Q15021 (CND1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Condensin complex subunit 1

Alternative name(s):
Chromosome condensation-related SMC-associated protein 1
Chromosome-associated protein D2
Short name=hCAP-D2
Non-SMC condensin I complex subunit D2
XCAP-D2 homolog

Gene names

Name:	NCAPD2
Synonyms:	CAPD2, CNAP1, KIAA0159

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	1401 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. May target the condensin complex to DNA via its C-terminal domain. Ref.6
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. Interacts with histones H1 and H3. Ref.5 Ref.6 Ref.7
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.5
Domain	The C-terminal domain interacts with histones H1 and H3, and may be responsible for condensin complex targeting to mitotic chromosomes. This domain is independent from the bipartite nuclear localization signal, although they are contained within the same region.
Post-translational modification	Phosphorylated by CDK1. Its phosphorylation, as well as that of NCAPH and NCAPG subunits, activates the condensin complex and is required for chromosome condensation By similarity.
Sequence similarities	Belongs to the CND1 (condensin subunit 1) family.
Sequence caution	The sequence BAA09930.2 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	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cell division Inferred from electronic annotation. Source: UniProtKB-KW mitotic chromosome condensation Inferred from direct assay Ref.6. Source: UniProtKB
Cellular_component	condensin core heterodimer Non-traceable author statement Ref.5. Source: UniProtKB cytoplasm Non-traceable author statement Ref.5. Source: UniProtKB nucleus Non-traceable author statement Ref.5. Source: UniProtKB pronucleus Inferred from electronic annotation. Source: Compara
Molecular_function	histone binding Inferred from direct assay Ref.7. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1401	1401	Condensin complex subunit 1		PRO_0000095035
Regions
	Region	1 – 603	603	Interactions with SMC2 and SMC4
	Motif	1342 – 1362	21	Bipartite nuclear localization signal
Amino acid modifications
	Modified residue	20	1	Phosphoserine Ref.15
	Modified residue	585	1	Phosphoserine Ref.13
	Modified residue	1310	1	Phosphoserine Ref.10
	Modified residue	1330	1	Phosphoserine Ref.13
	Modified residue	1331	1	Phosphothreonine Ref.13
	Modified residue	1333	1	Phosphoserine Ref.13 Ref.14 Ref.15 Ref.16
	Modified residue	1339	1	Phosphothreonine Ref.9 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15
	Modified residue	1366	1	Phosphoserine Ref.13
	Modified residue	1367	1	Phosphoserine Ref.13
	Modified residue	1370	1	Phosphoserine Ref.13
	Modified residue	1371	1	Phosphoserine Ref.13
	Modified residue	1376	1	Phosphoserine Ref.8
	Modified residue	1384	1	Phosphothreonine; by CDK1 By similarity
	Modified residue	1389	1	Phosphothreonine; by CDK1 By similarity
Natural variations
	Natural variant	83	1	Q → E. Ref.1 Ref.3 Ref.4 Ref.17 Corresponds to variant rs714774 [ dbSNP | Ensembl ].		VAR_024421
	Natural variant	580	1	K → R. Corresponds to variant rs17725914 [ dbSNP | Ensembl ].		VAR_057511
	Natural variant	797	1	V → M. Corresponds to variant rs10849482 [ dbSNP | Ensembl ].		VAR_024422
	Natural variant	1321	1	T → S. Ref.4 Corresponds to variant rs2240871 [ dbSNP | Ensembl ].		VAR_058713
Experimental info
	Mutagenesis	1343 – 1348	6	RRTTRR → AATTAA: Abolishes localization to the nucleus, while it only reduces chromosome binding. Ref.7
	Mutagenesis	1358 – 1360	3	KKK → AAA: Abolishes localization to the nucleus, while it only reduces chromosome binding. Ref.7
	Sequence conflict	1062	1	M → I in BAA09930. Ref.1
	Sequence conflict	1218	1	R → L in BAA09930. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q15021 [UniParc]. Last modified September 22, 2009. Version 3. Checksum: 35E31642B94B513D	FASTA	1,401	157,182
	10 20 30 40 50 60 MAPQMYEFHL PLSPEELLKS GGVNQYVVQE VLSIKHLPPQ LRAFQAAFRA QGPLAMLQHF 70 80 90 100 110 120 DTIYSILHHF RSIDPGLKED TLQFLIKVVS RHSQELPAIL DDTTLSGSDR NAHLNALKMN 130 140 150 160 170 180 CYALIRLLES FETMASQTNL VDLDLGGKGK KARTKAAHGF DWEEERQPIL QLLTQLLQLD 190 200 210 220 230 240 IRHLWNHSII EEEFVSLVTG CCYRLLENPT INHQKNRPTR EAITHLLGVA LTRYNHMLSA 250 260 270 280 290 300 TVKIIQMLQH FEHLAPVLVA AVSLWATDYG MKSIVGEIVR EIGQKCPQEL SRDPSGTKGF 310 320 330 340 350 360 AAFLTELAER VPAILMSSMC ILLDHLDGEN YMMRNAVLAA MAEMVLQVLS GDQLEAAARD 370 380 390 400 410 420 TRDQFLDTLQ AHGHDVNSFV RSRVLQLFTR IVQQKALPLT RFQAVVALAV GRLADKSVLV 430 440 450 460 470 480 CKNAIQLLAS FLANNPFSCK LSDADLAGPL QKETQKLQEM RAQRRTAAAS AVLDPEEEWE 490 500 510 520 530 540 AMLPELKSTL QQLLQLPQGE EEIPEQIANT ETTEDVKGRI YQLLAKASYK KAIILTREAT 550 560 570 580 590 600 GHFQESEPFS HIDPEESEET RLLNILGLIF KGPAASTQEK NPRESTGNMV TGQTVCKNKP 610 620 630 640 650 660 NMSDPEESRG NDELVKQEML VQYLQDAYSF SRKITEAIGI ISKMMYENTT TVVQEVIEFF 670 680 690 700 710 720 VMVFQFGVPQ ALFGVRRMLP LIWSKEPGVR EAVLNAYRQL YLNPKGDSAR AKAQALIQNL 730 740 750 760 770 780 SLLLVDASVG TIQCLEEILC EFVQKDELKP AVTQLLWERA TEKVACCPLE RCSSVMLLGM 790 800 810 820 830 840 MARGKPEIVG SNLDTLVSIG LDEKFPQDYR LAQQVCHAIA NISDRRKPSL GKRHPPFRLP 850 860 870 880 890 900 QEHRLFERLR ETVTKGFVHP DPLWIPFKEV AVTLIYQLAE GPEVICAQIL QGCAKQALEK 910 920 930 940 950 960 LEEKRTSQED PKESPAMLPT FLLMNLLSLA GDVALQQLVH LEQAVSGELC RRRVLREEQE 970 980 990 1000 1010 1020 HKTKDPKEKN TSSETTMEEE LGLVGATADD TEAELIRGIC EMELLDGKQT LAAFVPLLLK 1030 1040 1050 1060 1070 1080 VCNNPGLYSN PDLSAAASLA LGKFCMISAT FCDSQLRLLF TMLEKSPLPI VRSNLMVATG 1090 1100 1110 1120 1130 1140 DLAIRFPNLV DPWTPHLYAR LRDPAQQVRK TAGLVMTHLI LKDMVKVKGQ VSEMAVLLID 1150 1160 1170 1180 1190 1200 PEPQIAALAK NFFNELSHKG NAIYNLLPDI ISRLSDPELG VEEEPFHTIM KQLLSYITKD 1210 1220 1230 1240 1250 1260 KQTESLVEKL CQRFRTSRTE RQQRDLAYCV SQLPLTERGL RKMLDNFDCF GDKLSDESIF 1270 1280 1290 1300 1310 1320 SAFLSVVGKL RRGAKPEGKA IIDEFEQKLR ACHTRGLDGI KELEIGQAGS QRAPSAKKPS 1330 1340 1350 1360 1370 1380 TGSRYQPLAS TASDNDFVTP EPRRTTRRHP NTQQRASKKK PKVVFSSDES SEEDLSAEMT 1390 1400 EDETPKKTTP ILRASARRHR S

