Q9BPX3 (CND3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Condensin complex subunit 3

Alternative name(s):
Chromosome-associated protein G
Condensin subunit CAP-G
Short name=hCAP-G
Melanoma antigen NY-MEL-3
Non-SMC condensin I complex subunit G
XCAP-G homolog

Gene names

Name:	NCAPG
Synonyms:	CAPG, NYMEL3

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	1015 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.2
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.2
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.
Tissue specificity	Highly expressed in testis. Ref.1
Post-translational modification	Phosphorylated by CDK1. Its phosphorylation, as well as that of NCAPD2 and NCAPH subunits, activates the condensin complex and is required for chromosome condensation By similarity.
Miscellaneous	Overexpressed in some cancer lines and some tumor cells.
Sequence similarities	Belongs to the CND3 (condensin subunit 3) family. Contains 10 HEAT repeats.
Sequence caution	The sequence AAH00827.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence BAB14429.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence BAB55165.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
Biological process	Cell cycle Cell division DNA condensation Mitosis
Cellular component	Chromosome Cytoplasm Nucleus
Coding sequence diversity	Polymorphism
Domain	Repeat
PTM	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.2. Source: UniProtKB
Cellular_component	actin cytoskeleton Inferred from direct assay. Source: HPA centrosome Inferred from direct assay. Source: HPA condensin complex Inferred from direct assay Ref.2. Source: UniProtKB cytoplasm Inferred from direct assay. Source: HPA nucleus Non-traceable author statement Ref.1. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1015	1015	Condensin complex subunit 3		PRO_0000095041
Regions
	Repeat	94 – 131	38	HEAT 1
	Repeat	138 – 173	36	HEAT 2
	Repeat	174 – 212	39	HEAT 3
	Repeat	238 – 275	38	HEAT 4
	Repeat	276 – 313	38	HEAT 5
	Repeat	399 – 436	38	HEAT 6
	Repeat	439 – 478	40	HEAT 7
	Repeat	617 – 654	38	HEAT 8
	Repeat	687 – 724	38	HEAT 9
	Repeat	865 – 907	43	HEAT 10
	Compositional bias	88 – 91	4	Poly-Glu
	Compositional bias	912 – 917	6	Poly-Thr
Amino acid modifications
	Modified residue	390	1	Phosphoserine Ref.10 Ref.11
	Modified residue	674	1	Phosphoserine Ref.6 Ref.8 Ref.9 Ref.10 Ref.11 Ref.13
	Modified residue	931	1	Phosphothreonine Ref.11
	Modified residue	973	1	Phosphoserine Ref.9
	Modified residue	975	1	Phosphoserine Ref.9
	Modified residue	1002	1	Phosphoserine Ref.9
	Modified residue	1015	1	Phosphoserine Ref.6 Ref.8 Ref.10 Ref.11 Ref.13
Natural variations
	Natural variant	64	1	A → P. Corresponds to variant rs35722563 [ dbSNP | Ensembl ].		VAR_053041
	Natural variant	265	1	M → T in a colorectal cancer sample; somatic mutation. Ref.14		VAR_036125
	Natural variant	581	1	M → I. Ref.1 Corresponds to variant rs3795243 [ dbSNP | Ensembl ].		VAR_053042
Experimental info
	Sequence conflict	115	1	R → G in BAB14069. Ref.4
	Sequence conflict	276	1	F → V in AAG30732. Ref.1
	Sequence conflict	519	1	S → P in BAB55165. Ref.4
	Sequence conflict	676	1	D → V in BAB14069. Ref.4
	Sequence conflict	681	1	K → R in BAB14069. Ref.4
	Sequence conflict	704	1	V → A in BAB14069. Ref.4
	Sequence conflict	836	1	N → D in BAB55165. Ref.4
	Sequence conflict	1010	1	L → F in AAG30732. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q9BPX3 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: D9ACC205C48F3AF5	FASTA	1,015	114,334
	10 20 30 40 50 60 MGAERRLLSI KEAFRLAQQP HQNQAKLVVA LSRTYRTMDD KTVFHEEFIH YLKYVMVVYK 70 80 90 100 110 120 REPAVERVIE FAAKFVTSFH QSDMEDDEEE EDGGLLNYLF TFLLKSHEAN SNAVRFRVCL 130 140 150 160 170 180 LINKLLGSMP ENAQIDDDVF DKINKAMLIR LKDKIPNVRI QAVLALSRLQ DPKDDECPVV 190 200 210 220 230 240 NAYATLIEND SNPEVRRAVL SCIAPSAKTL PKIVGRTKDV KEAVRKLAYQ VLAEKVHMRA 250 260 270 280 290 300 MSIAQRVMLL QQGLNDRSDA VKQAMQKHLL QGWLRFSEGN ILELLHRLDV ENSSEVAVSV 310 320 330 340 350 360 LNALFSITPL SELVGLCKNN DGRKLIPVET LTPEIALYWC ALCEYLKSKG DEGEEFLEQI 370 380 390 400 410 420 LPEPVVYADY LLSYIQSIPV VNEEHRGDFS YIGNLMTKEF IGQQLILIIK SLDTSEEGGR 430 440 450 460 470 480 KKLLAVLQEI LILPTIPISL VSFLVERLLH IIIDDNKRTQ IVTEIISEIR APIVTVGVNN 490 500 510 520 530 540 DPADVRKKEL KMAEIKVKLI EAKEALENCI TLQDFNRASE LKEEIKALED ARINLLKETE 550 560 570 580 590 600 QLEIKEVHIE KNDAETLQKC LILCYELLKQ MSISTGLSAT MNGIIESLIL PGIISIHPVV 610 620 630 640 650 660 RNLAVLCLGC CGLQNQDFAR KHFVLLLQVL QIDDVTIKIS ALKAIFDQLM TFGIEPFKTK 670 680 690 700 710 720 KIKTLHCEGT EINSDDEQES KEVEETATAK NVLKLLSDFL DSEVSELRTG AAEGLAKLMF 730 740 750 760 770 780 SGLLVSSRIL SRLILLWYNP VTEEDVQLRH CLGVFFPVFA YASRTNQECF EEAFLPTLQT 790 800 810 820 830 840 LANAPASSPL AEIDITNVAE LLVDLTRPSG LNPQAKTSQD YQALTVHDNL AMKICNEILT 850 860 870 880 890 900 SPCSPEIRVY TKALSSLELS SHLAKDLLVL LNEILEQVKD RTCLRALEKI KIQLEKGNKE 910 920 930 940 950 960 FGDQAEAAQD ATLTTTTFQN EDEKNKEVYM TPLRGVKATQ ASKSTQLKTN RGQRKVTVSA 970 980 990 1000 1010 RTNRRCQTAE ADSESDHEVP EPESEMKMRL PRRAKTAALE KSKLNLAQFL NEDLS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Serological cloning of a melanocyte rab guanosine 5'-triphosphate-binding protein and a chromosome condensation protein from a melanoma complementary DNA library." Jaeger D., Stockert E., Jaeger E., Guere A.O., Scanlan M.J., Knuth A., Old L.J., Chen Y.