CNDH2_HUMAN
ID CNDH2_HUMAN Reviewed; 605 AA.
AC Q6IBW4; B7WPH1; O43788; Q13391; Q96C14; Q96GJ0; Q9BQ71; Q9BUT3; Q9BVD1;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Condensin-2 complex subunit H2;
DE AltName: Full=Chromosome-associated protein H2;
DE Short=hCAP-H2;
DE AltName: Full=Kleisin-beta;
DE AltName: Full=Non-SMC condensin II complex subunit H2;
GN Name=NCAPH2; Synonyms=CAPH2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
RX PubMed=12529303; DOI=10.1101/gr.695703;
RA Collins J.E., Goward M.E., Cole C.G., Smink L.J., Huckle E.J., Knowles S.,
RA Bye J.M., Beare D.M., Dunham I.;
RT "Reevaluating human gene annotation: a second-generation analysis of
RT chromosome 22.";
RL Genome Res. 13:27-36(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4).
RC TISSUE=Brain, Lung, Muscle, and Skin;
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 [6]
RP IDENTIFICATION IN CONDENSIN-2 COMPLEX WITH SMC2; SMC4; NCAPG2; NCAPH2 AND
RP NCAPD3, FUNCTION OF THE COMPLEX, AND SUBCELLULAR LOCATION.
RX PubMed=14532007; DOI=10.1016/s0092-8674(03)00724-4;
RA Ono T., Losada A., Hirano M., Myers M.P., Neuwald A.F., Hirano T.;
RT "Differential contributions of condensin I and condensin II to mitotic
RT chromosome architecture in vertebrate cells.";
RL Cell 115:109-121(2003).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-492, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-284 AND SER-492, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-282 AND SER-492, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-208, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-19; SER-95; SER-200; SER-208;
RP SER-284; SER-466 AND SER-492, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-284 AND SER-492, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
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
CC (PubMed:14532007). May promote the resolution of double-strand DNA
CC catenanes (intertwines) between sister chromatids. Condensin-mediated
CC compaction likely increases tension in catenated sister chromatids,
CC providing directionality for type II topoisomerase-mediated strand
CC exchanges toward chromatid decatenation. Required for decatenation of
CC chromatin bridges at anaphase. Early in neurogenesis, may play an
CC essential role to ensure accurate mitotic chromosome condensation in
CC neuron stem cells, ultimately affecting neuron pool and cortex size (By
CC similarity). Seems to have lineage-specific role in T-cell development
CC (PubMed:14532007). {ECO:0000250|UniProtKB:Q8BSP2,
CC ECO:0000269|PubMed:14532007}.
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.
CC {ECO:0000269|PubMed:14532007}.
CC -!- INTERACTION:
CC Q6IBW4; P42695: NCAPD3; NbExp=3; IntAct=EBI-2548296, EBI-722805;
CC Q6IBW4; Q86XI2: NCAPG2; NbExp=2; IntAct=EBI-2548296, EBI-1047404;
CC Q6IBW4; Q8WWY3: PRPF31; NbExp=3; IntAct=EBI-2548296, EBI-1567797;
CC Q6IBW4; O95347: SMC2; NbExp=2; IntAct=EBI-2548296, EBI-355822;
CC Q6IBW4; Q9NTJ3: SMC4; NbExp=2; IntAct=EBI-2548296, EBI-356173;
CC Q6IBW4-4; Q86W74-2: ANKRD46; NbExp=3; IntAct=EBI-10247000, EBI-12109402;
CC Q6IBW4-4; P05090: APOD; NbExp=3; IntAct=EBI-10247000, EBI-715495;
CC Q6IBW4-4; Q8WVX3-2: C4orf3; NbExp=3; IntAct=EBI-10247000, EBI-12003442;
CC Q6IBW4-4; Q4LDR2: CTXN3; NbExp=3; IntAct=EBI-10247000, EBI-12019274;
CC Q6IBW4-4; Q9H6Z9: EGLN3; NbExp=3; IntAct=EBI-10247000, EBI-1175354;
CC Q6IBW4-4; P50402: EMD; NbExp=3; IntAct=EBI-10247000, EBI-489887;
CC Q6IBW4-4; P37268: FDFT1; NbExp=3; IntAct=EBI-10247000, EBI-714550;
CC Q6IBW4-4; P24593: IGFBP5; NbExp=3; IntAct=EBI-10247000, EBI-720480;
CC Q6IBW4-4; P21145: MAL; NbExp=3; IntAct=EBI-10247000, EBI-3932027;
CC Q6IBW4-4; Q5TAL4: SNRPC; NbExp=3; IntAct=EBI-10247000, EBI-10246938;
CC Q6IBW4-4; A0PK00: TMEM120B; NbExp=3; IntAct=EBI-10247000, EBI-10171534;
CC Q6IBW4-4; Q9P0S9: TMEM14C; NbExp=3; IntAct=EBI-10247000, EBI-2339195;
CC Q6IBW4-4; Q8N2M4: TMEM86A; NbExp=3; IntAct=EBI-10247000, EBI-12015604;
CC Q6IBW4-4; Q9Y5Z9: UBIAD1; NbExp=3; IntAct=EBI-10247000, EBI-2819725;
CC Q6IBW4-4; Q8N6Y0: USHBP1; NbExp=3; IntAct=EBI-10247000, EBI-739895;
CC Q6IBW4-4; O95183: VAMP5; NbExp=3; IntAct=EBI-10247000, EBI-10191195;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14532007}. Chromosome
CC {ECO:0000269|PubMed:14532007}. Note=Distributed along the arms of
CC chromosomes assembled in vivo and in vitro.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q6IBW4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6IBW4-2; Sequence=VSP_032636;
CC Name=3;
CC IsoId=Q6IBW4-5; Sequence=VSP_032637, VSP_032638;
CC Name=4;
CC IsoId=Q6IBW4-4; Sequence=VSP_032639;
CC -!- SIMILARITY: Belongs to the CND2 H2 (condensin-2 subunit 2) family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB03345.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAH00473.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH01509.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH01833.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH01937.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH09441.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA16670.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=EAW73552.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL021682; CAA16670.1; ALT_FRAME; mRNA.
DR EMBL; CR456604; CAG30490.1; -; mRNA.
DR EMBL; U62317; AAB03345.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CH471138; EAW73554.1; -; Genomic_DNA.
DR EMBL; CH471138; EAW73556.1; -; Genomic_DNA.
DR EMBL; CH471138; EAW73552.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC000473; AAH00473.1; ALT_INIT; mRNA.
DR EMBL; BC001509; AAH01509.1; ALT_INIT; mRNA.
DR EMBL; BC001833; AAH01833.1; ALT_INIT; mRNA.
DR EMBL; BC001937; AAH01937.1; ALT_INIT; mRNA.
DR EMBL; BC009441; AAH09441.1; ALT_INIT; mRNA.
DR EMBL; BC014939; AAH14939.2; -; mRNA.
DR CCDS; CCDS14094.2; -. [Q6IBW4-1]
DR CCDS; CCDS43038.1; -. [Q6IBW4-5]
DR CCDS; CCDS54546.1; -. [Q6IBW4-4]
DR RefSeq; NP_001171940.1; NM_001185011.1. [Q6IBW4-4]
DR RefSeq; NP_055366.3; NM_014551.4. [Q6IBW4-5]
DR RefSeq; NP_689512.2; NM_152299.3. [Q6IBW4-1]
DR AlphaFoldDB; Q6IBW4; -.
DR BioGRID; 118913; 168.
DR ComplexPortal; CPX-985; Condensin II complex.
DR CORUM; Q6IBW4; -.
DR DIP; DIP-43901N; -.
DR IntAct; Q6IBW4; 105.
DR MINT; Q6IBW4; -.
DR STRING; 9606.ENSP00000299821; -.
DR GlyGen; Q6IBW4; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q6IBW4; -.
DR MetOSite; Q6IBW4; -.
DR PhosphoSitePlus; Q6IBW4; -.
DR BioMuta; NCAPH2; -.
DR DMDM; 74709496; -.
DR EPD; Q6IBW4; -.
DR jPOST; Q6IBW4; -.
DR MassIVE; Q6IBW4; -.
DR MaxQB; Q6IBW4; -.
DR PaxDb; Q6IBW4; -.
DR PeptideAtlas; Q6IBW4; -.
DR PRIDE; Q6IBW4; -.
DR ProteomicsDB; 66371; -. [Q6IBW4-1]
DR ProteomicsDB; 66372; -. [Q6IBW4-2]
DR ProteomicsDB; 66373; -. [Q6IBW4-4]
DR ProteomicsDB; 66374; -. [Q6IBW4-5]
DR Antibodypedia; 28671; 132 antibodies from 22 providers.
DR CPTC; Q6IBW4; 1 antibody.
DR DNASU; 29781; -.
DR Ensembl; ENST00000299821.15; ENSP00000299821.11; ENSG00000025770.19. [Q6IBW4-4]
DR Ensembl; ENST00000395698.7; ENSP00000379050.3; ENSG00000025770.19. [Q6IBW4-5]
DR Ensembl; ENST00000420993.7; ENSP00000410088.2; ENSG00000025770.19. [Q6IBW4-1]
DR GeneID; 29781; -.
DR KEGG; hsa:29781; -.
DR MANE-Select; ENST00000420993.7; ENSP00000410088.2; NM_152299.4; NP_689512.2.
DR UCSC; uc003blq.5; human. [Q6IBW4-1]
DR CTD; 29781; -.
DR DisGeNET; 29781; -.
DR GeneCards; NCAPH2; -.
DR HGNC; HGNC:25071; NCAPH2.
DR HPA; ENSG00000025770; Low tissue specificity.
DR MalaCards; NCAPH2; -.
DR MIM; 611230; gene.
DR neXtProt; NX_Q6IBW4; -.
DR OpenTargets; ENSG00000025770; -.
DR PharmGKB; PA162397314; -.
DR VEuPathDB; HostDB:ENSG00000025770; -.
DR eggNOG; KOG2359; Eukaryota.
DR GeneTree; ENSGT00390000014443; -.
DR HOGENOM; CLU_010569_0_0_1; -.
DR InParanoid; Q6IBW4; -.
DR OMA; PPEHKLK; -.
DR OrthoDB; 522566at2759; -.
DR PhylomeDB; Q6IBW4; -.
DR TreeFam; TF101164; -.
DR PathwayCommons; Q6IBW4; -.
DR Reactome; R-HSA-2299718; Condensation of Prophase Chromosomes.
DR SignaLink; Q6IBW4; -.
DR SIGNOR; Q6IBW4; -.
DR BioGRID-ORCS; 29781; 597 hits in 1085 CRISPR screens.
DR ChiTaRS; NCAPH2; human.
DR GeneWiki; NCAPH2; -.
DR GenomeRNAi; 29781; -.
DR Pharos; Q6IBW4; Tbio.
DR PRO; PR:Q6IBW4; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; Q6IBW4; protein.
DR Bgee; ENSG00000025770; Expressed in cerebellar hemisphere and 186 other tissues.
DR ExpressionAtlas; Q6IBW4; baseline and differential.
DR Genevisible; Q6IBW4; HS.
DR GO; GO:0030054; C:cell junction; IDA:HPA.
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; IDA:HPA.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
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 1: Evidence at protein level;
KW Alternative splicing; Chromosome; DNA condensation; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..605
FT /note="Condensin-2 complex subunit H2"
FT /id="PRO_0000326241"
FT REGION 194..331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 19
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 95
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 200
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 208
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 228
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q4V8I2"
FT MOD_RES 232
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BSP2"
FT MOD_RES 282
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 284
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 466
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 492
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17525332,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT VAR_SEQ 167..188
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_032636"
FT VAR_SEQ 288..299
FT /note="SAALPRRYMLRE -> VGPTWRPAEPEL (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_032637"
FT VAR_SEQ 300..605
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_032638"
FT VAR_SEQ 435
FT /note="A -> AA (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_032639"
FT CONFLICT 36
FT /note="E -> D (in Ref. 1; CAA16670)"
FT /evidence="ECO:0000305"
FT CONFLICT 61
FT /note="Q -> H (in Ref. 1; CAA16670)"
FT /evidence="ECO:0000305"
FT CONFLICT 76
FT /note="S -> W (in Ref. 1; CAA16670)"
FT /evidence="ECO:0000305"
FT CONFLICT 161
FT /note="N -> I (in Ref. 1; CAA16670)"
FT /evidence="ECO:0000305"
FT CONFLICT 190
FT /note="G -> R (in Ref. 1; CAA16670)"
FT /evidence="ECO:0000305"
FT CONFLICT 215
FT /note="K -> N (in Ref. 1; CAA16670)"
FT /evidence="ECO:0000305"
FT CONFLICT 249
FT /note="G -> R (in Ref. 1; CAA16670)"
FT /evidence="ECO:0000305"
FT CONFLICT 282
FT /note="S -> F (in Ref. 5; AAH09441)"
FT /evidence="ECO:0000305"
FT CONFLICT 316
FT /note="P -> L (in Ref. 1; CAA16670)"
FT /evidence="ECO:0000305"
FT CONFLICT 323..324
FT /note="FD -> LN (in Ref. 1; CAA16670)"
FT /evidence="ECO:0000305"
FT CONFLICT 368
FT /note="A -> V (in Ref. 1; CAA16670)"
FT /evidence="ECO:0000305"
FT CONFLICT 474
FT /note="N -> K (in Ref. 1; CAA16670)"
FT /evidence="ECO:0000305"
FT CONFLICT 486
FT /note="V -> I (in Ref. 1; CAA16670)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 605 AA; 68227 MW; 2C8A1070C27B4547 CRC64;
MEDVEARFAH LLQPIRDLTK NWEVDVAAQL GEYLEELDQI CISFDEGKTT MNFIEAALLI
QGSACVYSKK VEYLYSLVYQ ALDFISGKRR AKQLSSVQED RANGVASSGV PQEAENEFLS
LDDFPDSRTN VDLKNDQTPS EVLIIPLLPM ALVAPDEMEK NNNPLYSRQG EVLASRKDFR
MNTCVPHPRG AFMLEPEGMS PMEPAGVSPM PGTQKDTGRT EEQPMEVSVC RSPVPALGFS
QEPGPSPEGP MPLGGGEDED AEEAVELPEA SAPKAALEPK ESRSPQQSAA LPRRYMLRER
EGAPEPASCV KETPDPWQSL DPFDSLESKP FKKGRPYSVP PCVEEALGQK RKRKGAAKLQ
DFHQWYLAAY ADHADSRRLR RKGPSFADME VLYWTHVKEQ LETLRKLQRR EVAEQWLRPA
EEDHLEDSLE DLGAADDFLE PEEYMEPEGA DPREAADLDA VPMSLSYEEL VRRNVELFIA
TSQKFVQETE LSQRIRDWED TVQPLLQEQE QHVPFDIHTY GDQLVSRFPQ LNEWCPFAEL
VAGQPAFEVC RSMLASLQLA NDYTVEITQQ PGLEMAVDTM SLRLLTHQRA HKRFQTYAAP
SMAQP
