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Q8NB49

- AT11C_HUMAN

UniProt

Q8NB49 - AT11C_HUMAN

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Protein

Phospholipid-transporting ATPase IG

Gene

ATP11C

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

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

GO - Biological processi

  1. ion transmembrane transport Source: Reactome
  2. phospholipid translocation Source: UniProtKB
  3. positive regulation of B cell differentiation Source: Ensembl
  4. pre-B cell differentiation Source: Ensembl
  5. transmembrane transport Source: Reactome
Complete GO annotation...

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.

Protein family/group databases

TCDBi3.A.3.8.14. the p-type atpase (p-atpase) superfamily.

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. integral component of membrane Source: UniProtKB-KW
  3. lysosomal membrane Source: UniProtKB
  4. plasma membrane Source: UniProtKB
Complete GO annotation...

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. 12 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.
GeneTreeiENSGT00760000119246.
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

        10         20         30         40         50
MQMVPSLPPA SECAGEEKRV GTRTVFVGNH PVSETEAYIA QRFCDNRIVS
60 70 80 90 100
SKYTLWNFLP KNLFEQFRRI ANFYFLIIFL VQVTVDTPTS PVTSGLPLFF
110 120 130 140 150
VITVTAIKQG YEDCLRHRAD NEVNKSTVYI IENAKRVRKE SEKIKVGDVV
160 170 180 190 200
EVQADETFPC DLILLSSCTT DGTCYVTTAS LDGESNCKTH YAVRDTIALC
210 220 230 240 250
TAESIDTLRA AIECEQPQPD LYKFVGRINI YSNSLEAVAR SLGPENLLLK
260 270 280 290 300
GATLKNTEKI YGVAVYTGME TKMALNYQGK SQKRSAVEKS INAFLIVYLF
310 320 330 340 350
ILLTKAAVCT TLKYVWQSTP YNDEPWYNQK TQKERETLKV LKMFTDFLSF
360 370 380 390 400
MVLFNFIIPV SMYVTVEMQK FLGSFFISWD KDFYDEEINE GALVNTSDLN
410 420 430 440 450
EELGQVDYVF TDKTGTLTEN SMEFIECCID GHKYKGVTQE VDGLSQTDGT
460 470 480 490 500
LTYFDKVDKN REELFLRALC LCHTVEIKTN DAVDGATESA ELTYISSSPD
510 520 530 540 550
EIALVKGAKR YGFTFLGNRN GYMRVENQRK EIEEYELLHT LNFDAVRRRM
560 570 580 590 600
SVIVKTQEGD ILLFCKGADS AVFPRVQNHE IELTKVHVER NAMDGYRTLC
610 620 630 640 650
VAFKEIAPDD YERINRQLIE AKMALQDREE KMEKVFDDIE TNMNLIGATA
660 670 680 690 700
VEDKLQDQAA ETIEALHAAG LKVWVLTGDK METAKSTCYA CRLFQTNTEL
710 720 730 740 750
LELTTKTIEE SERKEDRLHE LLIEYRKKLL HEFPKSTRSF KKAWTEHQEY
760 770 780 790 800
GLIIDGSTLS LILNSSQDSS SNNYKSIFLQ ICMKCTAVLC CRMAPLQKAQ
810 820 830 840 850
IVRMVKNLKG SPITLSIGDG ANDVSMILES HVGIGIKGKE GRQAARNSDY
860 870 880 890 900
SVPKFKHLKK LLLAHGHLYY VRIAHLVQYF FYKNLCFILP QFLYQFFCGF
910 920 930 940 950
SQQPLYDAAY LTMYNICFTS LPILAYSLLE QHINIDTLTS DPRLYMKISG
960 970 980 990 1000
NAMLQLGPFL YWTFLAAFEG TVFFFGTYFL FQTASLEENG KVYGNWTFGT
1010 1020 1030 1040 1050
IVFTVLVFTV TLKLALDTRF WTWINHFVIW GSLAFYVFFS FFWGGIIWPF
1060 1070 1080 1090 1100
LKQQRMYFVF AQMLSSVSTW LAIILLIFIS LFPEILLIVL KNVRRRSARR
1110 1120 1130
NLSCRRASDS LSARPSVRPL LLRTFSDESN VL
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. 12 interactions.

Protein family/group databases

TCDBi 3.A.3.8.14. the p-type atpase (p-atpase) superfamily.

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.
GeneTreei ENSGT00760000119246.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 122 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