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Q8BSP2

- CNDH2_MOUSE

UniProt

Q8BSP2 - CNDH2_MOUSE

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Protein

Condensin-2 complex subunit H2

Gene

Ncaph2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 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. Seems to have lineage-specific role in T-cell development.By similarity

GO - Biological processi

  1. chromosome condensation Source: UniProtKB-KW
  2. T cell differentiation in thymus Source: MGI
Complete GO annotation...

Keywords - Biological processi

DNA condensation

Enzyme and pathway databases

ReactomeiREACT_196580. Condensation of Prophase Chromosomes.

Names & Taxonomyi

Protein namesi
Recommended name:
Condensin-2 complex subunit H2
Alternative name(s):
Kleisin-beta
Non-SMC condensin II complex subunit H2
Gene namesi
Name:Ncaph2
Synonyms:D15Ertd785e
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 15

Organism-specific databases

MGIiMGI:1289164. Ncaph2.

Subcellular locationi

Nucleus By similarity

GO - Cellular componenti

  1. nucleus Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

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.

Keywords - Diseasei

Disease mutation

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 607607Condensin-2 complex subunit H2PRO_0000326242Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei19 – 191PhosphothreonineBy similarity
Modified residuei95 – 951PhosphoserineBy similarity
Modified residuei494 – 4941Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ8BSP2.
PaxDbiQ8BSP2.
PRIDEiQ8BSP2.

PTM databases

PhosphoSiteiQ8BSP2.

Expressioni

Gene expression databases

BgeeiQ8BSP2.
CleanExiMM_NCAPH2.
ExpressionAtlasiQ8BSP2. baseline and differential.
GenevestigatoriQ8BSP2.

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.By similarity

Protein-protein interaction databases

BioGridi206732. 1 interaction.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG238357.
GeneTreeiENSGT00390000014443.
HOVERGENiHBG098083.
InParanoidiQ8BSP2.
KOiK11490.
OMAiPVFDIHD.
TreeFamiTF101164.

Family and domain databases

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

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q8BSP2-1) [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
MEDVEVRFAH LLQPIRDLTK NWEVDVAAQL GEYLEELDQI CISFDEGKTT
60 70 80 90 100
MNFIEAALLI QGSACVYSKK VEYLYSLVYQ ALDFISGKRR AKQLSLVQED
110 120 130 140 150
GSKKTVNSET PCETENEFLS LDDFPDSRAN VDLKNDQASS ELLIIPLLPM
160 170 180 190 200
ALVAPDEVEK NSSPLYSCQG DILASRKDFR MNTCMPNPRG CFMLDPVGMC
210 220 230 240 250
PVEPVVPVEP YPMSRSQKDP EDAEEQPMEV SRNGSPVPVP DISQEPDGPA
260 270 280 290 300
LSGGEEDAED GAEPLEVALE PAEPRTSQQS AILPRRYMLR ERQGAPEPAS
310 320 330 340 350
RLQETPDPWQ SLDPFDSLES KVFQKGKPYS VPPGVEEAPG QKRKRKGATK
360 370 380 390 400
LQDFHKWYLD AYAEHPDGRR ARRKGPTFAD MEVLYWKHVK EQLETLQKLR
410 420 430 440 450
RRKINERWLP GAKQDLWPTE EDRLEESLED LGVADDFLEP EEYVEEPAGV
460 470 480 490 500
MPEEAADLDA EAMPESLRYE ELVRRNVELF IATSQKFIQE TELSQRIRDW
510 520 530 540 550
EDTIQPLLQE QEQHVPFDIH IYGDQLASRF PQLNEWCPFS ELVAGQPAFE
560 570 580 590 600
VCRSMLASLQ LANDYTVEIT QQPGLEAAVD TMSLRLLTHQ RAHTRFQTYA

APSMAQP
Length:607
Mass (Da):68,945
Last modified:March 1, 2003 - v1
Checksum:i616CA03BDD647852
GO
Isoform 2 (identifier: Q8BSP2-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     434-434: A → AA

Show »
Length:608
Mass (Da):69,017
Checksum:i58FD3EE7F8E59483
GO
Isoform 3 (identifier: Q8BSP2-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-36: MEDVEVRFAHLLQPIRDLTKNWEVDVAAQLGEYLEE → MWRCALLTSCSPSGISLRTGRWTWRHSW

Note: No experimental confirmation available.

Show »
Length:599
Mass (Da):68,024
Checksum:i4332A8427EDA9AB8
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti83 – 831D → N in BAC39479. (PubMed:16141072)Curated
Sequence conflicti208 – 2081V → M in BAC29736. (PubMed:16141072)Curated
Sequence conflicti218 – 2181K → E in BAC37919. (PubMed:16141072)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti15 – 151I → N in Nessy. 1 Publication

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 3636MEDVE…EYLEE → MWRCALLTSCSPSGISLRTG RWTWRHSW in isoform 3. 1 PublicationVSP_032641Add
BLAST
Alternative sequencei434 – 4341A → AA in isoform 2. 1 PublicationVSP_032642

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS49700.1. [Q8BSP2-1]
CCDS70661.1. [Q8BSP2-2]
RefSeqiNP_001108604.1. NM_001115132.2. [Q8BSP2-1]
NP_001258530.1. NM_001271601.1. [Q8BSP2-2]
UniGeneiMm.143167.

Genome annotation databases

EnsembliENSMUST00000074552; ENSMUSP00000074139; ENSMUSG00000008690. [Q8BSP2-1]
ENSMUST00000088717; ENSMUSP00000086095; ENSMUSG00000008690. [Q8BSP2-2]
GeneIDi52683.
KEGGimmu:52683.
UCSCiuc007xgg.2. mouse. [Q8BSP2-2]
uc007xgh.2. mouse. [Q8BSP2-1]
uc007xgk.2. mouse. [Q8BSP2-3]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSi CCDS49700.1. [Q8BSP2-1 ]
CCDS70661.1. [Q8BSP2-2 ]
RefSeqi NP_001108604.1. NM_001115132.2. [Q8BSP2-1 ]
NP_001258530.1. NM_001271601.1. [Q8BSP2-2 ]
UniGenei Mm.143167.

3D structure databases

ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 206732. 1 interaction.

PTM databases

PhosphoSitei Q8BSP2.

Proteomic databases

MaxQBi Q8BSP2.
PaxDbi Q8BSP2.
PRIDEi Q8BSP2.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000074552 ; ENSMUSP00000074139 ; ENSMUSG00000008690 . [Q8BSP2-1 ]
ENSMUST00000088717 ; ENSMUSP00000086095 ; ENSMUSG00000008690 . [Q8BSP2-2 ]
GeneIDi 52683.
KEGGi mmu:52683.
UCSCi uc007xgg.2. mouse. [Q8BSP2-2 ]
uc007xgh.2. mouse. [Q8BSP2-1 ]
uc007xgk.2. mouse. [Q8BSP2-3 ]

Organism-specific databases

CTDi 29781.
MGIi MGI:1289164. Ncaph2.

Phylogenomic databases

eggNOGi NOG238357.
GeneTreei ENSGT00390000014443.
HOVERGENi HBG098083.
InParanoidi Q8BSP2.
KOi K11490.
OMAi PVFDIHD.
TreeFami TF101164.

Enzyme and pathway databases

Reactomei REACT_196580. Condensation of Prophase Chromosomes.

Miscellaneous databases

NextBioi 309335.
PROi Q8BSP2.
SOURCEi Search...

Gene expression databases

Bgeei Q8BSP2.
CleanExi MM_NCAPH2.
ExpressionAtlasi Q8BSP2. baseline and differential.
Genevestigatori Q8BSP2.

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. "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.
    , 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. Cited for: ALTERNATIVE SPLICING, VARIANT NESSY ASN-15.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-494, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiCNDH2_MOUSE
AccessioniPrimary (citable) accession number: Q8BSP2
Secondary accession number(s): Q3TNI4
, Q8C2N3, Q8C3K9, Q8C4X8, Q8CAZ3, Q99L21, Q9CT99
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: March 1, 2003
Last modified: November 26, 2014
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3