Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9BPX3 (CND3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 123. 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 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1015 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.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

Binary interactions

With

Entry

#Exp.

IntAct

Notes

NCAPD2Q150212EBI-970214,EBI-1044041
NCAPHQ150032EBI-970214,EBI-1046410

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10151015Condensin complex subunit 3
PRO_0000095041

Regions

Repeat94 – 13138HEAT 1
Repeat138 – 17336HEAT 2
Repeat174 – 21239HEAT 3
Repeat238 – 27538HEAT 4
Repeat276 – 31338HEAT 5
Repeat399 – 43638HEAT 6
Repeat439 – 47840HEAT 7
Repeat617 – 65438HEAT 8
Repeat687 – 72438HEAT 9
Repeat865 – 90743HEAT 10
Compositional bias88 – 914Poly-Glu
Compositional bias912 – 9176Poly-Thr

Amino acid modifications

Modified residue3901Phosphoserine Ref.11 Ref.12
Modified residue6741Phosphoserine Ref.6 Ref.8 Ref.9 Ref.11 Ref.12 Ref.14
Modified residue9311Phosphothreonine Ref.12
Modified residue9731Phosphoserine Ref.9
Modified residue9751Phosphoserine Ref.9
Modified residue10021Phosphoserine Ref.9
Modified residue10151Phosphoserine Ref.6 Ref.8 Ref.11 Ref.12 Ref.14

Natural variations

Natural variant641A → P.
Corresponds to variant rs35722563 [ dbSNP | Ensembl ].
VAR_053041
Natural variant2651M → T in a colorectal cancer sample; somatic mutation. Ref.15
VAR_036125
Natural variant5811M → I. Ref.1
Corresponds to variant rs3795243 [ dbSNP | Ensembl ].
VAR_053042

Experimental info

Sequence conflict1151R → G in BAB14069. Ref.4
Sequence conflict2761F → V in AAG30732. Ref.1
Sequence conflict5191S → P in BAB55165. Ref.4
Sequence conflict6761D → V in BAB14069. Ref.4
Sequence conflict6811K → R in BAB14069. Ref.4
Sequence conflict7041V → A in BAB14069. Ref.4
Sequence conflict8361N → D in BAB55165. Ref.4
Sequence conflict10101L → F in AAG30732. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9BPX3 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: D9ACC205C48F3AF5

FASTA1,015114,334
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"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].
[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-390; SER-674 AND SER-1015, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 SER-390; SER-674; THR-931 AND SER-1015, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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].
[14]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"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. expand/collapse author list , 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.
CCDSCCDS3424.1.
RefSeqNP_071741.2. NM_022346.4.
UniGeneHs.567567.

3D structure databases

ProteinModelPortalQ9BPX3.
SMRQ9BPX3. Positions 95-307, 408-451, 624-652, 692-718.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid122089. 22 interactions.
IntActQ9BPX3. 8 interactions.
MINTMINT-3060256.
STRING9606.ENSP00000251496.

PTM databases

PhosphoSiteQ9BPX3.

Polymorphism databases

DMDM30172941.

Proteomic databases

MaxQBQ9BPX3.
PaxDbQ9BPX3.
PeptideAtlasQ9BPX3.
PRIDEQ9BPX3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000251496; ENSP00000251496; ENSG00000109805.
GeneID64151.
KEGGhsa:64151.
UCSCuc003gpp.4. human.

Organism-specific databases

CTD64151.
GeneCardsGC04P017812.
HGNCHGNC:24304. NCAPG.
HPAHPA039613.
HPA040103.
MIM606280. gene.
neXtProtNX_Q9BPX3.
PharmGKBPA162397165.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5218.
HOVERGENHBG039407.
InParanoidQ9BPX3.
KOK06678.
OMAEACCYEP.
OrthoDBEOG7CVPWZ.
PhylomeDBQ9BPX3.
TreeFamTF101160.

Enzyme and pathway databases

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

Gene expression databases

ArrayExpressQ9BPX3.
BgeeQ9BPX3.
CleanExHS_CAPG.
HS_NCAPG.
GenevestigatorQ9BPX3.

Family and domain databases

Gene3D1.25.10.10. 3 hits.
InterProIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR027165. CND3.
IPR025977. Cnd3_C.
[Graphical view]
PANTHERPTHR14418. PTHR14418. 1 hit.
PfamPF12719. Cnd3. 1 hit.
[Graphical view]
SUPFAMSSF48371. SSF48371. 2 hits.
ProtoNetSearch...

Other

GeneWikiNCAPG.
GenomeRNAi64151.
NextBio66065.
PROQ9BPX3.
SOURCESearch...

Entry information

Entry nameCND3_HUMAN
AccessionPrimary (citable) accession number: Q9BPX3
Secondary accession number(s): Q3MJE0 expand/collapse secondary AC list , Q96SV9, Q9BUR3, Q9BVY1, Q9H914, Q9H9Z6, Q9HBI9
Entry history
Integrated into UniProtKB/Swiss-Prot: April 23, 2003
Last sequence update: June 1, 2001
Last modified: July 9, 2014
This is version 123 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 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 4

Human chromosome 4: entries, gene names and cross-references to MIM