CND2_MOUSE
ID CND2_MOUSE Reviewed; 731 AA.
AC Q8C156; Q8BY01; Q8VDM9;
DT 23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Condensin complex subunit 2;
DE AltName: Full=Barren homolog protein 1;
DE AltName: Full=Chromosome-associated protein H;
DE Short=mCAP-H;
DE AltName: Full=Non-SMC condensin I complex subunit H;
DE AltName: Full=XCAP-H homolog;
GN Name=Ncaph; Synonyms=Brrn, Brrn1, Caph;
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].
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, and Skin;
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].
RC 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25; THR-43 AND THR-182, 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).
CC -!- FUNCTION: Regulatory subunit of the condensin complex, a complex
CC required for conversion of interphase chromatin into mitotic-like
CC condense chromosomes. The condensin complex probably introduces
CC positive supercoils into relaxed DNA in the presence of type I
CC topoisomerases and converts nicked DNA into positive knotted forms in
CC the presence of type II topoisomerases. Early in neurogenesis, may play
CC an essential role to ensure accurate mitotic chromosome condensation in
CC neuron stem cells, ultimately affecting neuron pool and cortex size.
CC {ECO:0000250|UniProtKB:Q15003}.
CC -!- SUBUNIT: Component of the condensin complex, which contains the SMC2
CC and SMC4 heterodimer, and three non SMC subunits that probably regulate
CC the complex: NCAPH/BRRN1, NCAPD2/CAPD2 and NCAPG. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC Chromosome {ECO:0000250}. Note=In interphase cells, the majority of the
CC condensin complex is found in the cytoplasm, while a minority of the
CC complex is associated with chromatin. A subpopulation of the complex
CC however remains associated with chromosome foci in interphase cells.
CC During mitosis, most of the condensin complex is associated with the
CC chromatin. At the onset of prophase, the regulatory subunits of the
CC complex are phosphorylated by CDK1, leading to condensin's association
CC with chromosome arms and to chromosome condensation. Dissociation from
CC chromosomes is observed in late telophase (By similarity).
CC {ECO:0000250}.
CC -!- PTM: Phosphorylated by CDK1. Its phosphorylation, as well as that of
CC NCAPD2 and NCAPG subunits, activates the condensin complex and is
CC required for chromosome condensation (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the CND2 (condensin subunit 2) family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH21499.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH25060.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC31339.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK028919; BAC26195.1; -; mRNA.
DR EMBL; AK042706; BAC31339.1; ALT_SEQ; mRNA.
DR EMBL; BC021499; AAH21499.1; ALT_INIT; mRNA.
DR EMBL; BC025060; AAH25060.1; ALT_INIT; mRNA.
DR CCDS; CCDS16693.2; -.
DR RefSeq; NP_659067.2; NM_144818.3.
DR AlphaFoldDB; Q8C156; -.
DR SMR; Q8C156; -.
DR BioGRID; 229619; 32.
DR ComplexPortal; CPX-980; Condensin I complex.
DR IntAct; Q8C156; 20.
DR MINT; Q8C156; -.
DR STRING; 10090.ENSMUSP00000106017; -.
DR iPTMnet; Q8C156; -.
DR PhosphoSitePlus; Q8C156; -.
DR EPD; Q8C156; -.
DR jPOST; Q8C156; -.
DR MaxQB; Q8C156; -.
DR PaxDb; Q8C156; -.
DR PeptideAtlas; Q8C156; -.
DR PRIDE; Q8C156; -.
DR ProteomicsDB; 283397; -.
DR Antibodypedia; 1231; 352 antibodies from 38 providers.
DR DNASU; 215387; -.
DR Ensembl; ENSMUST00000110387; ENSMUSP00000106017; ENSMUSG00000034906.
DR GeneID; 215387; -.
DR KEGG; mmu:215387; -.
DR UCSC; uc008met.2; mouse.
DR CTD; 23397; -.
DR MGI; MGI:2444777; Ncaph.
DR VEuPathDB; HostDB:ENSMUSG00000034906; -.
DR eggNOG; KOG2328; Eukaryota.
DR GeneTree; ENSGT00390000004149; -.
DR HOGENOM; CLU_010510_1_0_1; -.
DR InParanoid; Q8C156; -.
DR OMA; KPKAKMG; -.
DR OrthoDB; 702078at2759; -.
DR PhylomeDB; Q8C156; -.
DR TreeFam; TF105678; -.
DR Reactome; R-MMU-2514853; Condensation of Prometaphase Chromosomes.
DR BioGRID-ORCS; 215387; 19 hits in 79 CRISPR screens.
DR ChiTaRS; Ncaph; mouse.
DR PRO; PR:Q8C156; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q8C156; protein.
DR Bgee; ENSMUSG00000034906; Expressed in otic placode and 182 other tissues.
DR ExpressionAtlas; Q8C156; baseline and differential.
DR Genevisible; Q8C156; MM.
DR GO; GO:0005694; C:chromosome; IGI:MGI.
DR GO; GO:0000794; C:condensed nuclear chromosome; IDA:ComplexPortal.
DR GO; GO:0000796; C:condensin complex; IDA:MGI.
DR GO; GO:0005829; C:cytosol; 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; IDA:MGI.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0051309; P:female meiosis chromosome separation; IGI: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:0045132; P:meiotic chromosome segregation; IMP:MGI.
DR GO; GO:0007076; P:mitotic chromosome condensation; ISS:UniProtKB.
DR GO; GO:1905821; P:positive regulation of chromosome condensation; ISO:MGI.
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 InterPro; IPR022816; Condensin_barren_su2.
DR PANTHER; PTHR13108; PTHR13108; 1.
DR Pfam; PF05786; Cnd2; 1.
DR PIRSF; PIRSF017126; Condensin_H; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell cycle; Cell division; Chromosome; Cytoplasm;
KW DNA condensation; Isopeptide bond; Mitosis; Nucleus; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..731
FT /note="Condensin complex subunit 2"
FT /id="PRO_0000095039"
FT REGION 1..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 178..214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 652..673
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15003"
FT MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 43
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 46
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q15003"
FT MOD_RES 67
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15003"
FT MOD_RES 75
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15003"
FT MOD_RES 78
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15003"
FT MOD_RES 83
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15003"
FT MOD_RES 91
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15003"
FT MOD_RES 182
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 195
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15003"
FT MOD_RES 227
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15003"
FT MOD_RES 425
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15003"
FT MOD_RES 489
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15003"
FT MOD_RES 587
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q15003"
FT MOD_RES 627
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q15003"
FT CROSSLNK 481
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q15003"
SQ SEQUENCE 731 AA; 82303 MW; 23D2504024C2F0D5 CRC64;
MRIPRSETMN SSFLKARGQQ DVLSSPLERV PPASRPGKAP LGTPKTPVLE DFPQNDDEKE
RMQRRRSRVF DLQFSTDSIH LASPNRNIDV STTISKFTNT QITEHYSTCI KLSSENKITT
KNAFGLHLID FMSEILKQKD AEPTNFKVAA GTLDASTKIY AVRVDAVHAD VYRVLGGLGK
DTPPQGEESH SGDGSTLETE RTKKPAKPKK KQSCKTIEQN LSNINVSEAD GKCAVDPMFQ
KTAASFDECS TTGVFLSTLH CQDYRSELLF PSDMQTLSSG EPLELPDLGF VDMTDLEASL
QQCVEDRPLC PSLAGFQFTK WDSETHNESV SALVDKFKKN DQVFDINAEA EDDEEDVPDG
PLVEDFVDND EPDLSAAGDH EEFRSWKELC QVQSNQEEVI SLEDRDIQVM CSFLSMKPGE
YSYFSPRTMK MWAGPDHWRF RPRPKQDATS CTEHKKKSAK KDFEINFDDD IDFDAYFQKT
KAATILTKST LENQNWKATT LPTDFHYETD NLIQLHLKPG KRSLKMDQDQ KAKTEHYEEI
EDYDYNNPND TSNYCPGLQA ADSDYEEADD LFADPVGTLD LESDPKTTQE NGHISPENQG
VDITTYQELN LVAEPQKVNK IEIHYAKTAK KMDMKKLKQS MWSLLTKFSR KEADTEANHT
ESGQEGAPEE VADEKKLSGL TKDLQTRLPP LMAQNLSIPL AFACLLHLAN EKNLKLEGTE
DLSDVLVMQG D
