CNDH2_BOVIN
ID CNDH2_BOVIN Reviewed; 622 AA.
AC Q3SZL8;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Condensin-2 complex subunit H2;
DE AltName: Full=Non-SMC condensin II complex subunit H2;
GN Name=NCAPH2;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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 (By
CC similarity). Seems to have lineage-specific role in T-cell development
CC (By similarity). {ECO:0000250|UniProtKB:Q6IBW4,
CC ECO:0000250|UniProtKB:Q8BSP2}.
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 -!- SIMILARITY: Belongs to the CND2 H2 (condensin-2 subunit 2) family.
CC {ECO:0000305}.
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DR EMBL; BC102795; AAI02796.1; -; mRNA.
DR RefSeq; NP_001070511.1; NM_001077043.1.
DR AlphaFoldDB; Q3SZL8; -.
DR STRING; 9913.ENSBTAP00000016741; -.
DR iPTMnet; Q3SZL8; -.
DR PaxDb; Q3SZL8; -.
DR PRIDE; Q3SZL8; -.
DR Ensembl; ENSBTAT00000016741; ENSBTAP00000016741; ENSBTAG00000012607.
DR GeneID; 767978; -.
DR KEGG; bta:767978; -.
DR CTD; 29781; -.
DR VEuPathDB; HostDB:ENSBTAG00000012607; -.
DR VGNC; VGNC:31906; NCAPH2.
DR eggNOG; KOG2359; Eukaryota.
DR GeneTree; ENSGT00390000014443; -.
DR InParanoid; Q3SZL8; -.
DR OMA; PPEHKLK; -.
DR OrthoDB; 522566at2759; -.
DR Proteomes; UP000009136; Chromosome 5.
DR Bgee; ENSBTAG00000012607; Expressed in retina and 109 other tissues.
DR ExpressionAtlas; Q3SZL8; differential.
DR GO; GO:0030054; C:cell junction; IEA:Ensembl.
DR GO; GO:0000794; C:condensed nuclear chromosome; IEA:Ensembl.
DR GO; GO:0000796; C:condensin complex; IBA:GO_Central.
DR GO; GO:0045171; C:intercellular bridge; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0051309; P:female meiosis chromosome separation; IEA:Ensembl.
DR GO; GO:0010032; P:meiotic chromosome condensation; IBA:GO_Central.
DR GO; GO:0007076; P:mitotic chromosome condensation; ISS:UniProtKB.
DR GO; GO:0051306; P:mitotic sister chromatid separation; IBA:GO_Central.
DR GO; GO:0051984; P:positive regulation of chromosome segregation; IEA:Ensembl.
DR GO; GO:1905820; P:positive regulation of chromosome separation; IEA:Ensembl.
DR GO; GO:0033077; P:T cell differentiation in thymus; IEA:Ensembl.
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 2: Evidence at transcript level;
KW DNA condensation; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..622
FT /note="Condensin-2 complex subunit H2"
FT /id="PRO_0000326240"
FT REGION 207..354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 270..284
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 291..307
FT /note="Basic and 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 199
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6IBW4"
FT MOD_RES 223
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q4V8I2"
FT MOD_RES 227
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BSP2"
FT MOD_RES 282
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6IBW4"
SQ SEQUENCE 622 AA; 69775 MW; E862AA2DC52C2518 CRC64;
MEDVEARFAH LLLPIRDLTR NWEVDVAAQL GEYLEELDQI CISFDKGKTT MNFIEAALLI
QGSACVYSKK VEYLYSLVYQ ALDFISGKKQ AKQLSSTPED GTIGDASSRA PQEAEQKFRA
LDDLSDSCAN VDLRDDQVVS GTLIPLLPNA LVAPDEMEKN SNPLYSCQGE VLASRKDFRV
NTCTPHPRGT FLLEPLGVSL MEALQPWNPK EPGRAEEQPM EVSVCGSPGP ALSTSQEPGS
SPEGPVPRGG GVGEDEEDAE GAAEPPEASA PEVPMEPPEP RSPEQSVAQP RRYTLRERKE
APEPASRLKD TPDPWQGLDP FDSPDSKPFR KGRPYSVPPR VEEAPGQKRK RKGAVKLQDF
HQWYLAAYAD HTDSRRSRRK GPSFADMEVL YWKHVKEQLE TLRKMQRREA AERWLPRAEQ
GLWPVEEDRL EDSVEDLGAA DDFLEPEEYA EPEGAEPGED ADMEAEAMPA SLRYEELVQR
NVELFVTASK QDVFVTTSRQ ELVQETELKQ HIRGWEDAIQ SLLQEQEEHV PFDIHTYGDQ
VVSRFSQLNQ WCPFAKLVAG QPAFEVCRSM LASLQLANDY TVEITQQPGL EAAVDTMSLR
LLTHQRARQR FQTYAAPSTV QP
