Q6IBW4 (CNDH2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

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	605 AA.
Sequence status	Complete.
Protein existence	Evidence 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 process	DNA condensation
Cellular component	Chromosome Nucleus
Coding sequence diversity	Alternative splicing
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	chromosome condensation Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	chromosome Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Complete GO annotation...

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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 605	605	Condensin-2 complex subunit H2		PRO_0000326241
Amino acid modifications
	Modified residue	19	1	Phosphothreonine Ref.12
	Modified residue	95	1	Phosphoserine Ref.12
	Modified residue	96	1	Phosphoserine Ref.12
	Modified residue	200	1	Phosphoserine Ref.12
	Modified residue	208	1	Phosphoserine Ref.11 Ref.12
	Modified residue	282	1	Phosphoserine Ref.10
	Modified residue	284	1	Phosphoserine Ref.9 Ref.12
	Modified residue	466	1	Phosphoserine Ref.12
	Modified residue	492	1	Phosphoserine Ref.8 Ref.9 Ref.10 Ref.12
Natural variations
	Alternative sequence	167 – 188	22	Missing in isoform 2.		VSP_032636
	Alternative sequence	288 – 299	12	SAALP…YMLRE → VGPTWRPAEPEL in isoform 3.		VSP_032637
	Alternative sequence	300 – 605	306	Missing in isoform 3.		VSP_032638
	Alternative sequence	435	1	A → AA in isoform 4.		VSP_032639
Experimental info
	Sequence conflict	36	1	E → D in CAA16670. Ref.1
	Sequence conflict	61	1	Q → H in CAA16670. Ref.1
	Sequence conflict	76	1	S → W in CAA16670. Ref.1
	Sequence conflict	161	1	N → I in CAA16670. Ref.1
	Sequence conflict	190	1	G → R in CAA16670. Ref.1
	Sequence conflict	215	1	K → N in CAA16670. Ref.1
	Sequence conflict	249	1	G → R in CAA16670. Ref.1
	Sequence conflict	282	1	S → F in AAH09441. Ref.5
	Sequence conflict	316	1	P → L in CAA16670. Ref.1
	Sequence conflict	323 – 324	2	FD → LN in CAA16670. Ref.1
	Sequence conflict	368	1	A → V in CAA16670. Ref.1
	Sequence conflict	474	1	N → K in CAA16670. Ref.1
	Sequence conflict	486	1	V → I in CAA16670. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: 2C8A1070C27B4547	FASTA	605	68,227
	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
	Isoform 2 [UniParc]. Checksum: 21B93C7E157E1E5C	FASTA	583	65,716
	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 NNNPLYRGAF MLEPEGMSPM 190 200 210 220 230 240 EPAGVSPMPG TQKDTGRTEE QPMEVSVCRS PVPALGFSQE PGPSPEGPMP LGGGEDEDAE 250 260 270 280 290 300 EAVELPEASA PKAALEPKES RSPQQSAALP RRYMLREREG APEPASCVKE TPDPWQSLDP 310 320 330 340 350 360 FDSLESKPFK KGRPYSVPPC VEEALGQKRK RKGAAKLQDF HQWYLAAYAD HADSRRLRRK 370 380 390 400 410 420 GPSFADMEVL YWTHVKEQLE TLRKLQRREV AEQWLRPAEE DHLEDSLEDL GAADDFLEPE 430 440 450 460 470 480 EYMEPEGADP REAADLDAVP MSLSYEELVR RNVELFIATS QKFVQETELS QRIRDWEDTV 490 500 510 520 530 540 QPLLQEQEQH VPFDIHTYGD QLVSRFPQLN EWCPFAELVA GQPAFEVCRS MLASLQLAND 550 560 570 580 YTVEITQQPG LEMAVDTMSL RLLTHQRAHK RFQTYAAPSM AQP
	Isoform 3 [UniParc]. Checksum: C47577DA567D7AAA	FASTA	299	32,819
	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 QEPGPSPEGP MPLGGGEDED AEEAVELPEA SAPKAALEPK ESRSPQQVGP TWRPAEPEL
	Isoform 4 [UniParc]. Checksum: 9D6FAEBA6500B608	FASTA	606	68,298
	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 DLGAAADDFL EPEEYMEPEG ADPREAADLD AVPMSLSYEE LVRRNVELFI 490 500 510 520 530 540 ATSQKFVQET ELSQRIRDWE DTVQPLLQEQ EQHVPFDIHT YGDQLVSRFP QLNEWCPFAE 550 560 570 580 590 600 LVAGQPAFEV CRSMLASLQL ANDYTVEITQ QPGLEMAVDT MSLRLLTHQR AHKRFQTYAA PSMAQP

References

	« Hide 'large scale' referencesShow '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. , 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. , 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[12]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[13]	"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.
IPI	IPI00745556. IPI00853120. IPI00853264. IPI00889043.
RefSeq	NP_001171940.1. NM_001185011.1. NP_055366.3. NM_014551.4. NP_689512.2. NM_152299.3.
UniGene	Hs.730607.
3D structure databases
ProteinModelPortal	Q6IBW4.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q6IBW4. 3 interactions.
MINT	MINT-4329914.
PTM databases
PhosphoSite	Q6IBW4.
Polymorphism databases
DMDM	74709496.
Proteomic databases
PaxDb	Q6IBW4.
PRIDE	Q6IBW4.
Protocols and materials databases
DNASU	29781.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000299821; ENSP00000299821; ENSG00000025770. ENST00000395698; ENSP00000379050; ENSG00000025770. ENST00000420993; ENSP00000410088; ENSG00000025770.
GeneID	29781.
KEGG	hsa:29781.
UCSC	uc003blq.4. human. uc003blr.4. human. uc003blx.4. human.
Organism-specific databases
CTD	29781.
GeneCards	GC22P050946.
H-InvDB	HIX0016615.
HGNC	HGNC:25071. NCAPH2.
MIM	611230. gene.
neXtProt	NX_Q6IBW4.
PharmGKB	PA162397314.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG238357.
HOVERGEN	HBG098083.
KO	K11490.
OMA	EVSVCRS.
OrthoDB	EOG408N7P.
Gene expression databases
ArrayExpress	Q6IBW4.
Bgee	Q6IBW4.
CleanEx	HS_NCAPH2.
Genevestigator	Q6IBW4.
Family and domain databases
InterPro	IPR009378. Condensin_II_H2-like. [Graphical view]
Pfam	PF06278. DUF1032. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	29781.
NextBio	52312.
SOURCE	Search...

Entry information

Entry name

CNDH2_HUMAN

Accession

Primary (citable) accession number: Q6IBW4
Secondary accession number(s): B7WPH1 , 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:	April 3, 2013
This is version 74 of the entry and version 1 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.