plays an important role in cell division and centrosome function by participating in centriole duplication. Inhibits microtubule nucleation from the centrosome.3 Publications

GO - Molecular functioni

  1. protein binding Source: UniProtKB
  2. protein domain specific binding Source: UniProtKB
  3. protein kinase binding Source: UniProtKB
  4. tubulin binding Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  1. G2/M transition of mitotic cell cycle Source: Reactome
  2. cell division Source: UniProtKB
  3. centriole replication Source: UniProtKB
  4. microtubule nucleation Source: UniProtKB
  5. microtubule polymerization Source: UniProtKB
  6. mitotic cell cycle Source: Reactome
  7. regulation of centriole replication Source: UniProtKB
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_15296. Recruitment of mitotic centrosome proteins and complexes.
REACT_15364. Loss of Nlp from mitotic centrosomes.
REACT_15451. Loss of proteins required for interphase microtubule organization from the centrosome.
REACT_160315. Regulation of PLK1 Activity at G2/M Transition.

Names & Taxonomyi

Protein namesi
Recommended name:
Centromere protein J
Short name:
CENP-J
Alternative name(s):
Centrosomal P4.1-associated protein
LAG-3-associated protein
LYST-interacting protein 1
Gene namesi
Name:CENPJ
Synonyms:CPAP, LAP, LIP1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 13

Organism-specific databases

HGNCiHGNC:17272. CENPJ.

Subcellular locationi

Cytoplasmcytoskeletonmicrotubule organizing centercentrosome. Cytoplasmcytoskeletonmicrotubule organizing centercentrosomecentriole
Note: Localized within the center of microtubule asters. During centriole biogenesis, it is concentrated within the proximal lumen of both parental centrioles and procentrioles.3 Publications

GO - Cellular componenti

  1. centriole Source: UniProtKB
  2. centrosome Source: UniProtKB
  3. cytosol Source: Reactome
  4. gamma-tubulin small complex Source: UniProtKB
  5. microtubule Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule

Pathology & Biotechi

Involvement in diseasei

Microcephaly 6, primary, autosomal recessive (MCPH6) [MIM:608393]: A disease defined as a head circumference more than 3 standard deviations below the age-related mean. Brain weight is markedly reduced and the cerebral cortex is disproportionately small. Despite this marked reduction in size, the gyral pattern is relatively well preserved, with no major abnormality in cortical architecture. Affected individuals are mentally retarded. Primary microcephaly is further defined by the absence of other syndromic features or significant neurological deficits due to degenerative brain disorder.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti1235 – 12351E → V in MCPH6. 1 Publication
VAR_032433
Seckel syndrome 4 (SCKL4) [MIM:613676]: A rare autosomal recessive disorder characterized by proportionate dwarfism of prenatal onset associated with low birth weight, growth retardation, severe microcephaly with a bird-headed like appearance, and mental retardation.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi589 – 5891S → A: Abolishes phosphorylation by PLK2 and procentriole formation; when associated with A-595. 1 Publication
Mutagenesisi595 – 5951S → A: Abolishes phosphorylation by PLK2 and procentriole formation; when associated with A-589. 1 Publication

Keywords - Diseasei

Disease mutation, Dwarfism, Mental retardation, Primary microcephaly

Organism-specific databases

MIMi608393. phenotype.
613676. phenotype.
Orphaneti2512. Autosomal recessive primary microcephaly.
808. Seckel syndrome.
PharmGKBiPA26403.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 13381338Centromere protein J
PRO_0000089480Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei589 – 5891Phosphoserine; by PLK21 Publication
Modified residuei595 – 5951Phosphoserine; by PLK2 and PLK41 Publication
Modified residuei759 – 7591Phosphoserine1 Publication

Post-translational modificationi

Phosphorylation at Ser-589 and Ser-595 by PLK2 is required for procentriole formation and centriole elongation. Phosphorylation by PLK2 oscillates during the cell cycle: it increases at G1/S transition and decreases during the exit from mitosis. Phosphorylation at Ser-595 is also mediated by PLK4 but is not a critical step in PLK4 function in procentriole assembly.

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9HC77.
PaxDbiQ9HC77.
PRIDEiQ9HC77.

PTM databases

PhosphoSiteiQ9HC77.

Expressioni

Gene expression databases

ArrayExpressiQ9HC77.
BgeeiQ9HC77.
CleanExiHS_CENPJ.
GenevestigatoriQ9HC77.

Interactioni

Subunit structurei

Part of a ternary complex composed of SASS6, CENPJ and CEP350. Associated with the gamma-tubulin complex. Interacts with the head domain of EPB41. Interacts with LYST. Interacts with CEP152 (via C-terminus).4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CEP135Q66GS98EBI-946194,EBI-1046993
CICQ96RK02EBI-946194,EBI-945857
GFI1BQ5VTD92EBI-946194,EBI-946212
PLK2Q9NYY33EBI-946194,EBI-721354
STILQ1546812EBI-946194,EBI-7488405
TNKSO952714EBI-946194,EBI-1105254

Protein-protein interaction databases

BioGridi120939. 13 interactions.
DIPiDIP-49904N.
IntActiQ9HC77. 16 interactions.
STRINGi9606.ENSP00000371308.

Structurei

3D structure databases

ProteinModelPortaliQ9HC77.
SMRiQ9HC77. Positions 1166-1318.

Family & Domainsi

Sequence similaritiesi

Belongs to the TCP10 family.

Phylogenomic databases

eggNOGiNOG83204.
HOGENOMiHOG000111541.
HOVERGENiHBG050894.
InParanoidiQ9HC77.
KOiK11502.
OMAiDSPQVCD.
OrthoDBiEOG77DJ60.
PhylomeDBiQ9HC77.
TreeFamiTF343156.

Family and domain databases

InterProiIPR009852. Tcp10_C_dom.
IPR026581. TCP10_fam.
[Graphical view]
PANTHERiPTHR10331. PTHR10331. 1 hit.
PfamiPF07202. Tcp10_C. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9HC77-1 [UniParc]FASTAAdd to Basket

« Hide

MFLMPTSSEL NSGQNFLTQW MTNPSRAGVI LNRGFPILEA DKEKRAAVDI     50
STSFPIKGTH FSDSFSFINE EDSLLEEQKL ESNNPYKPQS DKSETHTAFP 100
CIKKGPQVAA CHSAPGHQEE NKNDFIPDLA SEFKEGAYKD PLFKKLEQLK 150
EVQQKKQEQL KRQQLEQLQR LMEEQEKLLT MVSGQCTLPG LSLLPDDQSQ 200
KHRSPGNTTT GERATCCFPS YVYPDPTQEE TYPSNILSHE QSNFCRTAHG 250
DFVLTSKRAS PNLFSEAQYQ EAPVEKNNLK EENRNHPTGE SILCWEKVTE 300
QIQEANDKNL QKHDDSSEVA NIEERPIKAA IGERKQTFED YLEEQIQLEE 350
QELKQKQLKE AEGPLPIKAK PKQPFLKRGE GLARFTNAKS KFQKGKESKL 400
VTNQSTSEDQ PLFKMDRQQL QRKTALKNKE LCADNPILKK DSKARTKSGS 450
VTLSQKPKML KCSNRKSLSP SGLKIQTGKK CDGQFRDQIK FENKVTSNNK 500
ENVTECPKPC DTGCTGWNKT QGKDRLPLST GPASRLAAKS PIRETMKESE 550
SSLDVSLQKK LETWEREKEK ENLELDEFLF LEQAADEISF SSNSSFVLKI 600
LERDQQICKG HRMSSTPVKA VPQKTNPADP ISHCNRSEDL DHTAREKESE 650
CEVAPKQLHS LSSADELREQ PCKIRKAVQK STSENQTEWN ARDDEGVPNS 700
DSSTDSEEQL DVTIKPSTED RERGISSRED SPQVCDDKGP FKDTRTQEDK 750
RRDVDLDLSD KDYSSDESIM ESIKHKVSEP SRSSSLSLSK MDFDDERTWT 800
DLEENLCNHD VVLGNESTYG TPQTCYPNNE IGILDKTIKR KIAPVKRGED 850
LSKSRRSRSP PTSELMMKFF PSLKPKPKSD SHLGNELKLN ISQDQPPGDN 900
ARSQVLREKI IELETEIEKF KAENASLAKL RIERESALEK LRKEIADFEQ 950
QKAKELARIE EFKKEEMRKL QKERKVFEKY TTAARTFPDK KEREEIQTLK 1000
QQIADLREDL KRKETKWSST HSRLRSQIQM LVRENTDLRE EIKVMERFRL 1050
DAWKRAEAIE SSLEVEKKDK LANTSVRFQN SQISSGTQVE KYKKNYLPMQ 1100
GNPPRRSKSA PPRDLGNLDK GQAASPREPL EPLNFPDPEY KEEEEDQDIQ 1150
GEISHPDGKV EKVYKNGCRV ILFPNGTRKE VSADGKTITV TFFNGDVKQV 1200
MPDQRVIYYY AAAQTTHTTY PEGLEVLHFS SGQIEKHYPD GRKEITFPDQ 1250
TVKNLFPDGQ EESIFPDGTI VRVQRDGNKL IEFNNGQREL HTAQFKRREY 1300
PDGTVKTVYA NGHQETKYRS GRIRVKDKEG NVLMDTEL 1338
Length:1,338
Mass (Da):153,000
Last modified:April 26, 2005 - v2
Checksum:iB4E6531B62A30F2D
GO

Sequence cautioni

The sequence AAH24209.3 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti21 – 211M → V.
Corresponds to variant rs35498994 [ dbSNP | Ensembl ].
VAR_032427
Natural varianti55 – 551P → A.
Corresponds to variant rs17081389 [ dbSNP | Ensembl ].
VAR_032428
Natural varianti63 – 631D → H.
Corresponds to variant rs7336216 [ dbSNP | Ensembl ].
VAR_032429
Natural varianti85 – 851P → T.
Corresponds to variant rs9511510 [ dbSNP | Ensembl ].
VAR_032430
Natural varianti151 – 1511E → G.
Corresponds to variant rs34177811 [ dbSNP | Ensembl ].
VAR_032431
Natural varianti879 – 8791S → A.
Corresponds to variant rs17402892 [ dbSNP | Ensembl ].
VAR_032432
Natural varianti1235 – 12351E → V in MCPH6. 1 Publication
VAR_032433

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti129 – 1291L → R in AAG21074. 1 Publication
Sequence conflicti1142 – 11421E → R in AAG49440. 1 Publication
Sequence conflicti1224 – 12241L → W in AAG49440. 1 Publication
Sequence conflicti1333 – 13331L → S in AAG21074. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF139625 mRNA. Translation: AAG21074.1.
AL354798 Genomic DNA. Translation: CAI16635.1.
BC024209 mRNA. Translation: AAH24209.3. Different initiation.
BC113110 mRNA. Translation: AAI13111.1.
BC113662 mRNA. Translation: AAI13663.1.
BC113664 mRNA. Translation: AAI13665.1.
AJ303006 mRNA. Translation: CAC80028.1.
AF141337 mRNA. Translation: AAG49440.1.
CCDSiCCDS9310.1.
RefSeqiNP_060921.3. NM_018451.4.
UniGeneiHs.513379.
Hs.741581.

Genome annotation databases

EnsembliENST00000381884; ENSP00000371308; ENSG00000151849.
GeneIDi55835.
KEGGihsa:55835.
UCSCiuc001upt.5. human.

Polymorphism databases

DMDMi62899891.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF139625 mRNA. Translation: AAG21074.1 .
AL354798 Genomic DNA. Translation: CAI16635.1 .
BC024209 mRNA. Translation: AAH24209.3 . Different initiation.
BC113110 mRNA. Translation: AAI13111.1 .
BC113662 mRNA. Translation: AAI13663.1 .
BC113664 mRNA. Translation: AAI13665.1 .
AJ303006 mRNA. Translation: CAC80028.1 .
AF141337 mRNA. Translation: AAG49440.1 .
CCDSi CCDS9310.1.
RefSeqi NP_060921.3. NM_018451.4.
UniGenei Hs.513379.
Hs.741581.

3D structure databases

ProteinModelPortali Q9HC77.
SMRi Q9HC77. Positions 1166-1318.
ModBasei Search...

Protein-protein interaction databases

BioGridi 120939. 13 interactions.
DIPi DIP-49904N.
IntActi Q9HC77. 16 interactions.
STRINGi 9606.ENSP00000371308.

PTM databases

PhosphoSitei Q9HC77.

Polymorphism databases

DMDMi 62899891.

Proteomic databases

MaxQBi Q9HC77.
PaxDbi Q9HC77.
PRIDEi Q9HC77.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000381884 ; ENSP00000371308 ; ENSG00000151849 .
GeneIDi 55835.
KEGGi hsa:55835.
UCSCi uc001upt.5. human.

Organism-specific databases

CTDi 55835.
GeneCardsi GC13M025456.
GeneReviewsi CENPJ.
HGNCi HGNC:17272. CENPJ.
MIMi 608393. phenotype.
609279. gene.
613676. phenotype.
neXtProti NX_Q9HC77.
Orphaneti 2512. Autosomal recessive primary microcephaly.
808. Seckel syndrome.
PharmGKBi PA26403.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG83204.
HOGENOMi HOG000111541.
HOVERGENi HBG050894.
InParanoidi Q9HC77.
KOi K11502.
OMAi DSPQVCD.
OrthoDBi EOG77DJ60.
PhylomeDBi Q9HC77.
TreeFami TF343156.

Enzyme and pathway databases

Reactomei REACT_15296. Recruitment of mitotic centrosome proteins and complexes.
REACT_15364. Loss of Nlp from mitotic centrosomes.
REACT_15451. Loss of proteins required for interphase microtubule organization from the centrosome.
REACT_160315. Regulation of PLK1 Activity at G2/M Transition.

Miscellaneous databases

GeneWikii CENPJ.
GenomeRNAii 55835.
NextBioi 61057.
PROi Q9HC77.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9HC77.
Bgeei Q9HC77.
CleanExi HS_CENPJ.
Genevestigatori Q9HC77.

Family and domain databases

InterProi IPR009852. Tcp10_C_dom.
IPR026581. TCP10_fam.
[Graphical view ]
PANTHERi PTHR10331. PTHR10331. 1 hit.
Pfami PF07202. Tcp10_C. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Protein 4.1 R-135 interacts with a novel centrosomal protein (CPAP) which is associated with the gamma-tubulin complex."
    Hung L.-Y., Tang C.J., Tang T.K.
    Mol. Cell. Biol. 20:7813-7825(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, INTERACTION WITH EPB41.
  2. "The DNA sequence and analysis of human chromosome 13."
    Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.
    Nature 428:522-528(2004) [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].
    Tissue: Muscle.
  4. "LAP, a lymphocyte activation gene-3-associated protein that binds to a repeated EP motif in the intracellular region of LAG-3 may participate in the down-regulation of the CD3/TCR activation pathway."
    Andreae S., Triebel P.F.
    Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 967-1338.
  5. "The Chediak-Higashi protein interacts with SNARE complex and signal transduction proteins."
    Tchernev V.T., Mansfield T.A., Giot L., Kumar A.M., Nandabalan K., Li Y., Mishra V.S., Detter J.C., Rothberg J.M., Wallace M.R., Southwick F.S., Kingsmore S.F.
    Mol. Med. 8:56-64(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1142-1338, INTERACTION WITH LYST.
  6. "Identification of a novel microtubule-destabilizing motif in CPAP that binds to tubulin heterodimers and inhibits microtubule assembly."
    Hung L.-Y., Chen H.-L., Chang C.-W., Li B.-R., Tang T.K.
    Mol. Biol. Cell 15:2697-2706(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN MICROTUBULE DESTABILIZATION.
  7. Cited for: FUNCTION, SUBCELLULAR LOCATION.
  8. "Role of CAP350 in centriolar tubule stability and centriole assembly."
    Le Clech M.
    PLoS ONE 3:E3855-E3855(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A COMPLEX WITH SASS6 AND CEP350.
  9. "PLK2 phosphorylation is critical for CPAP function in procentriole formation during the centrosome cycle."
    Chang J., Cizmecioglu O., Hoffmann I., Rhee K.
    EMBO J. 29:2395-2406(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-589 AND SER-595, MUTAGENESIS OF SER-589 AND SER-595.
  10. Cited for: INVOLVEMENT IN SCKL4.
  11. Cited for: INTERACTION WITH CEP152.
  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-759, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. Cited for: VARIANT MCPH6 VAL-1235.

Entry informationi

Entry nameiCENPJ_HUMAN
AccessioniPrimary (citable) accession number: Q9HC77
Secondary accession number(s): Q2KHM6
, Q5T6R5, Q96KS5, Q9C067
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 26, 2005
Last sequence update: April 26, 2005
Last modified: September 3, 2014
This is version 108 of the entry and version 2 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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 13
    Human chromosome 13: 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

External Data

Dasty 3

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