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Protein

Chromosome alignment-maintaining phosphoprotein 1

Gene

CHAMP1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri738 – 76023C2H2-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

  • attachment of mitotic spindle microtubules to kinetochore Source: UniProtKB
  • protein localization to kinetochore Source: UniProtKB
  • protein localization to microtubule Source: UniProtKB
  • sister chromatid biorientation Source: UniProtKB
Complete GO annotation...

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Chromosome alignment-maintaining phosphoprotein 1
Alternative name(s):
Zinc finger protein 828
Gene namesi
Name:CHAMP1
Synonyms:C13orf8, CAMP, CHAMP, KIAA1802, ZNF828
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 13

Organism-specific databases

HGNCiHGNC:20311. CHAMP1.

Subcellular locationi

GO - Cellular componenti

  • condensed chromosome Source: UniProtKB
  • condensed chromosome kinetochore Source: UniProtKB
  • cytoplasm Source: UniProtKB-KW
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
  • spindle Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Centromere, Chromosome, Cytoplasm, Cytoskeleton, Kinetochore, Nucleus

Pathology & Biotechi

Involvement in diseasei

Mental retardation, autosomal dominant 40 (MRD40)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:616579

Keywords - Diseasei

Mental retardation

Organism-specific databases

MIMi616579. phenotype.
PharmGKBiPA162410749.

Polymorphism and mutation databases

BioMutaiCHAMP1.
DMDMi114149935.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 812812Chromosome alignment-maintaining phosphoprotein 1PRO_0000248319Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineCombined sources
Modified residuei87 – 871PhosphoserineCombined sources
Modified residuei108 – 1081PhosphoserineCombined sources
Modified residuei173 – 1731PhosphoserineCombined sources
Modified residuei184 – 1841PhosphoserineCombined sources
Modified residuei204 – 2041PhosphoserineCombined sources
Modified residuei214 – 2141PhosphoserineCombined sources
Modified residuei217 – 2171PhosphoserineCombined sources
Modified residuei244 – 2441PhosphoserineBy similarity
Modified residuei247 – 2471PhosphoserineCombined sources
Modified residuei253 – 2531PhosphoserineCombined sources
Modified residuei264 – 2641PhosphoserineCombined sources
Modified residuei275 – 2751PhosphoserineCombined sources
Modified residuei282 – 2821PhosphoserineCombined sources
Modified residuei286 – 2861PhosphoserineCombined sources
Modified residuei297 – 2971PhosphoserineCombined sources
Modified residuei308 – 3081PhosphoserineCombined sources
Modified residuei319 – 3191PhosphoserineCombined sources
Modified residuei344 – 3441PhosphoserineCombined sources
Modified residuei355 – 3551PhosphoserineCombined sources
Modified residuei376 – 3761PhosphoserineCombined sources
Modified residuei382 – 3821PhosphoserineCombined sources
Modified residuei386 – 3861PhosphoserineCombined sources
Modified residuei403 – 4031PhosphothreonineCombined sources
Modified residuei405 – 4051PhosphoserineCombined sources
Modified residuei416 – 4161PhosphoserineCombined sources
Modified residuei427 – 4271PhosphoserineCombined sources
Modified residuei432 – 4321PhosphoserineCombined sources
Modified residuei436 – 4361PhosphoserineCombined sources
Modified residuei443 – 4431PhosphoserineCombined sources
Modified residuei445 – 4451PhosphoserineCombined sources
Modified residuei452 – 4521PhosphoserineCombined sources
Modified residuei458 – 4581PhosphothreonineCombined sources
Modified residuei459 – 4591PhosphoserineCombined sources
Modified residuei462 – 4621PhosphoserineCombined sources
Modified residuei472 – 4721PhosphoserineCombined sources
Modified residuei476 – 4761PhosphoserineCombined sources
Modified residuei490 – 4901N6-acetyllysine; alternateCombined sources
Cross-linki490 – 490Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residuei507 – 5071PhosphoserineCombined sources
Modified residuei512 – 5121PhosphoserineCombined sources
Modified residuei542 – 5421PhosphoserineCombined sources
Modified residuei572 – 5721PhosphoserineCombined sources
Modified residuei603 – 6031PhosphoserineCombined sources
Modified residuei615 – 6151PhosphoserineCombined sources
Modified residuei626 – 6261PhosphoserineCombined sources
Modified residuei627 – 6271PhosphoserineCombined sources
Modified residuei632 – 6321PhosphoserineCombined sources
Modified residuei651 – 6511PhosphoserineCombined sources
Modified residuei652 – 6521PhosphoserineCombined sources
Modified residuei653 – 6531PhosphoserineCombined sources
Cross-linki670 – 670Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei675 – 6751PhosphoserineCombined sources
Modified residuei736 – 7361PhosphoserineCombined sources

Post-translational modificationi

Phosphorylated by CDK1. Mitotic phosphorylation is required for the attachment of spindle microtubules to the kinetochore.1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ96JM3.
MaxQBiQ96JM3.
PaxDbiQ96JM3.
PeptideAtlasiQ96JM3.
PRIDEiQ96JM3.

PTM databases

iPTMnetiQ96JM3.
PhosphoSiteiQ96JM3.

Expressioni

Gene expression databases

BgeeiQ96JM3.
CleanExiHS_ZNF828.
ExpressionAtlasiQ96JM3. baseline and differential.
GenevisibleiQ96JM3. HS.

Organism-specific databases

HPAiHPA006623.
HPA008900.

Interactioni

Subunit structurei

Interacts with MAD2L2. Interacts with POGZ, CBX1, CBX3 and CBX5.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
MAD2L2Q9UI954EBI-2560420,EBI-77889

Protein-protein interaction databases

BioGridi129584. 39 interactions.
IntActiQ96JM3. 23 interactions.

Structurei

3D structure databases

ProteinModelPortaliQ96JM3.
SMRiQ96JM3. Positions 12-37, 701-798.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni271 – 490220Mediates interaction with MAD2L2Add
BLAST
Regioni451 – 590140Mediates localization to the spindle and the kinetochore and is required for the attachment of spindle microtubules to the kinetochoreAdd
BLAST
Regioni591 – 812222Mediates localization to the chromosome and the spindle and negatively regulates chromosome alignmentAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi105 – 564460Pro-richAdd
BLAST

Sequence similaritiesi

Contains 1 C2H2-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri738 – 76023C2H2-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiENOG410IFC8. Eukaryota.
ENOG410XXII. LUCA.
GeneTreeiENSGT00730000111351.
HOGENOMiHOG000065731.
HOVERGENiHBG062352.
InParanoidiQ96JM3.
OMAiTIHPEFC.
OrthoDBiEOG773XKP.
PhylomeDBiQ96JM3.
TreeFamiTF350859.

Family and domain databases

Gene3Di3.30.160.60. 1 hit.
InterProiIPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]
SMARTiSM00355. ZnF_C2H2. 5 hits.
[Graphical view]
PROSITEiPS00028. ZINC_FINGER_C2H2_1. 1 hit.
PS50157. ZINC_FINGER_C2H2_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q96JM3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEAFQELRKP SARLECDHCS FRGTDYENVQ IHMGTIHPEF CDEMDAGGLG
60 70 80 90 100
KMIFYQKSAK LFHCHKCFFT SKMYSNVYYH ITSKHASPDK WNDKPKNQLN
110 120 130 140 150
KETDPVKSPP LPEHQKIPCN SAEPKSIPAL SMETQKLGSV LSPESPKPTP
160 170 180 190 200
LTPLEPQKPG SVVSPELQTP LPSPEPSKPA SVSSPEPPKS VPVCESQKLA
210 220 230 240 250
PVPSPEPQKP APVSPESVKA TLSNPKPQKQ SHFPETLGPP SASSPESPVL
260 270 280 290 300
AASPEPWGPS PAASPESRKS ARTTSPEPRK PSPSESPEPW KPFPAVSPEP
310 320 330 340 350
RRPAPAVSPG SWKPGPPGSP RPWKSNPSAS SGPWKPAKPA PSVSPGPWKP
360 370 380 390 400
IPSVSPGPWK PTPSVSSASW KSSSVSPSSW KSPPASPESW KSGPPELRKT
410 420 430 440 450
APTLSPEHWK AVPPVSPELR KPGPPLSPEI RSPAGSPELR KPSGSPDLWK
460 470 480 490 500
LSPDQRKTSP ASLDFPESQK SSRGGSPDLW KSSFFIEPQK PVFPETRKPG
510 520 530 540 550
PSGPSESPKA ASDIWKPVLS IDTEPRKPAL FPEPAKTAPP ASPEARKRAL
560 570 580 590 600
FPEPRKHALF PELPKSALFS ESQKAVELGD ELQIDAIDDQ KCDILVQEEL
610 620 630 640 650
LASPKKLLED TLFPSSKKLK KDNQESSDAE LSSSEYIKTD LDAMDIKGQE
660 670 680 690 700
SSSDQEQVDV ESIDFSKENK MDMTSPEQSR NVLQFTEEKE AFISEEEIAK
710 720 730 740 750
YMKRGKGKYY CKICCCRAMK KGAVLHHLVN KHNVHSPYKC TICGKAFLLE
760 770 780 790 800
SLLKNHVAAH GQSLLKCPRC NFESNFPRGF KKHLTHCQSR HNEEANKKLM
810
EALEPPLEEQ QI
Length:812
Mass (Da):89,099
Last modified:September 5, 2006 - v2
Checksum:i0276EF84795D89F2
GO

Sequence cautioni

The sequence BAB47431.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence BAC11273.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti81 – 811I → T in BAC11273 (PubMed:14702039).Curated
Sequence conflicti140 – 1401V → A in BAC11273 (PubMed:14702039).Curated
Sequence conflicti576 – 5761V → A in BAC11273 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti568 – 5681L → V.
Corresponds to variant rs3764522 [ dbSNP | Ensembl ].
VAR_027270
Natural varianti591 – 5911K → R.
Corresponds to variant rs35564629 [ dbSNP | Ensembl ].
VAR_052910
Natural varianti604 – 6041P → R.
Corresponds to variant rs12428067 [ dbSNP | Ensembl ].
VAR_027271

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB058705 mRNA. Translation: BAB47431.1. Different initiation.
AK074894 mRNA. Translation: BAC11273.1. Different initiation.
AK096346 mRNA. Translation: BAG53268.1.
AL845154 Genomic DNA. Translation: CAI23600.1.
CH471085 Genomic DNA. Translation: EAX09253.1.
BC004820 mRNA. Translation: AAH04820.1.
BC065237 mRNA. Translation: AAH65237.1.
CCDSiCCDS9545.1.
RefSeqiNP_001157616.1. NM_001164144.1.
NP_001157617.1. NM_001164145.1.
NP_115812.1. NM_032436.2.
UniGeneiHs.7542.

Genome annotation databases

EnsembliENST00000361283; ENSP00000354730; ENSG00000198824.
GeneIDi283489.
KEGGihsa:283489.
UCSCiuc001vuv.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB058705 mRNA. Translation: BAB47431.1. Different initiation.
AK074894 mRNA. Translation: BAC11273.1. Different initiation.
AK096346 mRNA. Translation: BAG53268.1.
AL845154 Genomic DNA. Translation: CAI23600.1.
CH471085 Genomic DNA. Translation: EAX09253.1.
BC004820 mRNA. Translation: AAH04820.1.
BC065237 mRNA. Translation: AAH65237.1.
CCDSiCCDS9545.1.
RefSeqiNP_001157616.1. NM_001164144.1.
NP_001157617.1. NM_001164145.1.
NP_115812.1. NM_032436.2.
UniGeneiHs.7542.

3D structure databases

ProteinModelPortaliQ96JM3.
SMRiQ96JM3. Positions 12-37, 701-798.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi129584. 39 interactions.
IntActiQ96JM3. 23 interactions.

PTM databases

iPTMnetiQ96JM3.
PhosphoSiteiQ96JM3.

Polymorphism and mutation databases

BioMutaiCHAMP1.
DMDMi114149935.

Proteomic databases

EPDiQ96JM3.
MaxQBiQ96JM3.
PaxDbiQ96JM3.
PeptideAtlasiQ96JM3.
PRIDEiQ96JM3.

Protocols and materials databases

DNASUi283489.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000361283; ENSP00000354730; ENSG00000198824.
GeneIDi283489.
KEGGihsa:283489.
UCSCiuc001vuv.4. human.

Organism-specific databases

CTDi283489.
GeneCardsiCHAMP1.
HGNCiHGNC:20311. CHAMP1.
HPAiHPA006623.
HPA008900.
MIMi616327. gene.
616579. phenotype.
neXtProtiNX_Q96JM3.
PharmGKBiPA162410749.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IFC8. Eukaryota.
ENOG410XXII. LUCA.
GeneTreeiENSGT00730000111351.
HOGENOMiHOG000065731.
HOVERGENiHBG062352.
InParanoidiQ96JM3.
OMAiTIHPEFC.
OrthoDBiEOG773XKP.
PhylomeDBiQ96JM3.
TreeFamiTF350859.

Miscellaneous databases

ChiTaRSiCHAMP1. human.
GeneWikiiC13orf8.
GenomeRNAii283489.
PROiQ96JM3.
SOURCEiSearch...

Gene expression databases

BgeeiQ96JM3.
CleanExiHS_ZNF828.
ExpressionAtlasiQ96JM3. baseline and differential.
GenevisibleiQ96JM3. HS.

Family and domain databases

Gene3Di3.30.160.60. 1 hit.
InterProiIPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]
SMARTiSM00355. ZnF_C2H2. 5 hits.
[Graphical view]
PROSITEiPS00028. ZINC_FINGER_C2H2_1. 1 hit.
PS50157. ZINC_FINGER_C2H2_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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."
    Nagase T., Nakayama M., Nakajima D., Kikuno R., Ohara O.
    DNA Res. 8:85-95(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    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.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Teratocarcinoma.
  3. "The DNA sequence and analysis of human chromosome 13."
    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.
    Nature 428:522-528(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Placenta and Skin.
  6. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-204; SER-217; SER-308; SER-319 AND SER-603, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. Cited for: 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  10. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-490, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Quantitative interaction proteomics and genome-wide profiling of epigenetic histone marks and their readers."
    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.
    Cell 142:967-980(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH POGZ; CBX1; CBX3 AND CBX5.
  12. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    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.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "CAMP (C13orf8, ZNF828) is a novel regulator of kinetochore-microtubule attachment."
    Itoh G., Kanno S., Uchida K.S., Chiba S., Sugino S., Watanabe K., Mizuno K., Yasui A., Hirota T., Tanaka K.
    EMBO J. 30:130-144(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, INTERACTION WITH MAD2L2, SUBCELLULAR LOCATION, PHOSPHORYLATION.
  15. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma and Erythroleukemia.
  18. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  19. "Uncovering global SUMOylation signaling networks in a site-specific manner."
    Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M., Vertegaal A.C.
    Nat. Struct. Mol. Biol. 21:927-936(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-670, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. Cited for: INVOLVEMENT IN MRD40.
  21. "SUMO-2 orchestrates chromatin modifiers in response to DNA damage."
    Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V., Vertegaal A.C.
    Cell Rep. 10:1778-1791(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-490, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  22. "Large-scale discovery of novel genetic causes of developmental disorders."
    Deciphering Developmental Disorders Study
    Nature 519:223-228(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN MRD40.

Entry informationi

Entry nameiCHAP1_HUMAN
AccessioniPrimary (citable) accession number: Q96JM3
Secondary accession number(s): B3KU06
, Q6P181, Q8NC88, Q9BST0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 5, 2006
Last sequence update: September 5, 2006
Last modified: July 6, 2016
This is version 120 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 13
    Human chromosome 13: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.