CNDH2_RAT
ID CNDH2_RAT Reviewed; 554 AA.
AC Q4V8I2;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Condensin-2 complex subunit H2;
DE AltName: Full=Non-SMC condensin II complex subunit H2;
GN Name=Ncaph2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
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 [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178; SER-199 AND SER-200, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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; BC097379; AAH97379.1; -; mRNA.
DR RefSeq; NP_001020048.1; NM_001024877.1.
DR AlphaFoldDB; Q4V8I2; -.
DR SMR; Q4V8I2; -.
DR STRING; 10116.ENSRNOP00000052664; -.
DR iPTMnet; Q4V8I2; -.
DR PhosphoSitePlus; Q4V8I2; -.
DR PaxDb; Q4V8I2; -.
DR GeneID; 300149; -.
DR KEGG; rno:300149; -.
DR CTD; 29781; -.
DR RGD; 1565937; Ncaph2.
DR VEuPathDB; HostDB:ENSRNOG00000009598; -.
DR eggNOG; KOG2359; Eukaryota.
DR InParanoid; Q4V8I2; -.
DR OrthoDB; 522566at2759; -.
DR Reactome; R-RNO-2299718; Condensation of Prophase Chromosomes.
DR PRO; PR:Q4V8I2; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000009598; Expressed in thymus and 19 other tissues.
DR ExpressionAtlas; Q4V8I2; baseline and differential.
DR Genevisible; Q4V8I2; RN.
DR GO; GO:0005694; C:chromosome; ISO:RGD.
DR GO; GO:0000793; C:condensed chromosome; ISO:RGD.
DR GO; GO:0000794; C:condensed nuclear chromosome; ISO:RGD.
DR GO; GO:0000796; C:condensin complex; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0051309; P:female meiosis chromosome separation; ISO:RGD.
DR GO; GO:0007143; P:female meiotic nuclear division; ISO:RGD.
DR GO; GO:0010032; P:meiotic chromosome condensation; ISO:RGD.
DR GO; GO:0007076; P:mitotic chromosome condensation; ISS:UniProtKB.
DR GO; GO:0051306; P:mitotic sister chromatid separation; ISO:RGD.
DR GO; GO:0051984; P:positive regulation of chromosome segregation; ISO:RGD.
DR GO; GO:1905820; P:positive regulation of chromosome separation; ISO:RGD.
DR GO; GO:0033077; P:T cell differentiation in thymus; ISO:RGD.
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 DNA condensation; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..554
FT /note="Condensin-2 complex subunit H2"
FT /id="PRO_0000326243"
FT REGION 154..296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 159..173
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 178..195
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 199..213
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 45
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6IBW4"
FT MOD_RES 178
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 182
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BSP2"
FT MOD_RES 199
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 200
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 441
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6IBW4"
SQ SEQUENCE 554 AA; 62637 MW; A079AFB7B66F8A35 CRC64;
MNFIEAALLI QGSACVYSKK VEYLYSLVYQ ALDFISGKRR AKQLSLVQED GSNRAVNSGT
PCETEDEFLS LDDFPDSRAN VDLKNDQASS ELLIIPLLPM ALVAPDEVEK SSNPLYSCQG
EVLASRKDFR MNTCTPDPRG SFMLDPVGMC PVEPVDVHPM PRSQKDAEEA EEQPMAVSRN
GSPVSVRSIS QEPDGPALSS GDEDAEDVAE LPEVALEPAE PRTSQQTAIL PRRYMLRERQ
GAPEPASQPQ ETPDPWQSLD PFDSLDSKLF QKGKPYSVPP GVEEAPGQKR KRKGATKLQD
FHQWYLDAYA EHPDGRRARR KGPSFADMEV LYWKHVKEQL ETLQKLRRRK MTERWLPGAK
QDLWPAEEER LEEPLEDLGV ADDFLEAEEY VEESEGVMPR EAAGLDAEAI PESLKYEELV
RRNVELFIAT SQKFIQETEL SQRIRDWEDT IQPLLQEQEQ HVPFDIHTYG DQLVSRFPQL
NEWCPFAELV AGQPAFEVCR SMLASLQLAN DYTVEITQQP GLEAAVDTMS LRLLTHQRAH
MRFQTYAAPS MAQP
