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P06239 (LCK_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 199. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | 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 kinase Lck

EC=2.7.10.2
Alternative name(s):
Leukocyte C-terminal Src kinase
Short name=LSK
Lymphocyte cell-specific protein-tyrosine kinase
Protein YT16
Proto-oncogene Lck
T cell-specific protein-tyrosine kinase
p56-LCK
Gene names
Name:LCK
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length509 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Non-receptor tyrosine-protein kinase that plays an essential role in the selection and maturation of developing T-cells in the thymus and in the function of mature T-cells. Plays a key role in T-cell antigen receptor (TCR)-linked signal transduction pathways. Constitutively associated with the cytoplasmic portions of the CD4 and CD8 surface receptors. Association of the TCR with a peptide antigen-bound MHC complex facilitates the interaction of CD4 and CD8 with MHC class II and class I molecules, respectively, thereby recruiting the associated LCK protein to the vicinity of the TCR/CD3 complex. LCK then phosphorylates tyrosines residues within the immunoreceptor tyrosine-based activation motifs (ITAM) of the cytoplasmic tails of the TCR-gamma chains and CD3 subunits, initiating the TCR/CD3 signaling pathway. Once stimulated, the TCR recruits the tyrosine kinase ZAP70, that becomes phosphorylated and activated by LCK. Following this, a large number of signaling molecules are recruited, ultimately leading to lymphokine production. LCK also contributes to signaling by other receptor molecules. Associates directly with the cytoplasmic tail of CD2, which leads to hyperphosphorylation and activation of LCK. Also plays a role in the IL2 receptor-linked signaling pathway that controls the T-cell proliferative response. Binding of IL2 to its receptor results in increased activity of LCK. Is expressed at all stages of thymocyte development and is required for the regulation of maturation events that are governed by both pre-TCR and mature alpha beta TCR. Phosphorylates other substrates including RUNX3, PTK2B/PYK2, the microtubule-associated protein MAPT, RHOH or TYROBP. Ref.28 Ref.31 Ref.36 Ref.37 Ref.38 Ref.39 Ref.40

Catalytic activity

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

Enzyme regulation

The relative activities of the inhibitory tyrosine-protein kinase CSK and the activating tyrosine-protein phosphatase PTPRC/CD45 determine the level of LCK activity. These interactions allow rapid and efficient activation of LCK in response to TCR stimulation. Ref.41

Subunit structure

Binds to the cytoplasmic domain of cell surface receptors, such as AXL, CD2, CD4, CD5, CD8, CD44, CD45 and CD122. Also binds to effector molecules, such as PI4K, VAV1, RASA1, FYB and to other protein kinases including CDK1, RAF1, ZAP70 and SYK. Binds to phosphatidylinositol 3'-kinase (PI3K) from T-lymphocytes through its SH3 domain and to the tyrosine phosphorylated form of KHDRBS1/p70 through its SH2 domain. Binds to HIV-1 Nef through its SH3 domain. This interaction inhibits its tyrosine-kinase activity. Interacts with SQSTM1. Interacts with phosphorylated LIME1. Interacts with CBLB and PTPRH. Interacts with RUNX3. Forms a signaling complex with EPHA1, PTK2B AND PI3-KINASE; upon activation by EFNA1 which may regulate T-lymphocyte migration. Associates with ZAP70 and RHOH; these interactions allow LCK-mediated RHOH and CD3 subunit phosphorylation in the presence of functional ZAP70. Ref.16 Ref.17 Ref.18 Ref.20 Ref.21 Ref.25 Ref.26 Ref.27 Ref.32

Subcellular location

Cytoplasm. Cell membrane; Lipid-anchor; Cytoplasmic side. Note: Present in lipid rafts in an inactive form. Ref.23

Tissue specificity

Expressed specifically in lymphoid cells.

Domain

The SH2 domain mediates interaction with SQSTM1. Interaction is regulated by Ser-59 phosphorylation.

Post-translational modification

Autophosphorylated on Tyr-394, increasing enzymatic activity, this site is dephosphorylated by PTN22. Phosphorylated on Tyr-505 by CSK, decreasing activity. Dephosphorylated by PTPRC/CD45. Dephosphorylation at Tyr-394 by PTPN2 negatively regulates T-cell receptor signaling. Ref.4 Ref.15 Ref.19 Ref.30 Ref.39

Myristoylation is required prior to palmitoylation By similarity.

Palmitoylation regulates subcellular location By similarity.

Involvement in disease

A chromosomal aberration involving LCK is found in leukemias. Translocation t(1;7)(p34;q34) with TCRB.

Sequence similarities

Belongs to the protein kinase superfamily. Tyr protein kinase family. SRC subfamily.

Contains 1 protein kinase domain.

Contains 1 SH2 domain.

Contains 1 SH3 domain.

Mass spectrometry

Molecular mass is 57869.42 Da from positions 2 - 509. Determined by MALDI. Ref.24

Sequence caution

The sequence CAI22320.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence CAI22321.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
   Biological processHost-virus interaction
   Cellular componentCell membrane
Cytoplasm
Membrane
   Coding sequence diversityAlternative splicing
Chromosomal rearrangement
Polymorphism
   DiseaseDisease mutation
Proto-oncogene
   DomainSH2 domain
SH3 domain
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
Tyrosine-protein kinase
   PTMLipoprotein
Myristate
Palmitate
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processB cell receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

Fc-epsilon receptor signaling pathway

Traceable author statement. Source: Reactome

T cell costimulation

Traceable author statement. Source: Reactome

T cell differentiation

Inferred from mutant phenotype PubMed 1579166. Source: UniProtKB

T cell receptor signaling pathway

Traceable author statement. Source: Reactome

activation of cysteine-type endopeptidase activity involved in apoptotic process

Inferred from direct assay PubMed 16116473. Source: UniProtKB

aging

Inferred from electronic annotation. Source: Ensembl

blood coagulation

Traceable author statement. Source: Reactome

cellular zinc ion homeostasis

Inferred from expression pattern PubMed 11739864. Source: UniProtKB

dephosphorylation

Inferred from direct assay PubMed 8506364. Source: GOC

epidermal growth factor receptor signaling pathway

Traceable author statement. Source: Reactome

fibroblast growth factor receptor signaling pathway

Traceable author statement. Source: Reactome

hemopoiesis

Non-traceable author statement PubMed 12884910. Source: UniProtKB

innate immune response

Traceable author statement. Source: Reactome

leukocyte migration

Traceable author statement. Source: Reactome

neurotrophin TRK receptor signaling pathway

Traceable author statement. Source: Reactome

phosphatidylinositol-mediated signaling

Traceable author statement. Source: Reactome

platelet activation

Traceable author statement. Source: Reactome

positive regulation of T cell activation

Inferred from direct assay PubMed 8943371. Source: UniProtKB

positive regulation of T cell receptor signaling pathway

Non-traceable author statement PubMed 12614355. Source: UniProtKB

positive regulation of gamma-delta T cell differentiation

Inferred from electronic annotation. Source: Ensembl

positive regulation of gene expression

Inferred from electronic annotation. Source: Ensembl

positive regulation of intrinsic apoptotic signaling pathway

Inferred from mutant phenotype PubMed 16116473. Source: UniProtKB

positive regulation of tyrosine phosphorylation of Stat5 protein

Inferred from electronic annotation. Source: Ensembl

positive regulation of uterine smooth muscle contraction

Inferred from electronic annotation. Source: Ensembl

protein autophosphorylation

Inferred from electronic annotation. Source: Ensembl

protein phosphorylation

Inferred from direct assay PubMed 214242. Source: UniProtKB

regulation of defense response to virus by virus

Traceable author statement. Source: Reactome

regulation of lymphocyte activation

Non-traceable author statement Ref.17. Source: UniProtKB

release of sequestered calcium ion into cytosol

Inferred from sequence or structural similarity. Source: UniProtKB

response to drug

Inferred from direct assay PubMed 16116473. Source: UniProtKB

response to hydrogen peroxide

Inferred from electronic annotation. Source: Ensembl

response to mechanical stimulus

Inferred from electronic annotation. Source: Ensembl

response to zinc ion

Inferred from electronic annotation. Source: Ensembl

viral process

Traceable author statement. Source: Reactome

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

endocytic vesicle

Inferred from electronic annotation. Source: Ensembl

extracellular vesicular exosome

Inferred from direct assay PubMed 20458337PubMed 23376485. Source: UniProt

immunological synapse

Inferred from direct assay PubMed 20007709. Source: MGI

membrane raft

Inferred from direct assay PubMed 12732664. Source: UniProtKB

pericentriolar material

Inferred from direct assay PubMed 7513706. Source: UniProtKB

plasma membrane

Inferred from direct assay PubMed 12150984. Source: BHF-UCL

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ATPase binding

Inferred from physical interaction PubMed 15671290. Source: UniProtKB

CD4 receptor binding

Inferred from physical interaction PubMed 7486703. Source: UniProtKB

CD8 receptor binding

Inferred from physical interaction PubMed 2470098. Source: UniProtKB

SH2 domain binding

Inferred from physical interaction Ref.17Ref.20. Source: UniProtKB

antigen binding

Inferred from electronic annotation. Source: Ensembl

glycoprotein binding

Inferred from physical interaction PubMed 14625311PubMed 15554700PubMed 7513706PubMed 8650207. Source: UniProtKB

identical protein binding

Inferred from physical interaction PubMed 17118402. Source: IntAct

non-membrane spanning protein tyrosine kinase activity

Inferred from electronic annotation. Source: UniProtKB-EC

phosphatidylinositol 3-kinase binding

Inferred from physical interaction Ref.16. Source: UniProtKB

protein C-terminus binding

Inferred from physical interaction PubMed 16245368. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 10209036PubMed 14757743PubMed 16195219PubMed 16245368PubMed 19192391Ref.36Ref.17PubMed 9045636PubMed 9341123. Source: UniProtKB

protein kinase binding

Inferred from physical interaction Ref.18. Source: UniProtKB

protein phosphatase binding

Inferred from physical interaction Ref.39. Source: UniProtKB

protein serine/threonine phosphatase activity

Inferred from direct assay PubMed 8506364. Source: UniProtKB

protein tyrosine kinase activity

Inferred from direct assay PubMed 214242. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform Long (identifier: P06239-1)

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 Short (identifier: P06239-2)

The sequence of this isoform differs from the canonical sequence as follows:
     348-363: IAEGMAFIEERNYIHR → VRRLGRGAGQGNRPVT
     364-509: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: P06239-3)

The sequence of this isoform differs from the canonical sequence as follows:
     321-321: N → NDTLLDSQLEEKGLGASPWGNLGQQLLLLPT
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 509508Tyrosine-protein kinase Lck
PRO_0000088124

Regions

Domain61 – 12161SH3
Domain127 – 22498SH2
Domain245 – 498254Protein kinase
Nucleotide binding251 – 2599ATP By similarity
Region2 – 7271Interactions with CD4 and CD8 By similarity
Region154 – 24289Interaction with PTPRH

Sites

Active site3641Proton acceptor By similarity
Binding site2731ATP By similarity

Amino acid modifications

Modified residue1021Phosphoserine Ref.35
Modified residue1591Phosphothreonine Ref.35
Modified residue1621Phosphoserine Ref.35
Modified residue1941Phosphoserine Ref.35
Modified residue3941Phosphotyrosine; by autocatalysis Ref.4 Ref.39
Modified residue5051Phosphotyrosine; by CSK Ref.4 Ref.15 Ref.19 Ref.29 Ref.33 Ref.34 Ref.35 Ref.42
Lipidation21N-myristoyl glycine By similarity
Lipidation31S-palmitoyl cysteine By similarity
Lipidation51S-palmitoyl cysteine By similarity

Natural variations

Alternative sequence3211N → NDTLLDSQLEEKGLGASPWG NLGQQLLLLPT in isoform 3.
VSP_016049
Alternative sequence348 – 36316IAEGM…NYIHR → VRRLGRGAGQGNRPVT in isoform Short.
VSP_005000
Alternative sequence364 – 509146Missing in isoform Short.
VSP_005001
Natural variant281V → L in leukemia. Ref.4
VAR_013463
Natural variant2011G → S.
Corresponds to variant rs11567841 [ dbSNP | Ensembl ].
VAR_051697
Natural variant2321P → PQKP in leukemia.
VAR_013464
Natural variant3531A → V in leukemia. Ref.4
VAR_013465
Natural variant4471P → L in leukemia. Ref.4
VAR_013466

Experimental info

Mutagenesis591S → E: Allows interaction with SQSTM1. Ref.18
Mutagenesis1541R → K: No effect on interaction with SQSTM1. Ref.18
Sequence conflict291P → R in AAA59502. Ref.2
Sequence conflict351T → R in AAA59502. Ref.2
Sequence conflict871Q → P in CAA31884. Ref.2
Sequence conflict871Q → P in AAA59502. Ref.2
Sequence conflict206 – 2116VRHYTN → ASAITPI in CAA28691. Ref.1
Sequence conflict2541G → A in AAA59502. Ref.2
Sequence conflict258 – 26710EVWMGYYNGH → RCGWGTTTGT in CAA28691. Ref.1
Sequence conflict282 – 2865PDAFL → AGRLP in CAA28691. Ref.1
Sequence conflict3751T → A in CAA28165. Ref.14
Sequence conflict4721L → H in CAA29667. Ref.13
Sequence conflict504 – 5096QYQPQP → STA in CAA28691. Ref.1

Secondary structure

.............................................................................................. 509
Helix Strand Turn

Details...

