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Q8NB49

- AT11C_HUMAN

UniProt

Q8NB49 - AT11C_HUMAN

Protein

Phospholipid-transporting ATPase IG

Gene

ATP11C

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 121 (01 Oct 2014)
      Sequence version 3 (12 Apr 2005)
      Previous versions | rss
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    Functioni

    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.By similarity

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei412 – 41214-aspartylphosphate intermediateBy similarity
    Metal bindingi819 – 8191MagnesiumBy similarity
    Metal bindingi823 – 8231MagnesiumBy similarity

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. cation-transporting ATPase activity Source: InterPro
    3. magnesium ion binding Source: InterPro
    4. phospholipid-translocating ATPase activity Source: UniProtKB-EC
    5. protein binding Source: UniProtKB

    GO - Biological processi

    1. ion transmembrane transport Source: Reactome
    2. phospholipid translocation Source: UniProtKB
    3. transmembrane transport Source: Reactome

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Lipid transport, Transport

    Keywords - Ligandi

    ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_25149. Ion transport by P-type ATPases.

    Names & Taxonomyi

    Protein namesi
    Recommended 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 namesi
    Name:ATP11C
    Synonyms:ATPIG, ATPIQ
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:13554. ATP11C.

    Subcellular locationi

    Cell membrane 1 Publication; Multi-pass membrane protein 1 Publication. Endoplasmic reticulum membrane 1 Publication
    Note: Efficient exit from the endoplasmic reticulum requires the presence of TMEM30A. Some cell membrane localization observed in the presence of TMEM30B.

    GO - Cellular componenti

    1. endoplasmic reticulum Source: UniProtKB
    2. endoplasmic reticulum membrane Source: UniProtKB-SubCell
    3. integral component of membrane Source: UniProtKB-KW
    4. lysosomal membrane Source: UniProtKB
    5. plasma membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Endoplasmic reticulum, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA25103.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 11321132Phospholipid-transporting ATPase IGPRO_0000046373Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei445 – 4451Phosphoserine1 Publication
    Modified residuei1108 – 11081Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ8NB49.
    PaxDbiQ8NB49.
    PRIDEiQ8NB49.

    PTM databases

    PhosphoSiteiQ8NB49.

    Expressioni

    Tissue specificityi

    Widely expressed.1 Publication

    Gene expression databases

    BgeeiQ8NB49.
    GenevestigatoriQ8NB49.

    Organism-specific databases

    HPAiHPA030830.

    Interactioni

    Subunit structurei

    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.1 PublicationCurated

    Protein-protein interaction databases

    BioGridi130370. 2 interactions.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8NB49.
    SMRiQ8NB49. Positions 390-702.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 6666CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini86 – 861ExtracellularSequence Analysis
    Topological domaini108 – 290183CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini312 – 34635ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini368 – 879512CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini901 – 9088ExtracellularSequence Analysis
    Topological domaini930 – 95526CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini977 – 99519ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini1017 – 102610CytoplasmicSequence Analysis
    Topological domaini1048 – 106922ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini1091 – 113242CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei67 – 8519HelicalSequence AnalysisAdd
    BLAST
    Transmembranei87 – 10721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei291 – 31121HelicalSequence AnalysisAdd
    BLAST
    Transmembranei347 – 36721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei880 – 90021HelicalSequence AnalysisAdd
    BLAST
    Transmembranei909 – 92921HelicalSequence AnalysisAdd
    BLAST
    Transmembranei956 – 97621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei996 – 101621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei1027 – 104721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei1070 – 109021HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0474.
    HOVERGENiHBG050601.
    InParanoidiQ8NB49.
    KOiK01530.
    OMAiPRLYMKI.
    OrthoDBiEOG7HHWRB.
    PhylomeDBiQ8NB49.
    TreeFamiTF326897.

    Family and domain databases

    Gene3Di2.70.150.10. 2 hits.
    3.40.1110.10. 1 hit.
    3.40.50.1000. 2 hits.
    InterProiIPR023299. 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]
    PANTHERiPTHR24092. PTHR24092. 1 hit.
    PfamiPF00122. E1-E2_ATPase. 1 hit.
    [Graphical view]
    SUPFAMiSSF56784. SSF56784. 3 hits.
    SSF81660. SSF81660. 1 hit.
    TIGRFAMsiTIGR01652. ATPase-Plipid. 1 hit.
    TIGR01494. ATPase_P-type. 3 hits.
    PROSITEiPS00154. ATPASE_E1_E2. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q8NB49-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MQMVPSLPPA SECAGEEKRV GTRTVFVGNH PVSETEAYIA QRFCDNRIVS     50
    SKYTLWNFLP KNLFEQFRRI ANFYFLIIFL VQVTVDTPTS PVTSGLPLFF 100
    VITVTAIKQG YEDCLRHRAD NEVNKSTVYI IENAKRVRKE SEKIKVGDVV 150
    EVQADETFPC DLILLSSCTT DGTCYVTTAS LDGESNCKTH YAVRDTIALC 200
    TAESIDTLRA AIECEQPQPD LYKFVGRINI YSNSLEAVAR SLGPENLLLK 250
    GATLKNTEKI YGVAVYTGME TKMALNYQGK SQKRSAVEKS INAFLIVYLF 300
    ILLTKAAVCT TLKYVWQSTP YNDEPWYNQK TQKERETLKV LKMFTDFLSF 350
    MVLFNFIIPV SMYVTVEMQK FLGSFFISWD KDFYDEEINE GALVNTSDLN 400
    EELGQVDYVF TDKTGTLTEN SMEFIECCID GHKYKGVTQE VDGLSQTDGT 450
    LTYFDKVDKN REELFLRALC LCHTVEIKTN DAVDGATESA ELTYISSSPD 500
    EIALVKGAKR YGFTFLGNRN GYMRVENQRK EIEEYELLHT LNFDAVRRRM 550
    SVIVKTQEGD ILLFCKGADS AVFPRVQNHE IELTKVHVER NAMDGYRTLC 600
    VAFKEIAPDD YERINRQLIE AKMALQDREE KMEKVFDDIE TNMNLIGATA 650
    VEDKLQDQAA ETIEALHAAG LKVWVLTGDK METAKSTCYA CRLFQTNTEL 700
    LELTTKTIEE SERKEDRLHE LLIEYRKKLL HEFPKSTRSF KKAWTEHQEY 750
    GLIIDGSTLS LILNSSQDSS SNNYKSIFLQ ICMKCTAVLC CRMAPLQKAQ 800
    IVRMVKNLKG SPITLSIGDG ANDVSMILES HVGIGIKGKE GRQAARNSDY 850
    SVPKFKHLKK LLLAHGHLYY VRIAHLVQYF FYKNLCFILP QFLYQFFCGF 900
    SQQPLYDAAY LTMYNICFTS LPILAYSLLE QHINIDTLTS DPRLYMKISG 950
    NAMLQLGPFL YWTFLAAFEG TVFFFGTYFL FQTASLEENG KVYGNWTFGT 1000
    IVFTVLVFTV TLKLALDTRF WTWINHFVIW GSLAFYVFFS FFWGGIIWPF 1050
    LKQQRMYFVF AQMLSSVSTW LAIILLIFIS LFPEILLIVL KNVRRRSARR 1100
    NLSCRRASDS LSARPSVRPL LLRTFSDESN VL 1132
    Length:1,132
    Mass (Da):129,477
    Last modified:April 12, 2005 - v3
    Checksum:i74B63B20A5C6E49D
    GO
    Isoform 2 (identifier: Q8NB49-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1100-1132: RNLSCRRASDSLSARPSVRPLLLRTFSDESNVL → VHHLISSSA

    Note: No experimental confirmation available.

    Show »
    Length:1,108
    Mass (Da):126,710
    Checksum:iADC1995E368B8C4E
    GO
    Isoform 3 (identifier: Q8NB49-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1100-1132: RNLSCRRASDSLSARPSVRPLLLRTFSDESNVL → NPNLELPMLLSYKHTDSGYS

    Show »
    Length:1,119
    Mass (Da):128,040
    Checksum:i2F1EF15A73AB3947
    GO
    Isoform 4 (identifier: Q8NB49-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1100-1132: RNLSCRRASDSLSARPSVRPLLLRTFSDESNVL → VTKRLPSSGTSAIFMLSQTSSNHSFSWSE

    Note: No experimental confirmation available.

    Show »
    Length:1,128
    Mass (Da):128,933
    Checksum:i5928DF8ED2988A7C
    GO

    Sequence cautioni

    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.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti537 – 5371L → P in BAC86377. (PubMed:14702039)Curated
    Sequence conflicti873 – 8731I → V in BAC86377. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti114 – 1141C → W.1 Publication
    Corresponds to variant rs2491014 [ dbSNP | Ensembl ].
    VAR_021827
    Natural varianti157 – 1571T → I in a colorectal cancer sample; somatic mutation. 1 Publication
    VAR_036501
    Natural varianti522 – 5221Y → C.
    Corresponds to variant rs17281983 [ dbSNP | Ensembl ].
    VAR_055546
    Natural varianti931 – 9311Q → P in a colorectal cancer sample; somatic mutation. 1 Publication
    VAR_036502
    Natural varianti972 – 9721V → M.
    Corresponds to variant rs55724992 [ dbSNP | Ensembl ].
    VAR_061036

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1100 – 113233RNLSC…ESNVL → VHHLISSSA in isoform 2. 1 PublicationVSP_007309Add
    BLAST
    Alternative sequencei1100 – 113233RNLSC…ESNVL → NPNLELPMLLSYKHTDSGYS in isoform 3. 1 PublicationVSP_013373Add
    BLAST
    Alternative sequencei1100 – 113233RNLSC…ESNVL → VTKRLPSSGTSAIFMLSQTS SNHSFSWSE in isoform 4. 1 PublicationVSP_013374Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS14668.1. [Q8NB49-1]
    CCDS35410.1. [Q8NB49-3]
    RefSeqiNP_001010986.1. NM_001010986.2.
    NP_775965.2. NM_173694.4.
    UniGeneiHs.88252.

    Genome annotation databases

    EnsembliENST00000327569; ENSP00000332756; ENSG00000101974. [Q8NB49-1]
    ENST00000361648; ENSP00000355165; ENSG00000101974. [Q8NB49-3]
    GeneIDi286410.
    KEGGihsa:286410.
    UCSCiuc004faz.3. human. [Q8NB49-1]
    uc004fba.3. human. [Q8NB49-3]

    Polymorphism databases

    DMDMi62512178.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSi CCDS14668.1. [Q8NB49-1 ]
    CCDS35410.1. [Q8NB49-3 ]
    RefSeqi NP_001010986.1. NM_001010986.2.
    NP_775965.2. NM_173694.4.
    UniGenei Hs.88252.

    3D structure databases

    ProteinModelPortali Q8NB49.
    SMRi Q8NB49. Positions 390-702.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 130370. 2 interactions.

    PTM databases

    PhosphoSitei Q8NB49.

    Polymorphism databases

    DMDMi 62512178.

    Proteomic databases

    MaxQBi Q8NB49.
    PaxDbi Q8NB49.
    PRIDEi Q8NB49.

    Protocols and materials databases

    DNASUi 286410.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000327569 ; ENSP00000332756 ; ENSG00000101974 . [Q8NB49-1 ]
    ENST00000361648 ; ENSP00000355165 ; ENSG00000101974 . [Q8NB49-3 ]
    GeneIDi 286410.
    KEGGi hsa:286410.
    UCSCi uc004faz.3. human. [Q8NB49-1 ]
    uc004fba.3. human. [Q8NB49-3 ]

    Organism-specific databases

    CTDi 286410.
    GeneCardsi GC0XM138808.
    HGNCi HGNC:13554. ATP11C.
    HPAi HPA030830.
    MIMi 300516. gene.
    neXtProti NX_Q8NB49.
    PharmGKBi PA25103.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0474.
    HOVERGENi HBG050601.
    InParanoidi Q8NB49.
    KOi K01530.
    OMAi PRLYMKI.
    OrthoDBi EOG7HHWRB.
    PhylomeDBi Q8NB49.
    TreeFami TF326897.

    Enzyme and pathway databases

    Reactomei REACT_25149. Ion transport by P-type ATPases.

    Miscellaneous databases

    GenomeRNAii 286410.
    NextBioi 96190.
    PROi Q8NB49.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q8NB49.
    Genevestigatori Q8NB49.

    Family and domain databases

    Gene3Di 2.70.150.10. 2 hits.
    3.40.1110.10. 1 hit.
    3.40.50.1000. 2 hits.
    InterProi IPR023299. 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 ]
    PANTHERi PTHR24092. PTHR24092. 1 hit.
    Pfami PF00122. E1-E2_ATPase. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56784. SSF56784. 3 hits.
    SSF81660. SSF81660. 1 hit.
    TIGRFAMsi TIGR01652. ATPase-Plipid. 1 hit.
    TIGR01494. ATPase_P-type. 3 hits.
    PROSITEi PS00154. ATPASE_E1_E2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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.
      , 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    5. 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. Cited for: VARIANTS [LARGE SCALE ANALYSIS] ILE-157 AND PRO-931.

    Entry informationi

    Entry nameiAT11C_HUMAN
    AccessioniPrimary (citable) accession number: Q8NB49
    Secondary accession number(s): Q5JT69
    , Q5JT70, Q5JT71, Q5JT72, Q5JT73, Q6ZND5, Q6ZU50, Q6ZUP7, Q70IJ9, Q70IK0, Q8WX24
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 30, 2003
    Last sequence update: April 12, 2005
    Last modified: October 1, 2014
    This is version 121 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome X
      Human chromosome X: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3