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Q15003

- CND2_HUMAN

UniProt

Q15003 - CND2_HUMAN

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Protein

Condensin complex subunit 2

Gene

NCAPH

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.1 Publication

GO - Biological processi

  1. mitotic cell cycle Source: Reactome
  2. mitotic chromosome condensation Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, DNA condensation, Mitosis

Enzyme and pathway databases

ReactomeiREACT_150260. Condensation of Prometaphase Chromosomes.

Names & Taxonomyi

Protein namesi
Recommended name:
Condensin complex subunit 2
Alternative name(s):
Barren homolog protein 1
Chromosome-associated protein H
Short name:
hCAP-H
Non-SMC condensin I complex subunit H
XCAP-H homolog
Gene namesi
Name:NCAPH
Synonyms:BRRN, BRRN1, CAPH, KIAA0074
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:1112. NCAPH.

Subcellular locationi

Nucleus 1 Publication. Cytoplasm 1 Publication. Chromosome 1 Publication
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.

GO - Cellular componenti

  1. condensin complex Source: UniProtKB
  2. cytoplasm Source: HPA
  3. cytosol Source: Reactome
  4. membrane Source: UniProtKB
  5. microtubule cytoskeleton Source: HPA
  6. nucleus Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162397273.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 741741Condensin complex subunit 2PRO_0000095038Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei15 – 151Phosphoserine1 Publication
Modified residuei25 – 251Phosphoserine1 Publication
Modified residuei49 – 491Phosphothreonine1 Publication
Modified residuei70 – 701Phosphoserine1 Publication
Modified residuei78 – 781Phosphoserine2 Publications
Modified residuei81 – 811Phosphoserine3 Publications
Modified residuei87 – 871Phosphoserine2 Publications
Modified residuei92 – 921Phosphoserine2 Publications
Modified residuei96 – 961Phosphoserine1 Publication
Modified residuei201 – 2011Phosphoserine2 Publications
Modified residuei432 – 4321Phosphoserine2 Publications
Modified residuei598 – 5981Phosphothreonine1 Publication
Modified residuei605 – 6051Phosphothreonine1 Publication
Modified residuei637 – 6371N6-acetyllysine1 Publication

Post-translational modificationi

Phosphorylated by CDK1. Its phosphorylation, as well as that of NCAPD2 and NCAPG subunits, activates the condensin complex and is required for chromosome condensation (By similarity).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ15003.
PaxDbiQ15003.
PeptideAtlasiQ15003.
PRIDEiQ15003.

PTM databases

PhosphoSiteiQ15003.

Miscellaneous databases

PMAP-CutDBQ15003.

Expressioni

Tissue specificityi

Widely expressed at low level. Expressed in proliferating cells.1 Publication

Gene expression databases

BgeeiQ15003.
CleanExiHS_NCAPH.
ExpressionAtlasiQ15003. baseline and differential.
GenevestigatoriQ15003.

Organism-specific databases

HPAiHPA002647.
HPA003008.

Interactioni

Subunit structurei

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.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
DDX3XO005712EBI-1046410,EBI-353779
NCAPD2Q150214EBI-1046410,EBI-1044041
NCAPGQ9BPX32EBI-1046410,EBI-970214
SMC2O953472EBI-1046410,EBI-355822

Protein-protein interaction databases

BioGridi116970. 24 interactions.
DIPiDIP-43899N.
IntActiQ15003. 7 interactions.
MINTiMINT-5004625.
STRINGi9606.ENSP00000240423.

Structurei

3D structure databases

ProteinModelPortaliQ15003.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the CND2 (condensin subunit 2) family.Curated

Phylogenomic databases

eggNOGiCOG5229.
GeneTreeiENSGT00390000004149.
HOGENOMiHOG000231887.
HOVERGENiHBG036823.
InParanoidiQ15003.
KOiK06676.
OMAiPYPCHPP.
OrthoDBiEOG7JMGDB.
PhylomeDBiQ15003.
TreeFamiTF105678.