Sequences

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

Last modified January 23, 2007. Version 6.
Checksum: 44BFF0D43FFB420D

FASTA50958,001
        10         20         30         40         50         60 
MGCGCSSHPE DDWMENIDVC ENCHYPIVPL DGKGTLLIRN GSEVRDPLVT YEGSNPPASP 

        70         80         90        100        110        120 
LQDNLVIALH SYEPSHDGDL GFEKGEQLRI LEQSGEWWKA QSLTTGQEGF IPFNFVAKAN 

       130        140        150        160        170        180 
SLEPEPWFFK NLSRKDAERQ LLAPGNTHGS FLIRESESTA GSFSLSVRDF DQNQGEVVKH 

       190        200        210        220        230        240 
YKIRNLDNGG FYISPRITFP GLHELVRHYT NASDGLCTRL SRPCQTQKPQ KPWWEDEWEV 

       250        260        270        280        290        300 
PRETLKLVER LGAGQFGEVW MGYYNGHTKV AVKSLKQGSM SPDAFLAEAN LMKQLQHQRL 

       310        320        330        340        350        360 
VRLYAVVTQE PIYIITEYME NGSLVDFLKT PSGIKLTINK LLDMAAQIAE GMAFIEERNY 

       370        380        390        400        410        420 
IHRDLRAANI LVSDTLSCKI ADFGLARLIE DNEYTAREGA KFPIKWTAPE AINYGTFTIK 

       430        440        450        460        470        480 
SDVWSFGILL TEIVTHGRIP YPGMTNPEVI QNLERGYRMV RPDNCPEELY QLMRLCWKER 

       490        500 
PEDRPTFDYL RSVLEDFFTA TEGQYQPQP 

« Hide

Isoform Short [UniParc].

Checksum: AC4AF1AB58D32577
Show »

FASTA36340,866
Isoform 3 [UniParc].

Checksum: D1024F47D18B289C
Show »

