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Q8NB49 (AT11C_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 119. 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·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phospholipid-transporting ATPase IG

EC=3.6.3.1
Alternative name(s):
ATPase IQ
ATPase class VI type 11C
P4-ATPase flippase complex alpha subunit ATP11C
Gene names
Name:ATP11C
Synonyms:ATPIG, ATPIQ
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1132 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalytic component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of aminophospholipids from the outer to the inner leaflet of various membranes and ensures the maintenance of asymmetric distribution of phospholipids. Phospholipid translocation seems also to be implicated in vesicle formation and in uptake of lipid signaling molecules. Required for B cell differentiation past the pro-B cell stage. Seems to mediate phosphatidylserine (PS) flipping in pro-B cells. May be involved in the transport of cholestatic bile acids By similarity.

Catalytic activity

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

Subunit structure

Component of a P4-ATPase flippase complex which consists of a catalytic alpha subunit and an accessory beta subunit Probable. Interacts with beta subunit TMEM30A. Ref.9

Subcellular location

Cell membrane; Multi-pass membrane protein. Endoplasmic reticulum membrane. Note: Efficient exit from the endoplasmic reticulum requires the presence of TMEM30A. Some cell membrane localization observed in the presence of TMEM30B. Ref.9

Tissue specificity

Widely expressed. Ref.1

Sequence similarities

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

Sequence caution

The sequence BAC03692.1 differs from that shown. Reason: Erroneous initiation.

The sequence BAC86172.1 differs from that shown. Reason: Erroneous initiation.

The sequence BAC86377.1 differs from that shown. Reason: Erroneous initiation.

The sequence BAD18440.1 differs from that shown. Reason: Erroneous initiation.

The sequence CAI39713.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAI39714.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAI39716.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAI40418.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAI41444.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAI41445.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAI41446.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAI41447.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Biological processLipid transport
Transport
   Cellular componentCell membrane
Endoplasmic reticulum
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainTransmembrane
Transmembrane helix
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionHydrolase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_procession transmembrane transport

Traceable author statement. Source: Reactome

phospholipid translocation

Non-traceable author statement Ref.9. Source: UniProtKB

transmembrane transport

Traceable author statement. Source: Reactome

   Cellular_componentendoplasmic reticulum

Inferred from direct assay Ref.9. Source: UniProtKB

endoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

lysosomal membrane

Inferred from direct assay PubMed 17897319. Source: UniProtKB

plasma membrane

Inferred from direct assay Ref.9. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

cation-transporting ATPase activity

Inferred from electronic annotation. Source: InterPro

magnesium ion binding

Inferred from electronic annotation. Source: InterPro

phospholipid-translocating ATPase activity

Inferred from electronic annotation. Source: UniProtKB-EC

protein binding

Inferred from physical interaction Ref.9. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8NB49-1)

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: Q8NB49-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1100-1132: RNLSCRRASDSLSARPSVRPLLLRTFSDESNVL → VHHLISSSA
Note: No experimental confirmation available.
Isoform 3 (identifier: Q8NB49-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1100-1132: RNLSCRRASDSLSARPSVRPLLLRTFSDESNVL → NPNLELPMLLSYKHTDSGYS
Isoform 4 (identifier: Q8NB49-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1100-1132: RNLSCRRASDSLSARPSVRPLLLRTFSDESNVL → VTKRLPSSGTSAIFMLSQTSSNHSFSWSE
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11321132Phospholipid-transporting ATPase IG
PRO_0000046373

Regions

Topological domain1 – 6666Cytoplasmic Potential
Transmembrane67 – 8519Helical; Potential
Topological domain861Extracellular Potential
Transmembrane87 – 10721Helical; Potential
Topological domain108 – 290183Cytoplasmic Potential
Transmembrane291 – 31121Helical; Potential
Topological domain312 – 34635Extracellular Potential
Transmembrane347 – 36721Helical; Potential
Topological domain368 – 879512Cytoplasmic Potential
Transmembrane880 – 90021Helical; Potential
Topological domain901 – 9088Extracellular Potential
Transmembrane909 – 92921Helical; Potential
Topological domain930 – 95526Cytoplasmic Potential
Transmembrane956 – 97621Helical; Potential
Topological domain977 – 99519Extracellular Potential
Transmembrane996 – 101621Helical; Potential
Topological domain1017 – 102610Cytoplasmic Potential
Transmembrane1027 – 104721Helical; Potential
Topological domain1048 – 106922Extracellular Potential
Transmembrane1070 – 109021Helical; Potential
Topological domain1091 – 113242Cytoplasmic Potential

Sites

Active site41214-aspartylphosphate intermediate By similarity
Metal binding8191Magnesium By similarity
Metal binding8231Magnesium By similarity

Amino acid modifications

Modified residue4451Phosphoserine Ref.5
Modified residue11081Phosphoserine Ref.8

Natural variations

Alternative sequence1100 – 113233RNLSC…ESNVL → VHHLISSSA in isoform 2.
VSP_007309
Alternative sequence1100 – 113233RNLSC…ESNVL → NPNLELPMLLSYKHTDSGYS in isoform 3.
VSP_013373
Alternative sequence1100 – 113233RNLSC…ESNVL → VTKRLPSSGTSAIFMLSQTS SNHSFSWSE in isoform 4.
VSP_013374
Natural variant1141C → W. Ref.1
Corresponds to variant rs2491014 [ dbSNP | Ensembl ].
VAR_021827
Natural variant1571T → I in a colorectal cancer sample; somatic mutation. Ref.11
VAR_036501
Natural variant5221Y → C.
Corresponds to variant rs17281983 [ dbSNP | Ensembl ].
VAR_055546
Natural variant9311Q → P in a colorectal cancer sample; somatic mutation. Ref.11
VAR_036502
Natural variant9721V → M.
Corresponds to variant rs55724992 [ dbSNP | Ensembl ].
VAR_061036

Experimental info

Sequence conflict5371L → P in BAC86377. Ref.3
Sequence conflict8731I → V in BAC86377. Ref.3

Sequences

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

Last modified April 12, 2005. Version 3.
Checksum: 74B63B20A5C6E49D

FASTA1,132129,477
        10         20         30         40         50         60 
MQMVPSLPPA SECAGEEKRV GTRTVFVGNH PVSETEAYIA QRFCDNRIVS SKYTLWNFLP 

        70         80         90        100        110        120 
KNLFEQFRRI ANFYFLIIFL VQVTVDTPTS PVTSGLPLFF VITVTAIKQG YEDCLRHRAD 

       130        140        150        160        170        180 
NEVNKSTVYI IENAKRVRKE SEKIKVGDVV EVQADETFPC DLILLSSCTT DGTCYVTTAS 

       190        200        210        220        230        240 
LDGESNCKTH YAVRDTIALC TAESIDTLRA AIECEQPQPD LYKFVGRINI YSNSLEAVAR 

       250        260        270        280        290        300 
SLGPENLLLK GATLKNTEKI YGVAVYTGME TKMALNYQGK SQKRSAVEKS INAFLIVYLF 

       310        320        330        340        350        360 
ILLTKAAVCT TLKYVWQSTP YNDEPWYNQK TQKERETLKV LKMFTDFLSF MVLFNFIIPV 

       370        380        390        400        410        420 
SMYVTVEMQK FLGSFFISWD KDFYDEEINE GALVNTSDLN EELGQVDYVF TDKTGTLTEN 

       430        440        450        460        470        480 
SMEFIECCID GHKYKGVTQE VDGLSQTDGT LTYFDKVDKN REELFLRALC LCHTVEIKTN 

       490        500        510        520        530        540 
DAVDGATESA ELTYISSSPD EIALVKGAKR YGFTFLGNRN GYMRVENQRK EIEEYELLHT 

       550        560        570        580        590        600 
LNFDAVRRRM SVIVKTQEGD ILLFCKGADS AVFPRVQNHE IELTKVHVER NAMDGYRTLC 

       610        620        630        640        650        660 
VAFKEIAPDD YERINRQLIE AKMALQDREE KMEKVFDDIE TNMNLIGATA VEDKLQDQAA 

       670        680        690        700        710        720 
ETIEALHAAG LKVWVLTGDK METAKSTCYA CRLFQTNTEL LELTTKTIEE SERKEDRLHE 

       730        740        750        760        770        780 
LLIEYRKKLL HEFPKSTRSF KKAWTEHQEY GLIIDGSTLS LILNSSQDSS SNNYKSIFLQ 

       790        800        810        820        830        840 
ICMKCTAVLC CRMAPLQKAQ IVRMVKNLKG SPITLSIGDG ANDVSMILES HVGIGIKGKE 

       850        860        870        880        890        900 
GRQAARNSDY SVPKFKHLKK LLLAHGHLYY VRIAHLVQYF FYKNLCFILP QFLYQFFCGF 

       910        920        930        940        950        960 
SQQPLYDAAY LTMYNICFTS LPILAYSLLE QHINIDTLTS DPRLYMKISG NAMLQLGPFL 

       970        980        990       1000       1010       1020 
YWTFLAAFEG TVFFFGTYFL FQTASLEENG KVYGNWTFGT IVFTVLVFTV TLKLALDTRF 

      1030       1040       1050       1060       1070       1080 
WTWINHFVIW GSLAFYVFFS FFWGGIIWPF LKQQRMYFVF AQMLSSVSTW LAIILLIFIS 

      1090       1100       1110       1120       1130 
LFPEILLIVL KNVRRRSARR NLSCRRASDS LSARPSVRPL LLRTFSDESN VL 

« Hide

Isoform 2 [UniParc].

Checksum: ADC1995E368B8C4E
Show »

FASTA1,108126,710
Isoform 3 [UniParc].

Checksum: 2F1EF15A73AB3947
Show »

FASTA1,119128,040
Isoform 4 [UniParc].

Checksum: 5928DF8ED2988A7C
Show »

FASTA1,128128,933

References

« Hide 'large scale' references
[1]"X-linked hypoparathyroidism region on Xq27 is evolutionarily conserved with regions on 3q26 and 13q34 and contains a novel P-type ATPase."
Andrew-Nesbit M., Bowl M.R., Harding B., Schlessinger D., Whyte M.P., Thakker R.V.
Genomics 84:1060-1070(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), TISSUE SPECIFICITY, VARIANT TRP-114.
Tissue: Liver.
[2]"The DNA sequence of the human X chromosome."
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. expand/collapse author list , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
Nature 434:325-337(2005) [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 305-1132 (ISOFORM 4), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 543-1132 (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 777-1132 (ISOFORM 2).
Tissue: Brain, Fetal brain, Testis and Thalamus.
[4]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[5]"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-445, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[6]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[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: 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-1108, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"ATP9B, a P4-ATPase (a putative aminophospholipid translocase), localizes to the trans-Golgi network in a CDC50 protein-independent manner."
Takatsu H., Baba K., Shima T., Umino H., Kato U., Umeda M., Nakayama K., Shin H.W.
J. Biol. Chem. 286:38159-38167(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TMEM30A, SUBCELLULAR LOCATION.
[10]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] ILE-157 AND PRO-931.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ580093 mRNA. Translation: CAE30472.1.
AJ580094 mRNA. Translation: CAE30473.1.
AL161777, AL356785 Genomic DNA. Translation: CAI39713.1. Sequence problems.
AL161777, AL356785 Genomic DNA. Translation: CAI39714.1. Sequence problems.
AL161777, AL356785, AL590077 Genomic DNA. Translation: CAI39716.1. Sequence problems.
AL356785, AL161777 Genomic DNA. Translation: CAI41444.1. Sequence problems.
AL356785, AL161777 Genomic DNA. Translation: CAI41445.1. Sequence problems.
AL356785, AL161777, AL590077 Genomic DNA. Translation: CAI41446.1. Sequence problems.
AL356785 Genomic DNA. Translation: CAI41447.1. Sequence problems.
AL590077, AL356785, AL161777 Genomic DNA. Translation: CAI40418.1. Sequence problems.
AK091552 mRNA. Translation: BAC03692.1. Different initiation.
AK125474 mRNA. Translation: BAC86172.1. Different initiation.
AK125986 mRNA. Translation: BAC86377.1. Different initiation.
AK131262 mRNA. Translation: BAD18440.1. Different initiation.
CCDSCCDS14668.1. [Q8NB49-1]
CCDS35410.1. [Q8NB49-3]
RefSeqNP_001010986.1. NM_001010986.2.
NP_775965.2. NM_173694.4.
UniGeneHs.88252.

3D structure databases

ProteinModelPortalQ8NB49.
SMRQ8NB49. Positions 390-702.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid130370. 2 interactions.

PTM databases

PhosphoSiteQ8NB49.

Polymorphism databases

DMDM62512178.

Proteomic databases

MaxQBQ8NB49.
PaxDbQ8NB49.
PRIDEQ8NB49.

Protocols and materials databases

DNASU286410.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000327569; ENSP00000332756; ENSG00000101974. [Q8NB49-1]
ENST00000359686; ENSP00000352715; ENSG00000101974. [Q8NB49-2]
ENST00000361648; ENSP00000355165; ENSG00000101974. [Q8NB49-3]
ENST00000370543; ENSP00000359574; ENSG00000101974. [Q8NB49-4]
GeneID286410.
KEGGhsa:286410.
UCSCuc004faz.3. human. [Q8NB49-1]
uc004fba.3. human. [Q8NB49-3]

Organism-specific databases

CTD286410.
GeneCardsGC0XM138808.
HGNCHGNC:13554. ATP11C.
HPAHPA030830.
MIM300516. gene.
neXtProtNX_Q8NB49.
PharmGKBPA25103.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0474.
HOVERGENHBG050601.
InParanoidQ8NB49.
KOK01530.
OMAPRLYMKI.
OrthoDBEOG7HHWRB.
PhylomeDBQ8NB49.
TreeFamTF326897.

Enzyme and pathway databases

ReactomeREACT_15518. Transmembrane transport of small molecules.

Gene expression databases

BgeeQ8NB49.
GenevestigatorQ8NB49.

Family and domain databases

Gene3D2.70.150.10. 2 hits.
3.40.1110.10. 1 hit.
3.40.50.1000. 2 hits.
InterProIPR023299. ATPase_P-typ_cyto_domN.
IPR018303. ATPase_P-typ_P_site.
IPR006539. ATPase_P-typ_Plipid-transp.
IPR008250. ATPase_P-typ_transduc_dom_A.
IPR001757. Cation_transp_P_typ_ATPase.
IPR023214. HAD-like_dom.
[Graphical view]
PANTHERPTHR24092. PTHR24092. 1 hit.
PfamPF00122. E1-E2_ATPase. 1 hit.
[Graphical view]
SUPFAMSSF56784. SSF56784. 3 hits.
SSF81660. SSF81660. 1 hit.
TIGRFAMsTIGR01652. ATPase-Plipid. 1 hit.
TIGR01494. ATPase_P-type. 3 hits.
PROSITEPS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi286410.
NextBio96190.
PROQ8NB49.
SOURCESearch...

Entry information

Entry nameAT11C_HUMAN
AccessionPrimary (citable) accession number: Q8NB49
Secondary accession number(s): Q5JT69 expand/collapse secondary AC list , Q5JT70, Q5JT71, Q5JT72, Q5JT73, Q6ZND5, Q6ZU50, Q6ZUP7, Q70IJ9, Q70IK0, Q8WX24
Entry history
Integrated into UniProtKB/Swiss-Prot: April 30, 2003
Last sequence update: April 12, 2005
Last modified: July 9, 2014
This is version 119 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 X

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