Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Chromosome alignment-maintaining phosphoprotein 1 (Zinc finger protein 828)

 CHAP1_HUMAN             Reviewed;         812 AA.
Q96JM3; B3KU06; Q6P181; Q8NC88; Q9BST0;
05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
05-SEP-2006, sequence version 2.
12-SEP-2018, entry version 141.
RecName: Full=Chromosome alignment-maintaining phosphoprotein 1;
AltName: Full=Zinc finger protein 828;
Name=CHAMP1; Synonyms=C13orf8, CAMP, CHAMP, KIAA1802, ZNF828;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=11347906; DOI=10.1093/dnares/8.2.85;
Nagase T., Nakayama M., Nakajima D., Kikuno R., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XX.
The complete sequences of 100 new cDNA clones from brain which code
for large proteins in vitro.";
DNA Res. 8:85-95(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Teratocarcinoma;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057823; DOI=10.1038/nature02379;
Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E.,
Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E.,
Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.,
Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R.,
Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S.,
Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M.,
Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J.,
Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E.,
Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L.,
Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J.,
Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S.,
Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J.,
Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M.,
King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A.,
Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S.,
Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S.,
Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A.,
Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L.,
Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M.,
Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.;
"The DNA sequence and analysis of human chromosome 13.";
Nature 428:522-528(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Placenta, and Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-204; SER-217; SER-308;
SER-319 AND SER-603, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-204; SER-214; SER-282;
SER-286; SER-297; SER-319; SER-405; SER-452; SER-459; SER-462;
SER-627; SER-651; SER-652 AND SER-653, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-204; SER-214; SER-282;
SER-286; SER-297; SER-382; SER-386; SER-507; SER-627; SER-651 AND
SER-652, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[10]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-490, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[11]
INTERACTION WITH POGZ; CBX1; CBX3 AND CBX5.
PubMed=20850016; DOI=10.1016/j.cell.2010.08.020;
Vermeulen M., Eberl H.C., Matarese F., Marks H., Denissov S.,
Butter F., Lee K.K., Olsen J.V., Hyman A.A., Stunnenberg H.G.,
Mann M.;
"Quantitative interaction proteomics and genome-wide profiling of
epigenetic histone marks and their readers.";
Cell 142:967-980(2010).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-87; SER-275; SER-282;
SER-286; SER-297; SER-308; SER-319; SER-405; SER-427; SER-432;
SER-436; SER-445; SER-459; SER-476; SER-542; SER-603; SER-627;
SER-632; SER-651; SER-653; SER-675 AND SER-736, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[14]
IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, INTERACTION WITH
MAD2L2, SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
PubMed=21063390; DOI=10.1038/emboj.2010.276;
Itoh G., Kanno S., Uchida K.S., Chiba S., Sugino S., Watanabe K.,
Mizuno K., Yasui A., Hirota T., Tanaka K.;
"CAMP (C13orf8, ZNF828) is a novel regulator of kinetochore-
microtubule attachment.";
EMBO J. 30:130-144(2011).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108; SER-184; SER-214;
SER-247; SER-253; SER-275; SER-286; SER-297; SER-308; SER-344;
SER-355; SER-382; SER-405; SER-416; SER-427; SER-443; SER-445;
SER-459; SER-476; SER-507; SER-626 AND SER-627, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[16]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-87; SER-108; SER-204;
SER-214; SER-282; SER-286; SER-308; SER-319; SER-376; SER-382;
SER-386; SER-405; SER-416; SER-427; SER-432; SER-436; SER-445;
SER-452; THR-458; SER-459; SER-462; SER-472; SER-476; SER-507;
SER-512; SER-542; SER-572; SER-603; SER-615; SER-627; SER-632 AND
SER-675, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173; SER-204; SER-214;
SER-247; SER-264; SER-282; SER-286; SER-376; THR-403; SER-405;
SER-416; SER-427; SER-476; SER-507 AND SER-542, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[19]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-670, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25218447; DOI=10.1038/nsmb.2890;
Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
Vertegaal A.C.;
"Uncovering global SUMOylation signaling networks in a site-specific
manner.";
Nat. Struct. Mol. Biol. 21:927-936(2014).
[20]
INVOLVEMENT IN MRD40.