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Prediction of the coding sequences of unidentified human genes. IV. The coding sequences of 40 new genes (KIAA0121-KIAA0160) deduced by analysis of cDNA clones from human cell line KG-1." Nagase T., Seki N., Tanaka A., Ishikawa K., Nomura N. DNA Res. 2:167-174(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT GLU-83. Tissue: Bone marrow.
[2]	"The finished DNA sequence of human chromosome 12." Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R. , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A. Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	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 (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT GLU-83.
[4]	"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], VARIANTS GLU-83 AND SER-1321. Tissue: Mammary gland.
[5]	"A human condensin complex containing hCAP-C-hCAP-E and CNAP1, a homolog of Xenopus XCAP-D2, colocalizes with phosphorylated histone H3 during the early stage of mitotic chromosome condensation." Schmiesing J.A., Gregson H.C., Zhou S., Yokomori K. Mol. Cell. Biol. 20:6996-7006(2000) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 359-365; 537-560; 698-709 AND 1324-1331, IDENTIFICATION IN A CONDENSIN COMPLEX WITH SMC2 AND SMC4, SUBCELLULAR LOCATION.
[6]	"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; NCAPH AND NCAPG, FUNCTION OF THE CONDENSIN COMPLEX.
[7]	"Identification of a chromosome-targeting domain in the human condensin subunit CNAP1/hCAP-D2/Eg7." Ball A.R. Jr., Schmiesing J.A., Zhou C., Gregson H.C., Okada Y., Doi T., Yokomori K. Mol. Cell. Biol. 22:5769-5781(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HISTONE H1 AND HISTONE H3, MUTAGENESIS OF 1343-ARG--ARG-1348 AND 1358-LYS--LYS-1360.
[8]	"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-1376, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1339, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"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-1310, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[11]	"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis." Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1339, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"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 THR-1339, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[13]	"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-585; SER-1330; THR-1331; SER-1333; THR-1339; SER-1366; SER-1367; SER-1370 AND SER-1371, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[14]	"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-1333 AND THR-1339, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[15]	"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-20; SER-1333 AND THR-1339, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[16]	"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-1333, MASS SPECTROMETRY.
[17]	"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: VARIANT [LARGE SCALE ANALYSIS] GLU-83, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D63880 mRNA. Translation: BAA09930.2. Different initiation. AC006064 Genomic DNA. No translation available. CH471116 Genomic DNA. Translation: EAW88788.1. CH471116 Genomic DNA. Translation: EAW88789.1. BC028182 mRNA. Translation: AAH28182.1.
IPI	IPI00299524.
RefSeq	NP_055680.3. NM_014865.3.
UniGene	Hs.5719.
3D structure databases
ProteinModelPortal	Q15021.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q15021. 2 interactions.
MINT	MINT-3030640.
STRING	9606.ENSP00000325017.
PTM databases
PhosphoSite	Q15021.
Polymorphism databases
DMDM	259016362.
Proteomic databases
PaxDb	Q15021.
PRIDE	Q15021.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000315579; ENSP00000325017; ENSG00000010292.
GeneID	9918.
KEGG	hsa:9918.
UCSC	uc001qoo.2. human.
Organism-specific databases
CTD	9918.
GeneCards	GC12P006602.
H-InvDB	HIX0201829.
HGNC	HGNC:24305. NCAPD2.
HPA	CAB012423. HPA036947. HPA037363.
neXtProt	NX_Q15021.
PharmGKB	PA162397021.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG5098.
HOGENOM	HOG000068001.
HOVERGEN	HBG038048.
InParanoid	Q15021.
KO	K06677.
OMA	TERQHRD.
PhylomeDB	Q15021.
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	Q15021.
Bgee	Q15021.
CleanEx	HS_NCAPD2.
Genevestigator	Q15021.
Family and domain databases
Gene3D	1.25.10.10. 3 hits.
InterPro	IPR011989. ARM-like. IPR016024. ARM-type_fold. IPR026971. CND1/NCAPD3. IPR007673. Condensin_cplx_su1. IPR024324. Condensin_cplx_su1_N. [Graphical view]
PANTHER	PTHR14222. PTHR14222. 1 hit.
Pfam	PF12922. Cnd1_N. 1 hit. [Graphical view]
PIRSF	PIRSF017127. Condensin_D2. 1 hit.
SUPFAM	SSF48371. ARM-type_fold. 1 hit.
ProtoNet	Search...
Other
ChiTaRS	NCAPD2. human.
GenomeRNAi	9918.
NextBio	37412.

Entry information

Entry name

CND1_HUMAN

Accession

Primary (citable) accession number: Q15021
Secondary accession number(s): D3DUR4, Q8N6U3

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 23, 2003
Last sequence update:	September 22, 2009
Last modified:	May 1, 2013
This is version 126 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.