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Q9H7F0 (AT133_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Probable cation-transporting ATPase 13A3

EC=3.6.3.-
Alternative name(s):
ATPase family homolog up-regulated in senescence cells 1
Gene names
Name:ATP13A3
Synonyms:AFURS1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1226 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

ATP + H2O = ADP + phosphate.

Subcellular location

Membrane; Multi-pass membrane protein By similarity.

Sequence similarities

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

Sequence caution

The sequence BAB14942.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence BAB14942.1 differs from that shown. Reason: Frameshift at position 1065.

The sequence BAC11398.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Cellular componentMembrane
   Coding sequence diversityAlternative splicing
   DomainTransmembrane
Transmembrane helix
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionHydrolase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Cellular_componentintegral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

cation-transporting ATPase activity

Inferred from electronic annotation. Source: InterPro

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9H7F0-1)

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: Q9H7F0-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-277: Missing.
     278-279: NE → MS
     936-978: FCVFKFMALY...LFIDLAIILV → SCELALFSIV...FHNCAFYSLV
     979-1226: Missing.
Note: Dubious isoform produced through aberrant splice sites.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12261226Probable cation-transporting ATPase 13A3
PRO_0000046425

Regions

Transmembrane29 – 4921Helical; Potential
Transmembrane206 – 22621Helical; Potential
Transmembrane233 – 25321Helical; Potential
Transmembrane410 – 43021Helical; Potential
Transmembrane449 – 46921Helical; Potential
Transmembrane941 – 96121Helical; Potential
Transmembrane963 – 98321Helical; Potential
Transmembrane1000 – 102021Helical; Potential
Transmembrane1074 – 109421Helical; Potential
Transmembrane1106 – 112621Helical; Potential
Transmembrane1144 – 116421Helical; Potential
Compositional bias231 – 2344Poly-Tyr

Sites

Active site49814-aspartylphosphate intermediate By similarity
Metal binding8831Magnesium By similarity
Metal binding8871Magnesium By similarity

Amino acid modifications

Modified residue981Phosphoserine Ref.6 Ref.7
Modified residue8171Phosphoserine Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9

Natural variations

Alternative sequence1 – 277277Missing in isoform 2.
VSP_007314
Alternative sequence278 – 2792NE → MS in isoform 2.
VSP_036300
Alternative sequence936 – 97843FCVFK…AIILV → SCELALFSIVTYSLDHFIIS ILISSMLVLFFSDFHNCAFY SLV in isoform 2.
VSP_007315
Alternative sequence979 – 1226248Missing in isoform 2.
VSP_007316

Experimental info

Sequence conflict3471E → Q in CAC84902. Ref.1
Sequence conflict7301T → P in CAC84902. Ref.1
Sequence conflict7841V → F in BAC11398. Ref.3
Sequence conflict8071E → G in BAC11398. Ref.3
Sequence conflict9641G → R in BAC11398. Ref.3

Sequences

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

Last modified February 10, 2009. Version 4.
Checksum: 8DD1C0451223C7AB

FASTA1,226138,043
        10         20         30         40         50         60 
MDREERKTIN QGQEDEMEIY GYNLSRWKLA IVSLGVICSG GFLLLLLYWM PEWRVKATCV 

        70         80         90        100        110        120 
RAAIKDCEVV LLRTTDEFKM WFCAKIRVLS LETYPVSSPK SMSNKLSNGH AVCLIENPTE 

       130        140        150        160        170        180 
ENRHRISKYS QTESQQIRYF THHSVKYFWN DTIHNFDFLK GLDEGVSCTS IYEKHSAGLT 

       190        200        210        220        230        240 
KGMHAYRKLL YGVNEIAVKV PSVFKLLIKE VLNPFYIFQL FSVILWSTDE YYYYALAIVV 

       250        260        270        280        290        300 
MSIVSIVSSL YSIRKQYVML HDMVATHSTV RVSVCRVNEE IEEIFSTDLV PGDVMVIPLN 

       310        320        330        340        350        360 
GTIMPCDAVL INGTCIVNES MLTGESVPVT KTNLPNPSVD VKGIGDELYN PETHKRHTLF 

       370        380        390        400        410        420 
CGTTVIQTRF YTGELVKAIV VRTGFSTSKG QLVRSILYPK PTDFKLYRDA YLFLLCLVAV 

       430        440        450        460        470        480 
AGIGFIYTII NSILNEVQVG VIIIESLDII TITVPPALPA AMTAGIVYAQ RRLKKIGIFC 

       490        500        510        520        530        540 
ISPQRINICG QLNLVCFDKT GTLTEDGLDL WGIQRVENAR FLSPEENVCN EMLVKSQFVA 

       550        560        570        580        590        600 
CMATCHSLTK IEGVLSGDPL DLKMFEAIGW ILEEATEEET ALHNRIMPTV VRPPKQLLPE 

       610        620        630        640        650        660 
STPAGNQEME LFELPATYEI GIVRQFPFSS ALQRMSVVAR VLGDRKMDAY MKGAPEAIAG 

       670        680        690        700        710        720 
LCKPETVPVD FQNVLEDFTK QGFRVIALAH RKLESKLTWH KVQNISRDAI ENNMDFMGLI 

       730        740        750        760        770        780 
IMQNKLKQET PAVLEDLHKA NIRTVMVTGD SMLTAVSVAR DCGMILPQDK VIIAEALPPK 

       790        800        810        820        830        840 
DGKVAKINWH YADSLTQCSH PSAIDPEAIP VKLVHDSLED LQMTRYHFAM NGKSFSVILE 

       850        860        870        880        890        900 
HFQDLVPKLM LHGTVFARMA PDQKTQLIEA LQNVDYFVGM CGDGANDCGA LKRAHGGISL 

       910        920        930        940        950        960 
SELEASVASP FTSKTPSISC VPNLIREGRA ALITSFCVFK FMALYSIIQY FSVTLLYSIL 

       970        980        990       1000       1010       1020 
SNLGDFQFLF IDLAIILVVV FTMSLNPAWK ELVAQRPPSG LISGALLFSV LSQIIICIGF 

      1030       1040       1050       1060       1070       1080 
QSLGFFWVKQ QPWYEVWHPK SDACNTTGSG FWNSSHVDNE TELDEHNIQN YENTTVFFIS 

      1090       1100       1110       1120       1130       1140 
SFQYLIVAIA FSKGKPFRQP CYKNYFFVFS VIFLYIFILF IMLYPVASVD QVLQIVCVPY 

      1150       1160       1170       1180       1190       1200 
QWRVTMLIIV LVNAFVSITV EESVDRWGKC CLPWALGCRK KTPKAKYMYL AQELLVDPEW 

      1210       1220 
PPKPQTTTEA KALVKENGSC QIITIT 

« Hide

Isoform 2 [UniParc].

Checksum: 7927AFFE8413247F
Show »

FASTA70177,310

References

« Hide 'large scale' references
[1]"Cloning the AFURS1 gene which is up-regulated in senescent human parenchymal kidney cells."
Habtemichael N., Kovacs G.
Gene 283:271-275(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[2]"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].
[3]"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] OF 402-1226 (ISOFORM 1).
Tissue: Coronary artery and Placenta.
[4]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-817, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[5]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-817, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[6]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98 AND SER-817, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[7]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98 AND SER-817, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[8]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-817, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-817, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ306929 mRNA. Translation: CAC84902.1.
AC108676 Genomic DNA. No translation available.
AC125362 Genomic DNA. No translation available.
AK024639 mRNA. Translation: BAB14942.1. Sequence problems.
AK075094 mRNA. Translation: BAC11398.1. Different initiation.
CCDSCCDS43187.1. [Q9H7F0-1]
RefSeqNP_078800.3. NM_024524.3. [Q9H7F0-1]
UniGeneHs.529609.

3D structure databases

ProteinModelPortalQ9H7F0.
SMRQ9H7F0. Positions 163-1027.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid122719. 1 interaction.

PTM databases

PhosphoSiteQ9H7F0.

Polymorphism databases

DMDM223590262.

Proteomic databases

MaxQBQ9H7F0.
PaxDbQ9H7F0.
PRIDEQ9H7F0.

Protocols and materials databases

DNASU79572.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000256031; ENSP00000256031; ENSG00000133657. [Q9H7F0-1]
ENST00000439040; ENSP00000416508; ENSG00000133657. [Q9H7F0-1]
GeneID79572.
KEGGhsa:79572.
UCSCuc003fty.4. human. [Q9H7F0-1]

Organism-specific databases

CTD79572.
GeneCardsGC03M194123.
HGNCHGNC:24113. ATP13A3.
HPAHPA029471.
MIM610232. gene.
neXtProtNX_Q9H7F0.
PharmGKBPA134971145.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0474.
HOGENOMHOG000171813.
HOVERGENHBG065757.
InParanoidQ9H7F0.
KOK14951.
OMAENRHRIS.
OrthoDBEOG7B5WV2.
PhylomeDBQ9H7F0.
TreeFamTF300331.

Gene expression databases

ArrayExpressQ9H7F0.
BgeeQ9H7F0.
CleanExHS_ATP13A3.
GenevestigatorQ9H7F0.

Family and domain databases

Gene3D2.70.150.10. 1 hit.
3.40.1110.10. 2 hits.
3.40.50.1000. 2 hits.
InterProIPR004014. ATPase_P-typ_cation-transptr_N.
IPR006544. ATPase_P-typ_Cation_typ_V.
IPR023299. ATPase_P-typ_cyto_domN.
IPR018303. ATPase_P-typ_P_site.
IPR008250. ATPase_P-typ_transduc_dom_A.
IPR001757. Cation_transp_P_typ_ATPase.
IPR023214. HAD-like_dom.
[Graphical view]
PfamPF00690. Cation_ATPase_N. 1 hit.
PF00122. E1-E2_ATPase. 1 hit.
PF12409. P5-ATPase. 1 hit.
[Graphical view]
PRINTSPR00119. CATATPASE.
SUPFAMSSF56784. SSF56784. 3 hits.
SSF81660. SSF81660. 2 hits.
TIGRFAMsTIGR01494. ATPase_P-type. 3 hits.
TIGR01657. P-ATPase-V. 1 hit.
PROSITEPS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiATP13A3.
GenomeRNAi79572.
NextBio68532.
PROQ9H7F0.
SOURCESearch...

Entry information

Entry nameAT133_HUMAN
AccessionPrimary (citable) accession number: Q9H7F0
Secondary accession number(s): Q8NC11, Q96KS1
Entry history
Integrated into UniProtKB/Swiss-Prot: October 18, 2001
Last sequence update: February 10, 2009
Last modified: July 9, 2014
This is version 116 of the entry and version 4 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 chromosome 3

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