Q15003 (CND2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	741 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Cell cycle Cell division DNA condensation Mitosis
Cellular component	Chromosome Cytoplasm Nucleus
Coding sequence diversity	Polymorphism
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell division Inferred from electronic annotation. Source: UniProtKB-KW mitotic chromosome condensation Inferred from direct assay Ref.4Ref.3. Source: UniProtKB
Cellular_component	condensin complex Inferred from direct assay Ref.4. Source: UniProtKB cytoplasm Inferred from direct assay. Source: HPA microtubule cytoskeleton Inferred from direct assay. Source: HPA nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
DDX3X	O00571	2	EBI-1046410,EBI-353779

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 741	741	Condensin complex subunit 2		PRO_0000095038
Amino acid modifications
	Modified residue	15	1	Phosphoserine Ref.9
	Modified residue	25	1	Phosphoserine Ref.9
	Modified residue	49	1	Phosphothreonine Ref.9
	Modified residue	70	1	Phosphoserine Ref.6
	Modified residue	78	1	Phosphoserine Ref.6 Ref.9
	Modified residue	81	1	Phosphoserine Ref.6 Ref.7 Ref.9
	Modified residue	87	1	Phosphoserine Ref.6 Ref.9
	Modified residue	92	1	Phosphoserine Ref.6 Ref.9
	Modified residue	96	1	Phosphoserine Ref.9
	Modified residue	201	1	Phosphoserine Ref.6 Ref.9
	Modified residue	432	1	Phosphoserine Ref.6 Ref.9
	Modified residue	598	1	Phosphothreonine Ref.9
	Modified residue	605	1	Phosphothreonine Ref.6
	Modified residue	637	1	N6-acetyllysine Ref.8
Natural variations
	Natural variant	539	1	V → A. Ref.2 Corresponds to variant rs2305935 [ dbSNP | Ensembl ].		VAR_027882

Sequences

	Sequence		Length	Mass (Da)
	Q15003 [UniParc]. Last modified October 17, 2006. Version 3. Checksum: B5B34A36CAE0C28E	FASTA	741	82,563
	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

References

	« Hide 'large scale' referencesShow '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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[7]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[8]	"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, MASS SPECTROMETRY.
[9]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"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].
[11]	"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].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D38553 mRNA. Translation: BAA07556.1. Different initiation. BC024211 mRNA. Translation: AAH24211.1.
IPI	IPI00299507.
RefSeq	NP_056156.2. NM_015341.3.
UniGene	Hs.308045.
3D structure databases
ProteinModelPortal	Q15003.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-43899N.
IntAct	Q15003. 1 interaction.
MINT	MINT-5004625.
STRING	9606.ENSP00000240423.
PTM databases
PhosphoSite	Q15003.
Polymorphism databases
DMDM	116241306.
Proteomic databases
PaxDb	Q15003.
PeptideAtlas	Q15003.
PRIDE	Q15003.
Protocols and materials databases
DNASU	23397.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000240423; ENSP00000240423; ENSG00000121152.
GeneID	23397.
KEGG	hsa:23397.
UCSC	uc002svz.1. human.
Organism-specific databases
CTD	23397.
GeneCards	GC02P097001.
HGNC	HGNC:1112. NCAPH.
HPA	HPA002647. HPA003008.
MIM	602332. gene.
neXtProt	NX_Q15003.
PharmGKB	PA162397273.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG5229.
HOGENOM	HOG000231887.
HOVERGEN	HBG036823.
InParanoid	Q15003.
KO	K06676.
OMA	ITEHYST.
OrthoDB	EOG48KR9Q.
PhylomeDB	Q15003.
Enzyme and pathway databases
Pathway_Interaction_DB	aurora_b_pathway. Aurora B signaling.
Reactome	REACT_115566. Cell Cycle. REACT_21300. Mitotic M-M/G1 phases.
Gene expression databases
ArrayExpress	Q15003.
Bgee	Q15003.
CleanEx	HS_NCAPH.
Genevestigator	Q15003.
GermOnline	ENSG00000121152. Homo sapiens.
Family and domain databases
InterPro	IPR022816. Condensin_barren_su2. [Graphical view]
Pfam	PF05786. Cnd2. 1 hit. [Graphical view]
PIRSF	PIRSF017126. Condensin_H. 1 hit.
ProtoNet	Search...
Other
GenomeRNAi	23397.
NextBio	45541.
PMAP-CutDB	Q15003.
SOURCE	Search...

Entry information

Entry name

CND2_HUMAN

Accession

Primary (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 3, 2013
This is version 112 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.