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Q15021

- CND1_HUMAN

UniProt

Q15021 - CND1_HUMAN

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Protein

Condensin complex subunit 1

Gene

NCAPD2

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. May target the condensin complex to DNA via its C-terminal domain.1 Publication

GO - Molecular functioni

  1. histone binding Source: UniProtKB

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 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 namesi
Name:NCAPD2
Synonyms:CAPD2, CNAP1, KIAA0159
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:24305. NCAPD2.

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. condensed chromosome Source: MGI
  2. condensin complex Source: UniProtKB
  3. condensin core heterodimer Source: UniProtKB
  4. cytoplasm Source: UniProtKB
  5. cytosol Source: Reactome
  6. membrane Source: UniProtKB
  7. nucleus Source: UniProtKB
  8. pronucleus Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi1343 – 13486RRTTRR → AATTAA: Abolishes localization to the nucleus, while it only reduces chromosome binding. 1 Publication
Mutagenesisi1358 – 13603KKK → AAA: Abolishes localization to the nucleus, while it only reduces chromosome binding. 1 Publication

Organism-specific databases

PharmGKBiPA162397021.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 14011401Condensin complex subunit 1PRO_0000095035Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei20 – 201Phosphoserine1 Publication
Modified residuei585 – 5851Phosphoserine1 Publication
Modified residuei1310 – 13101Phosphoserine1 Publication
Modified residuei1330 – 13301Phosphoserine1 Publication
Modified residuei1331 – 13311Phosphothreonine1 Publication
Modified residuei1333 – 13331Phosphoserine4 Publications
Modified residuei1339 – 13391Phosphothreonine6 Publications
Modified residuei1366 – 13661Phosphoserine1 Publication
Modified residuei1367 – 13671Phosphoserine1 Publication
Modified residuei1370 – 13701Phosphoserine1 Publication
Modified residuei1371 – 13711Phosphoserine1 Publication
Modified residuei1376 – 13761Phosphoserine1 Publication
Modified residuei1384 – 13841Phosphothreonine; by CDK1By similarity
Modified residuei1389 – 13891Phosphothreonine; by CDK1By similarity

Post-translational modificationi

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).By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ15021.
PaxDbiQ15021.
PRIDEiQ15021.

PTM databases

PhosphoSiteiQ15021.

Expressioni

Gene expression databases

BgeeiQ15021.
CleanExiHS_NCAPD2.
ExpressionAtlasiQ15021. baseline and differential.
GenevestigatoriQ15021.

Organism-specific databases

HPAiCAB012423.
HPA036947.
HPA037363.

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. Interacts with histones H1 and H3.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
NCAPGQ9BPX32EBI-1044041,EBI-970214
NCAPHQ150034EBI-1044041,EBI-1046410

Protein-protein interaction databases

BioGridi115246. 29 interactions.
IntActiQ15021. 7 interactions.
MINTiMINT-3030640.
STRINGi9606.ENSP00000325017.

Structurei

3D structure databases

ProteinModelPortaliQ15021.
SMRiQ15021. Positions 319-396, 767-824, 1068-1119.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 603603Interactions with SMC2 and SMC4Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi1342 – 136221Bipartite nuclear localization signalAdd
BLAST

Domaini

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.

Sequence similaritiesi

Belongs to the CND1 (condensin subunit 1) family.Curated

Phylogenomic databases

eggNOGiCOG5098.
GeneTreeiENSGT00390000017108.
HOGENOMiHOG000068001.
HOVERGENiHBG038048.
InParanoidiQ15021.
KOiK06677.
OMAiATEKVAC.
OrthoDBiEOG7FJGZN.
PhylomeDBiQ15021.
TreeFamiTF105712.

Family and domain databases

Gene3Di1.25.10.10. 3 hits.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR026971. CND1/NCAPD3.
IPR007673. Condensin_cplx_su1.
IPR024324. Condensin_cplx_su1_N.
[Graphical view]
PANTHERiPTHR14222. PTHR14222. 1 hit.
PfamiPF12922. Cnd1_N. 1 hit.
[Graphical view]
PIRSFiPIRSF017127. Condensin_D2. 1 hit.
SUPFAMiSSF48371. SSF48371. 4 hits.

Sequencei

Sequence statusi: Complete.

Q15021-1 [UniParc]FASTAAdd to Basket

« Hide

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

S
Length:1,401
Mass (Da):157,182
Last modified:September 22, 2009 - v3
Checksum:i35E31642B94B513D
GO

Sequence cautioni

The sequence BAA09930.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1062 – 10621M → I in BAA09930. (PubMed:8590280)Curated
Sequence conflicti1218 – 12181R → L in BAA09930. (PubMed:8590280)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti83 – 831Q → E.4 Publications
Corresponds to variant rs714774 [ dbSNP | Ensembl ].
VAR_024421
Natural varianti580 – 5801K → R.
Corresponds to variant rs17725914 [ dbSNP | Ensembl ].
VAR_057511
Natural varianti797 – 7971V → M.
Corresponds to variant rs10849482 [ dbSNP | Ensembl ].
VAR_024422
Natural varianti1321 – 13211T → S.1 Publication
Corresponds to variant rs2240871 [ dbSNP | Ensembl ].
VAR_058713

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS8548.1.
RefSeqiNP_055680.3. NM_014865.3.
UniGeneiHs.5719.

Genome annotation databases

EnsembliENST00000315579; ENSP00000325017; ENSG00000010292.
GeneIDi9918.
KEGGihsa:9918.
UCSCiuc001qoo.2. human.

Polymorphism databases

DMDMi259016362.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS8548.1.
RefSeqi NP_055680.3. NM_014865.3.
UniGenei Hs.5719.

3D structure databases

ProteinModelPortali Q15021.
SMRi Q15021. Positions 319-396, 767-824, 1068-1119.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115246. 29 interactions.
IntActi Q15021. 7 interactions.
MINTi MINT-3030640.
STRINGi 9606.ENSP00000325017.

PTM databases

PhosphoSitei Q15021.

Polymorphism databases

DMDMi 259016362.

Proteomic databases

MaxQBi Q15021.
PaxDbi Q15021.
PRIDEi Q15021.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000315579 ; ENSP00000325017 ; ENSG00000010292 .
GeneIDi 9918.
KEGGi hsa:9918.
UCSCi uc001qoo.2. human.

Organism-specific databases

CTDi 9918.
GeneCardsi GC12P006602.
H-InvDB HIX0201829.
HGNCi HGNC:24305. NCAPD2.
HPAi CAB012423.
HPA036947.
HPA037363.
MIMi 615638. gene.
neXtProti NX_Q15021.
PharmGKBi PA162397021.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5098.
GeneTreei ENSGT00390000017108.
HOGENOMi HOG000068001.
HOVERGENi HBG038048.
InParanoidi Q15021.
KOi K06677.
OMAi ATEKVAC.
OrthoDBi EOG7FJGZN.
PhylomeDBi Q15021.
TreeFami TF105712.

Enzyme and pathway databases

Reactomei REACT_150260. Condensation of Prometaphase Chromosomes.

Miscellaneous databases

ChiTaRSi NCAPD2. human.
GeneWikii NCAPD2.
GenomeRNAii 9918.
NextBioi 37412.
PROi Q15021.
SOURCEi Search...

Gene expression databases

Bgeei Q15021.
CleanExi HS_NCAPD2.
ExpressionAtlasi Q15021. baseline and differential.
Genevestigatori Q15021.

Family and domain databases

Gene3Di 1.25.10.10. 3 hits.
InterProi IPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR026971. CND1/NCAPD3.
IPR007673. Condensin_cplx_su1.
IPR024324. Condensin_cplx_su1_N.
[Graphical view ]
PANTHERi PTHR14222. PTHR14222. 1 hit.
Pfami PF12922. Cnd1_N. 1 hit.
[Graphical view ]
PIRSFi PIRSF017127. Condensin_D2. 1 hit.
SUPFAMi SSF48371. SSF48371. 4 hits.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1310, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. "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].
  15. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  16. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  17. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. Cited for: VARIANT [LARGE SCALE ANALYSIS] GLU-83, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiCND1_HUMAN
AccessioniPrimary (citable) accession number: Q15021
Secondary accession number(s): D3DUR4, Q8N6U3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 23, 2003
Last sequence update: September 22, 2009
Last modified: November 26, 2014
This is version 142 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: 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