CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-022527
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Probable phospholipid-transporting ATPase VD 
Protein Synonyms/Alias
 ATPase class V type 10D 
Gene Name
 ATP10D 
Gene Synonyms/Alias
 ATPVD; KIAA1487 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
626IKSLEEIKSLFQRWSacetylation[1]
942KLLEPDDKLFILNTQubiquitination[2, 3]
Reference
 [1] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786]
 [2] 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]
 [3] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965] 
Functional Description
  
Sequence Annotation
 NP_BIND 996 1003 ATP (Potential).
 NP_BIND 1364 1371 ATP (Potential).
 ACT_SITE 438 438 4-aspartylphosphate intermediate (By
 METAL 1056 1056 Magnesium (By similarity).
 METAL 1060 1060 Magnesium (By similarity).  
Keyword
 Alternative splicing; ATP-binding; Cell membrane; Complete proteome; Endoplasmic reticulum; Hydrolase; Magnesium; Membrane; Metal-binding; Nucleotide-binding; Polymorphism; Reference proteome; Transmembrane; Transmembrane helix. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1426 AA 
Protein Sequence
MTEALQWARY HWRRLIRGAT RDDDSGPYNY SSLLACGRKS SQTPKLSGRH RIVVPHIQPF 60
KDEYEKFSGA YVNNRIRTTK YTLLNFVPRN LFEQFHRAAN LYFLFLVVLN WVPLVEAFQK 120
EITMLPLVVV LTIIAIKDGL EDYRKYKIDK QINNLITKVY SRKEKKYIDR CWKDVTVGDF 180
IRLSCNEVIP ADMVLLFSTD PDGICHIETS GLDGESNLKQ RQVVRGYAEQ DSEVDPEKFS 240
SRIECESPNN DLSRFRGFLE HSNKERVGLS KENLLLRGCT IRNTEAVVGI VVYAGHETKA 300
MLNNSGPRYK RSKLERRANT DVLWCVMLLV IMCLTGAVGH GIWLSRYEKM HFFNVPEPDG 360
HIISPLLAGF YMFWTMIILL QVLIPISLYV SIEIVKLGQI YFIQSDVDFY NEKMDSIVQC 420
RALNIAEDLG QIQYLFSDKT GTLTENKMVF RRCSVAGFDY CHEENARRLE SYQEAVSEDE 480
DFIDTVSGSL SNMAKPRAPS CRTVHNGPLG NKPSNHLAGS SFTLGSGEGA SEVPHSRQAA 540
FSSPIETDVV PDTRLLDKFS QITPRLFMPL DETIQNPPME TLYIIDFFIA LAICNTVVVS 600
APNQPRQKIR HPSLGGLPIK SLEEIKSLFQ RWSVRRSSSP SLNSGKEPSS GVPNAFVSRL 660
PLFSRMKPAS PVEEEVSQVC ESPQCSSSSA CCTETEKQHG DAGLLNGKAE SLPGQPLACN 720
LCYEAESPDE AALVYAARAY QCTLRSRTPE QVMVDFAALG PLTFQLLHIL PFDSVRKRMS 780
VVVRHPLSNQ VVVYTKGADS VIMELLSVAS PDGASLEKQQ MIVREKTQKH LDDYAKQGLR 840
TLCIAKKVMS DTEYAEWLRN HFLAETSIDN REELLLESAM RLENKLTLLG ATGIEDRLQE 900
GVPESIEALH KAGIKIWMLT GDKQETAVNI AYACKLLEPD DKLFILNTQS KDACGMLMST 960
ILKELQKKTQ ALPEQVSLSE DLLQPPVPRD SGLRAGLIIT GKTLEFALQE SLQKQFLELT 1020
SWCQAVVCCR ATPLQKSEVV KLVRSHLQVM TLAIGDGAND VSMIQVADIG IGVSGQEGMQ 1080
AVMASDFAVS QFKHLSKLLL VHGHWCYTRL SNMILYFFYK NVAYVNLLFW YQFFCGFSGT 1140
SMTDYWVLIF FNLLFTSAPP VIYGVLEKDV SAETLMQLPE LYRSGQKSEA YLPHTFWITL 1200
LDAFYQSLVC FFVPYFTYQG SDTDIFAFGN PLNTAALFIV LLHLVIESKS LTWIHLLVII 1260
GSILSYFLFA IVFGAMCVTC NPPSNPYWIM QEHMLDPVFY LVCILTTSIA LLPRFVYRVL 1320
QGSLFPSPIL RAKHFDRLTP EERTKALKKW RGAGKMNQVT SKYANQSAGK SGRRPMPGPS 1380
AVFAMKSASS CAIEQGNLSL CETALDQGYS ETKAFEMAGP SKGKES 1426 
Gene Ontology
 GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
 GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
 GO:0016021; C:integral to membrane; NAS:UniProtKB.
 GO:0005886; C:plasma membrane; TAS:Reactome.
 GO:0005524; F:ATP binding; NAS:UniProtKB.
 GO:0019829; F:cation-transporting ATPase activity; IEA:InterPro.
 GO:0000287; F:magnesium ion binding; NAS:UniProtKB.
 GO:0004012; F:phospholipid-translocating ATPase activity; NAS:UniProtKB.
 GO:0006812; P:cation transport; NAS:UniProtKB.
 GO:0034220; P:ion transmembrane transport; TAS:Reactome.
 GO:0045332; P:phospholipid translocation; NAS:UniProtKB. 
Interpro
 IPR023299; ATPase_P-typ_cyto_domN.
 IPR018303; ATPase_P-typ_P_site.
 IPR006539; ATPase_P-typ_Plipid-transp.
 IPR008250; ATPase_P-typ_transduc_dom_A.
 IPR001757; Cation_transp_P_typ_ATPase.
 IPR023214; HAD-like_dom. 
Pfam
 PF00122; E1-E2_ATPase 
SMART
  
PROSITE
 PS00154; ATPASE_E1_E2 
PRINTS
 PR00119; CATATPASE.