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Protein

Caspase activity and apoptosis inhibitor 1

Gene

CAAP1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Anti-apoptotic protein that modulates a caspase-10 dependent mitochondrial caspase-3/9 feedback amplification loop.1 Publication

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Apoptosis

Names & Taxonomyi

Protein namesi
Recommended name:
Caspase activity and apoptosis inhibitor 1
Alternative name(s):
Conserved anti-apoptotic protein
Short name:
CAAP
Gene namesi
Name:CAAP1
Synonyms:C9orf82, CAAP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:25834. CAAP1.

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134943744.

Polymorphism and mutation databases

BioMutaiCAAP1.
DMDMi68565300.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 361361Caspase activity and apoptosis inhibitor 1PRO_0000089717Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei120 – 1201PhosphoserineCombined sources
Modified residuei203 – 2031PhosphoserineCombined sources
Modified residuei312 – 3121PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9H8G2.
MaxQBiQ9H8G2.
PaxDbiQ9H8G2.
PRIDEiQ9H8G2.

PTM databases

iPTMnetiQ9H8G2.
PhosphoSiteiQ9H8G2.

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Gene expression databases

BgeeiQ9H8G2.
CleanExiHS_C9orf82.
ExpressionAtlasiQ9H8G2. baseline and differential.
GenevisibleiQ9H8G2. HS.

Organism-specific databases

HPAiHPA020404.
HPA024029.
HPA024100.

Interactioni

Protein-protein interaction databases

BioGridi122971. 10 interactions.
IntActiQ9H8G2. 5 interactions.
STRINGi9606.ENSP00000369431.

Structurei

3D structure databases

ProteinModelPortaliQ9H8G2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili281 – 31131Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi19 – 257Poly-Ala

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG410IEVC. Eukaryota.
ENOG4111MJZ. LUCA.
GeneTreeiENSGT00390000017010.
HOGENOMiHOG000111649.
HOVERGENiHBG054538.
InParanoidiQ9H8G2.
OMAiKRSGQEA.
OrthoDBiEOG7FJH1H.
PhylomeDBiQ9H8G2.
TreeFamiTF332850.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9H8G2-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MTGKKSSREK RRKRSSQEAA AALAAPDIVP ALASGSSGST SGCGSAGGCG
60 70 80 90 100
SVSCCGNANF SGSVTGGGSG GSCWGGSSVE RSERRKRRST DSSSVSGSLQ
110 120 130 140 150
QETKYILPTL EKELFLAEHS DLEEGGLDLT VSLKPVSFYI SDKKEMLQQC
160 170 180 190 200
FCIIGEKKLQ KMLPDVLKNC SIEEIKKLCQ EQLELLSEKK ILKILEGDNG
210 220 230 240 250
MDSDMEEEAD DGSKMGSDLV SQQDICIDSA SSVRENKQPE GLELKQGKGE
260 270 280 290 300
DSDVLSINAD AYDSDIEGPC NEEAAAPEAP ENTVQSEAGQ IDDLEKDIEK
310 320 330 340 350
SVNEILGLAE SSPNEPKAAT LAVPPPEDVQ PSAQQLELLE LEMRARAIKA
360
LMKAGDIKKP A
Length:361
Mass (Da):38,368
Last modified:July 5, 2005 - v2
Checksum:iF04D8734436C0072
GO
Isoform 2 (identifier: Q9H8G2-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-145: Missing.

Show »
Length:216
Mass (Da):23,511
Checksum:iE6535352FC2FC0BF
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti34 – 341S → G in BAB14655 (PubMed:14702039).Curated
Sequence conflicti188 – 1881E → K in AAH14658 (PubMed:15489334).Curated
Sequence conflicti292 – 2921D → N in AAH71953 (PubMed:15489334).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti233 – 2331V → M.
Corresponds to variant rs12342214 [ dbSNP | Ensembl ].
VAR_056818

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 145145Missing in isoform 2. 1 PublicationVSP_044253Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK023719 mRNA. Translation: BAB14655.1.
AK301673 mRNA. Translation: BAG63146.1.
AL356133 Genomic DNA. Translation: CAH72640.1.
CH471071 Genomic DNA. Translation: EAW58576.1.
CH471071 Genomic DNA. Translation: EAW58577.1.
BC014658 mRNA. Translation: AAH14658.1.
BC071953 mRNA. Translation: AAH71953.1.
CCDSiCCDS55299.1. [Q9H8G2-2]
CCDS6516.1. [Q9H8G2-1]
RefSeqiNP_001161047.1. NM_001167575.1. [Q9H8G2-2]
NP_079104.3. NM_024828.3. [Q9H8G2-1]
UniGeneiHs.178357.

