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P98194 (AT2C1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 150. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Calcium-transporting ATPase type 2C member 1

Short name=ATPase 2C1
EC=3.6.3.8
Alternative name(s):
ATP-dependent Ca(2+) pump PMR1
Gene names
Name:ATP2C1
Synonyms:KIAA1347, PMR1L
ORF Names:HUSSY-28
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length919 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of the calcium.

Catalytic activity

ATP + H2O + Ca2+(Side 1) = ADP + phosphate + Ca2+(Side 2).

Subcellular location

Golgi apparatus membrane; Multi-pass membrane protein Ref.3.

Tissue specificity

Found in most tissues except colon, thymus, spleen and leukocytes. Most abundant in keratinocytes and kidney.

Involvement in disease

Hailey-Hailey disease (HHD) [MIM:169600]: 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.1 Ref.2 Ref.12 Ref.13

Sequence similarities

Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IIA subfamily. [View classification]

Sequence caution

The sequence BAA92585.1 differs from that shown. Reason: Frameshift at position 8.

The sequence BAC11142.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processCalcium transport
Ion transport
Transport
   Cellular componentGolgi apparatus
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
   DomainTransmembrane
Transmembrane helix
   LigandATP-binding
Calcium
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionHydrolase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processGolgi calcium ion homeostasis

Inferred from mutant phenotype PubMed 14632183. Source: UniProtKB

Golgi calcium ion transport

Inferred from mutant phenotype PubMed 14632183. Source: UniProtKB

actin cytoskeleton reorganization

Inferred from mutant phenotype PubMed 14632182. Source: UniProtKB

calcium ion transmembrane transport

Inferred from direct assay PubMed 12810057PubMed 16192278PubMed 16192278Ref.3PubMed 16192278. Source: GOC

calcium ion transport

Inferred from direct assay PubMed 12810057PubMed 16192278PubMed 16192278Ref.3PubMed 16192278. Source: UniProtKB

calcium-dependent cell-cell adhesion

Inferred from mutant phenotype PubMed 14632182. Source: UniProtKB

cellular calcium ion homeostasis

Inferred from direct assay PubMed 12810057Ref.3. Source: UniProtKB

cellular manganese ion homeostasis

Inferred from direct assay Ref.3. Source: UniProtKB

epidermis development

Inferred from mutant phenotype Ref.1. Source: UniProtKB

ion transmembrane transport

Traceable author statement. Source: Reactome

manganese ion transmembrane transport

Inferred from direct assay Ref.3. Source: GOC

manganese ion transport

Inferred from direct assay Ref.3. Source: UniProtKB

positive regulation of I-kappaB kinase/NF-kappaB signaling

Inferred from mutant phenotype PubMed 12761501. Source: UniProtKB

signal transduction

Inferred from mutant phenotype PubMed 12761501. Source: GOC

transmembrane transport

Traceable author statement. Source: Reactome

   Cellular_componentGolgi apparatus

Inferred from direct assay PubMed 11741891Ref.3. Source: UniProtKB

Golgi membrane

Inferred from direct assay PubMed 12804581. Source: UniProtKB

integral component of membrane

Non-traceable author statement Ref.1. Source: UniProtKB

trans-Golgi network

Inferred from direct assay PubMed 14632183. Source: UniProtKB

   Molecular_functionATP binding

Inferred from direct assay PubMed 16192278PubMed 16192278Ref.3PubMed 16192278. Source: UniProtKB

calcium ion binding

Inferred from direct assay PubMed 16192278PubMed 16192278Ref.3PubMed 16192278. Source: UniProtKB

calcium-transporting ATPase activity

Inferred from direct assay PubMed 12810057PubMed 16192278PubMed 16192278Ref.3PubMed 16192278. Source: UniProtKB

manganese ion binding

Inferred from direct assay Ref.3. Source: UniProtKB

manganese-transporting ATPase activity

Inferred from direct assay Ref.3. Source: UniProtKB

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

signal transducer activity

Inferred from mutant phenotype PubMed 12761501. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 8 isoforms produced by alternative splicing. [Align] [Select]

Note: Isoform 1 and isoform 2 are expressed in the same tissues.
Isoform 1 (identifier: P98194-1)

Also known as: ATP2C1A;

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.
Isoform 2 (identifier: P98194-2)

Also known as: ATP2C1B; ATP2C1C;

The sequence of this isoform differs from the canonical sequence as follows:
     877-919: DLLFLLGLTSSVCIVAEIIKKVERSREKIQKHVSSTSSSFLEV → GLALGEEWTAAG
Isoform 3 (identifier: P98194-3)

Also known as: ATP2C1B;

The sequence of this isoform differs from the canonical sequence as follows:
     1-16: Missing.
     910-919: SSTSSSFLEV → WLWERSGQQLVEIHPHLETGLPLTEDVSCV
Isoform 4 (identifier: P98194-4)

Also known as: ATP2C1A;

The sequence of this isoform differs from the canonical sequence as follows:
     1-16: Missing.
Isoform 5 (identifier: P98194-5)

Also known as: ATP2C1B;

The sequence of this isoform differs from the canonical sequence as follows:
     910-919: SSTSSSFLEV → WLWERSGQQLVEIHPHLETGLPLTEDVSCV
Isoform 6 (identifier: P98194-6)

Also known as: ATP2C1D;

The sequence of this isoform differs from the canonical sequence as follows:
     919-919: V → VSSTSSSFLEVWLWERSGQQLVEIHPHLETGLPLTEDVSCV
Isoform 7 (identifier: P98194-7)

The sequence of this isoform differs from the canonical sequence as follows:
     1-2: MK → MDSLLPPSRFSYFKKYPLHAIRRYLSTLRNQRAEEQ
     910-919: SSTSSSFLEV → WLWERSGQQLVEIHPHLETGLPLTEDVSCV
Note: No experimental confirmation available.
Isoform 8 (identifier: P98194-8)

The sequence of this isoform differs from the canonical sequence as follows:
     1-2: MK → MDSLLPPSRFSYFKKYPLHAIRRYLSTLRNQRAEEQ
     39-77: Missing.
     910-919: SSTSSSFLEV → WLWERSGQQLVEIHPHLETGLPLTEDVSCV
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 919919Calcium-transporting ATPase type 2C member 1
PRO_0000046223

Regions

Topological domain1 – 7070Cytoplasmic By similarity
Transmembrane71 – 9121Helical; Name=1; By similarity
Topological domain92 – 10413Lumenal By similarity
Transmembrane105 – 12319Helical; Name=2; By similarity
Topological domain124 – 262139Cytoplasmic By similarity
Transmembrane263 – 28220Helical; Name=3; By similarity
Topological domain283 – 29412Lumenal By similarity
Transmembrane295 – 31218Helical; Name=4; By similarity
Topological domain313 – 699387Cytoplasmic By similarity
Transmembrane700 – 71920Helical; Name=5; By similarity
Topological domain720 – 72910Lumenal By similarity
Transmembrane730 – 75021Helical; Name=6; By similarity
Topological domain751 – 77020Cytoplasmic By similarity
Transmembrane771 – 79323Helical; Name=7; By similarity
Topological domain794 – 80815Lumenal By similarity
Transmembrane809 – 82820Helical; Name=8; By similarity
Topological domain829 – 84113Cytoplasmic By similarity
Transmembrane842 – 86019Helical; Name=9; By similarity
Topological domain861 – 87515Lumenal By similarity
Transmembrane876 – 89621Helical; Name=10; By similarity
Topological domain897 – 91923Cytoplasmic By similarity

Sites

Active site35014-aspartylphosphate intermediate By similarity
Metal binding3031Calcium 2; via carbonyl oxygen By similarity
Metal binding3041Calcium 2; via carbonyl oxygen By similarity
Metal binding3061Calcium 2; via carbonyl oxygen By similarity
Metal binding3081Calcium 2 By similarity
Metal binding6441Magnesium By similarity
Metal binding6481Magnesium By similarity
Metal binding7381Calcium 2 By similarity
Metal binding7421Calcium 2 By similarity

Natural variations

Alternative sequence1 – 1616Missing in isoform 3 and isoform 4.
VSP_000408
Alternative sequence1 – 22MK → MDSLLPPSRFSYFKKYPLHA IRRYLSTLRNQRAEEQ in isoform 7 and isoform 8.
VSP_045892
Alternative sequence39 – 7739Missing in isoform 8.
VSP_045893
Alternative sequence877 – 91943DLLFL…SFLEV → GLALGEEWTAAG in isoform 2.
VSP_000409
Alternative sequence910 – 91910SSTSSSFLEV → WLWERSGQQLVEIHPHLETG LPLTEDVSCV in isoform 3, isoform 5, isoform 7 and isoform 8.
VSP_000410
Alternative sequence9191V → VSSTSSSFLEVWLWERSGQQ LVEIHPHLETGLPLTEDVSC V in isoform 6.
VSP_014102
Natural variant2011P → L in HHD. Ref.2
VAR_010130
Natural variant3041A → T in HHD. Ref.1
VAR_008803
Natural variant3091G → C in HHD; unable to bind manganese, reduced affinity for calcium. Ref.12
VAR_022672
Natural variant3181L → P in HHD. Ref.1
VAR_008804
Natural variant3411L → P in HHD; unstable protein. Ref.12
VAR_022673
Natural variant3441C → Y in HHD; unstable protein. Ref.2
VAR_010131
Natural variant4111C → R in HHD; unstable protein. Ref.12
VAR_022674
Natural variant4501A → T.
Corresponds to variant rs41434650 [ dbSNP | Ensembl ].
VAR_048373
Natural variant4901C → F in HHD. Ref.13
VAR_019523
Natural variant5701T → I in HHD; unstable protein. Ref.2
VAR_010132
Natural variant5801I → V in HHD; unable to undergo conformational change necessary for ion transport. Ref.12
VAR_022675
Natural variant5841L → P in HHD. Ref.13
VAR_019524
Natural variant6411M → R in HHD. Ref.1
VAR_008805
Natural variant6451G → R in HHD. Ref.1
VAR_008806
Natural variant7091T → M in HHD. Ref.1
VAR_008807
Natural variant7421D → Y in HHD; unable to bind calcium or manganese. Ref.12
VAR_022676
Natural variant7441P → R in HHD. Ref.1
VAR_008808
Natural variant7891G → R in HHD; unstable protein. Ref.12
VAR_022677

Experimental info

Sequence conflict621E → K in AAF26295. Ref.1
Sequence conflict621E → K in AAF26296. Ref.1
Sequence conflict1121I → F in AAF35375. Ref.2
Sequence conflict1501T → I in BAC11142. Ref.5
Sequence conflict3461V → A in BAH12365. Ref.5
Sequence conflict3731A → T in AAF26295. Ref.1
Sequence conflict3731A → T in AAF26296. Ref.1
Sequence conflict5161R → H in CAA09425. Ref.9
Sequence conflict7131A → T in BAC11142. Ref.5
Sequence conflict8681F → L in BAG61775. Ref.5
Sequence conflict9011S → G in BAC11142. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (ATP2C1A) [UniParc].

Last modified June 21, 2005. Version 3.
Checksum: 4C1495D58FDA7EA1

FASTA919100,577
        10         20         30         40         50         60 
MKVARFQKIP NGENETMIPV LTSKKASELP VSEVASILQA DLQNGLNKCE VSHRRAFHGW 

        70         80         90        100        110        120 
NEFDISEDEP LWKKYISQFK NPLIMLLLAS AVISVLMHQF DDAVSITVAI LIVVTVAFVQ 

       130        140        150        160        170        180 
EYRSEKSLEE LSKLVPPECH CVREGKLEHT LARDLVPGDT VCLSVGDRVP ADLRLFEAVD 

       190        200        210        220        230        240 
LSIDESSLTG ETTPCSKVTA PQPAATNGDL ASRSNIAFMG TLVRCGKAKG VVIGTGENSE 

       250        260        270        280        290        300 
FGEVFKMMQA EEAPKTPLQK SMDLLGKQLS FYSFGIIGII MLVGWLLGKD ILEMFTISVS 

       310        320        330        340        350        360 
LAVAAIPEGL PIVVTVTLAL GVMRMVKKRA IVKKLPIVET LGCCNVICSD KTGTLTKNEM 

       370        380        390        400        410        420 
TVTHIFTSDG LHAEVTGVGY NQFGEVIVDG DVVHGFYNPA VSRIVEAGCV CNDAVIRNNT 

       430        440        450        460        470        480 
LMGKPTEGAL IALAMKMGLD GLQQDYIRKA EYPFSSEQKW MAVKCVHRTQ QDRPEICFMK 

       490        500        510        520        530        540 
GAYEQVIKYC TTYQSKGQTL TLTQQQRDVY QQEKARMGSA GLRVLALASG PELGQLTFLG 

       550        560        570        580        590        600 
LVGIIDPPRT GVKEAVTTLI ASGVSIKMIT GDSQETAVAI ASRLGLYSKT SQSVSGEEID 

       610        620        630        640        650        660 
AMDVQQLSQI VPKVAVFYRA SPRHKMKIIK SLQKNGSVVA MTGDGVNDAV ALKAADIGVA 

       670        680        690        700        710        720 
MGQTGTDVCK EAADMILVDD DFQTIMSAIE EGKGIYNNIK NFVRFQLSTS IAALTLISLA 

       730        740        750        760        770        780 
TLMNFPNPLN AMQILWINII MDGPPAQSLG VEPVDKDVIR KPPRNWKDSI LTKNLILKIL 

       790        800        810        820        830        840 
VSSIIIVCGT LFVFWRELRD NVITPRDTTM TFTCFVFFDM FNALSSRSQT KSVFEIGLCS 

       850        860        870        880        890        900 
NRMFCYAVLG SIMGQLLVIY FPPLQKVFQT ESLSILDLLF LLGLTSSVCI VAEIIKKVER 

       910 
SREKIQKHVS STSSSFLEV 

« Hide

Isoform 2 (ATP2C1B) (ATP2C1C) [UniParc].

Checksum: 27E2B0E13378BB98
Show »

FASTA88896,960
Isoform 3 (ATP2C1B) [UniParc].

Checksum: A7962E652B936D76
Show »

FASTA923101,163
Isoform 4 (ATP2C1A) [UniParc].

Checksum: D15118E067B15ED4
Show »

FASTA90398,733
Isoform 5 (ATP2C1B) [UniParc].

Checksum: E6B6914D20DFD0B7
Show »

FASTA939103,007
Isoform 6 (ATP2C1D) [UniParc].

Checksum: C25B54ABDE014607
Show »

FASTA959105,057
Isoform 7 [UniParc].

Checksum: 0AC81DFDBA5DAB98
Show »

FASTA973107,143
Isoform 8 [UniParc].

Checksum: CAA887F3AEB7C056
Show »

FASTA934102,499

References

« Hide 'large scale' references
[1]"Mutations in ATP2C1, encoding a calcium pump, cause Hailey-Hailey disease."
Hu Z., Bonifas J.M., Beech J., Bench G., Shigihara T., Ogawa H., Ikeda S., Mauro T., Epstein E.H. Jr.
Nat. Genet. 24:61-65(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), VARIANTS HHD THR-304; PRO-318; ARG-641; ARG-645; MET-709 AND ARG-744.
[2]"Hailey-Hailey disease is caused by mutations in ATP2C1 encoding a novel Ca(2+) pump."
Sudbrak R., Brown J., Dobson-Stone C., Carter S., Ramser J., White J., Healy E., Dissanayake M., Larregue M., Perrussel M., Lehrach H., Munro C.S., Strachan T., Burge S., Hovnanian A., Monaco A.P.
Hum. Mol. Genet. 9:1131-1140(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4), VARIANTS HHD LEU-201; TYR-344 AND ILE-570.
Tissue: Keratinocyte.
[3]"Effect of Hailey-Hailey Disease mutations on the function of a new variant of human secretory pathway Ca2+/Mn2+-ATPase (hSPCA1)."
Fairclough R.J., Dode L., Vanoevelen J., Andersen J.P., Missiaen L., Raeymaekers L., Wuytack F., Hovnanian A.
J. Biol. Chem. 278:24721-24730(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 5 AND 6), SUBCELLULAR LOCATION, MUTAGENESIS.
Tissue: Keratinocyte.
[4]"Prediction of the coding sequences of unidentified human genes. XVI. The complete sequences of 150 new cDNA clones from brain which code for large proteins in vitro."
Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.
DNA Res. 7:65-73(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Brain.
[5]"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. expand/collapse author list , 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; 6; 7 AND 8), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 360-919 (ISOFORM 1).
Tissue: Mammary gland, Neuron and Thalamus.
[6]"The DNA sequence, annotation and analysis of human chromosome 3."
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J. expand/collapse author list , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"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 2).
Tissue: Blood.
[9]"Characterization of 16 novel human genes showing high similarity to yeast sequences."
Stanchi F., Bertocco E., Toppo S., Dioguardi R., Simionati B., Cannata N., Zimbello R., Lanfranchi G., Valle G.
Yeast 18:69-80(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 424-919.
[10]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"Hailey-Hailey disease: molecular and clinical characterization of novel mutations in the ATP2C1 gene."
Dobson-Stone C., Fairclough R., Dunne E., Brown J., Dissanayake M., Munro C.S., Strachan T., Burge S., Sudbrak R., Monaco A.P., Hovnanian A.
J. Invest. Dermatol. 118:338-343(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HHD CYS-309; PRO-341; ARG-411; VAL-580; TYR-742 AND ARG-789.
[13]"Analysis of ATP2C1 gene mutation in 10 unrelated Japanese families with Hailey-Hailey disease."
Yokota K., Yasukawa K., Shimizu H.
J. Invest. Dermatol. 118:550-551(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HHD PHE-490 AND PRO-584.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF181120 mRNA. Translation: AAF26295.1.
AF181121 mRNA. Translation: AAF26296.1.
AF189723 mRNA. Translation: AAF27813.2.
AF225981 mRNA. Translation: AAF35375.1.
AY268374 mRNA. Translation: AAP30008.1.
AY268375 mRNA. Translation: AAP30009.1.
AB037768 mRNA. Translation: BAA92585.1. Frameshift.
AK001684 mRNA. Translation: BAA91835.1.
AK074692 mRNA. Translation: BAC11142.1. Different initiation.
AK296470 mRNA. Translation: BAH12365.1.
AK299945 mRNA. Translation: BAG61775.1.
AK314342 mRNA. Translation: BAG36984.1.
AC055733 Genomic DNA. No translation available.
AC097105 Genomic DNA. No translation available.
CH471052 Genomic DNA. Translation: EAW79218.1.
CH471052 Genomic DNA. Translation: EAW79219.1.
BC028139 mRNA. Translation: AAH28139.1.
AJ010953 mRNA. Translation: CAA09425.1.
RefSeqNP_001001485.1. NM_001001485.2.
NP_001001486.1. NM_001001486.1.
NP_001001487.1. NM_001001487.1.
NP_001186108.1. NM_001199179.1.
NP_001186109.1. NM_001199180.1.
NP_001186110.1. NM_001199181.1.
NP_001186111.1. NM_001199182.1.
NP_001186112.1. NM_001199183.1.
NP_001186113.1. NM_001199184.1.
NP_001186114.1. NM_001199185.1.
NP_055197.2. NM_014382.3.
XP_005247412.1. XM_005247355.1.
XP_005247413.1. XM_005247356.1.
XP_005247414.1. XM_005247357.1.
UniGeneHs.584884.

3D structure databases

ProteinModelPortalP98194.
SMRP98194. Positions 45-901.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid117963. 2 interactions.
IntActP98194. 1 interaction.
STRING9606.ENSP00000352665.

Chemistry

DrugBankDB01169. Arsenic trioxide.
DB01189. Desflurane.
DB00228. Enflurane.
DB01159. Halothane.
DB00753. Isoflurane.
DB01028. Methoxyflurane.
DB01110. Miconazole.
DB01236. Sevoflurane.

Protein family/group databases

TCDB3.A.3.2.5. the p-type atpase (p-atpase) superfamily.

PTM databases

PhosphoSiteP98194.

Polymorphism databases

DMDM68068024.

Proteomic databases

PaxDbP98194.
PRIDEP98194.

Protocols and materials databases

DNASU27032.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000328560; ENSP00000329664; ENSG00000017260. [P98194-2]
ENST00000359644; ENSP00000352665; ENSG00000017260.
ENST00000393221; ENSP00000376914; ENSG00000017260. [P98194-7]
ENST00000422190; ENSP00000402677; ENSG00000017260. [P98194-5]
ENST00000428331; ENSP00000395809; ENSG00000017260. [P98194-1]
ENST00000504948; ENSP00000423330; ENSG00000017260. [P98194-4]
ENST00000505330; ENSP00000423774; ENSG00000017260. [P98194-4]
ENST00000507488; ENSP00000421326; ENSG00000017260. [P98194-3]
ENST00000508532; ENSP00000424783; ENSG00000017260. [P98194-1]
ENST00000510168; ENSP00000427461; ENSG00000017260. [P98194-1]
ENST00000513801; ENSP00000422872; ENSG00000017260. [P98194-3]
GeneID27032.
KEGGhsa:27032.
UCSCuc003enk.3. human. [P98194-1]
uc003enm.3. human. [P98194-2]
uc003enn.3. human. [P98194-3]
uc003ent.3. human. [P98194-5]
uc011bli.2. human.

Organism-specific databases

CTD27032.
GeneCardsGC03P130613.
HGNCHGNC:13211. ATP2C1.
HPACAB010207.
HPA035116.
HPA053533.
MIM169600. phenotype.
604384. gene.
neXtProtNX_P98194.
Orphanet2841. Familial benign chronic pemphigus.
PharmGKBPA25111.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0474.
HOVERGENHBG106478.
KOK01537.
OMADGQHAEV.
OrthoDBEOG7F7W81.
PhylomeDBP98194.
TreeFamTF354251.

Enzyme and pathway databases

BRENDA3.6.3.8. 2681.
ReactomeREACT_15518. Transmembrane transport of small molecules.

Gene expression databases

ArrayExpressP98194.
BgeeP98194.
CleanExHS_ATP2C1.
GenevestigatorP98194.

Family and domain databases

Gene3D1.20.1110.10. 3 hits.
InterProIPR006413. ATPase_P-typ_Ca-transp_PMR1.
IPR006068. ATPase_P-typ_cation-transptr_C.
IPR004014. ATPase_P-typ_cation-transptr_N.
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.
[Graphical view]
PfamPF00689. Cation_ATPase_C. 1 hit.
PF00690. Cation_ATPase_N. 1 hit.
PF00122. E1-E2_ATPase. 1 hit.
PF00702. Hydrolase. 1 hit.
[Graphical view]
PRINTSPR00119. CATATPASE.
PR00120. HATPASE.
SMARTSM00831. Cation_ATPase_N. 1 hit.
[Graphical view]
SUPFAMSSF56784. SSF56784. 2 hits.
TIGRFAMsTIGR01522. ATPase-IIA2_Ca. 1 hit.
TIGR01494. ATPase_P-type. 3 hits.
PROSITEPS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSATP2C1. human.
GeneWikiATP2C1.
GenomeRNAi27032.
NextBio49568.
PROP98194.
SOURCESearch...

Entry information

Entry nameAT2C1_HUMAN
AccessionPrimary (citable) accession number: P98194
Secondary accession number(s): B2RAT7 expand/collapse secondary AC list , B4DSW3, B7Z3X9, G3XAH8, G8JLN9, O76005, Q86V72, Q86V73, Q8N6V1, Q8NCJ7
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: June 21, 2005
Last modified: April 16, 2014
This is version 150 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM