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Q6IBW4

- CNDH2_HUMAN

UniProt

Q6IBW4 - CNDH2_HUMAN

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Protein

Condensin-2 complex subunit H2

Gene

NCAPH2

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

Functioni

Regulatory subunit of the condensin-2 complex, a complex that seems to provide chromosomes with an additional level of organization and rigidity and in establishing mitotic chromosome architecture. May play a role in lineage-specific role in T-cell development (By similarity).By similarity

GO - Biological processi

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

Keywords - Biological processi

DNA condensation

Enzyme and pathway databases

ReactomeiREACT_172744. Condensation of Prophase Chromosomes.

Names & Taxonomyi

Protein namesi
Recommended name:
Condensin-2 complex subunit H2
Alternative name(s):
Chromosome-associated protein H2
Short name:
hCAP-H2
Kleisin-beta
Non-SMC condensin II complex subunit H2
Gene namesi
Name:NCAPH2
Synonyms:CAPH2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 22

Organism-specific databases

HGNCiHGNC:25071. NCAPH2.

Subcellular locationi

Nucleus 1 Publication. Chromosome 1 Publication
Note: Distributed along the arms of chromosomes assembled in vivo and in vitro.

GO - Cellular componenti

  1. chromosome Source: UniProtKB-KW
  2. membrane Source: UniProtKB
  3. nucleoplasm Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162397314.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 605605Condensin-2 complex subunit H2PRO_0000326241Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei19 – 191Phosphothreonine1 Publication
Modified residuei95 – 951Phosphoserine1 Publication
Modified residuei96 – 961Phosphoserine1 Publication
Modified residuei200 – 2001Phosphoserine1 Publication
Modified residuei208 – 2081Phosphoserine2 Publications
Modified residuei282 – 2821Phosphoserine1 Publication
Modified residuei284 – 2841Phosphoserine2 Publications
Modified residuei466 – 4661Phosphoserine1 Publication
Modified residuei492 – 4921Phosphoserine4 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ6IBW4.
PaxDbiQ6IBW4.
PRIDEiQ6IBW4.

PTM databases

PhosphoSiteiQ6IBW4.

Expressioni

Gene expression databases

BgeeiQ6IBW4.
CleanExiHS_NCAPH2.
ExpressionAtlasiQ6IBW4. baseline and differential.
GenevestigatoriQ6IBW4.

Interactioni

Subunit structurei

Component of the condensin-2 complex, which contains the SMC2 and SMC4 heterodimer, and three non SMC subunits, NCAPG2, NCAPH2 and NCAPD3 that probably regulate the complex.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
NCAPD3P426952EBI-2548296,EBI-722805
NCAPG2Q86XI22EBI-2548296,EBI-1047404
SMC2O953472EBI-2548296,EBI-355822

Protein-protein interaction databases

BioGridi118913. 19 interactions.
DIPiDIP-43901N.
IntActiQ6IBW4. 10 interactions.
MINTiMINT-4329914.

Structurei

3D structure databases

ProteinModelPortaliQ6IBW4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG238357.
GeneTreeiENSGT00390000014443.
HOVERGENiHBG098083.
InParanoidiQ6IBW4.
KOiK11490.
OMAiAPEPASC.
OrthoDBiEOG7W41C5.
PhylomeDBiQ6IBW4.
TreeFamiTF101164.

