Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Cell cycle control protein 50A

Gene

TMEM30A

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

Functioni

Accessory 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. The beta subunit may assist in binding of the phospholipid substrate. Required for the proper folding, assembly and ER to Golgi exit of the ATP8A2:TMEM30A flippase complex. ATP8A2:TMEM30A may be involved in regulation of neurite outgrowth, and, reconstituted to liposomes, predomiminantly transports phosphatidylserine (PS) and to a lesser extent phosphatidylethanolamine (PE). The ATP8A1:TMEM30A flippase complex seems to play a role in regulation of cell migration probably involving flippase-mediated translocation of phosphatidylethanolamine (PE) at the plasma membrane. Required for the formation of the ATP8A2, ATP8B1 and ATP8B2 P-type ATPAse intermediate phosphoenzymes. Involved in uptake of platelet-activating factor (PAF), synthetic drug alkylphospholipid edelfosine, and, probably in association with ATP8B1, of perifosine. Also mediate the export of alpha subunits ATP8A1, ATP8B1, ATP8B2, ATP8B4, ATP10A, ATP10B, ATP10D, ATP11A, ATP11B and ATP11C from the ER to other membrane localizations.4 Publications

GO - Biological processi

  • drug transmembrane transport Source: UniProtKB
  • phospholipid translocation Source: UniProtKB
  • positive regulation of neuron projection development Source: Ensembl
  • positive regulation of protein exit from endoplasmic reticulum Source: UniProtKB
  • protein localization to endosome Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Lipid transport, Transport

Protein family/group databases

TCDBi8.A.27.1.5. the cdc50 p-type atpase lipid flippase subunit (cdc50) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Cell cycle control protein 50A
Alternative name(s):
P4-ATPase flippase complex beta subunit TMEM30A
Transmembrane protein 30A
Gene namesi
Name:TMEM30A
Synonyms:C6orf67, CDC50A
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:16667. TMEM30A.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini2 – 4948CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei50 – 7021HelicalSequence AnalysisAdd
BLAST
Topological domaini71 – 325255Exoplasmic loopSequence AnalysisAdd
BLAST
Transmembranei326 – 34621HelicalSequence AnalysisAdd
BLAST
Topological domaini347 – 36115CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • apical plasma membrane Source: UniProtKB-SubCell
  • endoplasmic reticulum Source: UniProtKB
  • Golgi apparatus Source: UniProtKB-SubCell
  • integral component of membrane Source: UniProtKB-KW
  • membrane Source: UniProtKB
  • transport vesicle membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasmic vesicle, Golgi apparatus, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134936902.

Polymorphism and mutation databases

BioMutaiTMEM30A.
DMDMi74752991.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 361360Cell cycle control protein 50APRO_0000244469Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Glycosylationi180 – 1801N-linked (GlcNAc...)Sequence Analysis
Glycosylationi190 – 1901N-linked (GlcNAc...)1 Publication
Glycosylationi294 – 2941N-linked (GlcNAc...)1 Publication

Post-translational modificationi

N-glycosylated. Contains high mannose-type oligosaccharides (By similarity).By similarity

Keywords - PTMi

Acetylation, Glycoprotein

Proteomic databases

MaxQBiQ9NV96.
PaxDbiQ9NV96.
PeptideAtlasiQ9NV96.
PRIDEiQ9NV96.

PTM databases

PhosphoSiteiQ9NV96.

Expressioni

Gene expression databases

BgeeiQ9NV96.
CleanExiHS_TMEM30A.
ExpressionAtlasiQ9NV96. baseline and differential.
GenevisibleiQ9NV96. HS.

Organism-specific databases

HPAiHPA014561.

Interactioni

Subunit structurei

Component of various P4-ATPase flippase complexes which consists of a catalytic alpha subunit and an accessory beta subunit. The ATP8A2:TMEM30A flippase complex has been purified, and ATP8B1:TMEM30A and ATP8B2:TMEM30A flippase complexes have been shown to form intermediate phosphoenzymes in vitro. Interacts with alpha subunits ATP8A1, ATP8B1, ATP8B2, ATP8B4, ATP11A, ATP11B and ATP11C.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ATP8B1O435203EBI-2836942,EBI-9524729

Protein-protein interaction databases

BioGridi120872. 45 interactions.
IntActiQ9NV96. 7 interactions.
MINTiMINT-5006648.
STRINGi9606.ENSP00000230461.

Structurei

3D structure databases

ProteinModelPortaliQ9NV96.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domaini

The N-terminal domain seems to play a role in the reaction cycle of the catalytic subunit such as ATP8A2.By similarity

Sequence similaritiesi

Belongs to the CDC50/LEM3 family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG5035.
GeneTreeiENSGT00390000004660.
HOGENOMiHOG000209057.
HOVERGENiHBG055537.
InParanoidiQ9NV96.
OMAiDVTPCIC.
OrthoDBiEOG7C5M8D.
PhylomeDBiQ9NV96.
TreeFamiTF300873.

Family and domain databases

InterProiIPR005045. CDC50/LEM3_fam.
IPR030351. TMEM30A.
[Graphical view]
PANTHERiPTHR10926. PTHR10926. 1 hit.
PTHR10926:SF17. PTHR10926:SF17. 1 hit.
PfamiPF03381. CDC50. 1 hit.
[Graphical view]
PIRSFiPIRSF015840. DUF284_TM_euk. 1 hit.

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9NV96-1) [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
MAMNYNAKDE VDGGPPCAPG GTAKTRRPDN TAFKQQRLPA WQPILTAGTV
60 70 80 90 100
LPIFFIIGLI FIPIGIGIFV TSNNIREIEI DYTGTEPSSP CNKCLSPDVT
110 120 130 140 150
PCFCTINFTL EKSFEGNVFM YYGLSNFYQN HRRYVKSRDD SQLNGDSSAL
160 170 180 190 200
LNPSKECEPY RRNEDKPIAP CGAIANSMFN DTLELFLIGN DSYPIPIALK
210 220 230 240 250
KKGIAWWTDK NVKFRNPPGG DNLEERFKGT TKPVNWLKPV YMLDSDPDNN
260 270 280 290 300
GFINEDFIVW MRTAALPTFR KLYRLIERKS DLHPTLPAGR YSLNVTYNYP
310 320 330 340 350
VHYFDGRKRM ILSTISWMGG KNPFLGIAYI AVGSISFLLG VVLLVINHKY
360
RNSSNTADIT I
Length:361
Mass (Da):40,684
Last modified:October 1, 2000 - v1
Checksum:i64B3F28C3EB7801B
GO
Isoform 2 (identifier: Q9NV96-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     79-114: Missing.

Show »
Length:325
Mass (Da):36,713
Checksum:i40D7000253A6787F
GO
Isoform 3 (identifier: Q9NV96-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-119: Missing.

Note: No experimental confirmation available.
Show »
Length:242
Mass (Da):27,729
Checksum:i262B426C680712B5
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 119119Missing in isoform 3. 1 PublicationVSP_019567Add
BLAST
Alternative sequencei79 – 11436Missing in isoform 2. 2 PublicationsVSP_019568Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK001718 mRNA. Translation: BAA91859.1.
AK292823 mRNA. Translation: BAF85512.1.
AL832815 mRNA. Translation: CAH56262.1.
AL832490 mRNA. Translation: CAH56205.1.
AL162046 mRNA. Translation: CAB82389.1.
AL080250 Genomic DNA. Translation: CAI19900.1.
CH471051 Genomic DNA. Translation: EAW48743.1.
CH471051 Genomic DNA. Translation: EAW48744.1.
CH471051 Genomic DNA. Translation: EAW48745.1.
BC009006 mRNA. Translation: AAH09006.1.
CCDSiCCDS47453.1. [Q9NV96-2]
CCDS4983.1. [Q9NV96-1]
PIRiT47140.
RefSeqiNP_001137430.1. NM_001143958.1. [Q9NV96-2]
NP_060717.1. NM_018247.3. [Q9NV96-1]
UniGeneiHs.108530.

Genome annotation databases

EnsembliENST00000230461; ENSP00000230461; ENSG00000112697.
ENST00000370050; ENSP00000359067; ENSG00000112697. [Q9NV96-3]
ENST00000475111; ENSP00000431007; ENSG00000112697. [Q9NV96-2]
GeneIDi55754.
KEGGihsa:55754.
UCSCiuc003phw.2. human. [Q9NV96-1]
uc003phx.2. human. [Q9NV96-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK001718 mRNA. Translation: BAA91859.1.
AK292823 mRNA. Translation: BAF85512.1.
AL832815 mRNA. Translation: CAH56262.1.
AL832490 mRNA. Translation: CAH56205.1.
AL162046 mRNA. Translation: CAB82389.1.
AL080250 Genomic DNA. Translation: CAI19900.1.
CH471051 Genomic DNA. Translation: EAW48743.1.
CH471051 Genomic DNA. Translation: EAW48744.1.
CH471051 Genomic DNA. Translation: EAW48745.1.
BC009006 mRNA. Translation: AAH09006.1.
CCDSiCCDS47453.1. [Q9NV96-2]
CCDS4983.1. [Q9NV96-1]
PIRiT47140.
RefSeqiNP_001137430.1. NM_001143958.1. [Q9NV96-2]
NP_060717.1. NM_018247.3. [Q9NV96-1]
UniGeneiHs.108530.

3D structure databases

ProteinModelPortaliQ9NV96.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120872. 45 interactions.
IntActiQ9NV96. 7 interactions.
MINTiMINT-5006648.
STRINGi9606.ENSP00000230461.

Protein family/group databases

TCDBi8.A.27.1.5. the cdc50 p-type atpase lipid flippase subunit (cdc50) family.

PTM databases

PhosphoSiteiQ9NV96.

Polymorphism and mutation databases

BioMutaiTMEM30A.
DMDMi74752991.

Proteomic databases

MaxQBiQ9NV96.
PaxDbiQ9NV96.
PeptideAtlasiQ9NV96.
PRIDEiQ9NV96.

Protocols and materials databases

DNASUi55754.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000230461; ENSP00000230461; ENSG00000112697.
ENST00000370050; ENSP00000359067; ENSG00000112697. [Q9NV96-3]
ENST00000475111; ENSP00000431007; ENSG00000112697. [Q9NV96-2]
GeneIDi55754.
KEGGihsa:55754.
UCSCiuc003phw.2. human. [Q9NV96-1]
uc003phx.2. human. [Q9NV96-2]

Organism-specific databases

CTDi55754.
GeneCardsiGC06M075962.
HGNCiHGNC:16667. TMEM30A.
HPAiHPA014561.
MIMi611028. gene.
neXtProtiNX_Q9NV96.
PharmGKBiPA134936902.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5035.
GeneTreeiENSGT00390000004660.
HOGENOMiHOG000209057.
HOVERGENiHBG055537.
InParanoidiQ9NV96.
OMAiDVTPCIC.
OrthoDBiEOG7C5M8D.
PhylomeDBiQ9NV96.
TreeFamiTF300873.

Miscellaneous databases

ChiTaRSiTMEM30A. human.
GenomeRNAii55754.
NextBioi60753.
PROiQ9NV96.
SOURCEiSearch...

Gene expression databases

BgeeiQ9NV96.
CleanExiHS_TMEM30A.
ExpressionAtlasiQ9NV96. baseline and differential.
GenevisibleiQ9NV96. HS.

Family and domain databases

InterProiIPR005045. CDC50/LEM3_fam.
IPR030351. TMEM30A.
[Graphical view]
PANTHERiPTHR10926. PTHR10926. 1 hit.
PTHR10926:SF17. PTHR10926:SF17. 1 hit.
PfamiPF03381. CDC50. 1 hit.
[Graphical view]
PIRSFiPIRSF015840. DUF284_TM_euk. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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] (ISOFORMS 1 AND 2).
    Tissue: Trachea.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
    Tissue: Amygdala, Lymph node and Testis.
  3. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Brain.
  6. "Identification and characterization of CDC50A, CDC50B and CDC50C genes in silico."
    Katoh Y., Katoh M.
    Oncol. Rep. 12:939-943(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION.
  7. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  8. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
    Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
    J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-294.
    Tissue: Liver.
  9. "Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
    Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
    Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-190.
    Tissue: Leukemic T-cell.
  10. "CDC50A plays a key role in the uptake of the anticancer drug perifosine in human carcinoma cells."
    Munoz-Martinez F., Torres C., Castanys S., Gamarro F.
    Biochem. Pharmacol. 80:793-800(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. "Heteromeric interactions required for abundance and subcellular localization of human CDC50 proteins and class 1 P4-ATPases."
    van der Velden L.M., Wichers C.G., van Breevoort A.E., Coleman J.A., Molday R.S., Berger R., Klomp L.W., van de Graaf S.F.
    J. Biol. Chem. 285:40088-40096(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH ATP8A1; ATP8A2; ATP8B1; ATP8B2 AND ATP8B4.
  12. "CDC50 proteins are critical components of the human class-1 P4-ATPase transport machinery."
    Bryde S., Hennrich H., Verhulst P.M., Devaux P.F., Lenoir G., Holthuis J.C.
    J. Biol. Chem. 285:40562-40572(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH ATP8A1; ATP8B1; ATP8B2 AND ATP8B4.
  13. "Critical role of the beta-subunit CDC50A in the stable expression, assembly, subcellular localization, and lipid transport activity of the P4-ATPase ATP8A2."
    Coleman J.A., Molday R.S.
    J. Biol. Chem. 286:17205-17216(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ATP8A2.
  14. "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 ATP11A; ATP11B AND ATP11C, SUBCELLULAR LOCATION.
  15. "Human TMEM30a promotes uptake of antitumor and bioactive choline phospholipids into mammalian cells."
    Chen R., Brady E., McIntyre T.M.
    J. Immunol. 186:3215-3225(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiCC50A_HUMAN
AccessioniPrimary (citable) accession number: Q9NV96
Secondary accession number(s): A8K9V8
, E1P539, Q658Z3, Q96H09, Q9NSL9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: October 1, 2000
Last modified: July 22, 2015
This is version 101 of the entry and version 1 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 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.