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Reviewed, UniProtKB/Swiss-Prot P43403 (ZAP70_HUMAN)

Last modified February 9, 2010. Version 124. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Tyrosine-protein kinase ZAP-70
    EC=2.7.10.2
Alternative name(s):
    70 kDa zeta-associated protein
    Syk-related tyrosine kinase
Gene names
Name: ZAP70
Synonyms: SRK
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length619 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Plays a role in T-cell development and lymphocyte activation. Essential for TCR-mediated IL-2 production. Isoform 1 induces TCR-mediated signal transduction, isoform 2 does not. Ref.1 Ref.5

Catalytic activity

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.

Subunit structure

Interacts with SLA2 when it is phosphorylated. Interacts with CD3Z and with phosphorylated NFAM1. Interacts with CBLB By similarity. Interacts with CBL and SLA when it is phosphorylated. The association with SLA (or SLA2) and CBL probably leads to its destruction. Interacts with SHB. Interacts with DEF6. Interacts (via SH2 domains) with RHOH By similarity. Interacts with FCRL3. Ref.1 Ref.8 Ref.9 Ref.10

Subcellular location

Cytoplasm By similarity. Cell membrane By similarity. Note: After antigen stimulation, isoform 1 concentrates at the immunological synapse and isoform 2 remains cytoplasmic. Co-localizes together with RHOH in the immunological synapse. RHOH is required for its proper localization to the cell membrane and cytoskeleton fractions in the thymocytes By similarity.

Tissue specificity

Expressed in T- and natural killer cells. Ref.1

Domain

The SH2 domains bind to the phosphorylated tyrosine-based activation motif (TAM) of CD3Z and the non-canonical phosphorylated tyrosine-based activation motif (TAM) of RHOH By similarity.

Post-translational modification

Phosphorylated on tyrosine residues upon T-cell antigen receptor (TCR) stimulation. Tyr-319 phosphorylation is essential for full activity. Ref.1 Ref.7 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16

Involvement in disease

Defects in ZAP70 are the cause of selective T-cell defect (STD) [MIM:176947]. STD is an autosomal recessive form of severe combined immunodeficiency characterized by a selective absence of CD8-type T-cells. Ref.5 Ref.19 Ref.20

Sequence similarities

Belongs to the protein kinase superfamily. Tyr protein kinase family. SYK/ZAP-70 subfamily.

Contains 1 protein kinase domain.

Contains 2 SH2 domains.

Binary interactions

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P43403-1)

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: P43403-2)

Also known as: TZK;

The sequence of this isoform differs from the canonical sequence as follows:
     1-307: Missing.
Isoform 3 (identifier: P43403-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-126: Missing.
     127-134: VRQTWKLE → MRLGPRWK
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 619619Tyrosine-protein kinase ZAP-70
PRO_0000088168

Regions

Domain10 – 10293SH2 1
Domain163 – 25492SH2 2
Domain338 – 600263Protein kinase
Nucleotide binding344 – 3529ATP By similarity

Sites

Active site4611Proton acceptor By similarity
Binding site3691ATP By similarity

Amino acid modifications

Modified residue2481Phosphotyrosine Ref.13 Ref.15
Modified residue2891Phosphoserine Ref.12
Modified residue2921Phosphotyrosine Ref.11 Ref.13 Ref.14 Ref.15 Ref.16
Modified residue3151Phosphotyrosine Ref.7 Ref.11 Ref.13 Ref.14
Modified residue3191Phosphotyrosine Ref.7 Ref.11 Ref.13 Ref.14
Modified residue4921Phosphotyrosine; by autocatalysis Ref.11 Ref.13 Ref.14 Ref.15 Ref.16
Modified residue4931Phosphotyrosine Ref.11 Ref.13 Ref.14
Modified residue6031N6-acetyllysine Ref.17

Natural variations

Alternative sequence1 – 307307Missing in isoform 2.
VSP_031156
Alternative sequence1 – 126126Missing in isoform 3.
VSP_031157
Alternative sequence127 – 1348VRQTWKLE → MRLGPRWK in isoform 3.
VSP_031158
Natural variant1751R → L: dbSNP rs55964305. Ref.21
VAR_041846
Natural variant1911P → L: dbSNP rs56403250. Ref.21
VAR_041847
Natural variant4481G → E in a head and neck squamous cell carcinoma sample; somatic mutation. Ref.21
VAR_041848
Natural variant4651R → H in STD. Ref.20
VAR_015538
Natural variant5181S → R in STD. Ref.19
VAR_006351
Natural variant5231W → L: dbSNP rs56189815. Ref.21
VAR_041849
Natural variant5411K → KLEQ in STD.
VAR_038688

Experimental info

Mutagenesis3151Y → F: No inhibition of activation. Ref.7
Mutagenesis3191Y → F: Inhibition of activation. Ref.7

Secondary structure

................................................................................ 619
Helix Strand Turn

Details...

