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Protein

Type 2 phosphatidylinositol 4,5-bisphosphate 4-phosphatase

Gene

TMEM55A

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the hydrolysis of the 4-position phosphate of phosphatidylinositol 4,5-bisphosphate. Does not hydrolyze phosphatidylinositol 3,4,5-trisphosphate, phosphatidylinositol 3,4-bisphosphate, inositol 3,5-bisphosphate, inositol 3,4-bisphosphate, phosphatidylinositol 5-monophosphate, phosphatidylinositol 4-monophosphate and phosphatidylinositol 3-monophosphate.1 Publication

Catalytic activityi

1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1-phosphatidyl-1D-myo-inositol 5-phosphate + phosphate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei107 – 1071By similarity

GO - Molecular functioni

  • phosphatidylinositol-4,5-bisphosphate 4-phosphatase activity Source: FlyBase

GO - Biological processi

  • phosphatidylinositol dephosphorylation Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Enzyme and pathway databases

BioCyciMetaCyc:HS14553-MONOMER.
BRENDAi3.1.3.78. 2681.

Chemistry

SwissLipidsiSLP:000000851.

Names & Taxonomyi

Protein namesi
Recommended name:
Type 2 phosphatidylinositol 4,5-bisphosphate 4-phosphatase (EC:3.1.3.78)
Short name:
Type 2 PtdIns-4,5-P2 4-Ptase
Alternative name(s):
PtdIns-4,5-P2 4-Ptase II
Transmembrane protein 55A
Gene namesi
Name:TMEM55A
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 8

Organism-specific databases

HGNCiHGNC:25452. TMEM55A.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei192 – 21221HelicalSequence analysisAdd
BLAST
Transmembranei227 – 24721HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

  • integral component of membrane Source: UniProtKB-KW
  • late endosome membrane Source: FlyBase
  • lysosomal membrane Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Endosome, Lysosome, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA142670771.

Polymorphism and mutation databases

BioMutaiTMEM55A.
DMDMi74728868.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 257257Type 2 phosphatidylinositol 4,5-bisphosphate 4-phosphatasePRO_0000235228Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei22 – 221PhosphothreonineCombined sources
Modified residuei33 – 331PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ8N4L2.
MaxQBiQ8N4L2.
PaxDbiQ8N4L2.
PeptideAtlasiQ8N4L2.
PRIDEiQ8N4L2.

PTM databases

iPTMnetiQ8N4L2.
PhosphoSiteiQ8N4L2.
SwissPalmiQ8N4L2.

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Gene expression databases

BgeeiQ8N4L2.
CleanExiHS_TMEM55A.
ExpressionAtlasiQ8N4L2. baseline and differential.
GenevisibleiQ8N4L2. HS.

Organism-specific databases

HPAiHPA014591.

Interactioni

Protein-protein interaction databases

BioGridi120700. 7 interactions.
IntActiQ8N4L2. 3 interactions.
STRINGi9606.ENSP00000285419.

Structurei

3D structure databases

ProteinModelPortaliQ8N4L2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi107 – 1137CX5R motif

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG4684. Eukaryota.
ENOG410XSVD. LUCA.
GeneTreeiENSGT00390000003680.
HOGENOMiHOG000231722.
HOVERGENiHBG080409.
InParanoidiQ8N4L2.
KOiK13084.
OMAiGMYFLYV.
OrthoDBiEOG7DZ8KH.
PhylomeDBiQ8N4L2.
TreeFamiTF316367.

Family and domain databases

InterProiIPR019178. PtdIns-P2-Ptase.
[Graphical view]
PANTHERiPTHR21014. PTHR21014. 1 hit.
PfamiPF09788. Tmemb_55A. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8N4L2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAADGVDERS PLLSASHSGN VTPTAPPYLQ ESSPRAELPP PYTAIASPDA
60 70 80 90 100
SGIPVINCRV CQSLINLDGK LHQHVVKCTV CNEATPIKNP PTGKKYVRCP
110 120 130 140 150
CNCLLICKDT SRRIGCPRPN CRRIINLGPV MLISEEQPAQ PALPIQPEGT
160 170 180 190 200
RVVCGHCGNT FLWMELRFNT LAKCPHCKKI SSVGSALPRR RCCAYITIGM
210 220 230 240 250
ICIFIGVGLT VGTPDFARRF RATYVSWAIA YLLGLICLIR ACYWGAIRVS

YPEHSFA
Length:257
Mass (Da):28,081
Last modified:October 1, 2002 - v1
Checksum:i2E059F7D07BA9227
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK313783 mRNA. Translation: BAG36521.1.
CH471060 Genomic DNA. Translation: EAW91672.1.
BC033892 mRNA. Translation: AAH33892.1.
CR749733 mRNA. Translation: CAH18492.1.
CCDSiCCDS6252.1.
RefSeqiNP_061180.1. NM_018710.2.
UniGeneiHs.202517.

Genome annotation databases

EnsembliENST00000285419; ENSP00000285419; ENSG00000155099.
GeneIDi55529.
KEGGihsa:55529.
UCSCiuc003yes.5. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK313783 mRNA. Translation: BAG36521.1.
CH471060 Genomic DNA. Translation: EAW91672.1.
BC033892 mRNA. Translation: AAH33892.1.
CR749733 mRNA. Translation: CAH18492.1.
CCDSiCCDS6252.1.
RefSeqiNP_061180.1. NM_018710.2.
UniGeneiHs.202517.

3D structure databases

ProteinModelPortaliQ8N4L2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120700. 7 interactions.
IntActiQ8N4L2. 3 interactions.
STRINGi9606.ENSP00000285419.

Chemistry

SwissLipidsiSLP:000000851.

PTM databases

iPTMnetiQ8N4L2.
PhosphoSiteiQ8N4L2.
SwissPalmiQ8N4L2.

Polymorphism and mutation databases

BioMutaiTMEM55A.
DMDMi74728868.

Proteomic databases

EPDiQ8N4L2.
MaxQBiQ8N4L2.
PaxDbiQ8N4L2.
PeptideAtlasiQ8N4L2.
PRIDEiQ8N4L2.

Protocols and materials databases

DNASUi55529.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000285419; ENSP00000285419; ENSG00000155099.
GeneIDi55529.
KEGGihsa:55529.
UCSCiuc003yes.5. human.

Organism-specific databases

CTDi55529.
GeneCardsiTMEM55A.
HGNCiHGNC:25452. TMEM55A.
HPAiHPA014591.
MIMi609864. gene.
neXtProtiNX_Q8N4L2.
PharmGKBiPA142670771.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4684. Eukaryota.
ENOG410XSVD. LUCA.
GeneTreeiENSGT00390000003680.
HOGENOMiHOG000231722.
HOVERGENiHBG080409.
InParanoidiQ8N4L2.
KOiK13084.
OMAiGMYFLYV.
OrthoDBiEOG7DZ8KH.
PhylomeDBiQ8N4L2.
TreeFamiTF316367.

Enzyme and pathway databases

BioCyciMetaCyc:HS14553-MONOMER.
BRENDAi3.1.3.78. 2681.

Miscellaneous databases

ChiTaRSiTMEM55A. human.
GenomeRNAii55529.
PROiQ8N4L2.
SOURCEiSearch...

Gene expression databases

BgeeiQ8N4L2.
CleanExiHS_TMEM55A.
ExpressionAtlasiQ8N4L2. baseline and differential.
GenevisibleiQ8N4L2. HS.

Family and domain databases

InterProiIPR019178. PtdIns-P2-Ptase.
[Graphical view]
PANTHERiPTHR21014. PTHR21014. 1 hit.
PfamiPF09788. Tmemb_55A. 1 hit.
[Graphical view]
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].
    Tissue: Kidney.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "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].
    Tissue: Brain.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Melanoma.
  5. "The identification and characterization of two phosphatidylinositol-4,5-bisphosphate 4-phosphatases."
    Ungewickell A., Hugge C., Kisseleva M., Chang S.-C., Zou J., Feng Y., Galyov E.E., Wilson M., Majerus P.W.
    Proc. Natl. Acad. Sci. U.S.A. 102:18854-18859(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  6. "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.
  7. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-22, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Erythroleukemia.
  8. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiTM55A_HUMAN
AccessioniPrimary (citable) accession number: Q8N4L2
Secondary accession number(s): B2R9H4, Q68CU2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 16, 2006
Last sequence update: October 1, 2002
Last modified: July 6, 2016
This is version 100 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 8
    Human chromosome 8: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

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 one 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.