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A8MT69 (CENPX_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 62. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Centromere protein X

Short name=CENP-X
Alternative name(s):
FANCM-interacting histone fold protein 2
Fanconi anemia-associated polypeptide of 10 kDa
Retinoic acid-inducible gene D9 protein homolog
Stimulated by retinoic acid gene 13 protein homolog
Gene names
Name:STRA13
Synonyms:CENPX, FAAP10, MHF2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length81 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

DNA-binding component of the FA core complex involved in DNA damage repair and genome maintenance. Recruited to forks stalled by DNA interstrand cross-links, and required for cellular resistance to such lesions. Component of the heterotetrameric CENP-T-W-S-X complex that binds and supercoils DNA, and plays an important role in kinetochore assembly. Component of the APITD1/CENPS complex that is essential for the stable assembly of the outer kinetochore. Plays an important role in mitotic progression and chromosome segregation. Ref.4 Ref.5 Ref.6

Subunit structure

Belongs to the multisubunit FA complex composed of APITD1/CENPS, FANCA, FANCB, FANCC, FANCE, FANCF, FANCG, FANCL/PHF9, FANCM, FAAP24 and STRA13/CENPX. Interacts with APITD1/CENPS, FANCM and FAAP24. Component of a discrete APITD1/CENPS complex composed of at least APITD1/CENPS and STRA13/CENPX; this complex binds DNA. The heterodimer composed of APITD1/CENPS and STRA13/CENPX can dimerize to form a heterotetramer. Component of a heterotetrameric CENP-T-W-S-X complex composed of APITD1/CENPS, STRA13/CENPX, CENPT and CENPW. Ref.4 Ref.5 Ref.6 Ref.7

Subcellular location

Nucleus. Chromosomecentromere. Chromosomecentromerekinetochore. Note: Constitutively localizes to centromeres throughout the cell cycle, and to kinetochores during mitosis. Ref.5 Ref.6

Sequence similarities

Belongs to the CENPX family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

APITD1Q8N2Z96EBI-5529694,EBI-5529649

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: A8MT69-1)

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.
Isoform 2 (identifier: A8MT69-2)

Also known as: Variant A;

The sequence of this isoform differs from the canonical sequence as follows:
     30-47: Missing.
Isoform 3 (identifier: A8MT69-3)

Also known as: Variant B;

The sequence of this isoform differs from the canonical sequence as follows:
     30-47: Missing.
     73-77: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 8181Centromere protein X
PRO_0000337180

Amino acid modifications

Modified residue11N-acetylmethionine Ref.8

Natural variations

Alternative sequence30 – 4718Missing in isoform 2 and isoform 3.
VSP_033948
Alternative sequence73 – 775Missing in isoform 3.
VSP_033949

Experimental info

Sequence conflict651V → A in AAH09571. Ref.3
Sequence conflict731V → L in AAB53638. Ref.1

Secondary structure

......... 81
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified December 4, 2007. Version 1.
Checksum: 0BA47A4F0FFD2978

FASTA818,959
        10         20         30         40         50         60 
MEGAGAGSGF RKELVSRLLH LHFKDDKTKV SGDALQLMVE LLKVFVVEAA VRGVRQAQAE 

        70         80 
DALRVDVDQL EKVLPQLLLD F 

« Hide

Isoform 2 (Variant A) [UniParc].

Checksum: B751CBF3D27E6B1A
Show »

FASTA637,017
Isoform 3 (Variant B) [UniParc].

Checksum: 5166DA91818795E5
Show »

FASTA586,466

References

« Hide 'large scale' references
[1]"Nucleotide sequence of two human D9 transcripts."
Scott L.M., Collins S.J.
Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3).
[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. expand/collapse author list , 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), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-81 (ISOFORM 3).
Tissue: Placenta and Skin.
[4]"The CENP-S complex is essential for the stable assembly of outer kinetochore structure."
Amano M., Suzuki A., Hori T., Backer C., Okawa K., Cheeseman I.M., Fukagawa T.
J. Cell Biol. 186:173-182(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH APITD1.
[5]"A histone-fold complex and FANCM form a conserved DNA-remodeling complex to maintain genome stability."
Yan Z., Delannoy M., Ling C., Daee D., Osman F., Muniandy P.A., Shen X., Oostra A.B., Du H., Steltenpool J., Lin T., Schuster B., Decaillet C., Stasiak A., Stasiak A.Z., Stone S., Hoatlin M.E., Schindler D. expand/collapse author list , Woodcock C.L., Joenje H., Sen R., de Winter J.P., Li L., Seidman M.M., Whitby M.C., Myung K., Constantinousend A., Wang W.
Mol. Cell 37:865-878(2010)
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE FA CORE COMPLEX, INTERACTION WITH FANCM AND APITD1, SUBCELLULAR LOCATION, DNA-BINDING, FUNCTION.
[6]"MHF1-MHF2, a histone-fold-containing protein complex, participates in the Fanconi anemia pathway via FANCM."
Singh T.R., Saro D., Ali A.M., Zheng X.-F., Du C., Killen M.W., Sachpatzidis A., Wahengbam K., Pierce A.J., Xiong Y., Sung P., Meetei A.R.
Mol. Cell 37:879-886(2010)
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE FA CORE COMPLEX, INTERACTION WITH FANCM AND APITD1, SUBCELLULAR LOCATION, DNA-BINDING, FUNCTION.
[7]"CENP-T-W-S-X forms a unique centromeric chromatin structure with a histone-like fold."
Nishino T., Takeuchi K., Gascoigne K.E., Suzuki A., Hori T., Oyama T., Morikawa K., Cheeseman I.M., Fukagawa T.
Cell 148:487-501(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT.
[8]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U95006 mRNA. Translation: AAB53638.1.
U95007 mRNA. Translation: AAB53639.1.
AC137723 Genomic DNA. No translation available.
BC009571 mRNA. Translation: AAH09571.1.
BC011610 mRNA. Translation: AAH11610.1.
CCDSCCDS32772.1. [A8MT69-2]
CCDS59302.1. [A8MT69-3]
CCDS59303.1. [A8MT69-1]
RefSeqNP_001257935.1. NM_001271006.1. [A8MT69-1]
NP_001257936.1. NM_001271007.1. [A8MT69-3]
NP_659435.2. NM_144998.3. [A8MT69-2]
UniGeneHs.37616.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4DRAX-ray2.41E/F/G/H1-81[»]
4DRBX-ray2.63J/K/L/M/N/O1-81[»]
4E44X-ray2.10B/D1-81[»]
4E45X-ray2.00B/D/G/I/L/N1-81[»]
4NDYX-ray7.00B/D/H/L/M/N/U/V/W/X8-81[»]
4NE1X-ray6.50B/D/H/L/M/N/U/V/W/X/Z/b/d/h/i/j/o/p/q/r8-81[»]
4NE3X-ray1.80B8-81[»]
4NE5X-ray2.50B/D/F/H8-81[»]
4NE6X-ray2.10B/D8-81[»]
ProteinModelPortalA8MT69.
SMRA8MT69. Positions 8-81.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid128376. 7 interactions.
IntActA8MT69. 1 interaction.
STRING9606.ENSP00000302951.

Proteomic databases

MaxQBA8MT69.
PaxDbA8MT69.
PRIDEA8MT69.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000306704; ENSP00000302951; ENSG00000169689. [A8MT69-2]
ENST00000392359; ENSP00000376168; ENSG00000169689. [A8MT69-1]
ENST00000580435; ENSP00000462015; ENSG00000169689. [A8MT69-3]
GeneID201254.
KEGGhsa:201254.
UCSCuc002kdc.4. human. [A8MT69-2]
uc002kdd.4. human. [A8MT69-3]
uc031rey.1. human. [A8MT69-1]

Organism-specific databases

CTD201254.
GeneCardsGC17M079977.
H-InvDBHIX0014271.
HGNCHGNC:11422. STRA13.
HPAHPA027348.
neXtProtNX_A8MT69.
PharmGKBPA36223.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG71130.
HOGENOMHOG000231242.
InParanoidA8MT69.
KOK15360.
PhylomeDBA8MT69.

Gene expression databases

ArrayExpressA8MT69.
BgeeA8MT69.
CleanExHS_STRA13.
GenevestigatorA8MT69.

Family and domain databases

InterProIPR018552. CENP-X.
[Graphical view]
PfamPF09415. CENP-X. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi201254.
NextBio90103.
PROA8MT69.

Entry information

Entry nameCENPX_HUMAN
AccessionPrimary (citable) accession number: A8MT69
Secondary accession number(s): O00281 expand/collapse secondary AC list , O00282, Q96DD4, Q96F51
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: December 4, 2007
Last modified: July 9, 2014
This is version 62 of the entry and version 1 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM