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Protein

Calcium-transporting ATPase

Gene

ATP2C1

Organism
Homo sapiens (Human)
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

HydrolaseUniRule annotationSAAS annotation

Keywords - Biological processi

Calcium transportUniRule annotation, Ion transport, Transport

Keywords - Ligandi

ATP-bindingUniRule annotationSAAS annotation, Calcium, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Calcium-transporting ATPaseUniRule annotation (EC:3.6.3.8UniRule annotation)
Gene namesi
Name:ATP2C1Imported
ORF Names:hCG_14809Imported
OrganismiHomo sapiens (Human)Imported
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:13211. ATP2C1.

Subcellular locationi

  • Membrane UniRule annotation; Multi-pass membrane protein UniRule annotation

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei113 – 13119HelicalUniRule annotationAdd
BLAST
Transmembranei137 – 15317HelicalUniRule annotationAdd
BLAST
Transmembranei303 – 32220HelicalUniRule annotationAdd
BLAST
Transmembranei328 – 35730HelicalUniRule annotationAdd
BLAST
Transmembranei736 – 75621HelicalUniRule annotationAdd
BLAST
Transmembranei809 – 82921HelicalUniRule annotationAdd
BLAST
Transmembranei878 – 89518HelicalUniRule annotationAdd
BLAST
Transmembranei907 – 92923HelicalUniRule annotationAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Proteomic databases

PeptideAtlasiB4E2Q0.

Interactioni

Protein-protein interaction databases

STRINGi9606.ENSP00000376914.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini59 – 13375Cation_ATPase_NInterPro annotationAdd
BLAST

Sequence similaritiesi

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

Keywords - Domaini

Transmembrane, Transmembrane helixUniRule annotationSAAS annotation

Phylogenomic databases

eggNOGiKOG0202. Eukaryota.
COG0474. LUCA.
GeneTreeiENSGT00840000129745.
HOGENOMiHOG000265621.
HOVERGENiHBG106478.

Family and domain databases

Gene3Di1.20.1110.10. 3 hits.
InterProiIPR030336. ATP2C1.
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.
IPR023214. HAD-like_dom.
IPR006413. P-type_ATPase_IIA_PMR1.
IPR001757. P_typ_ATPase.
[Graphical view]
PANTHERiPTHR24093:SF214. PTHR24093:SF214. 1 hit.
PfamiPF00689. Cation_ATPase_C. 1 hit.
PF00690. Cation_ATPase_N. 1 hit.
PF00122. E1-E2_ATPase. 1 hit.
[Graphical view]
PRINTSiPR00120. HATPASE.
SMARTiSM00831. Cation_ATPase_N. 1 hit.
[Graphical view]
SUPFAMiSSF56784. SSF56784. 2 hits.
TIGRFAMsiTIGR01522. ATPase-IIA2_Ca. 1 hit.
TIGR01494. ATPase_P-type. 3 hits.
PROSITEiPS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

B4E2Q0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDSLLPPSRF SYFKKYPLHA IRRYLSTLRN QRAEEQVARF QKIPNGENET
60 70 80 90 100
MIPVLTSKKA SELPVSEVAS ILQADLQNGL NKCEVSHRRA FHGWNEFDIS
110 120 130 140 150
EDEPLWKKYI SQFKNPLIML LLASAVISVL MHQFDDAVSI TVAILIVVTV
160 170 180 190 200
AFVQEYRSEK SLEELSKLVP PECHCVREGK LEHTLARDLV PGDTVCLSVG
210 220 230 240 250
DRVPADLRLF EAVDLSIDES SLTGETTPCS KVTAPQPAAT NGDLASRSNI
260 270 280 290 300
AFMGTLVRCG KAKGVVIGTG ENSEFGEVFK MMQAEEAPKT PLQKSMDLLG
310 320 330 340 350
KQLSFYSFGI IGIIMLVGWL LGKDILEMFT ISVSLAVAAI PEGLPIVVTV
360 370 380 390 400
TLALGVMRMV KKRAIVKKLP IVETLGCCNV ICSDKTGTLT KNEMTVTHIF
410 420 430 440 450
TSDGLHAEVT GVGYNQFGEV IVDGDVVHGF YNPAVSRIVE AGCVCNDAVI
460 470 480 490 500
RNNTLMGKPT EGALIALAMK MGLDGLQQDY IRKAEYPFSS EQKWMAVKCV
510 520 530 540 550
HRTQQDRPEI CFMKGAYEQV IKYCTTYQSK GQTLTLTQQQ RDVYQQEKAR
560 570 580 590 600
MGSAGLRVLA LASGPELGQL TFLGLVGIID PPRTGVKEAV TTLIASGVSI
610 620 630 640 650
KMITGDSQET AVAIASRLGL YSKTSQSVSG EEIDAMDVQQ LSQIVPKVAV
660 670 680 690 700
FYRASPRHKM KIIKSLQKNG SVVAMTGDGV NDAVALKAAD IGVAMGQTGT
710 720 730 740 750
DVCKEAADMI LVDDDFQTIM SAIEEGKGIY NNIKNFVRFQ LSTSIAALTL
760 770 780 790 800
ISLATLMNFP NPLNAMQILW INIIMDGPPA QSLGVEPVDK DVIRKPPRNW
810 820 830 840 850
KDSILTKNLI LKILVSSIII VCGTLFVFWR ELRDNVITPR DTTMTFTCFV
860 870 880 890 900
FFDMFNALSS RSQTKSVFEI GLCSNRMFCY AVLGSIMGQL LVIYFPPLQK
910 920 930 940 950
VFQTESLSIL DLLFLLGLTS SVCIVAEIIK KVERSREKIQ KHVSSTSSSF

LEV
Length:953
Mass (Da):104,713
Last modified:September 23, 2008 - v1
Checksum:i132AA4602598AE76
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC055733 Genomic DNA. No translation available.
AC097105 Genomic DNA. No translation available.
AK304374 mRNA. Translation: BAG65212.1.
CH471052 Genomic DNA. Translation: EAW79220.1.
RefSeqiNP_001186110.1. NM_001199181.1.
UniGeneiHs.584884.

Genome annotation databases

EnsembliENST00000505330; ENSP00000423774; ENSG00000017260.
GeneIDi27032.
UCSCiuc011blg.3. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC055733 Genomic DNA. No translation available.
AC097105 Genomic DNA. No translation available.
AK304374 mRNA. Translation: BAG65212.1.
CH471052 Genomic DNA. Translation: EAW79220.1.
RefSeqiNP_001186110.1. NM_001199181.1.
UniGeneiHs.584884.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9606.ENSP00000376914.

Proteomic databases

PeptideAtlasiB4E2Q0.

Protocols and materials databases

DNASUi27032.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000505330; ENSP00000423774; ENSG00000017260.
GeneIDi27032.
UCSCiuc011blg.3. human.

Organism-specific databases

CTDi27032.
HGNCiHGNC:13211. ATP2C1.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0202. Eukaryota.
COG0474. LUCA.
GeneTreeiENSGT00840000129745.
HOGENOMiHOG000265621.
HOVERGENiHBG106478.

Miscellaneous databases

ChiTaRSiATP2C1. human.
GenomeRNAii27032.