Sequences

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

Last modified November 1, 1995. Version 1.
Checksum: D1E1A8EC66FA116F

FASTA61969,872
        10         20         30         40         50         60 
MPDPAAHLPF FYGSISRAEA EEHLKLAGMA DGLFLLRQCL RSLGGYVLSL VHDVRFHHFP 

        70         80         90        100        110        120 
IERQLNGTYA IAGGKAHCGP AELCEFYSRD PDGLPCNLRK PCNRPSGLEP QPGVFDCLRD 

       130        140        150        160        170        180 
AMVRDYVRQT WKLEGEALEQ AIISQAPQVE KLIATTAHER MPWYHSSLTR EEAERKLYSG 

       190        200        210        220        230        240 
AQTDGKFLLR PRKEQGTYAL SLIYGKTVYH YLISQDKAGK YCIPEGTKFD TLWQLVEYLK 

       250        260        270        280        290        300 
LKADGLIYCL KEACPNSSAS NASGAAAPTL PAHPSTLTHP QRRIDTLNSD GYTPEPARIT 

       310        320        330        340        350        360 
SPDKPRPMPM DTSVYESPYS DPEELKDKKL FLKRDNLLIA DIELGCGNFG SVRQGVYRMR 

       370        380        390        400        410        420 
KKQIDVAIKV LKQGTEKADT EEMMREAQIM HQLDNPYIVR LIGVCQAEAL MLVMEMAGGG 

       430        440        450        460        470        480 
PLHKFLVGKR EEIPVSNVAE LLHQVSMGMK YLEEKNFVHR DLAARNVLLV NRHYAKISDF 

       490        500        510        520        530        540 
GLSKALGADD SYYTARSAGK WPLKWYAPEC INFRKFSSRS DVWSYGVTMW EALSYGQKPY 

       550        560        570        580        590        600 
KKMKGPEVMA FIEQGKRMEC PPECPPELYA LMSDCWIYKW EDRPDFLTVE QRMRACYYSL 

       610 
ASKVEGPPGS TQKAEAACA 

« Hide

Isoform 2 (TZK).

Checksum: B1D7A63A61D63215
Show »

FASTA31235,647
Isoform 3.

Checksum: 14F1841C3F898EEF
Show »

FASTA49355,873

References

« Hide 'large scale' references
[1]"ZAP-70: a 70 kd protein-tyrosine kinase that associates with the TCR zeta chain."
Chan A.C., Iwashima M., Turck C.W., Weiss A.
Cell 71:649-662(1992) [PubMed: 1423621] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH CD3Z, TISSUE SPECIFICITY, PHOSPHORYLATION.
[2]"Identification of a novel isoform of ZAP-70, truncated ZAP kinase."
Kuroyama H., Ikeda T., Kasai M., Yamasaki S., Tatsumi M., Utsuyama M., Saito T., Hirokawa K.
Biochem. Biophys. Res. Commun. 315:935-941(2004) [PubMed: 14985102] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Tissue: Leukocyte.
[3]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed: 15815621] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
Tissue: Blood and Brain.
[5]"Defective T cell receptor signaling and CD8+ thymic selection in humans lacking zap-70 kinase."
Arpaia E., Shahar M., Dadi H., Cohen A., Roifman C.M.
Cell 76:947-958(1994) [PubMed: 8124727] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 521-547, VARIANT STD LEU-GLU-GLN-541 INS, FUNCTION.
Tissue: Lymphoid tissue.
[6]"ZAP-70 binding specificity to T cell receptor tyrosine-based activation motifs: the tandem SH2 domains of ZAP-70 bind distinct tyrosine-based activation motifs with varying affinity."
Isakov N., Wange R.L., Burgess W.H., Watts J.D., Aebersold R., Samelson L.E.
J. Exp. Med. 181:375-380(1995) [PubMed: 7528772] [Abstract]
Cited for: CHARACTERIZATION OF TAM-BINDING.
[7]"Tyrosine 319, a newly identified phosphorylation site of ZAP-70, plays a critical role in T cell antigen receptor signaling."
Di Bartolo V., Mege D., Germain V., Pelosi M., Dufour E., Michel F., Magistrelli G., Isacchi A., Acuto O.
J. Biol. Chem. 274:6285-6294(1999) [PubMed: 10037717] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-315 AND TYR-319, MUTAGENESIS OF TYR-315 AND TYR-319.
[8]"SLAP, a dimeric adapter protein, plays a functional role in T cell receptor signaling."
Tang J., Sawasdikosol S., Chang J.-H., Burakoff S.J.
Proc. Natl. Acad. Sci. U.S.A. 96:9775-9780(1999) [PubMed: 10449770] [Abstract]
Cited for: INTERACTION WITH CBL AND SLA.
[9]"Molecular cloning and characterization of SPAP1, an inhibitory receptor."
Xu M.-J., Zhao R., Zhao Z.J.
Biochem. Biophys. Res. Commun. 280:768-775(2001) [PubMed: 11162587] [Abstract]
Cited for: INTERACTION WITH FCRL3.
[10]"Shb links SLP-76 and Vav with the CD3 complex in Jurkat T cells."
Lindholm C.K., Henriksson M.L., Hallberg B., Welsh M.
Eur. J. Biochem. 269:3279-3288(2002) [PubMed: 12084069] [Abstract]
Cited for: INTERACTION WITH SHB.
[11]"Profiling of tyrosine phosphorylation pathways in human cells using mass spectrometry."
Salomon A.R., Ficarro S.B., Brill L.M., Brinker A., Phung Q.T., Ericson C., Sauer K., Brock A., Horn D.M., Schultz P.G., Peters E.C.
Proc. Natl. Acad. Sci. U.S.A. 100:443-448(2003) [PubMed: 12522270] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-292; TYR-315; TYR-319; TYR-492 AND TYR-493, MASS SPECTROMETRY.
[12]"Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry."
Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C.
Anal. Chem. 76:2763-2772(2004) [PubMed: 15144186] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-289, MASS SPECTROMETRY.
Tissue: T-cell.
[13]"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
Nat. Biotechnol. 23:94-101(2005) [PubMed: 15592455] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-248; TYR-292; TYR-315; TYR-319; TYR-492 AND TYR-493, MASS SPECTROMETRY.
[14]"Quantitative phosphoproteome analysis using a dendrimer conjugation chemistry and tandem mass spectrometry."
Tao W.A., Wollscheid B., O'Brien R., Eng J.K., Li X.-J., Bodenmiller B., Watts J.D., Hood L., Aebersold R.
Nat. Methods 2:591-598(2005) [PubMed: 16094384] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-292; TYR-315; TYR-319; TYR-492 AND TYR-493, MASS SPECTROMETRY.
Tissue: T-cell.
[15]"Proteomics analysis of protein kinases by target class-selective prefractionation and tandem mass spectrometry."
Wissing J., Jaensch L., Nimtz M., Dieterich G., Hornberger R., Keri G., Wehland J., Daub H.
Mol. Cell. Proteomics 6:537-547(2007) [PubMed: 17192257] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-248; TYR-292 AND TYR-492, MASS SPECTROMETRY.
[16]"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: 19690332] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-292 AND TYR-492, MASS SPECTROMETRY.
Tissue: T-cell.
[17]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed: 19608861] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-603, MASS SPECTROMETRY.
[18]"Crystal structure and NMR studies of the apo SH2 domains of ZAP-70: two bikes rather than a tandem."
Folmer R.H., Geschwindner S., Xue Y.
Biochemistry 41:14176-14184(2002) [PubMed: 12450381] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1-256.
[19]"ZAP-70 deficiency in an autosomal recessive form of severe combined immunodeficiency."
Chan A.C., Kadlecek T.A., Elder M.E., Filipovich A.H., Kuo W.-L., Iwashima M., Parslow T.G., Weiss A.
Science 264:1599-1601(1994) [PubMed: 8202713] [Abstract]
Cited for: VARIANT STD ARG-518.
[20]"Specific immunoglobulin E responses in ZAP-70-deficient patients are mediated by Syk-dependent T-cell receptor signalling."
Toyabe S., Watanabe A., Harada W., Karasawa T., Uchiyama M.
Immunology 103:164-171(2001) [PubMed: 11412303] [Abstract]
Cited for: VARIANT STD HIS-465.
[21]"Patterns of somatic mutation in human cancer genomes."
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. expand/collapse author list , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
Nature 446:153-158(2007) [PubMed: 17344846] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] LEU-175; LEU-191; GLU-448 AND LEU-523.
+Additional computationally mapped references.

Web resources

ZAP70base

ZAP70 mutation db

GeneReviews

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L05148 mRNA. No translation available.
AB083211 mRNA. Translation: BAC43747.1.
AC016699 Genomic DNA. Translation: AAX93187.1.
BC039039 mRNA. Translation: AAH39039.1.
BC053878 mRNA. Translation: AAH53878.1.
IPIIPI00329789.
IPI00410185.
IPI00885038.
PIRA44266.
A49955.
RefSeqNP_001070.2.
NP_997402.1.
UniGeneHs.234569

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1M61X-ray2.50A1-256[»]
1U59X-ray2.30A327-606[»]
2OQ1X-ray1.90A3-256[»]
2OZOX-ray2.60A1-606[»]
ModBaseSearch...

Protein-protein interaction databases

IntActP43403. 2 interactions.
STRINGP43403.

PTM databases

PhosphoSiteP43403.

Proteomic databases

PRIDEP43403.

Genome annotation databases

EnsemblENST00000264972; ENSP00000264972; ENSG00000115085; Homo sapiens. [Genome view]
GeneID7535.
KEGGhsa:7535.
UCSCuc002syd.1. human.
uc002sye.1. human.

Organism-specific databases

CTD7535.
GeneCardsGC02P097788.
H-InvDBHIX0002292.
HGNCHGNC:12858. ZAP70.
HPACAB002625.
HPA003134.
MIM176947. gene+phenotype.
Orphanet911. Severe combined immunodeficiency due to ZAP70 deficiency.
PharmGKBPA37447.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG17394.
HOGENOMHBG714705.
HOVERGENP43403.
InParanoidP43403.
OMAFIEQGKR.
OrthoDBEOG908QT6.

Enzyme and pathway databases

BRENDA2.7.10.2. 247.
Pathway_Interaction_DBpi3kcipathway. Class I PI3K signaling events.
tcrpathway. TCR signaling in naive CD4+ T cells.
cd8tcrpathway. TCR signaling in naive CD8+ T cells.
ReactomeREACT_6900. Signaling in Immune system.

Gene expression databases

ArrayExpressP43403.
BgeeP43403.
CleanExHS_ZAP70.
GenevestigatorP43403.
GermOnlineENSG00000115085. Homo sapiens.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR000980. SH2.
IPR012234. Tyr_kinase_non-rcpt_SYK/ZAP70.
IPR020686. Tyr_kinase_non-rcpt_ZAP-70.
IPR020635. Tyr_Pkinase_cat_dom.
IPR020685. Tyr_prot_kinase.
IPR008266. Tyr_prot_kinase_AS.
[Graphical view]
Gene3DG3DSA:3.30.505.10. SH2. 2 hits.
PANTHERPTHR23256:SF98. Tyr_kinase_non-rcpt_ZAP-70. 1 hit.
PTHR23256. Tyr_prot_kinase. 1 hit.
PfamPF00017. SH2. 2 hits.
[Graphical view]
PIRSFPIRSF000604. TyrPK_SYK. 1 hit.
PRINTSPR00401. SH2DOMAIN.
SMARTSM00252. SH2. 2 hits.
SM00219. TyrKc. 1 hit.
[Graphical view]
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
PS50001. SH2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio29481.
PMAP-CutDBP43403.
SOURCESearch...

Entry information

Entry nameZAP70_HUMAN
AccessionPrimary (citable) accession number: P43403
Secondary accession number(s): A6NFP4 expand/collapse secondary AC list , Q6PIA4, Q8IXD6, Q9UBS6
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: February 9, 2010
This is version 124 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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.

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Human chromosome 2: entries, gene names and cross-references to MIM

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List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents