CHAP1_HUMAN
ID CHAP1_HUMAN Reviewed; 812 AA.
AC Q96JM3; B3KU06; Q6P181; Q8NC88; Q9BST0;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 2.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Chromosome alignment-maintaining phosphoprotein 1;
DE AltName: Full=Zinc finger protein 828;
GN Name=CHAMP1; Synonyms=C13orf8, CAMP, CHAMP, KIAA1802, ZNF828;
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].
RC TISSUE=Brain;
RX PubMed=11347906; DOI=10.1093/dnares/8.2.85;
RA Nagase T., Nakayama M., Nakajima D., Kikuno R., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XX. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 8:85-95(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Teratocarcinoma;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057823; DOI=10.1038/nature02379;
RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA Rogers J., Ross M.T.;
RT "The DNA sequence and analysis of human chromosome 13.";
RL Nature 428:522-528(2004).
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].
RC TISSUE=Placenta, 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-204; SER-217; SER-308;
RP SER-319 AND SER-603, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-204; SER-214; SER-282;
RP SER-286; SER-297; SER-319; SER-405; SER-452; SER-459; SER-462; SER-627;
RP SER-651; SER-652 AND SER-653, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [8]
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-204; SER-214; SER-282;
RP SER-286; SER-297; SER-382; SER-386; SER-507; SER-627; SER-651 AND SER-652,
RP AND IDENTIFICATION BY 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 [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-490, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [11]
RP INTERACTION WITH POGZ; CBX1; CBX3 AND CBX5.
RX PubMed=20850016; DOI=10.1016/j.cell.2010.08.020;
RA Vermeulen M., Eberl H.C., Matarese F., Marks H., Denissov S., Butter F.,
RA Lee K.K., Olsen J.V., Hyman A.A., Stunnenberg H.G., Mann M.;
RT "Quantitative interaction proteomics and genome-wide profiling of
RT epigenetic histone marks and their readers.";
RL Cell 142:967-980(2010).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-87; SER-275; SER-282;
RP SER-286; SER-297; SER-308; SER-319; SER-405; SER-427; SER-432; SER-436;
RP SER-445; SER-459; SER-476; SER-542; SER-603; SER-627; SER-632; SER-651;
RP SER-653; SER-675 AND SER-736, 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 [13]
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 [14]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, INTERACTION WITH MAD2L2,
RP SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
RX PubMed=21063390; DOI=10.1038/emboj.2010.276;
RA Itoh G., Kanno S., Uchida K.S., Chiba S., Sugino S., Watanabe K.,
RA Mizuno K., Yasui A., Hirota T., Tanaka K.;
RT "CAMP (C13orf8, ZNF828) is a novel regulator of kinetochore-microtubule
RT attachment.";
RL EMBO J. 30:130-144(2011).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108; SER-184; SER-214;
RP SER-247; SER-253; SER-275; SER-286; SER-297; SER-308; SER-344; SER-355;
RP SER-382; SER-405; SER-416; SER-427; SER-443; SER-445; SER-459; SER-476;
RP SER-507; SER-626 AND SER-627, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-87; SER-108; SER-204;
RP SER-214; SER-282; SER-286; SER-308; SER-319; SER-376; SER-382; SER-386;
RP SER-405; SER-416; SER-427; SER-432; SER-436; SER-445; SER-452; THR-458;
RP SER-459; SER-462; SER-472; SER-476; SER-507; SER-512; SER-542; SER-572;
RP SER-603; SER-615; SER-627; SER-632 AND SER-675, AND IDENTIFICATION BY MASS
RP 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).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173; SER-204; SER-214;
RP SER-247; SER-264; SER-282; SER-286; SER-376; THR-403; SER-405; SER-416;
RP SER-427; SER-476; SER-507 AND SER-542, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [19]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-670, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [20]
RP INVOLVEMENT IN NEDHILD.
RX PubMed=26340335; DOI=10.1016/j.ajhg.2015.08.003;
RA Hempel M., Cremer K., Ockeloen C.W., Lichtenbelt K.D., Herkert J.C.,
RA Denecke J., Haack T.B., Zink A.M., Becker J., Wohlleber E., Johannsen J.,
RA Alhaddad B., Pfundt R., Fuchs S., Wieczorek D., Strom T.M.,
RA van Gassen K.L., Kleefstra T., Kubisch C., Engels H., Lessel D.;
RT "De novo mutations in CHAMP1 cause intellectual disability with severe
RT speech impairment.";
RL Am. J. Hum. Genet. 97:493-500(2015).
RN [21]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-490, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA Vertegaal A.C.;
RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL Cell Rep. 10:1778-1791(2015).
RN [22]
RP INVOLVEMENT IN NEDHILD.
RX PubMed=25533962; DOI=10.1038/nature14135;
RG Deciphering Developmental Disorders Study;
RT "Large-scale discovery of novel genetic causes of developmental
RT disorders.";
RL Nature 519:223-228(2015).
RN [23]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-490; LYS-565; LYS-606; LYS-638;
RP LYS-670 AND LYS-689, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
CC -!- FUNCTION: Required for proper alignment of chromosomes at metaphase and
CC their accurate segregation during mitosis. Involved in the maintenance
CC of spindle microtubules attachment to the kinetochore during sister
CC chromatid biorientation. May recruit CENPE and CENPF to the
CC kinetochore. {ECO:0000269|PubMed:21063390}.
CC -!- SUBUNIT: Interacts with MAD2L2. Interacts with POGZ, CBX1, CBX3 and
CC CBX5. {ECO:0000269|PubMed:20850016, ECO:0000269|PubMed:21063390}.
CC -!- INTERACTION:
CC Q96JM3; Q9UI95: MAD2L2; NbExp=6; IntAct=EBI-2560420, EBI-77889;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21063390}. Chromosome
CC {ECO:0000269|PubMed:21063390}. Chromosome, centromere, kinetochore
CC {ECO:0000269|PubMed:21063390}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000269|PubMed:21063390}.
CC -!- PTM: Phosphorylated by CDK1. Mitotic phosphorylation is required for
CC the attachment of spindle microtubules to the kinetochore.
CC {ECO:0000269|PubMed:21063390}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB47431.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC11273.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB058705; BAB47431.1; ALT_INIT; mRNA.
DR EMBL; AK074894; BAC11273.1; ALT_INIT; mRNA.
DR EMBL; AK096346; BAG53268.1; -; mRNA.
DR EMBL; AL845154; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471085; EAX09253.1; -; Genomic_DNA.
DR EMBL; BC004820; AAH04820.1; -; mRNA.
DR EMBL; BC065237; AAH65237.1; -; mRNA.
DR CCDS; CCDS9545.1; -.
DR RefSeq; NP_001157616.1; NM_001164144.2.
DR RefSeq; NP_001157617.1; NM_001164145.2.
DR RefSeq; NP_115812.1; NM_032436.3.
DR PDB; 5XPT; X-ray; 2.10 A; B=325-344.
DR PDB; 5XPU; X-ray; 2.30 A; B=325-344.
DR PDB; 6EKJ; X-ray; 1.60 A; B=328-355.
DR PDB; 6EKL; X-ray; 1.60 A; B=328-355.
DR PDBsum; 5XPT; -.
DR PDBsum; 5XPU; -.
DR PDBsum; 6EKJ; -.
DR PDBsum; 6EKL; -.
DR AlphaFoldDB; Q96JM3; -.
DR SMR; Q96JM3; -.
DR BioGRID; 129584; 115.
DR IntAct; Q96JM3; 41.
DR MINT; Q96JM3; -.
DR STRING; 9606.ENSP00000354730; -.
DR GlyGen; Q96JM3; 7 sites, 2 O-linked glycans (7 sites).
DR iPTMnet; Q96JM3; -.
DR PhosphoSitePlus; Q96JM3; -.
DR SwissPalm; Q96JM3; -.
DR BioMuta; CHAMP1; -.
DR DMDM; 114149935; -.
DR EPD; Q96JM3; -.
