Javascript is not enabled on this browser. This site will not work properly without Javascript.
PhosphoSitePlus Homepage Cell Signaling Technology
PhosphoSitePlus
HomeAbout PhosphoSiteUsing PhosphoSiteCuration ProcessContact
NIH-logos NIGMS Logo NIAAA Logo NCI Logo NIH Logo
Protein Page:
ATP2C1 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
ATP2C1 This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of the calcium. Defects in ATP2C1 are the cause of Hailey-Hailey disease (HHD); also known as benign familial pemphigus. HHD is an autosomal dominant disorder characterized by persistent blisters and suprabasal cell separation (acantholysis) of the epidermis, due to impaired keratinocyte adhesion. Patients lacking all isoforms except isoform 2 have HHD. Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IIA subfamily. 6 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: Membrane protein, multi-pass; Transporter; Membrane protein, integral; EC 3.6.3.8; Transporter, ion channel; Hydrolase
Cellular Component: Golgi membrane; Golgi apparatus; membrane; integral to membrane; trans-Golgi network
Molecular Function: manganese-transporting ATPase activity; signal transducer activity; calcium-transporting ATPase activity; metal ion binding; manganese ion binding; calcium ion binding; ATP binding
Biological Process: cellular calcium ion homeostasis; Golgi calcium ion homeostasis; epidermis development; positive regulation of I-kappaB kinase/NF-kappaB cascade; metabolic process; calcium ion transport; actin cytoskeleton reorganization; calcium-dependent cell-cell adhesion; manganese ion transport; cellular manganese ion homeostasis; Golgi calcium ion transport; signal transduction; transmembrane transport
Reference #:  P98194 (UniProtKB)
Alt. Names/Synonyms: AT2C1; ATP-dependent Ca(2+) pump PMR1; ATP2C1; ATP2C1A; ATPase 2C1; ATPase, Ca(2+)-sequestering; ATPase, Ca++ transporting, type 2C, member 1; BCPM; Calcium-transporting ATPase type 2C member 1; HHD; hSPCA1; HUSSY-28; KIAA1347; PMR1; PMR1L; secretory pathway Ca2+/Mn2+ ATPase 1; SPCA1
Gene Symbols: ATP2C1
Molecular weight: 100,577 Da
Basal Isoelectric point: 6.34  Predict pI for various phosphorylation states
Select Structure to View Below

ATP2C1

Protein Structure Not Found.


STRING  |  Wikipedia  |  Reactome  |  neXtProt  |  Protein Atlas  |  BioGPS  |  DISEASE  |  Scansite  |  Pfam  |  ENZYME  |  Phospho.ELM  |  NetworKIN  |  UCSD-Nature  |  UniProtKB  |  Entrez-Gene  |  Ensembl Gene


Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

► Hide Isoforms
 
0 31 K8-ub MKVARFQkIPNGENE
0 2 K25-ub IPVLTSKkASELPVS
0 1 - gap
0 1 S182-p LFEAVDLsIDESSLT
0 1 K229 LVRCGKAKGVVIGTG
0 1 T235 AKGVVIGTGENSEFG
0 1 T315 EGLPIVVTVTLALGV
0 1 T317 LPIVVTVTLALGVMR
0 2 T420-p DAVIRNNtLMGkPtE
0 1 K424-ub RNNtLMGkPtEGALI
0 1 T426-p NtLMGkPtEGALIAL
0 1 Y452-p DYIRKAEyPFSSEQK
0 29 K496-ub YCTTYQSkGQTLTLT
0 4 K514-ub RDVYQQEkARMGSAG
0 2 T557-p TGVKEAVttLIASGV
0 2 T558-p GVKEAVttLIASGVS
0 1 S582-p ETAVAIAsRLGLYSk
0 1 K589-ub sRLGLYSkTSQSVSG
0 2 S608-p AMDVQQLsQIVPKVA
0 1 Y618-p VPKVAVFyRASPRHK
0 1 T804-p ELRDNVItPRDTTMT
0 1 S825-p FDMFNALssRSQTkS
0 1 S826-p DMFNALssRSQTkSV
0 4 K831-ub LssRSQTkSVFEIGL
0 2 K897-ac IVAEIIKkVERSREK
0 2 K907-ub RSREKIQkHVSSTss
0 1 S911 KIQkHVSSTssSFLE
0 1 S913-p QkHVSSTssSFLEV_
0 1 S914-p kHVSSTssSFLEV__
  ATP2C1 iso8  
- gap
- gap
S70-p LPVSEVAsILQFKNP
S177 LFEAVDLSIDESSLT
K224 LVRCGKAKGVVIGTG
T230 AKGVVIGTGENSEFG
T310 EGLPIVVTVTLALGV
T312 LPIVVTVTLALGVMR
T415 DAVIRNNTLMGKPTE
K419 RNNTLMGKPTEGALI
T421 NTLMGKPTEGALIAL
Y447 DYIRKAEYPFSSEQK
K491 YCTTYQSKGQTLTLT
K509 RDVYQQEKARMGSAG
T552 TGVKEAVTTLIASGV
T553 GVKEAVTTLIASGVS
S577 ETAVAIASRLGLYSK
K584 SRLGLYSKTSQSVSG
S603 AMDVQQLSQIVPKVA
Y613 VPKVAVFYRASPRHK
T799 ELRDNVITPRDTTMT
S820 FDMFNALSSRSQTKS
S821 DMFNALSSRSQTKSV
K826 LSSRSQTKSVFEIGL
K892 IVAEIIKKVERSREK
K902 RSREKIQKHVWLWER
- gap
- gap
- gap
  mouse

 
K8-ub MKVARFQkIPNVENE
R25 IPVLTSKRASELAVS
- gap
S182 LFEAVDLSVDESSLT
K228-ub LVRCGKAkGIVIGtG
T234-p AkGIVIGtGENSEFG
T314-p EGLPIVVtVtLALGV
T316-p LPIVVtVtLALGVMR
T419-p DAVIRNNtLMGKPTE
K423 RNNtLMGKPTEGALI
T425 NtLMGKPTEGALIAL
Y451 DYIRKAEYPFSSEQK
K495-ub YCTTYNSkGQTLALT
K513 RDLYQQEKARMGSAG
T556-p TGVKEAVttLIASGV
T557-p GVKEAVttLIASGVS
S581 ETAIAIASRLGLYSK
K588 SRLGLYSKTSQSVSG
S607 TMEVQHLSQIVPKVA
Y617 VPKVAVFYRASPRHK
T803 ELRDNVITPRDTTMT
S824 FDMFNALSSRSQTKS
S825 DMFNALSSRSQTKSV
K830 LSSRSQTKSVFEIGL
K896 IVSEIIKKVERSREK
K906-ub RSREKVQkNAGsASS
S910-p KVQkNAGsASSSFLE
S912 QkNAGsASSSFLEV_
S913 kNAGsASSSFLEV__
Home  |  Curator Login With enhanced literature mining using Linguamatics I2E I2E Logo Produced by 3rd Millennium  |  Design by Digizyme
©2003-2013 Cell Signaling Technology, Inc.