PubMed=26340335; DOI=10.1016/j.ajhg.2015.08.003;
Hempel M., Cremer K., Ockeloen C.W., Lichtenbelt K.D., Herkert J.C.,
Denecke J., Haack T.B., Zink A.M., Becker J., Wohlleber E.,
Johannsen J., Alhaddad B., Pfundt R., Fuchs S., Wieczorek D.,
Strom T.M., van Gassen K.L., Kleefstra T., Kubisch C., Engels H.,
Lessel D.;
"De novo mutations in CHAMP1 cause intellectual disability with severe
speech impairment.";
Am. J. Hum. Genet. 97:493-500(2015).
[21]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-490, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
Vertegaal A.C.;
"SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
Cell Rep. 10:1778-1791(2015).
[22]
INVOLVEMENT IN MRD40.
PubMed=25533962; DOI=10.1038/nature14135;
Deciphering Developmental Disorders Study;
"Large-scale discovery of novel genetic causes of developmental
disorders.";
Nature 519:223-228(2015).
[23]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-490; LYS-565; LYS-606;
LYS-638; LYS-670 AND LYS-689, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
-!- FUNCTION: Required for proper alignment of chromosomes at
metaphase and their accurate segregation during mitosis. Involved
in the maintenance of spindle microtubules attachment to the
kinetochore during sister chromatid biorientation. May recruit
CENPE and CENPF to the kinetochore. {ECO:0000269|PubMed:21063390}.
-!- SUBUNIT: Interacts with MAD2L2. Interacts with POGZ, CBX1, CBX3
and CBX5. {ECO:0000269|PubMed:20850016,
ECO:0000269|PubMed:21063390}.
-!- INTERACTION:
Q9UI95:MAD2L2; NbExp=5; IntAct=EBI-2560420, EBI-77889;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21063390}.
Chromosome {ECO:0000269|PubMed:21063390}. Chromosome, centromere,
kinetochore {ECO:0000269|PubMed:21063390}. Cytoplasm,
cytoskeleton, spindle {ECO:0000269|PubMed:21063390}.
-!- PTM: Phosphorylated by CDK1. Mitotic phosphorylation is required
for the attachment of spindle microtubules to the kinetochore.
{ECO:0000269|PubMed:21063390}.
-!- DISEASE: Mental retardation, autosomal dominant 40 (MRD40)
[MIM:616579]: A form of mental retardation, a disorder
characterized by significantly below average general intellectual
functioning associated with impairments in adaptive behavior and
manifested during the developmental period.
{ECO:0000269|PubMed:25533962, ECO:0000269|PubMed:26340335}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SEQUENCE CAUTION:
Sequence=BAB47431.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=BAC11273.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AB058705; BAB47431.1; ALT_INIT; mRNA.
EMBL; AK074894; BAC11273.1; ALT_INIT; mRNA.
EMBL; AK096346; BAG53268.1; -; mRNA.
EMBL; AL845154; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471085; EAX09253.1; -; Genomic_DNA.
EMBL; BC004820; AAH04820.1; -; mRNA.
EMBL; BC065237; AAH65237.1; -; mRNA.
CCDS; CCDS9545.1; -.
RefSeq; NP_001157616.1; NM_001164144.2.
RefSeq; NP_001157617.1; NM_001164145.2.
RefSeq; NP_115812.1; NM_032436.3.
UniGene; Hs.7542; -.
PDB; 5XPT; X-ray; 2.10 A; B=325-344.
PDB; 5XPU; X-ray; 2.30 A; B=325-344.
PDBsum; 5XPT; -.
PDBsum; 5XPU; -.
ProteinModelPortal; Q96JM3; -.
SMR; Q96JM3; -.
BioGrid; 129584; 43.
IntAct; Q96JM3; 27.
MINT; Q96JM3; -.
STRING; 9606.ENSP00000354730; -.
iPTMnet; Q96JM3; -.
PhosphoSitePlus; Q96JM3; -.
BioMuta; CHAMP1; -.
DMDM; 114149935; -.
EPD; Q96JM3; -.
MaxQB; Q96JM3; -.
PaxDb; Q96JM3; -.
PeptideAtlas; Q96JM3; -.
PRIDE; Q96JM3; -.
ProteomicsDB; 76984; -.
DNASU; 283489; -.
Ensembl; ENST00000361283; ENSP00000354730; ENSG00000198824.
Ensembl; ENST00000643483; ENSP00000496699; ENSG00000198824.
GeneID; 283489; -.
KEGG; hsa:283489; -.
UCSC; uc001vuv.4; human.
CTD; 283489; -.
DisGeNET; 283489; -.
EuPathDB; HostDB:ENSG00000198824.5; -.
GeneCards; CHAMP1; -.
HGNC; HGNC:20311; CHAMP1.
HPA; HPA006623; -.
HPA; HPA008900; -.
MalaCards; CHAMP1; -.
MIM; 616327; gene.
MIM; 616579; phenotype.
neXtProt; NX_Q96JM3; -.
OpenTargets; ENSG00000198824; -.
PharmGKB; PA162410749; -.
eggNOG; ENOG410IFC8; Eukaryota.
eggNOG; ENOG410XXII; LUCA.
GeneTree; ENSGT00730000111351; -.
HOGENOM; HOG000065731; -.
HOVERGEN; HBG062352; -.
InParanoid; Q96JM3; -.
KO; K22593; -.
OMA; PEFCDEM; -.
OrthoDB; EOG091G02UO; -.
PhylomeDB; Q96JM3; -.
TreeFam; TF350859; -.
ChiTaRS; CHAMP1; human.
GeneWiki; C13orf8; -.
GenomeRNAi; 283489; -.
PRO; PR:Q96JM3; -.
Proteomes; UP000005640; Chromosome 13.
Bgee; ENSG00000198824; Expressed in 188 organ(s), highest expression level in amniotic fluid.
CleanEx; HS_ZNF828; -.
ExpressionAtlas; Q96JM3; baseline and differential.
Genevisible; Q96JM3; HS.
GO; GO:0000793; C:condensed chromosome; IDA:UniProtKB.
GO; GO:0000777; C:condensed chromosome kinetochore; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
GO; GO:0090543; C:Flemming body; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005819; C:spindle; IDA:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
GO; GO:0051315; P:attachment of mitotic spindle microtubules to kinetochore; IMP:UniProtKB.
GO; GO:0034501; P:protein localization to kinetochore; IMP:UniProtKB.
GO; GO:0035372; P:protein localization to microtubule; IMP:UniProtKB.
GO; GO:0031134; P:sister chromatid biorientation; IMP:UniProtKB.
InterPro; IPR039330; CAMP.
InterPro; IPR036236; Znf_C2H2_sf.
InterPro; IPR013087; Znf_C2H2_type.
PANTHER; PTHR37354; PTHR37354; 1.
SMART; SM00355; ZnF_C2H2; 5.
SUPFAM; SSF57667; SSF57667; 1.
PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Centromere; Chromosome; Complete proteome;
Cytoplasm; Cytoskeleton; Isopeptide bond; Kinetochore;
Mental retardation; Metal-binding; Nucleus; Phosphoprotein;
Polymorphism; Reference proteome; Ubl conjugation; Zinc; Zinc-finger.
CHAIN 1 812 Chromosome alignment-maintaining
phosphoprotein 1.
/FTId=PRO_0000248319.
ZN_FING 738 760 C2H2-type. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
REGION 271 490 Mediates interaction with MAD2L2.
{ECO:0000269|PubMed:21063390}.
REGION 451 590 Mediates localization to the spindle and
the kinetochore and is required for the
attachment of spindle microtubules to the
kinetochore.
REGION 591 812 Mediates localization to the chromosome
and the spindle and negatively regulates
chromosome alignment.
COMPBIAS 105 564 Pro-rich.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:22814378}.
MOD_RES 87 87 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 108 108 Phosphoserine.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 173 173 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 184 184 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 204 204 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 214 214 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 217 217 Phosphoserine.
{ECO:0000244|PubMed:17081983}.
MOD_RES 244 244 Phosphoserine.
{ECO:0000250|UniProtKB:Q8K327}.
MOD_RES 247 247 Phosphoserine.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:24275569}.
MOD_RES 253 253 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 264 264 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 275 275 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692}.
MOD_RES 282 282 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 286 286 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 297 297 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692}.
MOD_RES 308 308 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 319 319 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 344 344 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 355 355 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 376 376 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 382 382 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 386 386 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 403 403 Phosphothreonine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 405 405 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 416 416 Phosphoserine.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 427 427 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 432 432 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 436 436 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 443 443 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 445 445 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 452 452 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 458 458 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 459 459 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 462 462 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 472 472 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 476 476 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 490 490 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 507 507 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 512 512 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 542 542 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 572 572 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 603 603 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 615 615 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 626 626 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 627 627 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 632 632 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 651 651 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231}.
MOD_RES 652 652 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332}.
MOD_RES 653 653 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231}.
MOD_RES 675 675 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 736 736 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
CROSSLNK 490 490 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
CROSSLNK 565 565 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 606 606 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 638 638 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 670 670 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:28112733}.
CROSSLNK 689 689 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VARIANT 568 568 L -> V (in dbSNP:rs3764522).
/FTId=VAR_027270.
VARIANT 591 591 K -> R (in dbSNP:rs35564629).
/FTId=VAR_052910.
VARIANT 604 604 P -> R (in dbSNP:rs12428067).
/FTId=VAR_027271.
CONFLICT 81 81 I -> T (in Ref. 2; BAC11273).
{ECO:0000305}.
CONFLICT 140 140 V -> A (in Ref. 2; BAC11273).
{ECO:0000305}.
CONFLICT 576 576 V -> A (in Ref. 2; BAC11273).
{ECO:0000305}.
STRAND 334 338 {ECO:0000244|PDB:5XPT}.
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


Related products :

Catalog number Product name Quantity
EIAAB47838 C13orf8,CAMP,Chromosome alignment-maintaining phosphoprotein,Homo sapiens,Human,KIAA1802,Zinc finger protein 828,ZNF828
EIAAB47340 BMZF5,BMZF-5,Bone marrow zinc finger 5,HD-ZNF1,Hematopoietic cell-derived zinc finger protein 1,Homo sapiens,Human,Zinc finger protein 254,Zinc finger protein 539,Zinc finger protein 91-like,ZNF254,ZN
EIAAB47314 BMZF2,BMZF-2,Bone marrow zinc finger 2,Homo sapiens,Human,KOX22,Zinc finger protein 224,Zinc finger protein 233,Zinc finger protein 255,Zinc finger protein 27,Zinc finger protein KOX22,ZNF224,ZNF233,Z
EIAAB47352 CT-ZFP48,EBV-induced zinc finger protein,Epstein-Barr virus-induced zinc finger protein,Homo sapiens,Human,Zinc finger protein 271,Zinc finger protein dp,Zinc finger protein HZF7,Zinc finger protein Z
