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   27-MAR-2024, entry version 153.
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};
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; 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; 33.
DR   ComplexPortal; CPX-980; Condensin I complex.
DR   IntAct; Q8C156; 20.
DR   MINT; Q8C156; -.
DR   STRING; 10090.ENSMUSP00000106017; -.
DR   GlyGen; Q8C156; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q8C156; -.
DR   PhosphoSitePlus; Q8C156; -.
DR   EPD; Q8C156; -.
DR   jPOST; Q8C156; -.
DR   MaxQB; Q8C156; -.
DR   PaxDb; 10090-ENSMUSP00000106017; -.
DR   PeptideAtlas; Q8C156; -.
DR   ProteomicsDB; 283397; -.
DR   Pumba; Q8C156; -.
DR   Antibodypedia; 1231; 393 antibodies from 38 providers.
DR   DNASU; 215387; -.
DR   Ensembl; ENSMUST00000110387.4; ENSMUSP00000106017.4; ENSMUSG00000034906.16.
DR   GeneID; 215387; -.
DR   KEGG; mmu:215387; -.
DR   UCSC; uc008met.2; mouse.
DR   AGR; MGI:2444777; -.
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; DMDEAFW; -.
DR   OrthoDB; 153509at2759; -.
DR   PhylomeDB; Q8C156; -.
DR   TreeFam; TF105678; -.
DR   Reactome; R-MMU-2514853; Condensation of Prometaphase Chromosomes.
DR   BioGRID-ORCS; 215387; 19 hits in 83 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 185 other cell types or tissues.
DR   ExpressionAtlas; Q8C156; baseline and differential.
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; CONDENSIN COMPLEX SUBUNIT 2; 1.
DR   PANTHER; PTHR13108:SF9; CONDENSIN COMPLEX SUBUNIT 2; 1.
DR   Pfam; PF05786; Cnd2; 1.
DR   PIRSF; PIRSF017126; Condensin_H; 1.
DR   Genevisible; Q8C156; MM.
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
//