-T. Cancer Res. 60:3584-3591(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, VARIANT ILE-581. Tissue: Melanocyte.
[2]	"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: NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION IN A CONDENSIN COMPLEX WITH SMC2; SMC4; NCAPD2 AND NCAPH, FUNCTION OF THE COMPLEX.
[3]	"Differentiation responsive gene." Minami T., Doi T., Tachibana K., Okada Y. Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Erythroleukemia.
[4]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Teratocarcinoma.
[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]. Tissue: Placenta.
[6]	"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-674 AND SER-1015, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[7]	"Phosphoproteome of resting human platelets." Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A. J. Proteome Res. 7:526-534(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Platelet.
[8]	"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-674 AND SER-1015, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"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-674; SER-973; SER-975 AND SER-1002, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"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-390; SER-674 AND SER-1015, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[11]	"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-390; SER-674; THR-931 AND SER-1015, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"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].
[13]	"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-674 AND SER-1015, MASS SPECTROMETRY.
[14]	"The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E. Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] THR-265.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF235023 mRNA. Translation: AAG30732.1. AF331796 mRNA. Translation: AAG49627.1. AB013299 mRNA. Translation: BAB21557.1. AK022512 mRNA. Translation: BAB14069.1. AK023147 mRNA. Translation: BAB14429.1. Different initiation. AK027511 mRNA. Translation: BAB55165.1. Different initiation. BC000827 mRNA. Translation: AAH00827.1. Different initiation. BC101476 mRNA. Translation: AAI01477.1.
IPI	IPI00106495.
RefSeq	NP_071741.2. NM_022346.4.
UniGene	Hs.446201. Hs.567567.
3D structure databases
ProteinModelPortal	Q9BPX3.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9BPX3. 3 interactions.
MINT	MINT-3060256.
STRING	9606.ENSP00000251496.
PTM databases
PhosphoSite	Q9BPX3.
Polymorphism databases
DMDM	30172941.
Proteomic databases
PaxDb	Q9BPX3.
PeptideAtlas	Q9BPX3.
PRIDE	Q9BPX3.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000251496; ENSP00000251496; ENSG00000109805.
GeneID	64151.
KEGG	hsa:64151.
UCSC	uc003gpp.3. human.
Organism-specific databases
CTD	64151.
GeneCards	GC04P017812.
HGNC	HGNC:24304. NCAPG.
HPA	HPA039613. HPA040103.
MIM	606280. gene.
neXtProt	NX_Q9BPX3.
PharmGKB	PA162397165.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG5218.
HOVERGEN	HBG039407.
InParanoid	Q9BPX3.
KO	K06678.
OMA	YIGNLMT.
OrthoDB	EOG4JDH62.
PhylomeDB	Q9BPX3.
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	Q9BPX3.
Bgee	Q9BPX3.
CleanEx	HS_CAPG. HS_NCAPG.
Genevestigator	Q9BPX3.
GermOnline	ENSG00000109805. Homo sapiens.
Family and domain databases
Gene3D	1.25.10.10. 3 hits.
InterPro	IPR011989. ARM-like. IPR016024. ARM-type_fold. IPR027165. CND3. IPR025977. Cnd3_C. [Graphical view]
PANTHER	PTHR14418. PTHR14418. 1 hit.
Pfam	PF12719. Cnd3. 1 hit. [Graphical view]
SUPFAM	SSF48371. ARM-type_fold. 1 hit.
PROSITE	PS50077. HEAT_REPEAT. False negative. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	64151.
NextBio	66065.
SOURCE	Search...

Entry information

Entry name

CND3_HUMAN

Accession

Primary (citable) accession number: Q9BPX3
Secondary accession number(s): Q3MJE0 , Q96SV9, Q9BUR3, Q9BVY1, Q9H914, Q9H9Z6, Q9HBI9

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 23, 2003
Last sequence update:	June 1, 2001
Last modified:	May 1, 2013
This is version 111 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.