Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q8BSP2 (CNDH2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Condensin-2 complex subunit H2
Alternative name(s):
Kleisin-beta
Non-SMC condensin II complex subunit H2
Gene names
Name:Ncaph2
Synonyms:D15Ertd785e
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length607 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 By similarity. Seems to have lineage-specific role in T-cell development By similarity.

Subunit structure

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 By similarity.

Subcellular location

Nucleus By similarity.

Involvement in disease

Defects in Ncaph2 are the cause of the nessy phenotype which is characterized by a specific defect in T-cell development. Nessy thymuses are smaller, with corticomedullary junctions less well defined, and cortical cells sparser than in wild-type. The thymocyte defect is typified by an increased proportion of CD4-CD8- DN T-cell progenitors. Only thymocyte differentiation is affected in Nessy mice and not cell differentiation.

Sequence similarities

Belongs to the CND2 H2 (condensin-2 subunit 2) family.

Sequence caution

The sequence AAH03900.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
   Biological processDNA condensation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   DiseaseDisease mutation
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processT cell differentiation in thymus

Inferred from mutant phenotype Ref.3. Source: MGI

chromosome condensation

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentnucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8BSP2-1)

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.
Isoform 2 (identifier: Q8BSP2-2)

The sequence of this isoform differs from the canonical sequence as follows:
     434-434: A → AA
Isoform 3 (identifier: Q8BSP2-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-36: MEDVEVRFAHLLQPIRDLTKNWEVDVAAQLGEYLEE → MWRCALLTSCSPSGISLRTGRWTWRHSW
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 607607Condensin-2 complex subunit H2
PRO_0000326242

Amino acid modifications

Modified residue191Phosphothreonine By similarity
Modified residue951Phosphoserine By similarity
Modified residue4941Phosphoserine Ref.4

Natural variations

Alternative sequence1 – 3636MEDVE…EYLEE → MWRCALLTSCSPSGISLRTG RWTWRHSW in isoform 3.
VSP_032641
Alternative sequence4341A → AA in isoform 2.
VSP_032642
Natural variant151I → N in Nessy. Ref.3

Experimental info

Sequence conflict831D → N in BAC39479. Ref.1
Sequence conflict2081V → M in BAC29736. Ref.1
Sequence conflict2181K → E in BAC37919. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 616CA03BDD647852

FASTA60768,945
        10         20         30         40         50         60 
MEDVEVRFAH LLQPIRDLTK NWEVDVAAQL GEYLEELDQI CISFDEGKTT MNFIEAALLI 

        70         80         90        100        110        120 
QGSACVYSKK VEYLYSLVYQ ALDFISGKRR AKQLSLVQED GSKKTVNSET PCETENEFLS 

       130        140        150        160        170        180 
LDDFPDSRAN VDLKNDQASS ELLIIPLLPM ALVAPDEVEK NSSPLYSCQG DILASRKDFR 

       190        200        210        220        230        240 
MNTCMPNPRG CFMLDPVGMC PVEPVVPVEP YPMSRSQKDP EDAEEQPMEV SRNGSPVPVP 

       250        260        270        280        290        300 
DISQEPDGPA LSGGEEDAED GAEPLEVALE PAEPRTSQQS AILPRRYMLR ERQGAPEPAS 

       310        320        330        340        350        360 
RLQETPDPWQ SLDPFDSLES KVFQKGKPYS VPPGVEEAPG QKRKRKGATK LQDFHKWYLD 

       370        380        390        400        410        420 
AYAEHPDGRR ARRKGPTFAD MEVLYWKHVK EQLETLQKLR RRKINERWLP GAKQDLWPTE 

       430        440        450        460        470        480 
EDRLEESLED LGVADDFLEP EEYVEEPAGV MPEEAADLDA EAMPESLRYE ELVRRNVELF 

       490        500        510        520        530        540 
IATSQKFIQE TELSQRIRDW EDTIQPLLQE QEQHVPFDIH IYGDQLASRF PQLNEWCPFS 

       550        560        570        580        590        600 
ELVAGQPAFE VCRSMLASLQ LANDYTVEIT QQPGLEAAVD TMSLRLLTHQ RAHTRFQTYA 


APSMAQP 

« Hide

Isoform 2 [UniParc].

Checksum: 58FD3EE7F8E59483
Show »

FASTA60869,017
Isoform 3 [UniParc].

Checksum: 4332A8427EDA9AB8
Show »

FASTA59968,024

References

« Hide 'large scale' references
[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
Strain: C57BL/6J and NOD.
Tissue: Cerebellum, Embryo, Kidney, Skin, Spleen and Thymus.
[2]"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] (ISOFORM 1).
Strain: FVB/N.
Tissue: Mammary tumor.
[3]"A mutation in a chromosome condensin II subunit, kleisin beta, specifically disrupts T cell development."
Gosling K.M., Makaroff L.E., Theodoratos A., Kim Y.-H., Whittle B., Rui L., Wu H., Hong N.A., Kennedy G.C., Fritz J.-A., Yates A.L., Goodnow C.C., Fahrer A.M.
Proc. Natl. Acad. Sci. U.S.A. 104:12445-12450(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE SPLICING, VARIANT NESSY ASN-15.
[4]"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-494, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK004160 mRNA. Translation: BAB23198.1.
AK031135 mRNA. Translation: BAC27270.1.
AK037175 mRNA. Translation: BAC29736.1.
AK080447 mRNA. Translation: BAC37919.1.
AK085584 mRNA. Translation: BAC39479.1.
AK088294 mRNA. Translation: BAC40265.1.
AK146642 mRNA. Translation: BAE27325.1.
AK152158 mRNA. Translation: BAE30993.1.
AK163958 mRNA. Translation: BAE37553.1.
AK165250 mRNA. Translation: BAE38104.1.
BC003900 mRNA. Translation: AAH03900.1. Different initiation.
CCDSCCDS49700.1. [Q8BSP2-1]
CCDS70661.1. [Q8BSP2-2]
RefSeqNP_001108604.1. NM_001115132.2. [Q8BSP2-1]
NP_001258530.1. NM_001271601.1. [Q8BSP2-2]
UniGeneMm.143167.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid206732. 1 interaction.

PTM databases

PhosphoSiteQ8BSP2.

Proteomic databases

MaxQBQ8BSP2.
PaxDbQ8BSP2.
PRIDEQ8BSP2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000074552; ENSMUSP00000074139; ENSMUSG00000008690. [Q8BSP2-1]
ENSMUST00000088717; ENSMUSP00000086095; ENSMUSG00000008690. [Q8BSP2-2]
GeneID52683.
KEGGmmu:52683.
UCSCuc007xgg.2. mouse. [Q8BSP2-2]
uc007xgh.2. mouse. [Q8BSP2-1]
uc007xgk.2. mouse. [Q8BSP2-3]

Organism-specific databases

CTD29781.
MGIMGI:1289164. Ncaph2.

Phylogenomic databases

eggNOGNOG238357.
GeneTreeENSGT00390000014443.
HOVERGENHBG098083.
KOK11490.
OMAPVFDIHD.
TreeFamTF101164.

Gene expression databases

BgeeQ8BSP2.
CleanExMM_NCAPH2.
GenevestigatorQ8BSP2.

Family and domain databases

InterProIPR009378. Condensin_II_H2-like.
[Graphical view]
PfamPF06278. DUF1032. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSNCAPH2. mouse.
NextBio309335.
PROQ8BSP2.
SOURCESearch...

Entry information

Entry nameCNDH2_MOUSE
AccessionPrimary (citable) accession number: Q8BSP2
Secondary accession number(s): Q3TNI4 expand/collapse secondary AC list , Q8C2N3, Q8C3K9, Q8C4X8, Q8CAZ3, Q99L21, Q9CT99
Entry history
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: March 1, 2003
Last modified: July 9, 2014
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot