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P35236 (PTN7_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 140. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tyrosine-protein phosphatase non-receptor type 7

EC=3.1.3.48
Alternative name(s):
Hematopoietic protein-tyrosine phosphatase
Short name=HEPTP
Protein-tyrosine phosphatase LC-PTP
Gene names
Name:PTPN7
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length360 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Protein phosphatase that acts preferentially on tyrosine-phosphorylated MAPK1. Plays a role in the regulation of T and B-lymphocyte development and signal transduction. Ref.1 Ref.2 Ref.7 Ref.8 Ref.9 Ref.10

Catalytic activity

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

Enzyme regulation

Inhibited in cells after FCER1A triggering By similarity.

Subunit structure

Monomer. Interacts with MAPK1, MAPK3 and several other MAP kinases. Ref.7 Ref.8 Ref.9 Ref.10 Ref.16

Subcellular location

Cytoplasm. Cytoplasmcytoskeleton By similarity Ref.11.

Tissue specificity

Expressed exclusively in thymus and spleen. Ref.1 Ref.2

Post-translational modification

Phosphorylated on serine residues in resting T-cells. Phosphorylation increases upon exposure to stimuli that increase intracellular cAMP levels. Phosphorylation leads to dissociation of bound MAP kinases. Ref.8 Ref.9 Ref.11

Oxidized at active site cysteine. Treatment with pervanadate (vanadate and H2O2) or with antigen enhanced oxidation of active site cysteine By similarity.

Sequence similarities

Belongs to the protein-tyrosine phosphatase family. Non-receptor class subfamily.

Contains 1 tyrosine-protein phosphatase domain.

Sequence caution

The sequence AAA59531.1 differs from that shown. Reason: Frameshift at position 5.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

MAPK1P284825EBI-2265723,EBI-959949

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P35236-1)

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.
Isoform 2 (identifier: P35236-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MGASFWPIRQAREQQRRALSFRQTSWLSEPPLGPAPHLSM
Isoform 3 (identifier: P35236-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MVGKAWPLTH...PLGPAPHLSM

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 360360Tyrosine-protein phosphatase non-receptor type 7
PRO_0000094761

Regions

Domain97 – 350254Tyrosine-protein phosphatase
Region38 – 5114Interaction with MAP kinases
Region291 – 2977Substrate binding

Sites

Active site2911Phosphocysteine intermediate Ref.7
Binding site2571Substrate
Binding site3351Substrate

Amino acid modifications

Modified residue441Phosphoserine Ref.9 Ref.11 Ref.14
Modified residue661Phosphothreonine Ref.8 Ref.13
Modified residue931Phosphoserine Ref.8
Modified residue1431Phosphoserine Ref.14
Modified residue2911Cysteine sulfenic acid (-SOH) By similarity

Natural variations

Alternative sequence11M → MGASFWPIRQAREQQRRALS FRQTSWLSEPPLGPAPHLSM in isoform 2.
VSP_026925
Alternative sequence11M → MVGKAWPLTHSQGTGPWAPE GHRREAADPWWQRQQAREGR MQLGCAWVAARRGGGRKLAS WSLLSPQRQTDRQTDSWQEA AWGPQLLQQTSWLSEPPLGP APHLSM in isoform 3.
VSP_047275

Experimental info

Mutagenesis441S → A: Prevents dissociation of bound MAP kinase and enhances their dephosphorylation. Ref.11
Mutagenesis441S → D: Reduces binding of MAP kinase. Ref.11
Mutagenesis661T → A: Prevents dissociation of bound MAP kinase and enhances their dephosphorylation; when associated with A-93. Ref.8
Mutagenesis931S → A: Prevents dissociation of bound MAP kinase and enhances their dephosphorylation; when associated with A-66. Ref.8
Mutagenesis1251Y → A: Strongly reduced catalytic activity. Ref.12
Mutagenesis2571D → A: Loss of catalytic activity. Ref.12
Mutagenesis2911C → S: Loss of catalytic activity. Ref.7
Mutagenesis3351Q → A: Reduced catalytic activity. Ref.12
Sequence conflict235 – 2362QL → HV in AAA59531. Ref.2
Sequence conflict3371A → D in BAA01946. Ref.1
Isoform 3:
Sequence conflict371R → Q in BAG54453. Ref.4

Secondary structure

.................................................. 360
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 23, 2002. Version 3.
Checksum: 388A154CC55AC0EE

FASTA36040,529
        10         20         30         40         50         60 
MVQAHGGRSR AQPLTLSLGA AMTQPPPEKT PAKKHVRLQE RRGSNVALML DVRSLGAVEP 

        70         80         90        100        110        120 
ICSVNTPREV TLHFLRTAGH PLTRWALQRQ PPSPKQLEEE FLKIPSNFVS PEDLDIPGHA 

       130        140        150        160        170        180 
SKDRYKTILP NPQSRVCLGR AQSQEDGDYI NANYIRGYDG KEKVYIATQG PMPNTVSDFW 

       190        200        210        220        230        240 
EMVWQEEVSL IVMLTQLREG KEKCVHYWPT EEETYGPFQI RIQDMKECPE YTVRQLTIQY 

       250        260        270        280        290        300 
QEERRSVKHI LFSAWPDHQT PESAGPLLRL VAEVEESPET AAHPGPIVVH CSAGIGRTGC 

       310        320        330        340        350        360 
FIATRIGCQQ LKARGEVDIL GIVCQLRLDR GGMIQTAEQY QFLHHTLALY AGQLPEEPSP 

« Hide

Isoform 2 [UniParc].

Checksum: 16690FDF358E20C8
Show »

FASTA39945,002
Isoform 3 [UniParc].

Checksum: 2B1F2D395F818BE4
Show »

FASTA46552,312

References

« Hide 'large scale' references
[1]"Molecular cloning and chromosomal mapping of a human protein-tyrosine phosphatase LC-PTP."
Adachi M., Sekiya M., Isobe M., Kumura Y., Ogita Z.I., Hinoda Y., Imai K., Yachi A.
Biochem. Biophys. Res. Commun. 186:1607-1615(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, FUNCTION.
[2]"Cloning and expression of an inducible lymphoid-specific, protein tyrosine phosphatase (HePTPase)."
Zanke B., Suzuki H., Kishihara K., Mizzen L., Minden M., Pawson A., Mak T.W.
Eur. J. Immunol. 22:235-239(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY.
Tissue: Lymphocyte.
[3]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[4]"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. expand/collapse author list , 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] (ISOFORM 3).
Tissue: Hippocampus.
[5]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], ALTERNATIVE SPLICING.
[6]"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: Lymph.
[7]"Negative regulation of T cell antigen receptor signal transduction by hematopoietic tyrosine phosphatase (HePTP)."
Saxena M., Williams S., Gilman J., Mustelin T.
J. Biol. Chem. 273:15340-15344(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH MAPK1, ACTIVE SITE, MUTAGENESIS OF CYS-291.
[8]"Inhibition of T cell signaling by mitogen-activated protein kinase-targeted hematopoietic tyrosine phosphatase (HePTP)."
Saxena M., Williams S., Brockdorff J., Gilman J., Mustelin T.
J. Biol. Chem. 274:11693-11700(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH MAPK1 AND MAPK3, PHOSPHORYLATION AT THR-66 AND SER-93, MUTAGENESIS OF THR-66 AND SER-93.
[9]"Crosstalk between cAMP-dependent kinase and MAP kinase through a protein tyrosine phosphatase."
Saxena M., Williams S., Tasken K., Mustelin T.
Nat. Cell Biol. 1:305-311(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH MAPK1, PHOSPHORYLATION AT SER-44.
[10]"The MAP-kinase ERK2 is a specific substrate of the protein tyrosine phosphatase HePTP."
Pettiford S.M., Herbst R.
Oncogene 19:858-869(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH MAPK1 AND MAPK3.
[11]"Haematopoietic protein tyrosine phosphatase (HePTP) phosphorylation by cAMP-dependent protein kinase in T-cells: dynamics and subcellular location."
Nika K., Hyunh H., Williams S., Paul S., Bottini N., Tasken K., Lombroso P.J., Mustelin T.
Biochem. J. 378:335-342(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-44, MUTAGENESIS OF SER-44.
[12]"Molecular determinants of substrate recognition in hematopoietic protein-tyrosine phosphatase."
Huang Z., Zhou B., Zhang Z.-Y.
J. Biol. Chem. 279:52150-52159(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF TYR-125; ASP-257 AND GLN-335.
[13]"Phosphoproteome of resting human platelets."
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.
J. Proteome Res. 7:526-534(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-66, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Platelet.
[14]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44 AND SER-143, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[15]"Structure of the hematopoietic tyrosine phosphatase (HePTP) catalytic domain: structure of a KIM phosphatase with phosphate bound at the active site."
Mustelin T., Tautz L., Page R.
J. Mol. Biol. 354:150-163(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 65-360 OF MUTANT ASP-246 IN COMPLEX WITH SUBSTRATE ANALOG.
[16]"Crystal structures and inhibitor identification for PTPN5, PTPRR and PTPN7: a family of human MAPK-specific protein tyrosine phosphatases."
Eswaran J., von Kries J.P., Marsden B., Longman E., Debreczeni J.E., Ugochukwu E., Turnbull A., Lee W.H., Knapp S., Barr A.J.
Biochem. J. 395:483-491(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF 65-358 IN COMPLEX WITH SUBSTRATE ANALOG, SUBUNIT.
[17]"Docking interactions induce exposure of activation loop in the MAP kinase ERK2."
Zhou T., Sun L., Humphreys J., Goldsmith E.J.
Structure 14:1011-1019(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 37-52 IN COMPLEX WITH MAPK1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D11327 mRNA. Translation: BAA01946.1.
M64322 mRNA. Translation: AAA59531.1. Frameshift.
BT009848 mRNA. Translation: AAP88850.1.
AK127214 mRNA. Translation: BAG54453.1.
AL592300 Genomic DNA. Translation: CAI13108.1.
BC001746 mRNA. Translation: AAH01746.2.
PIRJH0692.
RefSeqNP_542155.1. NM_080588.2.
UniGeneHs.402773.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZC0X-ray1.85A65-360[»]
2A3KX-ray2.55A65-358[»]
2GP0X-ray2.05A65-360[»]
2GPHX-ray1.90B37-51[»]
2HVLX-ray2.40A65-360[»]
2QDCX-ray2.00A65-360[»]
2QDMX-ray2.05A65-360[»]
2QDPX-ray2.72A65-360[»]
3D42X-ray2.46A65-360[»]
3D44X-ray1.90A65-360[»]
3O4SX-ray1.90A65-360[»]
3O4TX-ray2.60A65-360[»]
3O4UX-ray2.25A65-360[»]
ProteinModelPortalP35236.
SMRP35236. Positions 65-357.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111743. 4 interactions.
DIPDIP-29118N.
IntActP35236. 4 interactions.
MINTMINT-8206881.
STRING9606.ENSP00000356248.

Chemistry

BindingDBP35236.
ChEMBLCHEMBL2219.

PTM databases

PhosphoSiteP35236.

Polymorphism databases

DMDM20141721.

Proteomic databases

PaxDbP35236.
PRIDEP35236.

Protocols and materials databases

DNASU5778.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000308986; ENSP00000311133; ENSG00000143851. [P35236-1]
ENST00000367279; ENSP00000356248; ENSG00000143851. [P35236-2]
ENST00000495688; ENSP00000420506; ENSG00000143851. [P35236-1]
GeneID5778.
KEGGhsa:5778.
UCSCuc001gxl.2. human. [P35236-2]
uc001gxo.1. human. [P35236-1]

Organism-specific databases

CTD5778.
GeneCardsGC01M202116.
H-InvDBHIX0001472.
HGNCHGNC:9659. PTPN7.
HPACAB009530.
HPA019118.
MIM176889. gene.
neXtProtNX_P35236.
PharmGKBPA34003.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5599.
HOGENOMHOG000294188.
HOVERGENHBG001594.
InParanoidP35236.
KOK18019.
OrthoDBEOG7288QX.
PhylomeDBP35236.
TreeFamTF331016.

Enzyme and pathway databases

BRENDA3.1.3.48. 2681.

Gene expression databases

ArrayExpressP35236.
BgeeP35236.
CleanExHS_PTPN7.
GenevestigatorP35236.

Family and domain databases

InterProIPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
IPR008356. Tyr_Pase_KIM-con.
IPR000242. Tyr_Pase_rcpt/non-rcpt.
[Graphical view]
PfamPF00102. Y_phosphatase. 1 hit.
[Graphical view]
PRINTSPR01778. KIMPTPASE.
PR00700. PRTYPHPHTASE.
SMARTSM00194. PTPc. 1 hit.
[Graphical view]
PROSITEPS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50055. TYR_PHOSPHATASE_PTP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPTPN7. human.
EvolutionaryTraceP35236.
GeneWikiPTPN7.
GenomeRNAi5778.
NextBio22472.
PROP35236.
SOURCESearch...

Entry information

Entry namePTN7_HUMAN
AccessionPrimary (citable) accession number: P35236
Secondary accession number(s): B3KXE1 expand/collapse secondary AC list , Q53XK4, Q5SXQ0, Q5SXQ1, Q9BV05
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: January 23, 2002
Last modified: April 16, 2014
This is version 140 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM