CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-036987
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 Calcium-transporting ATPase type 2C member 1 
Protein Synonyms/Alias
  
Gene Name
 ATP2C1 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
91CHCVREGKLEHTLARubiquitination[1]
174LVRCGKAKGVVIGTGubiquitination[2]
369RNNTLMGKPTEGALIubiquitination[1]
394LQQDYIRKAEYPFSSubiquitination[1]
441YCTTYQSKGQTLTLTubiquitination[1, 2, 3, 4, 5, 6, 7]
459RDVYQQEKARMGSAGubiquitination[1, 4]
534SRLGLYSKTSQSVSGubiquitination[2, 4, 5]
579KIIKSLQKNGSVVAMubiquitination[1]
776LSSRSQTKSVFEIGLubiquitination[4, 7]
852RSREKIQKHVSSTSSubiquitination[3]
Reference
 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [2] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [3] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [4] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [5] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [6] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [7] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302
Functional Description
  
Sequence Annotation
  
Keyword
 ATP-binding; Complete proteome; Hydrolase; Membrane; Nucleotide-binding; Reference proteome; Transmembrane; Transmembrane helix. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 894 AA 
Protein Sequence
MIPVLTSKKA SELPVSEVAS ILQFKNPLIM LLLASAVISV LMHQFDDAVS ITVAILIVVT 60
VAFVQEYRSE KSLEELSKLV PPECHCVREG KLEHTLARDL VPGDTVCLSV GDRVPADLRL 120
FEAVDLSIDE SSLTGETTPC SKVTAPQPAA TNGDLASRSN IAFMGTLVRC GKAKGVVIGT 180
GENSEFGEVF KMMQAEEAPK TPLQKSMDLL GKQLSFYSFG IIGIIMLVGW LLGKDILEMF 240
TISVSLAVAA IPEGLPIVVT VTLALGVMRM VKKRAIVKKL PIVETLGCCN VICSDKTGTL 300
TKNEMTVTHI FTSDGLHAEV TGVGYNQFGE VIVDGDVVHG FYNPAVSRIV EAGCVCNDAV 360
IRNNTLMGKP TEGALIALAM KMGLDGLQQD YIRKAEYPFS SEQKWMAVKC VHRTQQDRPE 420
ICFMKGAYEQ VIKYCTTYQS KGQTLTLTQQ QRDVYQQEKA RMGSAGLRVL ALASGPELGQ 480
LTFLGLVGII DPPRTGVKEA VTTLIASGVS IKMITGDSQE TAVAIASRLG LYSKTSQSVS 540
GEEIDAMDVQ QLSQIVPKVA VFYRASPRHK MKIIKSLQKN GSVVAMTGDG VNDAVALKAA 600
DIGVAMGQTG TDVCKEAADM ILVDDDFQTI MSAIEEGKGI YNNIKNFVRF QLSTSIAALT 660
LISLATLMNF PNPLNAMQIL WINIIMDGPP AQSLGVEPVD KDVIRKPPRN WKDSILTKNL 720
ILKILVSSII IVCGTLFVFW RELRDNVITP RDTTMTFTCF VFFDMFNALS SRSQTKSVFE 780
IGLCSNRMFC YAVLGSIMGQ LLVIYFPPLQ KVFQTESLSI LDLLFLLGLT SSVCIVAEII 840
KKVERSREKI QKHVSSTSSS FLEVWLWERS GQQLVEIHPH LETGLPLTED VSCV 894 
Gene Ontology
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0005388; F:calcium-transporting ATPase activity; IEA:InterPro.
 GO:0046872; F:metal ion binding; IEA:InterPro. 
Interpro
 IPR006413; ATPase_P-typ_Ca-transp_PMR1.
 IPR006068; ATPase_P-typ_cation-transptr_C.
 IPR023299; ATPase_P-typ_cyto_domN.
 IPR018303; ATPase_P-typ_P_site.
 IPR023298; ATPase_P-typ_TM_dom.
 IPR008250; ATPase_P-typ_transduc_dom_A.
 IPR001757; Cation_transp_P_typ_ATPase.
 IPR023214; HAD-like_dom. 
Pfam
 PF00689; Cation_ATPase_C
 PF00122; E1-E2_ATPase
 PF00702; Hydrolase 
SMART
  
PROSITE
 PS00154; ATPASE_E1_E2 
PRINTS
 PR00119; CATATPASE.
 PR00120; HATPASE.