EIAAB47194 Homo sapiens,Human,Zf47,ZFP47,Zfp-47,Zinc finger and SCAN domain-containing protein 13,Zinc finger protein 306,Zinc finger protein 309,Zinc finger protein 47 homolog,Zinc finger protein with KRAB and
EIAAB47193 Mouse,Mus musculus,SCAN-KRAB-zinc finger protein,Skz1,Zf47,Zfp306,Zfp307,Zfp47,Zfp-47,Zinc finger protein 306,Zinc finger protein 307,Zinc finger protein 47 homolog,Zinc finger protein with KRAB and S
EIAAB46826 FANCC-interacting protein,Fanconi anemia zinc finger protein,FAZF,Homo sapiens,Human,Testis zinc finger protein,TZFP,ZBTB32,Zinc finger and BTB domain-containing protein 32,Zinc finger protein 538,ZNF
EIAAB47355 Homo sapiens,Human,Neurotrophin receptor-interacting factor homolog,SP2114,Zf2,Zinc finger protein 274,Zinc finger protein HFB101,Zinc finger protein with KRAB and SCAN domains 19,Zinc finger protein
EIAAB47395 C2H2-like zinc finger protein rearranged in thyroid adenomas,Homo sapiens,Human,RITA,Zinc finger protein 331,Zinc finger protein 361,Zinc finger protein 463,ZNF331,ZNF361,ZNF463
EIAAB47457 Early B-cell factor-associated zinc finger protein,Ebfaz,Kiaa0760,Mouse,Mus musculus,Nur12,Oaz,Olf1_EBF-associated zinc finger protein,Smad- and Olf-interacting zinc finger protein,Zfp423,Zinc finger
EIAAB46861 BOZF1,BOZ-F1,BTB_POZ and zinc-finger domain-containing factor,BTB_POZ and zinc-finger domains factor on chromosome 1,Homo sapiens,Human,ZBTB8A,Zinc finger and BTB domain-containing protein 8A
EIAAB14743 Fez family zinc finger protein 2,FEZF2,FEZL,FKSG36,Forebrain embryonic zinc finger-like protein 2,Homo sapiens,Human,Zinc finger protein 312,Zinc finger protein Fez-like,ZNF312
EIAAB47275 Homo sapiens,Human,Zinc finger protein 167,Zinc finger protein 448,Zinc finger protein 64,Zinc finger protein with KRAB and SCAN domains 7,ZKSCAN7,ZNF167,ZNF448,ZNF64
EIAAB46812 Homo sapiens,Human,MIZ1,Miz-1,Myc-interacting zinc finger protein 1,ZBTB17,Zinc finger and BTB domain-containing protein 17,Zinc finger protein 151,Zinc finger protein 60,ZNF151,ZNF60
EIAAB47878 HDSG1,Heart development-specific gene 1 protein,Homo sapiens,Human,KOX11,Zinc finger protein 18,Zinc finger protein 535,Zinc finger protein KOX11,Zinc finger protein with KRAB and SCAN domains 6,ZKSCA
EIAAB47384 Homo sapiens,Human,Zinc finger protein 322,Zinc finger protein 322A,Zinc finger protein 388,Zinc finger protein 489,ZNF322,ZNF322A,ZNF388,ZNF489
EIAAB14741 Fez,Fez family zinc finger protein 2,Fezf2,Fezl,Forebrain embryonic zinc finger-like protein 2,Mouse,Mus musculus,Zfp312,Zinc finger protein 312,Zinc finger protein Fez-like
EIAAB14742 Bos taurus,Bovine,Fez family zinc finger protein 2,FEZF2,FEZL,Forebrain embryonic zinc finger-like protein 2,Zinc finger protein 312,Zinc finger protein Fez-like,ZNF312
EIAAB47325 Homo sapiens,Human,ZFP93,Zfp-93,Zinc finger protein 235,Zinc finger protein 270,Zinc finger protein 93 homolog,Zinc finger protein HZF6,ZNF235,ZNF270
18-003-42276 Zinc finger and BTB domain-containing protein 7B - Zinc finger protein 67 homolog; Zfp-67; Zinc finger protein Th-POK; T-helper-inducing POZ_Krueppel-like factor; Krueppel-related zinc finger protein 0.1 mg Protein A
EIAAB47907 GIOT2,GIOT-2,Gonadotropin-inducible ovary transcription repressor 2,Homo sapiens,Human,KOX7,Zinc finger protein 44,Zinc finger protein 55,Zinc finger protein 58,Zinc finger protein KOX7,ZNF44,ZNF55,ZN
EIAAB47401 Homo sapiens,Human,KIAA0065,KOX31,Zinc finger and ZAK-associated protein with KRAB domain,Zinc finger protein 11A,Zinc finger protein 33A,Zinc finger protein KOX31,ZNF11,ZNF11A,ZNF33,ZNF33A,ZZaPK
EIAAB47892 Homo sapiens,Human,KOX17,Retinoic acid suppression protein A,RSG-A,Zinc finger and SCAN domain-containing protein 3,Zinc finger protein 191,Zinc finger protein 24,Zinc finger protein KOX17,ZNF191,ZNF2
18-003-42388 Zinc finger protein 24 - Zinc finger protein 191; Zinc finger protein KOX17; Retinoic acid suppression protein A; RSG-A; Zinc finger and SCAN domain-containing protein 3 Polyclonal 0.05 mg Aff Pur
EIAAB47372 Homo sapiens,Human,Zinc finger protein 135-like,Zinc finger protein 140-like,Zinc finger protein 302,Zinc finger protein 327,ZNF135L,ZNF140L,ZNF302,ZNF327


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur