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Q93096

- TP4A1_HUMAN

UniProt

Q93096 - TP4A1_HUMAN

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Protein

Protein tyrosine phosphatase type IVA 1

Gene

PTP4A1

Organism
Homo sapiens (Human)
Status
Reviewed - 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. 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. cytoskeleton Source: UniProtKB-KW
  4. endoplasmic reticulum Source: UniProtKB-KW
  5. endosome Source: UniProtKB-KW
  6. extracellular vesicular exosome Source: UniProt
  7. nucleus Source: Ensembl
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

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 – 145
Beta strandi17 – 215
Helixi27 – 293
Helixi30 – 3910
Beta strandi42 – 476
Helixi56 – 605
Beta strandi64 – 674
Beta strandi72 – 743
Helixi78 – 9417
Beta strandi99 – 1035
Beta strandi105 – 1084
Turni109 – 1113
Helixi112 – 12110
Helixi126 – 1349
Helixi143 – 1519

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.
OMAiDKSIAVH.
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:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS4965.1.
RefSeqi NP_003454.1. NM_003463.4.
XP_006715626.1. XM_006715563.1.
UniGenei Hs.227777.
Hs.706850.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1RXD X-ray 1.90 A/B/C 2-160 [» ]
1XM2 X-ray 2.70 A/B/C/D/E/F 1-173 [» ]
DisProti DP00255.
ProteinModelPortali Q93096.
SMRi Q93096. Positions 9-160.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 113578. 16 interactions.
IntActi Q93096. 4 interactions.
MINTi MINT-194351.
STRINGi 9606.ENSP00000359685.

Chemistry

BindingDBi Q93096.
ChEMBLi CHEMBL1075169.

PTM databases

PhosphoSitei Q93096.

Polymorphism databases

DMDMi 68566217.

Proteomic databases

MaxQBi Q93096.
PaxDbi Q93096.
PRIDEi Q93096.

Protocols and materials databases

DNASUi 7803.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000370651 ; ENSP00000359685 ; ENSG00000112245 .
GeneIDi 7803.
KEGGi hsa:7803.
UCSCi uc003pek.3. human.

Organism-specific databases

CTDi 7803.
GeneCardsi GC06P064279.
HGNCi HGNC:9634. PTP4A1.
HPAi HPA003281.
MIMi 601585. gene.
neXtProti NX_Q93096.
PharmGKBi PA33977.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG265664.
GeneTreei ENSGT00390000009788.
HOGENOMi HOG000231265.
HOVERGENi HBG071295.
InParanoidi Q93096.
KOi K18041.
OMAi DKSIAVH.
OrthoDBi EOG7C8GJD.
PhylomeDBi Q93096.
TreeFami TF313384.

Miscellaneous databases

EvolutionaryTracei Q93096.
GeneWikii PTP4A1.
GenomeRNAii 7803.
NextBioi 30184.
PROi Q93096.
SOURCEi Search...

Gene expression databases

Bgeei Q93096.
CleanExi HS_PTP4A1.
ExpressionAtlasi Q93096. baseline and differential.
Genevestigatori Q93096.

Family and domain databases

Gene3Di 3.90.190.10. 1 hit.
InterProi IPR029021. Prot-tyrosine_phosphatase-like.
IPR000387. Tyr/Dual-sp_Pase.
IPR000242. Tyr_Pase_rcpt/non-rcpt.
[Graphical view ]
Pfami PF00102. Y_phosphatase. 1 hit.
[Graphical view ]
SUPFAMi SSF52799. SSF52799. 1 hit.
PROSITEi PS50056. TYR_PHOSPHATASE_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: October 29, 2014
This is version 125 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