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Q9HC77 (CENPJ_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 107. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:CENPJ
Synonyms:CPAP, LAP, LIP1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1338 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Plays an important role in cell division and centrosome function by participating in centriole duplication. Inhibits microtubule nucleation from the centrosome. Ref.6 Ref.7 Ref.9

Subunit structure

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). Ref.1 Ref.5 Ref.8 Ref.11

Subcellular location

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. Ref.1 Ref.7 Ref.9

Post-translational modification

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.

Involvement in disease

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. Ref.13

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. Ref.10

Sequence similarities

Belongs to the TCP10 family.

Sequence caution

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

Ontologies

Keywords
   Cellular componentCytoplasm
Cytoskeleton
Microtubule
   Coding sequence diversityPolymorphism
   DiseaseDisease mutation
Dwarfism
Mental retardation
Primary microcephaly
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processG2/M transition of mitotic cell cycle

Traceable author statement. Source: Reactome

cell division

Non-traceable author statement Ref.1. Source: UniProtKB

centriole replication

Inferred from mutant phenotype Ref.7. Source: UniProtKB

microtubule nucleation

Traceable author statement Ref.1. Source: UniProtKB

microtubule polymerization

Inferred from mutant phenotype Ref.6. Source: UniProtKB

mitotic cell cycle

Traceable author statement. Source: Reactome

regulation of centriole replication

Inferred from mutant phenotype Ref.9. Source: UniProtKB

   Cellular_componentcentriole

Inferred from direct assay Ref.7Ref.9. Source: UniProtKB

centrosome

Inferred from direct assay PubMed 21399614. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

gamma-tubulin small complex

Non-traceable author statement Ref.1. Source: UniProtKB

microtubule

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionprotein binding

Inferred from physical interaction Ref.1Ref.11. Source: UniProtKB

protein domain specific binding

Inferred from physical interaction Ref.5. Source: UniProtKB

protein kinase binding

Inferred from physical interaction Ref.9. Source: UniProtKB

tubulin binding

Inferred from direct assay Ref.6. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 13381338Centromere protein J
PRO_0000089480

Amino acid modifications

Modified residue5891Phosphoserine; by PLK2 Ref.9
Modified residue5951Phosphoserine; by PLK2 and PLK4 Ref.9
Modified residue7591Phosphoserine Ref.12

Natural variations

Natural variant211M → V.
Corresponds to variant rs35498994 [ dbSNP | Ensembl ].
VAR_032427
Natural variant551P → A.
Corresponds to variant rs17081389 [ dbSNP | Ensembl ].
VAR_032428
Natural variant631D → H.
Corresponds to variant rs7336216 [ dbSNP | Ensembl ].
VAR_032429
Natural variant851P → T.
Corresponds to variant rs9511510 [ dbSNP | Ensembl ].
VAR_032430
Natural variant1511E → G.
Corresponds to variant rs34177811 [ dbSNP | Ensembl ].
VAR_032431
Natural variant8791S → A.
Corresponds to variant rs17402892 [ dbSNP | Ensembl ].
VAR_032432
Natural variant12351E → V in MCPH6. Ref.13
VAR_032433

Experimental info

Mutagenesis5891S → A: Abolishes phosphorylation by PLK2 and procentriole formation; when associated with A-595. Ref.9
Mutagenesis5951S → A: Abolishes phosphorylation by PLK2 and procentriole formation; when associated with A-589. Ref.9
Sequence conflict1291L → R in AAG21074. Ref.1
Sequence conflict11421E → R in AAG49440. Ref.5
Sequence conflict12241L → W in AAG49440. Ref.5
Sequence conflict13331L → S in AAG21074. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9HC77 [UniParc].

Last modified April 26, 2005. Version 2.
Checksum: B4E6531B62A30F2D

FASTA1,338153,000
        10         20         30         40         50         60 
MFLMPTSSEL NSGQNFLTQW MTNPSRAGVI LNRGFPILEA DKEKRAAVDI STSFPIKGTH 

        70         80         90        100        110        120 
FSDSFSFINE EDSLLEEQKL ESNNPYKPQS DKSETHTAFP CIKKGPQVAA CHSAPGHQEE 

       130        140        150        160        170        180 
NKNDFIPDLA SEFKEGAYKD PLFKKLEQLK EVQQKKQEQL KRQQLEQLQR LMEEQEKLLT 

       190        200        210        220        230        240 
MVSGQCTLPG LSLLPDDQSQ KHRSPGNTTT GERATCCFPS YVYPDPTQEE TYPSNILSHE 

       250        260        270        280        290        300 
QSNFCRTAHG DFVLTSKRAS PNLFSEAQYQ EAPVEKNNLK EENRNHPTGE SILCWEKVTE 

       310        320        330        340        350        360 
QIQEANDKNL QKHDDSSEVA NIEERPIKAA IGERKQTFED YLEEQIQLEE QELKQKQLKE 

       370        380        390        400        410        420 
AEGPLPIKAK PKQPFLKRGE GLARFTNAKS KFQKGKESKL VTNQSTSEDQ PLFKMDRQQL 

       430        440        450        460        470        480 
QRKTALKNKE LCADNPILKK DSKARTKSGS VTLSQKPKML KCSNRKSLSP SGLKIQTGKK 

       490        500        510        520        530        540 
CDGQFRDQIK FENKVTSNNK ENVTECPKPC DTGCTGWNKT QGKDRLPLST GPASRLAAKS 

       550        560        570        580        590        600 
PIRETMKESE SSLDVSLQKK LETWEREKEK ENLELDEFLF LEQAADEISF SSNSSFVLKI 

       610        620        630        640        650        660 
LERDQQICKG HRMSSTPVKA VPQKTNPADP ISHCNRSEDL DHTAREKESE CEVAPKQLHS 

       670        680        690        700        710        720 
LSSADELREQ PCKIRKAVQK STSENQTEWN ARDDEGVPNS DSSTDSEEQL DVTIKPSTED 

       730        740        750        760        770        780 
RERGISSRED SPQVCDDKGP FKDTRTQEDK RRDVDLDLSD KDYSSDESIM ESIKHKVSEP 

       790        800        810        820        830        840 
SRSSSLSLSK MDFDDERTWT DLEENLCNHD VVLGNESTYG TPQTCYPNNE IGILDKTIKR 

       850        860        870        880        890        900 
KIAPVKRGED LSKSRRSRSP PTSELMMKFF PSLKPKPKSD SHLGNELKLN ISQDQPPGDN 

       910        920        930        940        950        960 
ARSQVLREKI IELETEIEKF KAENASLAKL RIERESALEK LRKEIADFEQ QKAKELARIE 

       970        980        990       1000       1010       1020 
EFKKEEMRKL QKERKVFEKY TTAARTFPDK KEREEIQTLK QQIADLREDL KRKETKWSST 

      1030       1040       1050       1060       1070       1080 
HSRLRSQIQM LVRENTDLRE EIKVMERFRL DAWKRAEAIE SSLEVEKKDK LANTSVRFQN 

      1090       1100       1110       1120       1130       1140 
SQISSGTQVE KYKKNYLPMQ GNPPRRSKSA PPRDLGNLDK GQAASPREPL EPLNFPDPEY 

      1150       1160       1170       1180       1190       1200 
KEEEEDQDIQ GEISHPDGKV EKVYKNGCRV ILFPNGTRKE VSADGKTITV TFFNGDVKQV 

      1210       1220       1230       1240       1250       1260 
MPDQRVIYYY AAAQTTHTTY PEGLEVLHFS SGQIEKHYPD GRKEITFPDQ TVKNLFPDGQ 

      1270       1280       1290       1300       1310       1320 
EESIFPDGTI VRVQRDGNKL IEFNNGQREL HTAQFKRREY PDGTVKTVYA NGHQETKYRS 

      1330 
GRIRVKDKEG NVLMDTEL 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Plk4-induced centriole biogenesis in human cells."
Kleylein-Sohn J., Westendorf J., Le Clech M., Habedanck R., Stierhof Y.-D., Nigg E.A.
Dev. Cell 13:190-202(2007) [PubMed] [Europe PMC] [Abstract]
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]"Novel CENPJ mutation causes Seckel syndrome."
Al-Dosari M.S., Shaheen R., Colak D., Alkuraya F.S.
J. Med. Genet. 47:411-414(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN SCKL4.
[11]"Asterless is a scaffold for the onset of centriole assembly."
Dzhindzhev N.S., Yu Q.D., Weiskopf K., Tzolovsky G., Cunha-Ferreira I., Riparbelli M., Rodrigues-Martins A., Bettencourt-Dias M., Callaini G., Glover D.M.
Nature 467:714-718(2010) [PubMed] [Europe PMC] [Abstract]
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]"A centrosomal mechanism involving CDK5RAP2 and CENPJ controls brain size."
Bond J., Roberts E., Springell K., Lizarraga S.B., Scott S., Higgins J., Hampshire D.J., Morrison E.E., Leal G.F., Silva E.O., Costa S.M.R., Baralle D., Raponi M., Karbani G., Rashid Y., Jafri H., Bennett C., Corry P., Walsh C.A., Woods C.G.
Nat. Genet. 37:353-355(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT MCPH6 VAL-1235.
[14]Erratum
Bond J., Roberts E., Springell K., Lizarraga S.B., Scott S., Higgins J., Hampshire D.J., Morrison E.E., Leal G.F., Silva E.O., Costa S.M.R., Baralle D., Raponi M., Karbani G., Rashid Y., Jafri H., Bennett C., Corry P., Walsh C.A., Woods C.G.
Nat. Genet. 37:555-555(2005)
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS9310.1.
RefSeqNP_060921.3. NM_018451.4.
UniGeneHs.513379.
Hs.741581.

3D structure databases

ProteinModelPortalQ9HC77.
SMRQ9HC77. Positions 1166-1318.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid120939. 13 interactions.
DIPDIP-49904N.
IntActQ9HC77. 16 interactions.
STRING9606.ENSP00000371308.

PTM databases

PhosphoSiteQ9HC77.

Polymorphism databases

DMDM62899891.

Proteomic databases

MaxQBQ9HC77.
PaxDbQ9HC77.
PRIDEQ9HC77.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000381884; ENSP00000371308; ENSG00000151849.
GeneID55835.
KEGGhsa:55835.
UCSCuc001upt.5. human.

Organism-specific databases

CTD55835.
GeneCardsGC13M025456.
GeneReviewsCENPJ.
HGNCHGNC:17272. CENPJ.
MIM608393. phenotype.
609279. gene.
613676. phenotype.
neXtProtNX_Q9HC77.
Orphanet2512. Autosomal recessive primary microcephaly.
808. Seckel syndrome.
PharmGKBPA26403.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG83204.
HOGENOMHOG000111541.
HOVERGENHBG050894.
InParanoidQ9HC77.
KOK11502.
OMADSPQVCD.
OrthoDBEOG77DJ60.
PhylomeDBQ9HC77.
TreeFamTF343156.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.

Gene expression databases

ArrayExpressQ9HC77.
BgeeQ9HC77.
CleanExHS_CENPJ.
GenevestigatorQ9HC77.

Family and domain databases

InterProIPR009852. Tcp10_C_dom.
IPR026581. TCP10_fam.
[Graphical view]
PANTHERPTHR10331. PTHR10331. 1 hit.
PfamPF07202. Tcp10_C. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiCENPJ.
GenomeRNAi55835.
NextBio61057.
PROQ9HC77.
SOURCESearch...

Entry information

Entry nameCENPJ_HUMAN
AccessionPrimary (citable) accession number: Q9HC77
Secondary accession number(s): Q2KHM6 expand/collapse secondary AC list , Q5T6R5, Q96KS5, Q9C067
Entry history
Integrated into UniProtKB/Swiss-Prot: April 26, 2005
Last sequence update: April 26, 2005
Last modified: July 9, 2014
This is version 107 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 13

Human chromosome 13: entries, gene names and cross-references to MIM