Family and domain databases

Gene3Di1.20.1110.10. 3 hits.
InterProiIPR030336. ATP2C1.
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.
IPR023214. HAD-like_dom.
IPR006413. P-type_ATPase_IIA_PMR1.
IPR001757. P_typ_ATPase.
[Graphical view]
PANTHERiPTHR24093:SF214. PTHR24093:SF214. 1 hit.
PfamiPF00689. Cation_ATPase_C. 1 hit.
PF00690. Cation_ATPase_N. 1 hit.
PF00122. E1-E2_ATPase. 1 hit.
[Graphical view]
PRINTSiPR00120. HATPASE.
SMARTiSM00831. Cation_ATPase_N. 1 hit.
[Graphical view]
SUPFAMiSSF56784. SSF56784. 2 hits.
TIGRFAMsiTIGR01522. ATPase-IIA2_Ca. 1 hit.
TIGR01494. ATPase_P-type. 3 hits.
PROSITEiPS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The sequence of the human genome."
    Venter J.C., Adams M.D., Myers E.W., Li P.W., Mural R.J., Sutton G.G., Smith H.O., Yandell M., Evans C.A., Holt R.A., Gocayne J.D., Amanatides P., Ballew R.M., Huson D.H., Wortman J.R., Zhang Q., Kodira C.D., Zheng X.H.
    , Chen L., Skupski M., Subramanian G., Thomas P.D., Zhang J., Gabor Miklos G.L., Nelson C., Broder S., Clark A.G., Nadeau J., McKusick V.A., Zinder N., Levine A.J., Roberts R.J., Simon M., Slayman C., Hunkapiller M., Bolanos R., Delcher A., Dew I., Fasulo D., Flanigan M., Florea L., Halpern A., Hannenhalli S., Kravitz S., Levy S., Mobarry C., Reinert K., Remington K., Abu-Threideh J., Beasley E., Biddick K., Bonazzi V., Brandon R., Cargill M., Chandramouliswaran I., Charlab R., Chaturvedi K., Deng Z., Di Francesco V., Dunn P., Eilbeck K., Evangelista C., Gabrielian A.E., Gan W., Ge W., Gong F., Gu Z., Guan P., Heiman T.J., Higgins M.E., Ji R.R., Ke Z., Ketchum K.A., Lai Z., Lei Y., Li Z., Li J., Liang Y., Lin X., Lu F., Merkulov G.V., Milshina N., Moore H.M., Naik A.K., Narayan V.A., Neelam B., Nusskern D., Rusch D.B., Salzberg S., Shao W., Shue B., Sun J., Wang Z., Wang A., Wang X., Wang J., Wei M., Wides R., Xiao C., Yan C., Yao A., Ye J., Zhan M., Zhang W., Zhang H., Zhao Q., Zheng L., Zhong F., Zhong W., Zhu S., Zhao S., Gilbert D., Baumhueter S., Spier G., Carter C., Cravchik A., Woodage T., Ali F., An H., Awe A., Baldwin D., Baden H., Barnstead M., Barrow I., Beeson K., Busam D., Carver A., Center A., Cheng M.L., Curry L., Danaher S., Davenport L., Desilets R., Dietz S., Dodson K., Doup L., Ferriera S., Garg N., Gluecksmann A., Hart B., Haynes J., Haynes C., Heiner C., Hladun S., Hostin D., Houck J., Howland T., Ibegwam C., Johnson J., Kalush F., Kline L., Koduru S., Love A., Mann F., May D., McCawley S., McIntosh T., McMullen I., Moy M., Moy L., Murphy B., Nelson K., Pfannkoch C., Pratts E., Puri V., Qureshi H., Reardon M., Rodriguez R., Rogers Y.H., Romblad D., Ruhfel B., Scott R., Sitter C., Smallwood M., Stewart E., Strong R., Suh E., Thomas R., Tint N.N., Tse S., Vech C., Wang G., Wetter J., Williams S., Williams M., Windsor S., Winn-Deen E., Wolfe K., Zaveri J., Zaveri K., Abril J.F., Guigo R., Campbell M.J., Sjolander K.V., Karlak B., Kejariwal A., Mi H., Lazareva B., Hatton T., Narechania A., Diemer K., Muruganujan A., Guo N., Sato S., Bafna V., Istrail S., Lippert R., Schwartz R., Walenz B., Yooseph S., Allen D., Basu A., Baxendale J., Blick L., Caminha M., Carnes-Stine J., Caulk P., Chiang Y.H., Coyne M., Dahlke C., Mays A., Dombroski M., Donnelly M., Ely D., Esparham S., Fosler C., Gire H., Glanowski S., Glasser K., Glodek A., Gorokhov M., Graham K., Gropman B., Harris M., Heil J., Henderson S., Hoover J., Jennings D., Jordan C., Jordan J., Kasha J., Kagan L., Kraft C., Levitsky A., Lewis M., Liu X., Lopez J., Ma D., Majoros W., McDaniel J., Murphy S., Newman M., Nguyen T., Nguyen N., Nodell M., Pan S., Peck J., Peterson M., Rowe W., Sanders R., Scott J., Simpson M., Smith T., Sprague A., Stockwell T., Turner R., Venter E., Wang M., Wen M., Wu D., Wu M., Xia A., Zandieh A., Zhu X.
    Science 291:1304-1351(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
  2. Cited for: NUCLEOTIDE SEQUENCE.
  3. "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.
    , 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., 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].
  4. "NEDO human cDNA sequencing project focused on splicing variants."
    Wakamatsu A., Yamamoto J., Kimura K., Ishii S., Watanabe K., Sugiyama A., Murakawa K., Kaida T., Tsuchiya K., Fukuzumi Y., Kumagai A., Oishi Y., Yamamoto S., Ono Y., Komori Y., Yamazaki M., Kisu Y., Nishikawa T.
    , Sugano S., Nomura N., Isogai T.
    Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Tissue: TracheaImported.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. Ensembl
    Submitted (NOV-2014) to UniProtKB
    Cited for: IDENTIFICATION.

Entry informationi

Entry nameiB4E2Q0_HUMAN
AccessioniPrimary (citable) accession number: B4E2Q0
Entry historyi
Integrated into UniProtKB/TrEMBL: September 23, 2008
Last sequence update: September 23, 2008
Last modified: July 6, 2016
This is version 69 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)
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.

Miscellaneousi

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.UniRule annotation

Keywords - Technical termi

Complete proteome, Proteomics identificationCombined sources, Reference proteomeImported

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.