CNDH2_MOUSE
ID CNDH2_MOUSE Reviewed; 607 AA.
AC Q8BSP2; Q3TNI4; Q8C2N3; Q8C3K9; Q8C4X8; Q8CAZ3; Q99L21; Q9CT99;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Condensin-2 complex subunit H2;
DE AltName: Full=Kleisin-beta;
DE AltName: Full=Non-SMC condensin II complex subunit H2;
GN Name=Ncaph2 {ECO:0000303|PubMed:27737959, ECO:0000312|MGI:MGI:1289164};
GN Synonyms=D15Ertd785e;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC STRAIN=C57BL/6J, and NOD;
RC TISSUE=Cerebellum, Embryo, Kidney, Skin, Spleen, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP ALTERNATIVE SPLICING, AND VARIANT NESSY ASN-15.
RX PubMed=17640884; DOI=10.1073/pnas.0704870104;
RA Gosling K.M., Makaroff L.E., Theodoratos A., Kim Y.-H., Whittle B., Rui L.,
RA Wu H., Hong N.A., Kennedy G.C., Fritz J.-A., Yates A.L., Goodnow C.C.,
RA Fahrer A.M.;
RT "A mutation in a chromosome condensin II subunit, kleisin beta,
RT specifically disrupts T cell development.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:12445-12450(2007).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-494, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-235 AND SER-252, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP FUNCTION.
RX PubMed=27737959; DOI=10.1101/gad.286351.116;
RG Deciphering Developmental Disorders Study;
RA Martin C.A., Murray J.E., Carroll P., Leitch A., Mackenzie K.J.,
RA Halachev M., Fetit A.E., Keith C., Bicknell L.S., Fluteau A., Gautier P.,
RA Hall E.A., Joss S., Soares G., Silva J., Bober M.B., Duker A., Wise C.A.,
RA Quigley A.J., Phadke S.R., Wood A.J., Vagnarelli P., Jackson A.P.;
RT "Mutations in genes encoding condensin complex proteins cause microcephaly
RT through decatenation failure at mitosis.";
RL Genes Dev. 30:2158-2172(2016).
CC -!- FUNCTION: Regulatory subunit of the condensin-2 complex, a complex that
CC seems to provide chromosomes with an additional level of organization
CC and rigidity and in establishing mitotic chromosome architecture (By
CC similarity). May promote the resolution of double-strand DNA catenanes
CC (intertwines) between sister chromatids. Condensin-mediated compaction
CC likely increases tension in catenated sister chromatids, providing
CC directionality for type II topoisomerase-mediated strand exchanges
CC toward chromatid decatenation. Required for decatenation of chromatin
CC bridges at anaphase. Early in neurogenesis, may play an essential role
CC to ensure accurate mitotic chromosome condensation in neuron stem
CC cells, ultimately affecting neuron pool and cortex size
CC (PubMed:27737959). Seems to have lineage-specific role in T-cell
CC development (By similarity). {ECO:0000250|UniProtKB:Q6IBW4,
CC ECO:0000269|PubMed:27737959}.
CC -!- SUBUNIT: Component of the condensin-2 complex, which contains the SMC2
CC and SMC4 heterodimer, and three non SMC subunits, NCAPG2, NCAPH2 and
CC NCAPD3 that probably regulate the complex. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8BSP2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BSP2-2; Sequence=VSP_032642;
CC Name=3;
CC IsoId=Q8BSP2-3; Sequence=VSP_032641;
CC -!- DISEASE: Note=Defects in Ncaph2 are the cause of the nessy phenotype
CC which is characterized by a specific defect in T-cell development.
CC Nessy thymuses are smaller, with corticomedullary junctions less well
CC defined, and cortical cells sparser than in wild-type. The thymocyte
CC defect is typified by an increased proportion of CD4-CD8- DN T-cell
CC progenitors. Only thymocyte differentiation is affected in Nessy mice
CC and not cell differentiation.
CC -!- SIMILARITY: Belongs to the CND2 H2 (condensin-2 subunit 2) family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH03900.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK004160; BAB23198.1; -; mRNA.
DR EMBL; AK031135; BAC27270.1; -; mRNA.
DR EMBL; AK037175; BAC29736.1; -; mRNA.
DR EMBL; AK080447; BAC37919.1; -; mRNA.
DR EMBL; AK085584; BAC39479.1; -; mRNA.
DR EMBL; AK088294; BAC40265.1; -; mRNA.
DR EMBL; AK146642; BAE27325.1; -; mRNA.
DR EMBL; AK152158; BAE30993.1; -; mRNA.
DR EMBL; AK163958; BAE37553.1; -; mRNA.
DR EMBL; AK165250; BAE38104.1; -; mRNA.
DR EMBL; BC003900; AAH03900.1; ALT_INIT; mRNA.
DR CCDS; CCDS49700.1; -. [Q8BSP2-1]
DR CCDS; CCDS70661.1; -. [Q8BSP2-2]
DR RefSeq; NP_001108604.1; NM_001115132.2. [Q8BSP2-1]
DR RefSeq; NP_001258530.1; NM_001271601.1. [Q8BSP2-2]
DR AlphaFoldDB; Q8BSP2; -.
DR BioGRID; 206732; 1.
DR ComplexPortal; CPX-986; Condensin II complex.
DR IntAct; Q8BSP2; 1.
DR STRING; 10090.ENSMUSP00000074139; -.
DR iPTMnet; Q8BSP2; -.
DR PhosphoSitePlus; Q8BSP2; -.
DR EPD; Q8BSP2; -.
DR MaxQB; Q8BSP2; -.
DR PaxDb; Q8BSP2; -.
DR PeptideAtlas; Q8BSP2; -.
DR PRIDE; Q8BSP2; -.
DR ProteomicsDB; 283539; -. [Q8BSP2-1]
DR ProteomicsDB; 283540; -. [Q8BSP2-2]
DR ProteomicsDB; 283541; -. [Q8BSP2-3]
DR Antibodypedia; 28671; 132 antibodies from 22 providers.
DR DNASU; 52683; -.
DR Ensembl; ENSMUST00000074552; ENSMUSP00000074139; ENSMUSG00000008690. [Q8BSP2-1]
DR Ensembl; ENSMUST00000088717; ENSMUSP00000086095; ENSMUSG00000008690. [Q8BSP2-2]
DR GeneID; 52683; -.
DR KEGG; mmu:52683; -.
DR UCSC; uc007xgg.3; mouse. [Q8BSP2-2]
DR UCSC; uc007xgh.3; mouse. [Q8BSP2-1]
DR UCSC; uc007xgk.3; mouse. [Q8BSP2-3]
DR CTD; 29781; -.
DR MGI; MGI:1289164; Ncaph2.
DR VEuPathDB; HostDB:ENSMUSG00000008690; -.
DR eggNOG; KOG2359; Eukaryota.
DR GeneTree; ENSGT00390000014443; -.
DR HOGENOM; CLU_010569_0_0_1; -.
DR InParanoid; Q8BSP2; -.
DR OMA; PPEHKLK; -.
DR OrthoDB; 522566at2759; -.
DR TreeFam; TF101164; -.
DR Reactome; R-MMU-2299718; Condensation of Prophase Chromosomes.
DR BioGRID-ORCS; 52683; 20 hits in 73 CRISPR screens.
DR ChiTaRS; Ncaph2; mouse.
DR PRO; PR:Q8BSP2; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q8BSP2; protein.
DR Bgee; ENSMUSG00000008690; Expressed in spermatocyte and 217 other tissues.
DR ExpressionAtlas; Q8BSP2; baseline and differential.
DR Genevisible; Q8BSP2; MM.
DR GO; GO:0030054; C:cell junction; ISO:MGI.
DR GO; GO:0005694; C:chromosome; IDA:MGI.
DR GO; GO:0000793; C:condensed chromosome; IDA:MGI.
DR GO; GO:0000794; C:condensed nuclear chromosome; IDA:ComplexPortal.
DR GO; GO:0000796; C:condensin complex; IDA:MGI.
DR GO; GO:0045171; C:intercellular bridge; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0051309; P:female meiosis chromosome separation; IMP:MGI.
DR GO; GO:0007143; P:female meiotic nuclear division; IMP:MGI.
DR GO; GO:0010032; P:meiotic chromosome condensation; IMP:MGI.
DR GO; GO:0007076; P:mitotic chromosome condensation; IMP:UniProtKB.
DR GO; GO:0051306; P:mitotic sister chromatid separation; IMP:MGI.
DR GO; GO:1905821; P:positive regulation of chromosome condensation; IC:ComplexPortal.
DR GO; GO:0051984; P:positive regulation of chromosome segregation; IMP:ComplexPortal.
DR GO; GO:1905820; P:positive regulation of chromosome separation; IMP:ComplexPortal.
DR GO; GO:0033077; P:T cell differentiation in thymus; IMP:MGI.
DR InterPro; IPR031737; CNDH2_C.
DR InterPro; IPR031719; H2_M.
DR InterPro; IPR009378; H2_N.
DR InterPro; IPR031739; Ncaph2.
DR PANTHER; PTHR14324; PTHR14324; 1.
DR Pfam; PF16858; CNDH2_C; 1.
DR Pfam; PF16869; CNDH2_M; 1.
DR Pfam; PF06278; CNDH2_N; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Disease variant; DNA condensation; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..607
FT /note="Condensin-2 complex subunit H2"
FT /id="PRO_0000326242"
FT REGION 211..312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 325..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 252..266
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 19
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6IBW4"
FT MOD_RES 95
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6IBW4"
FT MOD_RES 231
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q4V8I2"
FT MOD_RES 235
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 252
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 494
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17525332"
FT VAR_SEQ 1..36
FT /note="MEDVEVRFAHLLQPIRDLTKNWEVDVAAQLGEYLEE -> MWRCALLTSCSP
FT SGISLRTGRWTWRHSW (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_032641"
FT VAR_SEQ 434
FT /note="A -> AA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_032642"
FT VARIANT 15
FT /note="I -> N (in Nessy)"
FT /evidence="ECO:0000269|PubMed:17640884"
FT CONFLICT 83
FT /note="D -> N (in Ref. 1; BAC39479)"
FT /evidence="ECO:0000305"
FT CONFLICT 208
FT /note="V -> M (in Ref. 1; BAC29736)"
FT /evidence="ECO:0000305"
FT CONFLICT 218
FT /note="K -> E (in Ref. 1; BAC37919)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 607 AA; 68945 MW; 616CA03BDD647852 CRC64;
MEDVEVRFAH LLQPIRDLTK NWEVDVAAQL GEYLEELDQI CISFDEGKTT MNFIEAALLI
QGSACVYSKK VEYLYSLVYQ ALDFISGKRR AKQLSLVQED GSKKTVNSET PCETENEFLS
LDDFPDSRAN VDLKNDQASS ELLIIPLLPM ALVAPDEVEK NSSPLYSCQG DILASRKDFR
MNTCMPNPRG CFMLDPVGMC PVEPVVPVEP YPMSRSQKDP EDAEEQPMEV SRNGSPVPVP
DISQEPDGPA LSGGEEDAED GAEPLEVALE PAEPRTSQQS AILPRRYMLR ERQGAPEPAS
RLQETPDPWQ SLDPFDSLES KVFQKGKPYS VPPGVEEAPG QKRKRKGATK LQDFHKWYLD
AYAEHPDGRR ARRKGPTFAD MEVLYWKHVK EQLETLQKLR RRKINERWLP GAKQDLWPTE
EDRLEESLED LGVADDFLEP EEYVEEPAGV MPEEAADLDA EAMPESLRYE ELVRRNVELF
IATSQKFIQE TELSQRIRDW EDTIQPLLQE QEQHVPFDIH IYGDQLASRF PQLNEWCPFS
ELVAGQPAFE VCRSMLASLQ LANDYTVEIT QQPGLEAAVD TMSLRLLTHQ RAHTRFQTYA
APSMAQP