Family and domain databases

InterProiIPR009378. Condensin_II_H2-like.
[Graphical view]
PfamiPF06278. DUF1032. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q6IBW4-1) [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
MEDVEARFAH LLQPIRDLTK NWEVDVAAQL GEYLEELDQI CISFDEGKTT
60 70 80 90 100
MNFIEAALLI QGSACVYSKK VEYLYSLVYQ ALDFISGKRR AKQLSSVQED
110 120 130 140 150
RANGVASSGV PQEAENEFLS LDDFPDSRTN VDLKNDQTPS EVLIIPLLPM
160 170 180 190 200
ALVAPDEMEK NNNPLYSRQG EVLASRKDFR MNTCVPHPRG AFMLEPEGMS
210 220 230 240 250
PMEPAGVSPM PGTQKDTGRT EEQPMEVSVC RSPVPALGFS QEPGPSPEGP
260 270 280 290 300
MPLGGGEDED AEEAVELPEA SAPKAALEPK ESRSPQQSAA LPRRYMLRER
310 320 330 340 350
EGAPEPASCV KETPDPWQSL DPFDSLESKP FKKGRPYSVP PCVEEALGQK
360 370 380 390 400
RKRKGAAKLQ DFHQWYLAAY ADHADSRRLR RKGPSFADME VLYWTHVKEQ
410 420 430 440 450
LETLRKLQRR EVAEQWLRPA EEDHLEDSLE DLGAADDFLE PEEYMEPEGA
460 470 480 490 500
DPREAADLDA VPMSLSYEEL VRRNVELFIA TSQKFVQETE LSQRIRDWED
510 520 530 540 550
TVQPLLQEQE QHVPFDIHTY GDQLVSRFPQ LNEWCPFAEL VAGQPAFEVC
560 570 580 590 600
RSMLASLQLA NDYTVEITQQ PGLEMAVDTM SLRLLTHQRA HKRFQTYAAP

SMAQP
Length:605
Mass (Da):68,227
Last modified:July 5, 2004 - v1
Checksum:i2C8A1070C27B4547
GO
Isoform 2 (identifier: Q6IBW4-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     167-188: Missing.

Note: Gene prediction based on EST data.

Show »
Length:583
Mass (Da):65,716
Checksum:i21B93C7E157E1E5C
GO
Isoform 3 (identifier: Q6IBW4-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     288-299: SAALPRRYMLRE → VGPTWRPAEPEL
     300-605: Missing.

Note: No experimental confirmation available.

Show »
Length:299
Mass (Da):32,819
Checksum:iC47577DA567D7AAA
GO
Isoform 4 (identifier: Q6IBW4-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     435-435: A → AA

Note: No experimental confirmation available.

Show »
Length:606
Mass (Da):68,298
Checksum:i9D6FAEBA6500B608
GO

Sequence cautioni

The sequence CAA16670.1 differs from that shown. Reason: Frameshift at positions 56 and 429.
The sequence AAH00473.1 differs from that shown. Reason: Erroneous initiation.
The sequence AAH01509.1 differs from that shown. Reason: Erroneous initiation.
The sequence AAH01833.1 differs from that shown. Reason: Erroneous initiation.
The sequence AAH01937.1 differs from that shown. Reason: Erroneous initiation.
The sequence AAH09441.1 differs from that shown. Reason: Erroneous initiation.
The sequence AAB03345.1 differs from that shown. Reason: Erroneous gene model prediction.
The sequence EAW73552.1 differs from that shown. Reason: Erroneous gene model prediction.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti36 – 361E → D in CAA16670. (PubMed:12529303)Curated
Sequence conflicti61 – 611Q → H in CAA16670. (PubMed:12529303)Curated
Sequence conflicti76 – 761S → W in CAA16670. (PubMed:12529303)Curated
Sequence conflicti161 – 1611N → I in CAA16670. (PubMed:12529303)Curated
Sequence conflicti190 – 1901G → R in CAA16670. (PubMed:12529303)Curated
Sequence conflicti215 – 2151K → N in CAA16670. (PubMed:12529303)Curated
Sequence conflicti249 – 2491G → R in CAA16670. (PubMed:12529303)Curated
Sequence conflicti282 – 2821S → F in AAH09441. (PubMed:15489334)Curated
Sequence conflicti316 – 3161P → L in CAA16670. (PubMed:12529303)Curated
Sequence conflicti323 – 3242FD → LN in CAA16670. (PubMed:12529303)Curated
Sequence conflicti368 – 3681A → V in CAA16670. (PubMed:12529303)Curated
Sequence conflicti474 – 4741N → K in CAA16670. (PubMed:12529303)Curated
Sequence conflicti486 – 4861V → I in CAA16670. (PubMed:12529303)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei167 – 18822Missing in isoform 2. CuratedVSP_032636Add
BLAST
Alternative sequencei288 – 29912SAALP…YMLRE → VGPTWRPAEPEL in isoform 3. 1 PublicationVSP_032637Add
BLAST
Alternative sequencei300 – 605306Missing in isoform 3. 1 PublicationVSP_032638Add
BLAST
Alternative sequencei435 – 4351A → AA in isoform 4. 1 PublicationVSP_032639

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AL021682 mRNA. Translation: CAA16670.1. Frameshift.
CR456604 mRNA. Translation: CAG30490.1.
U62317 Genomic DNA. Translation: AAB03345.1. Sequence problems.
CH471138 Genomic DNA. Translation: EAW73554.1.
CH471138 Genomic DNA. Translation: EAW73556.1.
CH471138 Genomic DNA. Translation: EAW73552.1. Sequence problems.
BC000473 mRNA. Translation: AAH00473.1. Different initiation.
BC001509 mRNA. Translation: AAH01509.1. Different initiation.
BC001833 mRNA. Translation: AAH01833.1. Different initiation.
BC001937 mRNA. Translation: AAH01937.1. Different initiation.
BC009441 mRNA. Translation: AAH09441.1. Different initiation.
BC014939 mRNA. Translation: AAH14939.2.
CCDSiCCDS14094.2. [Q6IBW4-1]
CCDS43038.1. [Q6IBW4-5]
CCDS54546.1. [Q6IBW4-4]
RefSeqiNP_001171940.1. NM_001185011.1. [Q6IBW4-4]
NP_055366.3. NM_014551.4. [Q6IBW4-5]
NP_689512.2. NM_152299.3. [Q6IBW4-1]
UniGeneiHs.730607.

Genome annotation databases

EnsembliENST00000299821; ENSP00000299821; ENSG00000025770. [Q6IBW4-4]
ENST00000395698; ENSP00000379050; ENSG00000025770. [Q6IBW4-5]
ENST00000420993; ENSP00000410088; ENSG00000025770. [Q6IBW4-1]
GeneIDi29781.
KEGGihsa:29781.
UCSCiuc003blq.4. human. [Q6IBW4-5]
uc003blr.4. human. [Q6IBW4-1]
uc003blx.4. human. [Q6IBW4-4]

Polymorphism databases

DMDMi74709496.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AL021682 mRNA. Translation: CAA16670.1 . Frameshift.
CR456604 mRNA. Translation: CAG30490.1 .
U62317 Genomic DNA. Translation: AAB03345.1 . Sequence problems.
CH471138 Genomic DNA. Translation: EAW73554.1 .
CH471138 Genomic DNA. Translation: EAW73556.1 .
CH471138 Genomic DNA. Translation: EAW73552.1 . Sequence problems.
BC000473 mRNA. Translation: AAH00473.1 . Different initiation.
BC001509 mRNA. Translation: AAH01509.1 . Different initiation.
BC001833 mRNA. Translation: AAH01833.1 . Different initiation.
BC001937 mRNA. Translation: AAH01937.1 . Different initiation.
BC009441 mRNA. Translation: AAH09441.1 . Different initiation.
BC014939 mRNA. Translation: AAH14939.2 .
CCDSi CCDS14094.2. [Q6IBW4-1 ]
CCDS43038.1. [Q6IBW4-5 ]
CCDS54546.1. [Q6IBW4-4 ]
RefSeqi NP_001171940.1. NM_001185011.1. [Q6IBW4-4 ]
NP_055366.3. NM_014551.4. [Q6IBW4-5 ]
NP_689512.2. NM_152299.3. [Q6IBW4-1 ]
UniGenei Hs.730607.

3D structure databases

ProteinModelPortali Q6IBW4.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 118913. 19 interactions.
DIPi DIP-43901N.
IntActi Q6IBW4. 10 interactions.
MINTi MINT-4329914.

PTM databases

PhosphoSitei Q6IBW4.

Polymorphism databases

DMDMi 74709496.

Proteomic databases

MaxQBi Q6IBW4.
PaxDbi Q6IBW4.
PRIDEi Q6IBW4.

Protocols and materials databases

DNASUi 29781.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000299821 ; ENSP00000299821 ; ENSG00000025770 . [Q6IBW4-4 ]
ENST00000395698 ; ENSP00000379050 ; ENSG00000025770 . [Q6IBW4-5 ]
ENST00000420993 ; ENSP00000410088 ; ENSG00000025770 . [Q6IBW4-1 ]
GeneIDi 29781.
KEGGi hsa:29781.
UCSCi uc003blq.4. human. [Q6IBW4-5 ]
uc003blr.4. human. [Q6IBW4-1 ]
uc003blx.4. human. [Q6IBW4-4 ]

Organism-specific databases

CTDi 29781.
GeneCardsi GC22P050946.
H-InvDB HIX0016615.
HGNCi HGNC:25071. NCAPH2.
MIMi 611230. gene.
neXtProti NX_Q6IBW4.
PharmGKBi PA162397314.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG238357.
GeneTreei ENSGT00390000014443.
HOVERGENi HBG098083.
InParanoidi Q6IBW4.
KOi K11490.
OMAi APEPASC.
OrthoDBi EOG7W41C5.
PhylomeDBi Q6IBW4.
TreeFami TF101164.

Enzyme and pathway databases

Reactomei REACT_172744. Condensation of Prophase Chromosomes.

Miscellaneous databases

GeneWikii NCAPH2.
GenomeRNAii 29781.
NextBioi 52312.
PROi Q6IBW4.
SOURCEi Search...

Gene expression databases

Bgeei Q6IBW4.
CleanExi HS_NCAPH2.
ExpressionAtlasi Q6IBW4. baseline and differential.
Genevestigatori Q6IBW4.

Family and domain databases

InterProi IPR009378. Condensin_II_H2-like.
[Graphical view ]
Pfami PF06278. DUF1032. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Reevaluating human gene annotation: a second-generation analysis of chromosome 22."
    Collins J.E., Goward M.E., Cole C.G., Smink L.J., Huckle E.J., Knowles S., Bye J.M., Beare D.M., Dunham I.
    Genome Res. 13:27-36(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Placenta.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  3. "The DNA sequence of human chromosome 22."
    Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
    , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
    Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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] (ISOFORMS 1; 3 AND 4).
    Tissue: Brain, Lung, Muscle and Skin.
  6. "Differential contributions of condensin I and condensin II to mitotic chromosome architecture in vertebrate cells."
    Ono T., Losada A., Hirano M., Myers M.P., Neuwald A.F., Hirano T.
    Cell 115:109-121(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN CONDENSIN-2 COMPLEX WITH SMC2; SMC4; NCAPG2; NCAPH2 AND NCAPD3, FUNCTION OF THE COMPLEX, SUBCELLULAR LOCATION.
  7. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-492, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  9. "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-284 AND SER-492, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-282 AND SER-492, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "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].
  12. "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-208, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  13. "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 THR-19; SER-95; SER-96; SER-200; SER-208; SER-284; SER-466 AND SER-492, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiCNDH2_HUMAN
AccessioniPrimary (citable) accession number: Q6IBW4
Secondary accession number(s): B7WPH1
, O43788, Q13391, Q96C14, Q96GJ0, Q9BQ71, Q9BUT3, Q9BVD1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: July 5, 2004
Last modified: October 29, 2014
This is version 88 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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 22
    Human chromosome 22: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3