FASTA53961,190

References

« Hide 'large scale' references
[1]"A human T cell-specific cDNA clone (YT16) encodes a protein with extensive homology to a family of protein-tyrosine kinases."
Koga Y., Caccia N., Toyonaga B., Spolski R., Yanagi Y., Yoshikai Y., Mak T.W.
Eur. J. Immunol. 16:1643-1646(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Structure and expression of lck transcripts in human lymphoid cells."
Perlmutter R.M., Marth J.D., Lewis D.B., Peet R., Ziegler S.F., Wilson C.B.
J. Cell. Biochem. 38:117-126(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Structure of the human lck gene: differences in genomic organisation within src-related genes affect only N-terminal exons."
Rouer E., van Huynh T., de Souza S.L., Lang M.C., Fischer S., Benarous R.
Gene 84:105-113(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"Oncogenic activation of the Lck protein accompanies translocation of the LCK gene in the human HSB2 T-cell leukemia."
Wright D.D., Sefton B.M., Kamps M.P.
Mol. Cell. Biol. 14:2429-2437(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS LEU-28; GLN-LYS-PRO-232 INS; VAL-353 AND LEU-447, PHOSPHORYLATION AT TYR-394 AND TYR-505.
Tissue: Leukemia.
[5]"An aberrant lck mRNA in two human T-cell lines."
Vogel L.B., Arthur R., Fujita D.J.
Biochim. Biophys. Acta 1264:168-172(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT), ALTERNATIVE SPLICING.
Tissue: Leukemic T-cell.
[6]"No association between lck gene polymorphisms and protein level in type 1 diabetes."
Nervi S., Nicodeme S., Gartioux C., Atlan C., Lathrop M., Reviron D., Naquet P., Matsuda F., Imbert J., Vialettes B.
Diabetes 51:3326-3330(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[7]"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].
[8]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]"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 3).
Tissue: Lymph.
[10]"Structure of the murine lck gene and its rearrangement in a murine lymphoma cell line."
Garvin A.M., Pawar S., Marth J.D., Perlmutter R.M.
Mol. Cell. Biol. 8:3058-3064(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-35.
[11]"Structure of the two promoters of the human lck gene: differential accumulation of two classes of lck transcripts in T cells."
Takadera T., Leung S., Gernone A., Koga Y., Takihara Y., Miyamoto N.G., Mak T.W.
Mol. Cell. Biol. 9:2173-2180(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-35.
[12]"Defective recruitment and activation of ZAP-70 in common variable immunodeficiency patients with T cell defects."
Boncristiano M., Majolini M.B., D'Elios M.M., Pacini S., Valensin S., Ulivieri C., Amedei A., Falini B., Del Prete G., Telford J.L., Baldari C.T.
Eur. J. Immunol. 30:2632-2638(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 14-509.
Tissue: Peripheral blood lymphocyte.
[13]"Expression of the lck tyrosine kinase gene in human colon carcinoma and other non-lymphoid human tumor cell lines."
Veillette A., Foss F.M., Sausville E.A., Bolen J.B., Rosen N.
Oncogene Res. 1:357-374(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 368-509.
[14]"Human T lymphocytes express a protein-tyrosine kinase homologous to p56LSTRA."
Trevillyan J.M., Lin Y., Chen S.J., Phillips C.A., Canna C., Linna T.J.
Biochim. Biophys. Acta 888:286-295(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 375-509.
[15]"The human p50csk tyrosine kinase phosphorylates p56lck at Tyr-505 and down regulates its catalytic activity."
Bergman M., Mustelin T., Oetken C., Partanen J., Flint N.A., Amrein K.E., Autero M., Burn P., Alitalo K.
EMBO J. 11:2919-2924(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-505.
[16]"The SH3 domain of p56lck is involved in binding to phosphatidylinositol 3'-kinase from T lymphocytes."
Vogel L.B., Fujita D.J.
Mol. Cell. Biol. 13:7408-7417(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PI3K.
[17]"p70 phosphorylation and binding to p56lck is an early event in interleukin-2-induced onset of cell cycle progression in T-lymphocytes."
Vogel L.B., Fujita D.J.
J. Biol. Chem. 270:2506-2511(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH KHDRBS1.
[18]"Phosphotyrosine-independent binding of a 62-kDa protein to the src homology 2 (SH2) domain of p56lck and its regulation by phosphorylation of Ser-59 in the lck unique N-terminal region."
Park I., Chung J., Walsh C.T., Yun Y., Strominger J.L., Shin J.
Proc. Natl. Acad. Sci. U.S.A. 92:12338-12342(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SQSTM1, MUTAGENESIS OF SER-59 AND ARG-154.
[19]"Detection of a physical and functional interaction between Csk and Lck which involves the SH2 domain of Csk and is mediated by autophosphorylation of Lck on tyrosine 394."
Bougeret C., Delaunay T., Romero F., Jullien P., Sabe H., Hanafusa H., Benarous R., Fischer S.
J. Biol. Chem. 271:7465-7472(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-505 BY CSK, AUTOPHOSPHORYLATION.
[20]"Human immunodeficiency virus type 1 Nef binds directly to LCK and mitogen-activated protein kinase, inhibiting kinase activity."
Greenway A.L., Azad A., Mills J., McPhee D.A.
J. Virol. 70:6701-6708(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HIV-1 NEF.
[21]"Intracellular signaling of the Ufo/Axl receptor tyrosine kinase is mediated mainly by a multi-substrate docking-site."
Braunger J., Schleithoff L., Schulz A.S., Kessler H., Lammers R., Ullrich A., Bartram C.R., Janssen J.W.
Oncogene 14:2619-2631(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH AXL.
[22]"Lck protein tyrosine kinase is a key regulator of T-cell activation and a target for signal intervention by Herpesvirus saimiri and other viral gene products."
Isakov N., Biesinger B.
Eur. J. Biochem. 267:3413-3421(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[23]"Fyn is essential for tyrosine phosphorylation of Csk-binding protein/phosphoprotein associated with glycolipid-enriched microdomains in lipid rafts in resting T cells."
Yasuda K., Nagafuku M., Shima T., Okada M., Yagi T., Yamada T., Minaki Y., Kato A., Tani-Ichi S., Hamaoka T., Kosugi A.
J. Immunol. 169:2813-2817(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[24]"Cluster analysis of an extensive human breast cancer cell line protein expression map database."
Harris R.A., Yang A., Stein R.C., Lucy K., Brusten L., Herath A., Parekh R., Waterfield M.D., O'Hare M.J., Neville M.A., Page M.J., Zvelebil M.J.
Proteomics 2:212-223(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: MASS SPECTROMETRY.
Tissue: Mammary cancer.
[25]"LIME: a new membrane raft-associated adaptor protein involved in CD4 and CD8 coreceptor signaling."
Brdickova N., Brdicka T., Angelisova P., Horvath O., Spicka J., Hilgert I., Paces J., Simeoni L., Kliche S., Merten C., Schraven B., Horejsi V.
J. Exp. Med. 198:1453-1462(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH LIME1.
[26]"LIME, a novel transmembrane adaptor protein, associates with p56lck and mediates T cell activation."
Hur E.M., Son M., Lee O.-H., Choi Y.B., Park C., Lee H., Yun Y.
J. Exp. Med. 198:1463-1473(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH LIME1.
[27]"Interaction of SAP-1, a transmembrane-type protein-tyrosine phosphatase, with the tyrosine kinase Lck. Roles in regulation of T cell function."
Ito T., Okazawa H., Maruyama K., Tomizawa K., Motegi S., Ohnishi H., Kuwano H., Kosugi A., Matozaki T.
J. Biol. Chem. 278:34854-34863(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PTPRH.
[28]"T cell activation-induced CrkII binding to the Zap70 protein tyrosine kinase is mediated by Lck-dependent phosphorylation of Zap70 tyrosine 315."
Gelkop S., Gish G.D., Babichev Y., Pawson T., Isakov N.
J. Immunol. 175:8123-8132(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF ZAP70.
[29]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-505, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[30]"Identification of substrates of human protein-tyrosine phosphatase PTPN22."
Wu J., Katrekar A., Honigberg L.A., Smith A.M., Conn M.T., Tang J., Jeffery D., Mortara K., Sampang J., Williams S.R., Buggy J., Clark J.M.
J. Biol. Chem. 281:11002-11010(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: DEPHOSPHORYLATION BY PTN22.
[31]"Regulation of Ly49D/DAP12 signal transduction by Src-family kinases and CD45."
Mason L.H., Willette-Brown J., Taylor L.S., McVicar D.W.
J. Immunol. 176:6615-6623(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF TYROBP.
[32]"Ephrin-A1 stimulates migration of CD8+CCR7+ T lymphocytes."
Hjorthaug H.S., Aasheim H.C.
Eur. J. Immunol. 37:2326-2336(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH EPHA1; PTK2B AND PI3-KINASE.
[33]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-505, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[34]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-505, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[35]"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-102; THR-159; SER-162; SER-194 AND TYR-505, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[36]"Src kinase phosphorylates RUNX3 at tyrosine residues and localizes the protein in the cytoplasm."
Goh Y.M., Cinghu S., Hong E.T., Lee Y.S., Kim J.H., Jang J.W., Li Y.H., Chi X.Z., Lee K.S., Wee H., Ito Y., Oh B.C., Bae S.C.
J. Biol. Chem. 285:10122-10129(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF RUNX3.
[37]"The T cell receptor-mediated phosphorylation of Pyk2 tyrosines 402 and 580 occurs via a distinct mechanism than other receptor systems."
Collins M., Tremblay M., Chapman N., Curtiss M., Rothman P.B., Houtman J.C.
J. Leukoc. Biol. 87:691-701(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PTK2B/PYK2 PHOSPHORYLATION.
[38]"RhoH modulates pre-TCR and TCR signalling by regulating LCK."
Wang H., Zeng X., Fan Z., Lim B.
Cell. Signal. 23:249-258(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF RHOH.