Family and domain databases

InterProiIPR022816. Condensin_barren_su2.
[Graphical view]
PfamiPF05786. Cnd2. 1 hit.
[Graphical view]
PIRSFiPIRSF017126. Condensin_H. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q15003) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MGPPGPALPA TMNNSSSETR GHPHSASSPS ERVFPMPLPR KAPLNIPGTP
60 70 80 90 100
VLEDFPQNDD EKERLQRRRS RVFDLQFSTD SPRLLASPSS RSIDISATIP
110 120 130 140 150
KFTNTQITEH YSTCIKLSTE NKITTKNAFG LHLIDFMSEI LKQKDTEPTN
160 170 180 190 200
FKVAAGTLDA STKIYAVRVD AVHADVYRVL GGLGKDAPSL EEVEGHVADG
210 220 230 240 250
SATEMGTTKK AVKPKKKHLH RTIEQNINNL NVSEADRKCE IDPMFQKTAA
260 270 280 290 300
SFDECSTAGV FLSTLHCQDY RSELLFPSDV QTLSTGEPLE LPELGCVEMT
310 320 330 340 350
DLKAPLQQCA EDRQICPSLA GFQFTQWDSE THNESVSALV DKFKKNDQVF
360 370 380 390 400
DINAEVDESD CGDFPDGSLG DDFDANDEPD HTAVGDHEEF RSWKEPCQVQ
410 420 430 440 450
SCQEEMISLG DGDIRTMCPL LSMKPGEYSY FSPRTMSMWA GPDHWRFRPR
460 470 480 490 500
RKQDAPSQSE NKKKSTKKDF EIDFEDDIDF DVYFRKTKAA TILTKSTLEN
510 520 530 540 550
QNWRATTLPT DFNYNVDTLV QLHLKPGTRL LKMAQGHRVE TEHYEEIEDY
560 570 580 590 600
DYNNPNDTSN FCPGLQAADS DDEDLDDLFV GPVGNSDLSP YPCHPPKTAQ
610 620 630 640 650
QNGDTPEAQG LDITTYGESN LVAEPQKVNK IEIHYAKTAK KMDMKKLKQS
660 670 680 690 700
MWSLLTALSG KEADAEANHR EAGKEAALAE VADEKMLSGL TKDLQRSLPP
710 720 730 740
VMAQNLSIPL AFACLLHLAN EKNLKLEGTE DLSDVLVRQG D
Length:741
Mass (Da):82,563
Last modified:October 17, 2006 - v3
Checksum:iB5B34A36CAE0C28E
GO
Isoform 2 (identifier: Q15003-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-136: Missing.

Note: No experimental confirmation available.

Show »
Length:605
Mass (Da):67,495
Checksum:i4ABE503B4CB20935
GO

Sequence cautioni

The sequence BAA07556.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti539 – 5391V → A.1 Publication
Corresponds to variant rs2305935 [ dbSNP | Ensembl ].
VAR_027882

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 136136Missing in isoform 2. 1 PublicationVSP_055179Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D38553 mRNA. Translation: BAA07556.1. Different initiation.
AK303725 mRNA. Translation: BAG64701.1.
AC021188 Genomic DNA. No translation available.
BC024211 mRNA. Translation: AAH24211.1.
CCDSiCCDS2021.1. [Q15003-1]
CCDS62960.1. [Q15003-2]
RefSeqiNP_001268639.1. NM_001281710.1.
NP_001268640.1. NM_001281711.1.
NP_001268641.1. NM_001281712.1. [Q15003-2]
NP_056156.2. NM_015341.4. [Q15003-1]
UniGeneiHs.308045.

Genome annotation databases

EnsembliENST00000240423; ENSP00000240423; ENSG00000121152. [Q15003-1]
ENST00000427946; ENSP00000400774; ENSG00000121152. [Q15003-2]
GeneIDi23397.
KEGGihsa:23397.
UCSCiuc002svz.1. human. [Q15003-1]

Polymorphism databases

DMDMi116241306.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D38553 mRNA. Translation: BAA07556.1 . Different initiation.
AK303725 mRNA. Translation: BAG64701.1 .
AC021188 Genomic DNA. No translation available.
BC024211 mRNA. Translation: AAH24211.1 .
CCDSi CCDS2021.1. [Q15003-1 ]
CCDS62960.1. [Q15003-2 ]
RefSeqi NP_001268639.1. NM_001281710.1.
NP_001268640.1. NM_001281711.1.
NP_001268641.1. NM_001281712.1. [Q15003-2 ]
NP_056156.2. NM_015341.4. [Q15003-1 ]
UniGenei Hs.308045.

