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Q9BPX3

- CND3_HUMAN

UniProt

Q9BPX3 - CND3_HUMAN

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Protein

Condensin complex subunit 3

Gene

NCAPG

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 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 namesi
Name:NCAPG
Synonyms:CAPG, NYMEL3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 4

Organism-specific databases

HGNCiHGNC:24304. NCAPG.

Subcellular locationi

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.

GO - Cellular componenti

  1. actin cytoskeleton Source: HPA
  2. centrosome Source: HPA
  3. condensin complex Source: UniProtKB
  4. cytoplasm Source: HPA
  5. cytosol Source: Reactome
  6. membrane Source: UniProtKB
  7. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162397165.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10151015Condensin complex subunit 3PRO_0000095041Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei390 – 3901Phosphoserine2 Publications
Modified residuei674 – 6741Phosphoserine6 Publications
Modified residuei931 – 9311Phosphothreonine1 Publication
Modified residuei973 – 9731Phosphoserine1 Publication
Modified residuei975 – 9751Phosphoserine1 Publication
Modified residuei1002 – 10021Phosphoserine1 Publication
Modified residuei1015 – 10151Phosphoserine5 Publications

Post-translational modificationi

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).By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9BPX3.
PaxDbiQ9BPX3.
PeptideAtlasiQ9BPX3.
PRIDEiQ9BPX3.

PTM databases

PhosphoSiteiQ9BPX3.

Expressioni

Tissue specificityi

Highly expressed in testis.1 Publication

Gene expression databases

BgeeiQ9BPX3.
CleanExiHS_CAPG.
HS_NCAPG.
ExpressionAtlasiQ9BPX3. baseline and differential.
GenevestigatoriQ9BPX3.

Organism-specific databases

HPAiHPA039613.
HPA040103.

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

Protein-protein interaction databases

BioGridi122089. 27 interactions.
IntActiQ9BPX3. 8 interactions.
MINTiMINT-3060256.
STRINGi9606.ENSP00000251496.

Structurei

3D structure databases

ProteinModelPortaliQ9BPX3.
SMRiQ9BPX3. Positions 95-307, 408-451, 624-652, 692-718.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati94 – 13138HEAT 1Add
BLAST
Repeati138 – 17336HEAT 2Add
BLAST
Repeati174 – 21239HEAT 3Add
BLAST
Repeati238 – 27538HEAT 4Add
BLAST
Repeati276 – 31338HEAT 5Add
BLAST
Repeati399 – 43638HEAT 6Add
BLAST
Repeati439 – 47840HEAT 7Add
BLAST
Repeati617 – 65438HEAT 8Add
BLAST
Repeati687 – 72438HEAT 9Add
BLAST
Repeati865 – 90743HEAT 10Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi88 – 914Poly-Glu
Compositional biasi912 – 9176Poly-Thr

Sequence similaritiesi

Belongs to the CND3 (condensin subunit 3) family.Curated
Contains 10 HEAT repeats.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG5218.
GeneTreeiENSGT00390000001577.
HOVERGENiHBG039407.
InParanoidiQ9BPX3.
KOiK06678.
OMAiEACCYEP.
OrthoDBiEOG7CVPWZ.
PhylomeDBiQ9BPX3.
TreeFamiTF101160.

Family and domain databases

Gene3Di1.25.10.10. 3 hits.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR027165. CND3.
IPR025977. Cnd3_C.
[Graphical view]
PANTHERiPTHR14418. PTHR14418. 1 hit.
PfamiPF12719. Cnd3. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 2 hits.

Sequencei

Sequence statusi: Complete.

Q9BPX3-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGAERRLLSI KEAFRLAQQP HQNQAKLVVA LSRTYRTMDD KTVFHEEFIH
60 70 80 90 100
YLKYVMVVYK REPAVERVIE FAAKFVTSFH QSDMEDDEEE EDGGLLNYLF
110 120 130 140 150
TFLLKSHEAN SNAVRFRVCL LINKLLGSMP ENAQIDDDVF DKINKAMLIR
160 170 180 190 200
LKDKIPNVRI QAVLALSRLQ DPKDDECPVV NAYATLIEND SNPEVRRAVL
210 220 230 240 250
SCIAPSAKTL PKIVGRTKDV KEAVRKLAYQ VLAEKVHMRA MSIAQRVMLL
260 270 280 290 300
QQGLNDRSDA VKQAMQKHLL QGWLRFSEGN ILELLHRLDV ENSSEVAVSV
310 320 330 340 350
LNALFSITPL SELVGLCKNN DGRKLIPVET LTPEIALYWC ALCEYLKSKG
360 370 380 390 400
DEGEEFLEQI LPEPVVYADY LLSYIQSIPV VNEEHRGDFS YIGNLMTKEF
410 420 430 440 450
IGQQLILIIK SLDTSEEGGR KKLLAVLQEI LILPTIPISL VSFLVERLLH
460 470 480 490 500
IIIDDNKRTQ IVTEIISEIR APIVTVGVNN DPADVRKKEL KMAEIKVKLI
510 520 530 540 550
EAKEALENCI TLQDFNRASE LKEEIKALED ARINLLKETE QLEIKEVHIE
560 570 580 590 600
KNDAETLQKC LILCYELLKQ MSISTGLSAT MNGIIESLIL PGIISIHPVV
610 620 630 640 650
RNLAVLCLGC CGLQNQDFAR KHFVLLLQVL QIDDVTIKIS ALKAIFDQLM
660 670 680 690 700
TFGIEPFKTK KIKTLHCEGT EINSDDEQES KEVEETATAK NVLKLLSDFL
710 720 730 740 750
DSEVSELRTG AAEGLAKLMF SGLLVSSRIL SRLILLWYNP VTEEDVQLRH
760 770 780 790 800
CLGVFFPVFA YASRTNQECF EEAFLPTLQT LANAPASSPL AEIDITNVAE
810 820 830 840 850
LLVDLTRPSG LNPQAKTSQD YQALTVHDNL AMKICNEILT SPCSPEIRVY
860 870 880 890 900
TKALSSLELS SHLAKDLLVL LNEILEQVKD RTCLRALEKI KIQLEKGNKE
910 920 930 940 950
FGDQAEAAQD ATLTTTTFQN EDEKNKEVYM TPLRGVKATQ ASKSTQLKTN
960 970 980 990 1000
RGQRKVTVSA RTNRRCQTAE ADSESDHEVP EPESEMKMRL PRRAKTAALE
1010
KSKLNLAQFL NEDLS
Length:1,015
Mass (Da):114,334
Last modified:June 1, 2001 - v1
Checksum:iD9ACC205C48F3AF5
GO

Sequence cautioni

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.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti115 – 1151R → G in BAB14069. (PubMed:14702039)Curated
Sequence conflicti276 – 2761F → V in AAG30732. (PubMed:10910072)Curated
Sequence conflicti519 – 5191S → P in BAB55165. (PubMed:14702039)Curated
Sequence conflicti676 – 6761D → V in BAB14069. (PubMed:14702039)Curated
Sequence conflicti681 – 6811K → R in BAB14069. (PubMed:14702039)Curated
Sequence conflicti704 – 7041V → A in BAB14069. (PubMed:14702039)Curated
Sequence conflicti836 – 8361N → D in BAB55165. (PubMed:14702039)Curated
Sequence conflicti1010 – 10101L → F in AAG30732. (PubMed:10910072)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti64 – 641A → P.
Corresponds to variant rs35722563 [ dbSNP | Ensembl ].
VAR_053041
Natural varianti265 – 2651M → T in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_036125
Natural varianti581 – 5811M → I.1 Publication
Corresponds to variant rs3795243 [ dbSNP | Ensembl ].
VAR_053042

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS3424.1.
RefSeqiNP_071741.2. NM_022346.4.
UniGeneiHs.567567.

Genome annotation databases

EnsembliENST00000251496; ENSP00000251496; ENSG00000109805.
GeneIDi64151.
KEGGihsa:64151.
UCSCiuc003gpp.4. human.

Polymorphism databases

DMDMi30172941.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS3424.1.
RefSeqi NP_071741.2. NM_022346.4.
UniGenei Hs.567567.

3D structure databases

ProteinModelPortali Q9BPX3.
SMRi Q9BPX3. Positions 95-307, 408-451, 624-652, 692-718.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 122089. 27 interactions.
IntActi Q9BPX3. 8 interactions.
MINTi MINT-3060256.
STRINGi 9606.ENSP00000251496.

PTM databases

PhosphoSitei Q9BPX3.

Polymorphism databases

DMDMi 30172941.

Proteomic databases

MaxQBi Q9BPX3.
PaxDbi Q9BPX3.
PeptideAtlasi Q9BPX3.
PRIDEi Q9BPX3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000251496 ; ENSP00000251496 ; ENSG00000109805 .
GeneIDi 64151.
KEGGi hsa:64151.
UCSCi uc003gpp.4. human.

Organism-specific databases

CTDi 64151.
GeneCardsi GC04P017812.
HGNCi HGNC:24304. NCAPG.
HPAi HPA039613.
HPA040103.
MIMi 606280. gene.
neXtProti NX_Q9BPX3.
PharmGKBi PA162397165.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5218.
GeneTreei ENSGT00390000001577.
HOVERGENi HBG039407.
InParanoidi Q9BPX3.
KOi K06678.
OMAi EACCYEP.
OrthoDBi EOG7CVPWZ.
PhylomeDBi Q9BPX3.
TreeFami TF101160.

Enzyme and pathway databases

Reactomei REACT_150260. Condensation of Prometaphase Chromosomes.

Miscellaneous databases

GeneWikii NCAPG.
GenomeRNAii 64151.
NextBioi 66065.
PROi Q9BPX3.
SOURCEi Search...

Gene expression databases

Bgeei Q9BPX3.
CleanExi HS_CAPG.
HS_NCAPG.
ExpressionAtlasi Q9BPX3. baseline and differential.
Genevestigatori Q9BPX3.

Family and domain databases

Gene3Di 1.25.10.10. 3 hits.
InterProi IPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR027165. CND3.
IPR025977. Cnd3_C.
[Graphical view ]
PANTHERi PTHR14418. PTHR14418. 1 hit.
Pfami PF12719. Cnd3. 1 hit.
[Graphical view ]
SUPFAMi SSF48371. SSF48371. 2 hits.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. 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. 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. 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. Cited for: VARIANT [LARGE SCALE ANALYSIS] THR-265.

Entry informationi

Entry nameiCND3_HUMAN
AccessioniPrimary (citable) accession number: Q9BPX3
Secondary accession number(s): Q3MJE0
, Q96SV9, Q9BUR3, Q9BVY1, Q9H914, Q9H9Z6, Q9HBI9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 23, 2003
Last sequence update: June 1, 2001
Last modified: October 29, 2014
This is version 126 of the entry and version 1 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

Miscellaneous

Overexpressed in some cancer lines and some tumor cells.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: 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