Q5JXY1 (Q5JXY1_HUMAN) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Submitted name:
ATPase type 13A2, isoform CRA_b EMBL EAW94825.1

Submitted name:
Probable cation-transporting ATPase 13A2 Ensembl ENSP00000341115

Gene names

Name:	ATP13A2 EMBL EAW94825.1 Ensembl ENSP00000341115
ORF Names:	hCG_25128 EMBL EAW94825.1

Organism

Homo sapiens (Human) [Reference proteome] Ensembl ENSP00000341115

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1158 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Sequence similarities

Belongs to the cation transport ATPase (P-type) family. RuleBase RU000653

Ontologies

Keywords
Cellular component	Membrane
Domain	Transmembrane Transmembrane helix SAAS SAAS004014
Ligand	ATP-binding RuleBase RU000653 SAAS SAAS004014 Nucleotide-binding
Molecular function	Hydrolase SAAS SAAS023306 RuleBase RU000653
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	ATP catabolic process Inferred from electronic annotation. Source: GOC
Cellular_component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	ATP 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: InterPro
Complete GO annotation...

Sequences

	Sequence		Length	Mass (Da)
	Q5JXY1 [UniParc]. Last modified February 15, 2005. Version 1. Checksum: 1A7D35DF1CD34396	FASTA	1,158	125,977
	10 20 30 40 50 60 MSADSSPLVG STPTGYGTLT IGTSIDPLSS SVSSVRLSGY CGSPWRVIGY HVVVWMMAGI 70 80 90 100 110 120 PLLLFRWKPL WGVRLRLRPC NLAHAETLVI EIRDKEDSSW QLFTVQVQTE AIGEGSLEPS 130 140 150 160 170 180 PQSQAEDGRS QAAVGAVPEG AWKDTAQLHK SEEAKRVLRY YLFQGQRYIW IETQQAFYQV 190 200 210 220 230 240 SLLDHGRSCD DVHRSRHGLS LQDQMVRKAI YGPNVISIPV KSYPQLLVDE ALNPYYGFQA 250 260 270 280 290 300 FSIALWLADH YYWYALCIFL ISSISICLSL YKTRKQSQTL RDMVKLSMRV CVCRPGGEEE 310 320 330 340 350 360 WVDSSELVPG DCLVLPQEGG LMPCDAALVA GECMVNESSL TGESIPVLKT ALPEGLGPYC 370 380 390 400 410 420 AETHRRHTLF CGTLILQARA YVGPHVLAVV TRTGFCTAKG GLVSSILHPR PINFKFYKHS 430 440 450 460 470 480 MKFVAALSVL ALLGTIYSIF ILYRNRVPLN EIVIRALDLV TVVVPPALPA AMTVCTLYAQ 490 500 510 520 530 540 SRLRRQGIFC IHPLRINLGG KLQLVCFDKT GTLTEDGLDV MGVVPLKGQA FLPLVPEPRR 550 560 570 580 590 600 LPVGPLLRAL ATCHALSRLQ DTPVGDPMDL KMVESTGWVL EEEPAADSAF GTQVLAVMRP 610 620 630 640 650 660 PLWEPQLQAM EEPPVPVSVL HRFPFSSALQ RMSVVVAWPG ATQPEAYVKG SPELVAGLCN 670 680 690 700 710 720 PETVPTDFAQ MLQSYTAAGY RVVALASKPL PTVPSLEAAQ QLTRDTVEGD LSLLGLLVMR 730 740 750 760 770 780 NLLKPQTTPV IQALRRTRIR AVMVTGDNLQ TAVTVARGCG MVAPQEHLII VHATHPERGQ 790 800 810 820 830 840 PASLEFLPME SPTAVNGVKV LVQGTVFARM APEQKTELVC ELQKLQYCVG MCGDGANDCG 850 860 870 880 890 900 ALKAADVGIS LSQAEASVVS PFTSSMASIE CVPMVIREGR CSLDTSFSVF KYMALYSLTQ 910 920 930 940 950 960 FISVLILYTI NTNLGDLQFL AIDLVITTTV AVLMSRTGPA LVLGRVRPPG ALLSVPVLSS 970 980 990 1000 1010 1020 LLLQMVLVTG VQLGGYFLTL AQPWFVPLNR TVAAPDNLPN YENTVVFSLS SFQYLILAAA 1030 1040 1050 1060 1070 1080 VSKGAPFRRP LYTNERARPV PPRLPAPPPA QAGLQEALQA AGTRAGRAAL AAAARRPPEV 1090 1100 1110 1120 1130 1140 VQAHGHPRHW NSLPLSHQLD PSPATPPPPP PTSLRLATVY TPPPRPPPPW GSVDYCPLPW 1150 TIPRRGGSPQ LPSVLLSV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	Mural R.J., Istrail S., Sutton 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. , 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE.
[2]	"The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S., McLaren S., Milne S., Mistry S., Moore M.J., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R., Banerjee R., Bryant S.P., Burford D.C., Burrill W.D., Clegg S.M., Dhami P., Dovey O., Faulkner L.M., Gribble S.M., Langford C.F., Pandian R.D., Porter K.M., Prigmore E. Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	Ensembl Submitted (FEB-2012) to UniProtKB Cited for: IDENTIFICATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL049569 Genomic DNA. No translation available. CH471134 Genomic DNA. Translation: EAW94825.1.
IPI	IPI00177535.
RefSeq	NP_001135446.1. NM_001141974.1.
UniGene	Hs.128866.
3D structure databases
SMR	Q5JXY1. Positions 249-988.
ModBase	Search...
Proteomic databases
PRIDE	Q5JXY1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000341676; ENSP00000341115; ENSG00000159363.
GeneID	23400.
KEGG	hsa:23400.
UCSC	uc001bac.2. human.
Organism-specific databases
CTD	23400.
HGNC	HGNC:30213. ATP13A2.
PharmGKB	PA134897221.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	HOG000171813.
HOVERGEN	HBG065757.
KO	K13526.
Gene expression databases
ArrayExpress	Q5JXY1.
Family and domain databases
Gene3D	2.70.150.10. 1 hit. 3.40.1110.10. 2 hits. 3.40.50.1000. 1 hit.
InterPro	IPR004014. 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]
PANTHER	PTHR24093. PTHR24093. 1 hit.
Pfam	PF00122. E1-E2_ATPase. 1 hit. PF12409. P5-ATPase. 1 hit. [Graphical view]
PRINTS	PR00119. CATATPASE.
SMART	SM00831. Cation_ATPase_N. 1 hit. [Graphical view]
SUPFAM	SSF81660. ATPase_cation_domN. 1 hit. SSF56784. HAD-like_dom. 1 hit.
TIGRFAMs	TIGR01494. ATPase_P-type. 2 hits. TIGR01657. P-ATPase-V. 1 hit.
PROSITE	PS00154. ATPASE_E1_E2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	ATP13A2. human.
GenomeRNAi	23400.
NextBio	45553.

Entry information

Entry name

Q5JXY1_HUMAN

Accession

Primary (citable) accession number: Q5JXY1

Entry history

Integrated into UniProtKB/TrEMBL:	February 15, 2005
Last sequence update:	February 15, 2005
Last modified:	May 1, 2013
This is version 88 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)

Disclaimer

Any 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.