3D structure databases

ProteinModelPortali Q15003.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116970. 24 interactions.
DIPi DIP-43899N.
IntActi Q15003. 7 interactions.
MINTi MINT-5004625.
STRINGi 9606.ENSP00000240423.

PTM databases

PhosphoSitei Q15003.

Polymorphism databases

DMDMi 116241306.

Proteomic databases

MaxQBi Q15003.
PaxDbi Q15003.
PeptideAtlasi Q15003.
PRIDEi Q15003.

Protocols and materials databases

DNASUi 23397.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000240423 ; ENSP00000240423 ; ENSG00000121152 . [Q15003-1 ]
ENST00000427946 ; ENSP00000400774 ; ENSG00000121152 . [Q15003-2 ]
GeneIDi 23397.
KEGGi hsa:23397.
UCSCi uc002svz.1. human. [Q15003-1 ]

Organism-specific databases

CTDi 23397.
GeneCardsi GC02P097001.
HGNCi HGNC:1112. NCAPH.
HPAi HPA002647.
HPA003008.
MIMi 602332. gene.
neXtProti NX_Q15003.
PharmGKBi PA162397273.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5229.
GeneTreei ENSGT00390000004149.
HOGENOMi HOG000231887.
HOVERGENi HBG036823.
InParanoidi Q15003.
KOi K06676.
OMAi PYPCHPP.
OrthoDBi EOG7JMGDB.
PhylomeDBi Q15003.
TreeFami TF105678.

Enzyme and pathway databases

Reactomei REACT_150260. Condensation of Prometaphase Chromosomes.

Miscellaneous databases

GeneWikii NCAPH.
GenomeRNAii 23397.
NextBioi 35476965.
PMAP-CutDB Q15003.
PROi Q15003.
SOURCEi Search...

Gene expression databases

Bgeei Q15003.
CleanExi HS_NCAPH.
ExpressionAtlasi Q15003. baseline and differential.
Genevestigatori Q15003.

Family and domain databases

InterProi IPR022816. Condensin_barren_su2.
[Graphical view ]
Pfami PF05786. Cnd2. 1 hit.
[Graphical view ]
PIRSFi PIRSF017126. Condensin_H. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Prediction of the coding sequences of unidentified human genes. II. The coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by analysis of cDNA clones from human cell line KG-1."
    Nomura N., Nagase T., Miyajima N., Sazuka T., Tanaka A., Sato S., Seki N., Kawarabayasi Y., Ishikawa K., Tabata S.
    DNA Res. 1:223-229(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Bone marrow.
  2. "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] (ISOFORM 2).
    Tissue: Kidney.
  3. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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], VARIANT ALA-539.
    Tissue: Placenta.
  5. "Cell cycle-dependent expression and nucleolar localization of hCAP-H."
    Cabello O.A., Eliseeva E., He W.G., Youssoufian H., Plon S.E., Brinkley B.R., Belmont J.W.
    Mol. Biol. Cell 12:3527-3537(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION DURING THE CELL CYCLE, TISSUE SPECIFICITY.
  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; NCAPD2 AND NCAPG, FUNCTION OF THE COMPLEX.
  7. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70; SER-78; SER-81; SER-87; SER-92; SER-201; SER-432 AND THR-605, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "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].
  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-81, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  11. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-637, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  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-15; SER-25; THR-49; SER-78; SER-81; SER-87; SER-92; SER-96; SER-201; SER-432 AND THR-598, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. 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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiCND2_HUMAN
AccessioniPrimary (citable) accession number: Q15003
Secondary accession number(s): B4E189, Q8TB87
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 23, 2003
Last sequence update: October 17, 2006
Last modified: October 29, 2014
This is version 127 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3