[39]"T cell protein tyrosine phosphatase attenuates T cell signaling to maintain tolerance in mice."
Wiede F., Shields B.J., Chew S.H., Kyparissoudis K., van Vliet C., Galic S., Tremblay M.L., Russell S.M., Godfrey D.I., Tiganis T.
J. Clin. Invest. 121:4758-4774(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN TCR SIGNALING, PHOSPHORYLATION, DEPHOSPHORYLATION AT TYR-394 BY PTPN2.
[40]"Tyrosine phosphorylation of tau by the SRC family kinases lck and fyn."
Scales T.M., Derkinderen P., Leung K.Y., Byers H.L., Ward M.A., Price C., Bird I.N., Perera T., Kellie S., Williamson R., Anderton B.H., Reynolds C.H.
Mol. Neurodegener. 6:12-12(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF MAPT.
[41]"Feedback circuits monitor and adjust Basal lck-dependent events in T cell receptor signaling."
Schoenborn J.R., Tan Y.X., Zhang C., Shokat K.M., Weiss A.
Sci. Signal. 4:RA59-RA59(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYME REGULATION.
[42]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-505, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[43]"Structure of the regulatory domains of the Src-family tyrosine kinase Lck."
Eck M.J., Atweell S.K., Shoelson S.E., Harrison S.C.
Nature 368:764-769(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 53-226.
[44]"The crystal structures of the SH2 domain of p56lck complexed with two phosphonopeptides suggest a gated peptide binding site."
Mikol V., Baumann G., Keller T.H., Manning U.M., Zurini M.G.M.
J. Mol. Biol. 246:344-355(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 127-221.
[45]"Crystal structures of the human p56lck SH2 domain in complex with two short phosphotyrosyl peptides at 1.0-A and 1.8-A resolution."
Tong L., Warren T.C., King J., Betageri R., Rose J., Jakes S.
J. Mol. Biol. 256:601-610(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.0 ANGSTROMS) OF 122-226.
[46]"Structural basis for activation of human lymphocyte kinase Lck upon tyrosine phosphorylation."
Yamaguchi H., Hendrickson W.A.
Nature 384:484-489(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 231-501.
[47]"Carboxymethyl-phenylalanine as a replacement for phosphotyrosine in SH2 domain binding."
Tong L., Warren T.C., Lukas S., Schembri-King J., Betageri R., Proudfoot J.R., Jakes S.
J. Biol. Chem. 273:20238-20242(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 119-226.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X05027 mRNA. Translation: CAA28691.1.
X13529 mRNA. Translation: CAA31884.1.
M36881 mRNA. Translation: AAA59502.1.
X14055, X14053, X14054 Genomic DNA. Translation: CAA32211.1.
U07236 mRNA. Translation: AAA18225.1.
U23852 mRNA. Translation: AAC50287.1.
BN000073 Genomic DNA. Translation: CAD55807.1.
AL121991 Genomic DNA. Translation: CAI22320.1. Different initiation.
AL121991 Genomic DNA. Translation: CAI22321.1. Different initiation.
CH471059 Genomic DNA. Translation: EAX07543.1.
CH471059 Genomic DNA. Translation: EAX07546.1.
BC013200 mRNA. Translation: AAH13200.1.
M21510 Genomic DNA. Translation: AAA59501.1. Different termination.
M26692 Genomic DNA. Translation: AAA59503.1.
AF228313 mRNA. Translation: AAF34794.1.
X06369 mRNA. Translation: CAA29667.1.
X04476 mRNA. Translation: CAA28165.1.
CCDSCCDS359.1. [P06239-1]
PIROKHULK. JQ0152.
RefSeqNP_001036236.1. NM_001042771.2. [P06239-1]
NP_005347.3. NM_005356.4. [P06239-1]
UniGeneHs.470627.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BHFX-ray1.80A119-226[»]
1BHHX-ray1.90A119-226[»]
B124-226[»]
1CWDX-ray2.25L127-222[»]
1CWEX-ray2.30A/C127-222[»]
1FBZX-ray2.40A/B123-226[»]
1H92NMR-A59-120[»]
1IJRX-ray2.20A124-226[»]
1KIKNMR-A64-120[»]
1LCJX-ray1.80A119-226[»]
1LCKX-ray2.50A53-226[»]
B502-509[»]
1LKKX-ray1.00A122-226[»]
1LKLX-ray1.80A123-226[»]
1Q68NMR-B7-35[»]
1Q69NMR-B7-35[»]
1QPCX-ray1.60A231-509[»]
1QPDX-ray2.00A231-509[»]
1QPEX-ray2.00A231-509[»]
1QPJX-ray2.20A231-509[»]
1X27X-ray2.70A/B/C/D/E/F64-226[»]
2IIMX-ray1.00A59-119[»]
2OF2X-ray2.00A231-501[»]
2OF4X-ray2.70A231-501[»]
2OFUX-ray2.00A229-501[»]
2OFVX-ray2.00A/B232-498[»]
2OG8X-ray2.30A/B237-499[»]
2PL0X-ray2.80A225-509[»]
2ZM1X-ray2.10A225-509[»]
2ZM4X-ray2.70A225-509[»]
2ZYBX-ray2.55A225-509[»]
3AC1X-ray1.99A225-509[»]
3AC2X-ray2.10A225-509[»]
3AC3X-ray2.55A225-509[»]
3AC4X-ray2.70A225-509[»]
3AC5X-ray2.50A225-509[»]
3AC8X-ray2.30A225-509[»]
3ACJX-ray2.20A225-509[»]
3ACKX-ray2.60A225-509[»]
3AD4X-ray2.20A225-509[»]
3AD5X-ray2.00A225-509[»]
3AD6X-ray2.15A225-509[»]
3B2WX-ray2.30A226-502[»]
3BRHX-ray2.20C/D391-397[»]
3BYMX-ray2.00A230-501[»]
3BYOX-ray2.00A231-501[»]
3BYSX-ray2.20A225-501[»]
3BYUX-ray2.30A225-501[»]
3KMMX-ray2.80A229-509[»]
3KXZX-ray2.37A225-509[»]
3LCKX-ray1.70A231-501[»]
3MPMX-ray1.95A237-501[»]
4C3FX-ray1.72A237-501[»]
4D8KX-ray2.36A53-226[»]
ProteinModelPortalP06239.
SMRP06239. Positions 7-35, 64-509.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110124. 81 interactions.
DIPDIP-553N.
IntActP06239. 62 interactions.
MINTMINT-110378.

Chemistry

BindingDBP06239.
ChEMBLCHEMBL2363074.
DrugBankDB01254. Dasatinib.
GuidetoPHARMACOLOGY2053.

PTM databases

PhosphoSiteP06239.

Polymorphism databases

DMDM125474.

Proteomic databases

MaxQBP06239.
PaxDbP06239.
PRIDEP06239.

Protocols and materials databases

DNASU3932.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000333070; ENSP00000328213; ENSG00000182866. [P06239-3]
ENST00000336890; ENSP00000337825; ENSG00000182866. [P06239-1]
GeneID3932.
KEGGhsa:3932.
UCSCuc001bux.3. human. [P06239-1]
uc001buz.3. human. [P06239-3]

Organism-specific databases

CTD3932.
GeneCardsGC01P032716.
H-InvDBHIX0019954.
HGNCHGNC:6524. LCK.
HPACAB003816.
HPA003494.
MIM153390. gene.
neXtProtNX_P06239.
Orphanet280142. Severe combined immunodeficiency due to LCK deficiency.
PharmGKBPA30307.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOVERGENHBG008761.
KOK05856.
OMAEYMENDT.
OrthoDBEOG7GTT2V.
PhylomeDBP06239.
TreeFamTF351634.

Enzyme and pathway databases

BRENDA2.7.10.2. 2681.
ReactomeREACT_111102. Signal Transduction.
REACT_116125. Disease.
REACT_604. Hemostasis.
REACT_6900. Immune System.
SignaLinkP06239.

Gene expression databases

ArrayExpressP06239.
BgeeP06239.
CleanExHS_LCK.
GenevestigatorP06239.

Family and domain databases

Gene3D3.30.505.10. 1 hit.
InterProIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR000980. SH2.
IPR001452. SH3_domain.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
[Graphical view]
PfamPF07714. Pkinase_Tyr. 1 hit.
PF00017. SH2. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
PRINTSPR00401. SH2DOMAIN.
PR00452. SH3DOMAIN.
PR00109. TYRKINASE.
SMARTSM00252. SH2. 1 hit.
SM00326. SH3. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMSSF50044. SSF50044. 1 hit.
SSF55550. SSF55550. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
PS50001. SH2. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSLCK. human.
EvolutionaryTraceP06239.
GeneWikiLck.
GenomeRNAi3932.
NextBio15441.
PROP06239.
SOURCESearch...

Entry information

Entry nameLCK_HUMAN
AccessionPrimary (citable) accession number: P06239
Secondary accession number(s): D3DPP8 expand/collapse secondary AC list , P07100, Q12850, Q13152, Q5TDH8, Q5TDH9, Q7RTZ3, Q96DW4, Q9NYT8
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 199 of the entry and version 6 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

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

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 polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

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