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Protein

Protein tyrosine phosphatase type IVA 1

Gene

PTP4A1

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

Functioni

Protein tyrosine phosphatase which stimulates progression from G1 into S phase during mitosis. May play a role in the development and maintenance of differentiating epithelial tissues. Enhances cell proliferation, cell motility and invasive activity, and promotes cancer metastasis.3 Publications

Catalytic activityi

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.1 Publication

Enzyme regulationi

Inhibited by sodium orthovanadate and pentamidine.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei72 – 721Proton donorCurated
Active sitei104 – 1041Phosphocysteine intermediate
Binding sitei110 – 1101Substrate

GO - Molecular functioni

  1. protein tyrosine phosphatase activity Source: UniProtKB

GO - Biological processi

  1. cell cycle Source: UniProtKB-KW
  2. multicellular organismal development Source: UniProtKB-KW
  3. peptidyl-tyrosine dephosphorylation Source: GOC
  4. positive regulation of cell migration Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Hydrolase, Protein phosphatase

Keywords - Biological processi

Cell cycle

Names & Taxonomyi

Protein namesi
Recommended name:
Protein tyrosine phosphatase type IVA 1 (EC:3.1.3.48)
Alternative name(s):
PTP(CAAXI)
Protein-tyrosine phosphatase 4a1
Protein-tyrosine phosphatase of regenerating liver 1
Short name:
PRL-1
Gene namesi
Name:PTP4A1
Synonyms:PRL1, PTPCAAX1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 6

Organism-specific databases

HGNCiHGNC:9634. PTP4A1.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytoplasmic side of plasma membrane Source: UniProtKB
  3. early endosome Source: UniProtKB-SubCell
  4. endoplasmic reticulum Source: UniProtKB-SubCell
  5. extracellular vesicular exosome Source: UniProtKB
  6. spindle Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoskeleton, Endoplasmic reticulum, Endosome, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi13 – 131T → F: Reduces trimerization. 1 Publication
Mutagenesisi71 – 711D → A: No effect on catalytic activity. 1 Publication
Mutagenesisi72 – 721D → A: 80% loss of catalytic activity; delay in progression through G2/M. 1 Publication
Mutagenesisi104 – 1041C → S: Abolishes enzymatic activity. 1 Publication
Mutagenesisi131 – 1311Q → A: Reduces trimerization. 1 Publication
Mutagenesisi170 – 1701C → S: Redistributes to the nucleus in resting cells, but still locates to the mitotic spindle in dividing cells. Induces defects in cytokinesis. 1 Publication
Mutagenesisi171 – 1711C → S: No effect on subcellular location. 1 Publication

Organism-specific databases

PharmGKBiPA33977.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 170170Protein tyrosine phosphatase type IVA 1PRO_0000094780Add
BLAST
Propeptidei171 – 1733Removed in mature formCuratedPRO_0000396726

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi49 ↔ 1041 Publication
Modified residuei170 – 1701Cysteine methyl esterCurated
Lipidationi170 – 1701S-farnesyl cysteine1 Publication

Post-translational modificationi

Farnesylated. Farnesylation is required for membrane targeting. Unfarnesylated forms are shifted into the nucleus.

Keywords - PTMi

Disulfide bond, Lipoprotein, Methylation, Prenylation

Proteomic databases

MaxQBiQ93096.
PaxDbiQ93096.
PRIDEiQ93096.

PTM databases

DEPODiQ93096.
PhosphoSiteiQ93096.

Expressioni

Tissue specificityi

Expressed in bone marrow, lymph nodes, T lymphocytes, spleen, thymus and tonsil. Overexpressed in tumor cell lines.2 Publications

Developmental stagei

Expressed in fetal liver.1 Publication

Inductioni

Strongly down-regulated upon tetrodotoxin treatment.1 Publication

Gene expression databases

BgeeiQ93096.
CleanExiHS_PTP4A1.
ExpressionAtlasiQ93096. baseline and differential.
GenevestigatoriQ93096.

Organism-specific databases

HPAiHPA003281.

Interactioni

Subunit structurei

Homotrimer. Interacts with ATF5 (By similarity). Interacts with tubulin.By similarity2 Publications

Protein-protein interaction databases

BioGridi113578. 16 interactions.
IntActiQ93096. 4 interactions.
MINTiMINT-194351.
STRINGi9606.ENSP00000359685.

Structurei

Secondary structure

1
173
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi10 – 145Combined sources
Beta strandi17 – 215Combined sources
Helixi27 – 293Combined sources
Helixi30 – 3910Combined sources
Beta strandi42 – 476Combined sources
Helixi56 – 605Combined sources
Beta strandi64 – 674Combined sources
Beta strandi72 – 743Combined sources
Helixi78 – 9417Combined sources
Beta strandi99 – 1035Combined sources
Beta strandi105 – 1084Combined sources
Turni109 – 1113Combined sources
Helixi112 – 12110Combined sources
Helixi126 – 1349Combined sources
Helixi143 – 1519Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1RXDX-ray1.90A/B/C2-160[»]
1XM2X-ray2.70A/B/C/D/E/F1-173[»]
DisProtiDP00255.
ProteinModelPortaliQ93096.
SMRiQ93096. Positions 9-160.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ93096.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini82 – 14867Tyrosine-protein phosphataseAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni97 – 13236Interaction with ATF5By similarityAdd
BLAST
Regioni105 – 1106Phosphate binding

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG265664.
GeneTreeiENSGT00390000009788.
HOGENOMiHOG000231265.
HOVERGENiHBG071295.
InParanoidiQ93096.
KOiK18041.
OMAiNGHRNTC.
OrthoDBiEOG7C8GJD.
PhylomeDBiQ93096.
TreeFamiTF313384.

Family and domain databases

Gene3Di3.90.190.10. 1 hit.
InterProiIPR029021. Prot-tyrosine_phosphatase-like.
IPR000387. Tyr/Dual-sp_Pase.
IPR000242. Tyr_Pase_rcpt/non-rcpt.
[Graphical view]
PfamiPF00102. Y_phosphatase. 1 hit.
[Graphical view]
SUPFAMiSSF52799. SSF52799. 1 hit.
PROSITEiPS50056. TYR_PHOSPHATASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q93096-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MARMNRPAPV EVTYKNMRFL ITHNPTNATL NKFIEELKKY GVTTIVRVCE
60 70 80 90 100
ATYDTTLVEK EGIHVLDWPF DDGAPPSNQI VDDWLSLVKI KFREEPGCCI
110 120 130 140 150
AVHCVAGLGR APVLVALALI EGGMKYEDAV QFIRQKRRGA FNSKQLLYLE
160 170
KYRPKMRLRF KDSNGHRNNC CIQ
Length:173
Mass (Da):19,815
Last modified:July 5, 2005 - v2
Checksum:i702008013D3F3835
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U48296 mRNA. Translation: AAB40597.1.
AF051160 Genomic DNA. Translation: AAC39836.1.
AK312526 mRNA. Translation: BAG35425.1.
CR749458 mRNA. Translation: CAH18292.1.
AL135905 Genomic DNA. Translation: CAC12761.1.
CH471143 Genomic DNA. Translation: EAW88494.1.
BC023975 mRNA. Translation: AAH23975.1.
BC045571 mRNA. Translation: AAH45571.1.
U69701 mRNA. Translation: AAB09080.1.
CCDSiCCDS4965.1.
RefSeqiNP_003454.1. NM_003463.4.
XP_006715626.1. XM_006715563.1.
UniGeneiHs.227777.
Hs.706850.

Genome annotation databases

EnsembliENST00000370651; ENSP00000359685; ENSG00000112245.
GeneIDi7803.
KEGGihsa:7803.
UCSCiuc003pek.3. human.

Polymorphism databases

DMDMi68566217.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U48296 mRNA. Translation: AAB40597.1.
AF051160 Genomic DNA. Translation: AAC39836.1.
AK312526 mRNA. Translation: BAG35425.1.
CR749458 mRNA. Translation: CAH18292.1.
AL135905 Genomic DNA. Translation: CAC12761.1.
CH471143 Genomic DNA. Translation: EAW88494.1.
BC023975 mRNA. Translation: AAH23975.1.
BC045571 mRNA. Translation: AAH45571.1.
U69701 mRNA. Translation: AAB09080.1.
CCDSiCCDS4965.1.
RefSeqiNP_003454.1. NM_003463.4.
XP_006715626.1. XM_006715563.1.
UniGeneiHs.227777.
Hs.706850.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1RXDX-ray1.90A/B/C2-160[»]
1XM2X-ray2.70A/B/C/D/E/F1-173[»]
DisProtiDP00255.
ProteinModelPortaliQ93096.
SMRiQ93096. Positions 9-160.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113578. 16 interactions.
IntActiQ93096. 4 interactions.
MINTiMINT-194351.
STRINGi9606.ENSP00000359685.

Chemistry

BindingDBiQ93096.
ChEMBLiCHEMBL1075169.

PTM databases

DEPODiQ93096.
PhosphoSiteiQ93096.

Polymorphism databases

DMDMi68566217.

Proteomic databases

MaxQBiQ93096.
PaxDbiQ93096.
PRIDEiQ93096.

Protocols and materials databases

DNASUi7803.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000370651; ENSP00000359685; ENSG00000112245.
GeneIDi7803.
KEGGihsa:7803.
UCSCiuc003pek.3. human.

Organism-specific databases

CTDi7803.
GeneCardsiGC06P064279.
HGNCiHGNC:9634. PTP4A1.
HPAiHPA003281.
MIMi601585. gene.
neXtProtiNX_Q93096.
PharmGKBiPA33977.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG265664.
GeneTreeiENSGT00390000009788.
HOGENOMiHOG000231265.
HOVERGENiHBG071295.
InParanoidiQ93096.
KOiK18041.
OMAiNGHRNTC.
OrthoDBiEOG7C8GJD.
PhylomeDBiQ93096.
TreeFamiTF313384.

Miscellaneous databases

ChiTaRSiPTP4A1. human.
EvolutionaryTraceiQ93096.
GeneWikiiPTP4A1.
GenomeRNAii7803.
NextBioi30184.
PROiQ93096.
SOURCEiSearch...

Gene expression databases

BgeeiQ93096.
CleanExiHS_PTP4A1.
ExpressionAtlasiQ93096. baseline and differential.
GenevestigatoriQ93096.

Family and domain databases

Gene3Di3.90.190.10. 1 hit.
InterProiIPR029021. Prot-tyrosine_phosphatase-like.
IPR000387. Tyr/Dual-sp_Pase.
IPR000242. Tyr_Pase_rcpt/non-rcpt.
[Graphical view]
PfamiPF00102. Y_phosphatase. 1 hit.
[Graphical view]
SUPFAMiSSF52799. SSF52799. 1 hit.
PROSITEiPS50056. TYR_PHOSPHATASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Prenylation of oncogenic human PTP(CAAX) protein tyrosine phosphatases."
    Cates C.A., Michael R.L., Stayrook K.R., Harvey K.A., Burke Y.D., Randall S.K., Crowell P.L., Crowell D.N.
    Cancer Lett. 110:49-55(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], ENZYME ACTIVITY, ISOPRENYLATION AT CYS-170.
    Tissue: Mammary carcinoma.
  2. "The gene encoding human nuclear protein tyrosine phosphatase, PRL-1. Cloning, chromosomal localization, and identification of an intron enhancer."
    Peng Y., Genin A., Spinner N.B., Diamond R.H., Taub R.
    J. Biol. Chem. 273:17286-17295(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Tissue: Regenerating liver.
  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].
    Tissue: Thalamus.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Fetal liver.
  5. "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].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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: Muscle and Testis.
  8. "Multiple phosphotyrosine phosphatase mRNAs are expressed in the human lung fibroblast cell line WI-38."
    Dayton M.A., Knobloch T.J.
    Recept. Signal Transduct. 7:241-256(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 80-163.
    Tissue: Lung fibroblast.
  9. "Subcellular localization of intracellular protein tyrosine phosphatases in T cells."
    Gjoerloff-Wingren A., Saxena M., Han S., Wang X., Alonso A., Renedo M., Oh P., Williams S., Schnitzer J., Mustelin T.
    Eur. J. Immunol. 30:2412-2421(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
  10. "The tyrosine phosphatase PRL-1 localizes to the endoplasmic reticulum and the mitotic spindle and is required for normal mitosis."
    Wang J., Kirby C.E., Herbst R.
    J. Biol. Chem. 277:46659-46668(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF ASP-71; ASP-72; CYS-104; CYS-170 AND CYS-171, INTERACTION WITH TUBULIN, FUNCTION.
  11. "Pentamidine is an inhibitor of PRL phosphatases with anticancer activity."
    Pathak M.K., Dhawan D., Lindner D.J., Borden E.C., Farver C., Yi T.
    Mol. Cancer Ther. 1:1255-1264(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION.
  12. "Enhanced cell cycle progression and down regulation of p21(Cip1/Waf1) by PRL tyrosine phosphatases."
    Werner S.R., Lee P.A., DeCamp M.W., Crowell D.N., Randall S.K., Crowell P.L.
    Cancer Lett. 202:201-211(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  13. "PRL-3 and PRL-1 promote cell migration, invasion, and metastasis."
    Zeng Q., Dong J.-M., Guo K., Li J., Tan H.-X., Koh V., Pallen C.J., Manser E., Hong W.
    Cancer Res. 63:2716-2722(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  14. "Potential effects of tetrodotoxin exposure to human glial cells postulated using microarray approach."
    Raghavendra Prasad H.S., Qi Z., Srinivasan K.N., Gopalakrishnakone P.
    Toxicon 44:597-608(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "Trimeric structure of PRL-1 phosphatase reveals an active enzyme conformation and regulation mechanisms."
    Jeong D.G., Kim S.J., Kim J.H., Son J.H., Park M.R., Lim S.M., Yoon T.-S., Ryu S.E.
    J. Mol. Biol. 345:401-413(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF MUTANT SER-104, DISULFIDE BOND, SUBCELLULAR LOCATION, SUBUNIT, MUTAGENESIS OF THR-13 AND GLN-131, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiTP4A1_HUMAN
AccessioniPrimary (citable) accession number: Q93096
Secondary accession number(s): B2R6C8, O00648, Q49A54
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: July 5, 2005
Last modified: January 7, 2015
This is version 127 of the entry and version 2 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

3D-structure, 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.