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Q15003 (CND2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 121. 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:
Condensin complex subunit 2
Alternative name(s):
Barren homolog protein 1
Chromosome-associated protein H
Short name=hCAP-H
Non-SMC condensin I complex subunit H
XCAP-H homolog
Gene names
Name:NCAPH
Synonyms:BRRN, BRRN1, CAPH, KIAA0074
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length741 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Regulatory subunit of the condensin complex, a complex required for conversion of interphase chromatin into mitotic-like condense chromosomes. The condensin complex probably introduces positive supercoils into relaxed DNA in the presence of type I topoisomerases and converts nicked DNA into positive knotted forms in the presence of type II topoisomerases. Ref.4

Subunit structure

Component of the condensin complex, which contains the SMC2 and SMC4 heterodimer, and three non SMC subunits that probably regulate the complex: NCAPH/BRRN1, NCAPD2/CAPD2 and NCAPG. Ref.4

Subcellular location

Nucleus. Cytoplasm. Chromosome. Note: In interphase cells, the majority of the condensin complex is found in the cytoplasm, while a minority of the complex is associated with chromatin. A subpopulation of the complex however remains associated with chromosome foci in interphase cells. During mitosis, most of the condensin complex is associated with the chromatin. At the onset of prophase, the regulatory subunits of the complex are phosphorylated by CDK1, leading to condensin's association with chromosome arms and to chromosome condensation. Dissociation from chromosomes is observed in late telophase. Ref.3

Tissue specificity

Widely expressed at low level. Expressed in proliferating cells. Ref.3

Post-translational modification

Phosphorylated by CDK1. Its phosphorylation, as well as that of NCAPD2 and NCAPG subunits, activates the condensin complex and is required for chromosome condensation By similarity.

Sequence similarities

Belongs to the CND2 (condensin subunit 2) family.

Sequence caution

The sequence BAA07556.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 741741Condensin complex subunit 2
PRO_0000095038

Amino acid modifications

Modified residue151Phosphoserine Ref.10
Modified residue251Phosphoserine Ref.10
Modified residue491Phosphothreonine Ref.10
Modified residue701Phosphoserine Ref.6
Modified residue781Phosphoserine Ref.6 Ref.10
Modified residue811Phosphoserine Ref.6 Ref.8 Ref.10
Modified residue871Phosphoserine Ref.6 Ref.10
Modified residue921Phosphoserine Ref.6 Ref.10
Modified residue961Phosphoserine Ref.10
Modified residue2011Phosphoserine Ref.6 Ref.10
Modified residue4321Phosphoserine Ref.6 Ref.10
Modified residue5981Phosphothreonine Ref.10
Modified residue6051Phosphothreonine Ref.6
Modified residue6371N6-acetyllysine Ref.9

Natural variations

Natural variant5391V → A. Ref.2
Corresponds to variant rs2305935 [ dbSNP | Ensembl ].
VAR_027882

Sequences

Sequence LengthMass (Da)Tools
Q15003 [UniParc].

Last modified October 17, 2006. Version 3.
Checksum: B5B34A36CAE0C28E

FASTA74182,563
        10         20         30         40         50         60 
MGPPGPALPA TMNNSSSETR GHPHSASSPS ERVFPMPLPR KAPLNIPGTP VLEDFPQNDD 

        70         80         90        100        110        120 
EKERLQRRRS RVFDLQFSTD SPRLLASPSS RSIDISATIP KFTNTQITEH YSTCIKLSTE 

       130        140        150        160        170        180 
NKITTKNAFG LHLIDFMSEI LKQKDTEPTN FKVAAGTLDA STKIYAVRVD AVHADVYRVL 

       190        200        210        220        230        240 
GGLGKDAPSL EEVEGHVADG SATEMGTTKK AVKPKKKHLH RTIEQNINNL NVSEADRKCE 

       250        260        270        280        290        300 
IDPMFQKTAA SFDECSTAGV FLSTLHCQDY RSELLFPSDV QTLSTGEPLE LPELGCVEMT 

       310        320        330        340        350        360 
DLKAPLQQCA EDRQICPSLA GFQFTQWDSE THNESVSALV DKFKKNDQVF DINAEVDESD 

       370        380        390        400        410        420 
CGDFPDGSLG DDFDANDEPD HTAVGDHEEF RSWKEPCQVQ SCQEEMISLG DGDIRTMCPL 

       430        440        450        460        470        480 
LSMKPGEYSY FSPRTMSMWA GPDHWRFRPR RKQDAPSQSE NKKKSTKKDF EIDFEDDIDF 

       490        500        510        520        530        540 
DVYFRKTKAA TILTKSTLEN QNWRATTLPT DFNYNVDTLV QLHLKPGTRL LKMAQGHRVE 

       550        560        570        580        590        600 
TEHYEEIEDY DYNNPNDTSN FCPGLQAADS DDEDLDDLFV GPVGNSDLSP YPCHPPKTAQ 

       610        620        630        640        650        660 
QNGDTPEAQG LDITTYGESN LVAEPQKVNK IEIHYAKTAK KMDMKKLKQS MWSLLTALSG 

       670        680        690        700        710        720 
KEADAEANHR EAGKEAALAE VADEKMLSGL TKDLQRSLPP VMAQNLSIPL AFACLLHLAN 

       730        740 
EKNLKLEGTE DLSDVLVRQG D 

« Hide

References

« Hide 'large scale' references
[1]"Prediction of the coding sequences of unidentified human genes. II. The coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by analysis of cDNA clones from human cell line KG-1."
Nomura N., Nagase T., Miyajima N., Sazuka T., Tanaka A., Sato S., Seki N., Kawarabayasi Y., Ishikawa K., Tabata S.
DNA Res. 1:223-229(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Bone marrow.
[2]"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], VARIANT ALA-539.
Tissue: Placenta.
[3]"Cell cycle-dependent expression and nucleolar localization of hCAP-H."
Cabello O.A., Eliseeva E., He W.G., Youssoufian H., Plon S.E., Brinkley B.R., Belmont J.W.
Mol. Biol. Cell 12:3527-3537(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION DURING THE CELL CYCLE, TISSUE SPECIFICITY.
[4]"Chromosome condensation by a human condensin complex in Xenopus egg extracts."
Kimura K., Cuvier O., Hirano T.
J. Biol. Chem. 276:5417-5420(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A CONDENSIN COMPLEX WITH SMC2; SMC4; NCAPD2 AND NCAPG, FUNCTION OF THE COMPLEX.
[5]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[6]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70; SER-78; SER-81; SER-87; SER-92; SER-201; SER-432 AND THR-605, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[7]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[8]"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-81, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[9]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-637, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15; SER-25; THR-49; SER-78; SER-81; SER-87; SER-92; SER-96; SER-201; SER-432 AND THR-598, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D38553 mRNA. Translation: BAA07556.1. Different initiation.
BC024211 mRNA. Translation: AAH24211.1.
RefSeqNP_001268639.1. NM_001281710.1.
NP_001268640.1. NM_001281711.1.
NP_056156.2. NM_015341.4.
UniGeneHs.308045.

3D structure databases

ProteinModelPortalQ15003.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116970. 17 interactions.
DIPDIP-43899N.
IntActQ15003. 7 interactions.
MINTMINT-5004625.
STRING9606.ENSP00000240423.

PTM databases

PhosphoSiteQ15003.

Polymorphism databases

DMDM116241306.

Proteomic databases

PaxDbQ15003.
PeptideAtlasQ15003.
PRIDEQ15003.

Protocols and materials databases

DNASU23397.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000240423; ENSP00000240423; ENSG00000121152.
GeneID23397.
KEGGhsa:23397.
UCSCuc002svz.1. human.

Organism-specific databases

CTD23397.
GeneCardsGC02P097001.
HGNCHGNC:1112. NCAPH.
HPAHPA002647.
HPA003008.
MIM602332. gene.
neXtProtNX_Q15003.
PharmGKBPA162397273.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5229.
HOGENOMHOG000231887.
HOVERGENHBG036823.
InParanoidQ15003.
KOK06676.
OMASERVFPM.
OrthoDBEOG7JMGDB.
PhylomeDBQ15003.
TreeFamTF105678.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.
REACT_21300. Mitotic M-M/G1 phases.

Gene expression databases

ArrayExpressQ15003.
BgeeQ15003.
CleanExHS_NCAPH.
GenevestigatorQ15003.

Family and domain databases

InterProIPR022816. Condensin_barren_su2.
[Graphical view]
PfamPF05786. Cnd2. 1 hit.
[Graphical view]
PIRSFPIRSF017126. Condensin_H. 1 hit.
ProtoNetSearch...

Other

GeneWikiNCAPH.
GenomeRNAi23397.
NextBio45541.
PMAP-CutDBQ15003.
PROQ15003.
SOURCESearch...

Entry information

Entry nameCND2_HUMAN
AccessionPrimary (citable) accession number: Q15003
Secondary accession number(s): Q8TB87
Entry history
Integrated into UniProtKB/Swiss-Prot: April 23, 2003
Last sequence update: October 17, 2006
Last modified: April 16, 2014
This is version 121 of the entry and version 3 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 2

Human chromosome 2: entries, gene names and cross-references to MIM