DR jPOST; Q96JM3; -.
DR MassIVE; Q96JM3; -.
DR MaxQB; Q96JM3; -.
DR PaxDb; Q96JM3; -.
DR PeptideAtlas; Q96JM3; -.
DR PRIDE; Q96JM3; -.
DR ProteomicsDB; 76984; -.
DR Antibodypedia; 1883; 146 antibodies from 23 providers.
DR DNASU; 283489; -.
DR Ensembl; ENST00000361283.4; ENSP00000354730.1; ENSG00000198824.7.
DR Ensembl; ENST00000643483.1; ENSP00000496699.1; ENSG00000198824.7.
DR GeneID; 283489; -.
DR KEGG; hsa:283489; -.
DR MANE-Select; ENST00000361283.4; ENSP00000354730.1; NM_032436.4; NP_115812.1.
DR UCSC; uc001vuv.4; human.
DR CTD; 283489; -.
DR DisGeNET; 283489; -.
DR GeneCards; CHAMP1; -.
DR HGNC; HGNC:20311; CHAMP1.
DR HPA; ENSG00000198824; Low tissue specificity.
DR MalaCards; CHAMP1; -.
DR MIM; 616327; gene.
DR MIM; 616579; phenotype.
DR neXtProt; NX_Q96JM3; -.
DR OpenTargets; ENSG00000198824; -.
DR Orphanet; 178469; Autosomal dominant non-syndromic intellectual disability.
DR PharmGKB; PA162410749; -.
DR VEuPathDB; HostDB:ENSG00000198824; -.
DR eggNOG; ENOG502QXNS; Eukaryota.
DR GeneTree; ENSGT00730000111351; -.
DR HOGENOM; CLU_019515_0_0_1; -.
DR InParanoid; Q96JM3; -.
DR OMA; WKPIPSI; -.
DR OrthoDB; 277957at2759; -.
DR PhylomeDB; Q96JM3; -.
DR TreeFam; TF350859; -.
DR PathwayCommons; Q96JM3; -.
DR SignaLink; Q96JM3; -.
DR SIGNOR; Q96JM3; -.
DR BioGRID-ORCS; 283489; 44 hits in 1085 CRISPR screens.
DR ChiTaRS; CHAMP1; human.
DR GeneWiki; C13orf8; -.
DR GenomeRNAi; 283489; -.
DR Pharos; Q96JM3; Tbio.
DR PRO; PR:Q96JM3; -.
DR Proteomes; UP000005640; Chromosome 13.
DR RNAct; Q96JM3; protein.
DR Bgee; ENSG00000198824; Expressed in ileal mucosa and 173 other tissues.
DR ExpressionAtlas; Q96JM3; baseline and differential.
DR Genevisible; Q96JM3; HS.
DR GO; GO:0000793; C:condensed chromosome; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0090543; C:Flemming body; IDA:HPA.
DR GO; GO:0000776; C:kinetochore; IDA:UniProtKB.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005819; C:spindle; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051315; P:attachment of mitotic spindle microtubules to kinetochore; IMP:UniProtKB.
DR GO; GO:0034501; P:protein localization to kinetochore; IMP:UniProtKB.
DR GO; GO:0035372; P:protein localization to microtubule; IMP:UniProtKB.
DR GO; GO:0031134; P:sister chromatid biorientation; IMP:UniProtKB.
DR InterPro; IPR039330; CAMP.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR37354; PTHR37354; 1.
DR SMART; SM00355; ZnF_C2H2; 5.
DR SUPFAM; SSF57667; SSF57667; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Centromere; Chromosome; Cytoplasm; Cytoskeleton;
KW Intellectual disability; Isopeptide bond; Kinetochore; Metal-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..812
FT /note="Chromosome alignment-maintaining phosphoprotein 1"
FT /id="PRO_0000248319"
FT ZN_FING 738..760
FT /note="C2H2-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 86..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 136..546
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 271..490
FT /note="Mediates interaction with MAD2L2"
FT /evidence="ECO:0000269|PubMed:21063390"
FT REGION 451..590
FT /note="Mediates localization to the spindle and the
FT kinetochore and is required for the attachment of spindle
FT microtubules to the kinetochore"
FT REGION 591..812
FT /note="Mediates localization to the chromosome and the
FT spindle and negatively regulates chromosome alignment"
FT COMPBIAS 86..101
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 169..186
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..248
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..323
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 338..359
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 360..386
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 417..431
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 455..478
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 87
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 108
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 173
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 184
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 204
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 214
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 217
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983"
FT MOD_RES 244
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8K327"
FT MOD_RES 247
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 253
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 264
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 275
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 282
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 286
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 297
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 308
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 319
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 344
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 355
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 376
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 382
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 386
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 403
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 405
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 416
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 427
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 432
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 436
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 443
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 445
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 452
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 458
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 459
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 462
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 472
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 476
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 490
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 507
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 512
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 542
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 572
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 603
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 615
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 626
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 627
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 632
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 651
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231"
FT MOD_RES 652
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332"
FT MOD_RES 653
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 675
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 736
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT CROSSLNK 490
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25772364,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 565
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 606
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 638
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 670
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 689
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 568
FT /note="L -> V (in dbSNP:rs3764522)"
FT /id="VAR_027270"
FT VARIANT 591
FT /note="K -> R (in dbSNP:rs35564629)"
FT /id="VAR_052910"
FT VARIANT 604
FT /note="P -> R (in dbSNP:rs12428067)"
FT /id="VAR_027271"
FT CONFLICT 81
FT /note="I -> T (in Ref. 2; BAC11273)"
FT /evidence="ECO:0000305"
FT CONFLICT 140
FT /note="V -> A (in Ref. 2; BAC11273)"
FT /evidence="ECO:0000305"
FT CONFLICT 576
FT /note="V -> A (in Ref. 2; BAC11273)"
FT /evidence="ECO:0000305"
FT STRAND 331..338
FT /evidence="ECO:0007829|PDB:6EKJ"
SQ SEQUENCE 812 AA; 89099 MW; 0276EF84795D89F2 CRC64;
MEAFQELRKP SARLECDHCS FRGTDYENVQ IHMGTIHPEF CDEMDAGGLG KMIFYQKSAK
LFHCHKCFFT SKMYSNVYYH ITSKHASPDK WNDKPKNQLN KETDPVKSPP LPEHQKIPCN
SAEPKSIPAL SMETQKLGSV LSPESPKPTP LTPLEPQKPG SVVSPELQTP LPSPEPSKPA
SVSSPEPPKS VPVCESQKLA PVPSPEPQKP APVSPESVKA TLSNPKPQKQ SHFPETLGPP
SASSPESPVL AASPEPWGPS PAASPESRKS ARTTSPEPRK PSPSESPEPW KPFPAVSPEP
RRPAPAVSPG SWKPGPPGSP RPWKSNPSAS SGPWKPAKPA PSVSPGPWKP IPSVSPGPWK
PTPSVSSASW KSSSVSPSSW KSPPASPESW KSGPPELRKT APTLSPEHWK AVPPVSPELR
KPGPPLSPEI RSPAGSPELR KPSGSPDLWK LSPDQRKTSP ASLDFPESQK SSRGGSPDLW
KSSFFIEPQK PVFPETRKPG PSGPSESPKA ASDIWKPVLS IDTEPRKPAL FPEPAKTAPP
ASPEARKRAL FPEPRKHALF PELPKSALFS ESQKAVELGD ELQIDAIDDQ KCDILVQEEL
LASPKKLLED TLFPSSKKLK KDNQESSDAE LSSSEYIKTD LDAMDIKGQE SSSDQEQVDV
ESIDFSKENK MDMTSPEQSR NVLQFTEEKE AFISEEEIAK YMKRGKGKYY CKICCCRAMK
KGAVLHHLVN KHNVHSPYKC TICGKAFLLE SLLKNHVAAH GQSLLKCPRC NFESNFPRGF
KKHLTHCQSR HNEEANKKLM EALEPPLEEQ QI
