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Q6IBW4 (CNDH2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 85. 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:
Condensin-2 complex subunit H2
Alternative name(s):
Chromosome-associated protein H2
Short name=hCAP-H2
Kleisin-beta
Non-SMC condensin II complex subunit H2
Gene names
Name:NCAPH2
Synonyms:CAPH2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length605 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Regulatory subunit of the condensin-2 complex, a complex that seems to provide chromosomes with an additional level of organization and rigidity and in establishing mitotic chromosome architecture. May play a role in lineage-specific role in T-cell development By similarity. Ref.6

Subunit structure

Component of the condensin-2 complex, which contains the SMC2 and SMC4 heterodimer, and three non SMC subunits, NCAPG2, NCAPH2 and NCAPD3 that probably regulate the complex. Ref.6

Subcellular location

Nucleus. Chromosome. Note: Distributed along the arms of chromosomes assembled in vivo and in vitro. Ref.6

Sequence similarities

Belongs to the CND2 H2 (condensin-2 subunit 2) family.

Sequence caution

The sequence AAB03345.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence AAH00473.1 differs from that shown. Reason: Erroneous initiation.

The sequence AAH01509.1 differs from that shown. Reason: Erroneous initiation.

The sequence AAH01833.1 differs from that shown. Reason: Erroneous initiation.

The sequence AAH01937.1 differs from that shown. Reason: Erroneous initiation.

The sequence AAH09441.1 differs from that shown. Reason: Erroneous initiation.

The sequence CAA16670.1 differs from that shown. Reason: Frameshift at positions 56 and 429.

The sequence EAW73552.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Biological processDNA condensation
   Cellular componentChromosome
Nucleus
   Coding sequence diversityAlternative splicing
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processchromosome condensation

Inferred from electronic annotation. Source: UniProtKB-KW

mitotic cell cycle

Traceable author statement. Source: Reactome

   Cellular_componentchromosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleoplasm

Traceable author statement. Source: Reactome

   Molecular_functionprotein binding

Inferred from physical interaction PubMed 17268547. Source: IntAct

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q6IBW4-1)

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: Q6IBW4-2)

The sequence of this isoform differs from the canonical sequence as follows:
     167-188: Missing.
Note: Gene prediction based on EST data.
Isoform 3 (identifier: Q6IBW4-5)

The sequence of this isoform differs from the canonical sequence as follows:
     288-299: SAALPRRYMLRE → VGPTWRPAEPEL
     300-605: Missing.
Note: No experimental confirmation available.
Isoform 4 (identifier: Q6IBW4-4)

The sequence of this isoform differs from the canonical sequence as follows:
     435-435: A → AA
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 605605Condensin-2 complex subunit H2
PRO_0000326241

Amino acid modifications

Modified residue191Phosphothreonine Ref.13
Modified residue951Phosphoserine Ref.13
Modified residue961Phosphoserine Ref.13
Modified residue2001Phosphoserine Ref.13
Modified residue2081Phosphoserine Ref.12 Ref.13
Modified residue2821Phosphoserine Ref.10
Modified residue2841Phosphoserine Ref.9 Ref.13
Modified residue4661Phosphoserine Ref.13
Modified residue4921Phosphoserine Ref.8 Ref.9 Ref.10 Ref.13

Natural variations

Alternative sequence167 – 18822Missing in isoform 2.
VSP_032636
Alternative sequence288 – 29912SAALP…YMLRE → VGPTWRPAEPEL in isoform 3.
VSP_032637
Alternative sequence300 – 605306Missing in isoform 3.
VSP_032638
Alternative sequence4351A → AA in isoform 4.
VSP_032639

Experimental info

Sequence conflict361E → D in CAA16670. Ref.1
Sequence conflict611Q → H in CAA16670. Ref.1
Sequence conflict761S → W in CAA16670. Ref.1
Sequence conflict1611N → I in CAA16670. Ref.1
Sequence conflict1901G → R in CAA16670. Ref.1
Sequence conflict2151K → N in CAA16670. Ref.1
Sequence conflict2491G → R in CAA16670. Ref.1
Sequence conflict2821S → F in AAH09441. Ref.5
Sequence conflict3161P → L in CAA16670. Ref.1
Sequence conflict323 – 3242FD → LN in CAA16670. Ref.1
Sequence conflict3681A → V in CAA16670. Ref.1
Sequence conflict4741N → K in CAA16670. Ref.1
Sequence conflict4861V → I in CAA16670. Ref.1

Sequences

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

Last modified July 5, 2004. Version 1.
Checksum: 2C8A1070C27B4547

FASTA60568,227
        10         20         30         40         50         60 
MEDVEARFAH LLQPIRDLTK NWEVDVAAQL GEYLEELDQI CISFDEGKTT MNFIEAALLI 

        70         80         90        100        110        120 
QGSACVYSKK VEYLYSLVYQ ALDFISGKRR AKQLSSVQED RANGVASSGV PQEAENEFLS 

       130        140        150        160        170        180 
LDDFPDSRTN VDLKNDQTPS EVLIIPLLPM ALVAPDEMEK NNNPLYSRQG EVLASRKDFR 

       190        200        210        220        230        240 
MNTCVPHPRG AFMLEPEGMS PMEPAGVSPM PGTQKDTGRT EEQPMEVSVC RSPVPALGFS 

       250        260        270        280        290        300 
QEPGPSPEGP MPLGGGEDED AEEAVELPEA SAPKAALEPK ESRSPQQSAA LPRRYMLRER 

       310        320        330        340        350        360 
EGAPEPASCV KETPDPWQSL DPFDSLESKP FKKGRPYSVP PCVEEALGQK RKRKGAAKLQ 

       370        380        390        400        410        420 
DFHQWYLAAY ADHADSRRLR RKGPSFADME VLYWTHVKEQ LETLRKLQRR EVAEQWLRPA 

       430        440        450        460        470        480 
EEDHLEDSLE DLGAADDFLE PEEYMEPEGA DPREAADLDA VPMSLSYEEL VRRNVELFIA 

       490        500        510        520        530        540 
TSQKFVQETE LSQRIRDWED TVQPLLQEQE QHVPFDIHTY GDQLVSRFPQ LNEWCPFAEL 

       550        560        570        580        590        600 
VAGQPAFEVC RSMLASLQLA NDYTVEITQQ PGLEMAVDTM SLRLLTHQRA HKRFQTYAAP 


SMAQP 

« Hide

Isoform 2 [UniParc].

Checksum: 21B93C7E157E1E5C
Show »

FASTA58365,716
Isoform 3 [UniParc].

Checksum: C47577DA567D7AAA
Show »

FASTA29932,819
Isoform 4 [UniParc].

Checksum: 9D6FAEBA6500B608
Show »

FASTA60668,298

References

« Hide 'large scale' references
[1]"Reevaluating human gene annotation: a second-generation analysis of chromosome 22."
Collins J.E., Goward M.E., Cole C.G., Smink L.J., Huckle E.J., Knowles S., Bye J.M., Beare D.M., Dunham I.
Genome Res. 13:27-36(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Placenta.
[2]"A genome annotation-driven approach to cloning the human ORFeome."
Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., Beare D.M., Dunham I.
Genome Biol. 5:R84.1-R84.11(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[3]"The DNA sequence of human chromosome 22."
Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M. expand/collapse author list , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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] (ISOFORMS 1; 3 AND 4).
Tissue: Brain, Lung, Muscle and Skin.
[6]"Differential contributions of condensin I and condensin II to mitotic chromosome architecture in vertebrate cells."
Ono T., Losada A., Hirano M., Myers M.P., Neuwald A.F., Hirano T.
Cell 115:109-121(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN CONDENSIN-2 COMPLEX WITH SMC2; SMC4; NCAPG2; NCAPH2 AND NCAPD3, FUNCTION OF THE COMPLEX, SUBCELLULAR LOCATION.
[7]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-492, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[9]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-284 AND SER-492, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"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-282 AND SER-492, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"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].
[12]"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-208, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[13]"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 THR-19; SER-95; SER-96; SER-200; SER-208; SER-284; SER-466 AND SER-492, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL021682 mRNA. Translation: CAA16670.1. Frameshift.
CR456604 mRNA. Translation: CAG30490.1.
U62317 Genomic DNA. Translation: AAB03345.1. Sequence problems.
CH471138 Genomic DNA. Translation: EAW73554.1.
CH471138 Genomic DNA. Translation: EAW73556.1.
CH471138 Genomic DNA. Translation: EAW73552.1. Sequence problems.
BC000473 mRNA. Translation: AAH00473.1. Different initiation.
BC001509 mRNA. Translation: AAH01509.1. Different initiation.
BC001833 mRNA. Translation: AAH01833.1. Different initiation.
BC001937 mRNA. Translation: AAH01937.1. Different initiation.
BC009441 mRNA. Translation: AAH09441.1. Different initiation.
BC014939 mRNA. Translation: AAH14939.2.
CCDSCCDS14094.2. [Q6IBW4-1]
CCDS43038.1. [Q6IBW4-5]
CCDS54546.1. [Q6IBW4-4]
RefSeqNP_001171940.1. NM_001185011.1. [Q6IBW4-4]
NP_055366.3. NM_014551.4. [Q6IBW4-5]
NP_689512.2. NM_152299.3. [Q6IBW4-1]
UniGeneHs.730607.

3D structure databases

ProteinModelPortalQ6IBW4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid118913. 8 interactions.
DIPDIP-43901N.
IntActQ6IBW4. 10 interactions.
MINTMINT-4329914.

PTM databases

PhosphoSiteQ6IBW4.

Polymorphism databases

DMDM74709496.

Proteomic databases

MaxQBQ6IBW4.
PaxDbQ6IBW4.
PRIDEQ6IBW4.

Protocols and materials databases

DNASU29781.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000299821; ENSP00000299821; ENSG00000025770. [Q6IBW4-4]
ENST00000395698; ENSP00000379050; ENSG00000025770. [Q6IBW4-5]
ENST00000420993; ENSP00000410088; ENSG00000025770. [Q6IBW4-1]
GeneID29781.
KEGGhsa:29781.
UCSCuc003blq.4. human. [Q6IBW4-5]
uc003blr.4. human. [Q6IBW4-1]
uc003blx.4. human. [Q6IBW4-4]

Organism-specific databases

CTD29781.
GeneCardsGC22P050946.
H-InvDBHIX0016615.
HGNCHGNC:25071. NCAPH2.
MIM611230. gene.
neXtProtNX_Q6IBW4.
PharmGKBPA162397314.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG238357.
HOVERGENHBG098083.
KOK11490.
OMAAPEPASC.
OrthoDBEOG7W41C5.
PhylomeDBQ6IBW4.
TreeFamTF101164.

Enzyme and pathway databases

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

Gene expression databases

ArrayExpressQ6IBW4.
BgeeQ6IBW4.
CleanExHS_NCAPH2.
GenevestigatorQ6IBW4.

Family and domain databases

InterProIPR009378. Condensin_II_H2-like.
[Graphical view]
PfamPF06278. DUF1032. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiNCAPH2.
GenomeRNAi29781.
NextBio52312.
PROQ6IBW4.
SOURCESearch...

Entry information

Entry nameCNDH2_HUMAN
AccessionPrimary (citable) accession number: Q6IBW4
Secondary accession number(s): B7WPH1 expand/collapse secondary AC list , O43788, Q13391, Q96C14, Q96GJ0, Q9BQ71, Q9BUT3, Q9BVD1
Entry history
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: July 5, 2004
Last modified: July 9, 2014
This is version 85 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

MIM cross-references

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

Human chromosome 22

Human chromosome 22: entries, gene names and cross-references to MIM