CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-030638
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Sarcoplasmic/endoplasmic reticulum calcium ATPase 1 
Protein Synonyms/Alias
 cDNA FLJ46599 fis, clone THYMU3047115, highly similar to Sarcoplasmic/endoplasmic reticulum calcium ATPase 1 (EC 3.6.3.8) 
Gene Name
 ATP2A1 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
80RAVNQDKKNMLFSGTubiquitination[1]
127DKTPLQQKLDEFGEQubiquitination[2]
356VIRQLMKKEFTLEFSubiquitination[3, 4]
390VGNKMFVKGAPEGVIubiquitination[2, 3, 4]
587VNDAPALKKAEIGIAubiquitination[5]
588NDAPALKKAEIGIAMubiquitination[4, 5, 6]
633RAIYNNMKQFIRYLIubiquitination[1, 2, 4, 5, 6, 7]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [4] 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]
 [5] 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]
 [6] 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]
 [7] 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
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
 869 AA 
Protein Sequence
MGKVYRADRK SVQRIKARDI VPGDIVEVAV GDKVPADIRI LAIKSTTLRV DQSILTGESV 60
SVIKHTEPVP DPRAVNQDKK NMLFSGTNIA AGKALGIVAT TGVGTEIGKI RDQMAATEQD 120
KTPLQQKLDE FGEQLSKVIS LICVAVWLIN IGHFNDPVHG GSWFRGAIYY FKIAVALAVA 180
AIPEGLPAVI TTCLALGTRR MAKKNAIVRS LPSVETLGCT SVICSDKTGT LTTNQMSVCK 240
MFIIDKVDGD ICLLNEFSIT GSTYAPEGEV LKNDKPVRPG QYDGLVELAT ICALCNDSSL 300
DFNEAKGVYE KVGEATETAL TTLVEKMNVF NTDVRSLSKV ERANACNSVI RQLMKKEFTL 360
EFSRDRKSMS VYCSPAKSSR AAVGNKMFVK GAPEGVIDRC NYVRVGTTRV PLTGPVKEKI 420
MAVIKEWGTG RDTLRCLALA TRDTPPKREE MVLDDSARFL EYETDLTFVG VVGMLDPPRK 480
EVTGSIQLCR DAGIRVIMIT GDNKGTAIAI CRRIGIFGEN EEVADRAYTG REFDDLPLAE 540
QREACRRACC FARVEPSHKS KIVEYLQSYD EITAMTGDGV NDAPALKKAE IGIAMGSGTA 600
VAKTASEMVL ADDNFSTIVA AVEEGRAIYN NMKQFIRYLI SSNVGEVVCI FLTAALGLPE 660
ALIPVQLLWV NLVTDGLPAT ALGFNPPDLD IMDRPPRSPK EPLISGWLFF RYMAIGGYVG 720
AATVGAAAWW FLYAEDGPHV NYSQLTHFMQ CTEDNTHFEG IDCEVFEAPE PMTMALSVLV 780
TIEMCNALNS LSENQSLLRM PPWVNIWLLG SICLSMSLHF LILYVDPLPM IFKLRALDLT 840
QWLMVLKISL PVIGLDEILK FVARNYLEG 869 
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
 IPR005782; ATPase_P-typ_Ca-transp_IIA.
 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
 PF08282; Hydrolase_3 
SMART
  
PROSITE
 PS00154; ATPASE_E1_E2 
PRINTS
 PR00119; CATATPASE.
 PR00120; HATPASE.