Genome annotation databases

EnsembliENST00000333916; ENSP00000369431; ENSG00000120159. [Q9H8G2-1]
ENST00000625311; ENSP00000487373; ENSG00000120159. [Q9H8G2-2]
GeneIDi79886.
KEGGihsa:79886.
UCSCiuc003zqc.4. human. [Q9H8G2-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK023719 mRNA. Translation: BAB14655.1.
AK301673 mRNA. Translation: BAG63146.1.
AL356133 Genomic DNA. Translation: CAH72640.1.
CH471071 Genomic DNA. Translation: EAW58576.1.
CH471071 Genomic DNA. Translation: EAW58577.1.
BC014658 mRNA. Translation: AAH14658.1.
BC071953 mRNA. Translation: AAH71953.1.
CCDSiCCDS55299.1. [Q9H8G2-2]
CCDS6516.1. [Q9H8G2-1]
RefSeqiNP_001161047.1. NM_001167575.1. [Q9H8G2-2]
NP_079104.3. NM_024828.3. [Q9H8G2-1]
UniGeneiHs.178357.

3D structure databases

ProteinModelPortaliQ9H8G2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi122971. 10 interactions.
IntActiQ9H8G2. 5 interactions.
STRINGi9606.ENSP00000369431.

PTM databases

iPTMnetiQ9H8G2.
PhosphoSiteiQ9H8G2.

Polymorphism and mutation databases

BioMutaiCAAP1.
DMDMi68565300.

Proteomic databases

EPDiQ9H8G2.
MaxQBiQ9H8G2.
PaxDbiQ9H8G2.
PRIDEiQ9H8G2.

Protocols and materials databases

DNASUi79886.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000333916; ENSP00000369431; ENSG00000120159. [Q9H8G2-1]
ENST00000625311; ENSP00000487373; ENSG00000120159. [Q9H8G2-2]
GeneIDi79886.
KEGGihsa:79886.
UCSCiuc003zqc.4. human. [Q9H8G2-1]

Organism-specific databases

CTDi79886.
GeneCardsiCAAP1.
H-InvDBHIX0201356.
HGNCiHGNC:25834. CAAP1.
HPAiHPA020404.
HPA024029.
HPA024100.
neXtProtiNX_Q9H8G2.
PharmGKBiPA134943744.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IEVC. Eukaryota.
ENOG4111MJZ. LUCA.
GeneTreeiENSGT00390000017010.
HOGENOMiHOG000111649.
HOVERGENiHBG054538.
InParanoidiQ9H8G2.
OMAiKRSGQEA.
OrthoDBiEOG7FJH1H.
PhylomeDBiQ9H8G2.
TreeFamiTF332850.

Miscellaneous databases

GeneWikiiC9orf82.
GenomeRNAii79886.
PROiQ9H8G2.

Gene expression databases

BgeeiQ9H8G2.
CleanExiHS_C9orf82.
ExpressionAtlasiQ9H8G2. baseline and differential.
GenevisibleiQ9H8G2. HS.

Family and domain databases

ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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] (ISOFORMS 1 AND 2).
    Tissue: Esophagus and Placenta.
  2. "DNA sequence and analysis of human chromosome 9."
    Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
    , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
    Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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] (ISOFORM 1).
    Tissue: Brain and Eye.
  5. "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-203, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  6. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  8. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203 AND SER-312, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
    Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
    Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  11. "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].
  12. "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-203 AND SER-312, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  13. "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-203 AND SER-312, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. "Identification of a conserved anti-apoptotic protein that modulates the mitochondrial apoptosis pathway."
    Zhang Y., Johansson E., Miller M.L., Janicke R.U., Ferguson D.J., Plas D., Meller J., Anderson M.W.
    PLoS ONE 6:E25284-E25284(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY.
  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-203 AND SER-312, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "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-120; SER-203 AND SER-312, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiCAAP1_HUMAN
AccessioniPrimary (citable) accession number: Q9H8G2
Secondary accession number(s): B4DWT4
, D3DRK4, Q5VY32, Q6IPE6, Q96C59
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: July 5, 2005
Last modified: June 8, 2016
This is version 103 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 9
    Human chromosome 9: 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

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.