[1]	NUCLEOTIDE SEQUENCE [MRNA]. DOI=10.1016/0092-8674(85)90169-2; PubMed=2416464 [NCBI, ExPASy, EBI, Israel, Japan] Marth J.D., Peet R., Krebs E.G., Perlmutter R.M.; "A lymphocyte-specific protein-tyrosine kinase gene is rearranged and overexpressed in the murine T cell lymphoma LSTRA."; Cell 43:393-404(1985).
[2]	NUCLEOTIDE SEQUENCE [MRNA]. DOI=10.1038/319682a0; PubMed=3081813 [NCBI, ExPASy, EBI, Israel, Japan] Voronova A.F., Sefton B.M.; "Expression of a new tyrosine protein kinase is stimulated by retrovirus promoter insertion."; Nature 319:682-685(1986).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. STRAIN=NOD; TISSUE=Thymus; DOI=10.1126/science.1112014; PubMed=16141072 [NCBI, ExPASy, EBI, Israel, Japan] Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.; "The transcriptional landscape of the mammalian genome."; Science 309:1559-1563(2005).
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. STRAIN=FVB/N; TISSUE=Salivary gland; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[5]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-35. PubMed=2850479 [NCBI, ExPASy, EBI, Israel, Japan] Garvin A.M., Pawar S., Marth J.D., Perlmutter R.M.; "Structure of the murine lck gene and its rearrangement in a murine lymphoma cell line."; Mol. Cell. Biol. 8:3058-3064(1988).
[6]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-11. PubMed=3501824 [NCBI, ExPASy, EBI, Israel, Japan] Voronova A.F., Adler H.T., Sefton B.M.; "Two lck transcripts containing different 5' untranslated regions are present in T cells."; Mol. Cell. Biol. 7:4407-4413(1987).
[7]	MUTAGENESIS OF TYR-505. PubMed=3380790 [NCBI, ExPASy, EBI, Israel, Japan] Amrein K.E., Sefton B.M.; "Avian reovirus mRNAs are nonfunctional in infected mouse cells: translational basis for virus host-range restriction."; Proc. Natl. Acad. Sci. U.S.A. 85:4257-4261(1988).
[8]	INTERACTION WITH CD4 AND CD8, AND MUTAGENESIS OF 3-CYS--CYS-5; CYS-20 AND CYS-23. DOI=10.1016/0092-8674(90)90090-2; PubMed=2107025 [NCBI, ExPASy, EBI, Israel, Japan] Turner J.M., Brodsky M.H., Irving B.A., Levin S.D., Perlmutter R.M., Littman D.R.; "Interaction of the unique N-terminal region of tyrosine kinase p56lck with cytoplasmic domains of CD4 and CD8 is mediated by cysteine motifs."; Cell 60:755-765(1990).
[9]	MUTAGENESIS. PubMed=1279202 [NCBI, ExPASy, EBI, Israel, Japan] Hurley T.R., Amrein K.E., Sefton B.M.; "Creation and characterization of temperature-sensitive mutants of the lck tyrosine protein kinase."; J. Virol. 66:7406-7413(1992).
[10]	MUTAGENESIS OF LYS-273. DOI=10.1038/350062a0; PubMed=1706070 [NCBI, ExPASy, EBI, Israel, Japan] Abraham N., Miceli M.C., Parnes J.C., Veillette A.; "Enhancement of T-cell responsiveness by the lymphocyte-specific tyrosine protein kinase p56lck."; Nature 350:62-66(1991).
[11]	PHOSPHORYLATION AT TYR-505, AND MUTAGENESIS OF TYR-505. PubMed=1708890 [NCBI, ExPASy, EBI, Israel, Japan] Abraham K.M., Levin S.D., Marth J.D., Forbush K.A., Perlmutter R.M.; "Thymic tumorigenesis induced by overexpression of p56lck."; Proc. Natl. Acad. Sci. U.S.A. 88:3977-3981(1991).
[12]	PHOSPHORYLATION BY CSK. DOI=10.1038/365156a0; PubMed=8371758 [NCBI, ExPASy, EBI, Israel, Japan] Chow L.M., Fournel M., Davidson D., Veillette A.; "Negative regulation of T-cell receptor signalling by tyrosine protein kinase p50csk."; Nature 365:156-160(1993).
[13]	MUTAGENESIS. PubMed=8421674 [NCBI, ExPASy, EBI, Israel, Japan] Carrera A.C., Alexandrov K., Roberts T.M.; "The conserved lysine of the catalytic domain of protein kinases is actively involved in the phosphotransfer reaction and not required for anchoring ATP."; Proc. Natl. Acad. Sci. U.S.A. 90:442-446(1993).
[14]	PALMITOYLATION AT CYS-3 AND CYS-5, AND MUTAGENESIS OF CYS-3 AND CYS-5. PubMed=8413237 [NCBI, ExPASy, EBI, Israel, Japan] Shenoy-Scaria A.M., Timson L.K., Kwong J., Shaw A.S., Lublin D.M.; "Palmitylation of an amino-terminal cysteine motif of protein tyrosine kinases p56lck and p59fyn mediates interaction with glycosyl-phosphatidylinositol-anchored proteins."; Mol. Cell. Biol. 13:6385-6392(1993).
[15]	PALMITOYLATION AT CYS-3 AND CYS-5, MYRISTOYLATION AT GLY-2, AND MUTAGENESIS OF GLY-2; CYS-3 AND CYS-5. PubMed=7980442 [NCBI, ExPASy, EBI, Israel, Japan] Koegl M., Zlatkine P., Ley S.C., Courtneidge S.A., Magee A.I.; "Palmitoylation of multiple Src-family kinases at a homologous N-terminal motif."; Biochem. J. 303:749-753(1994).
[16]	INTERACTION WITH CBLB. DOI=10.1038/35003228; PubMed=10646608 [NCBI, ExPASy, EBI, Israel, Japan] Bachmaier K., Krawczyk C., Kozieradzki I., Kong Y.-Y., Sasaki T., Oliveira-dos-Santos A., Mariathasan S., Bouchard D., Wakeham A., Itie A., Le J., Ohashi P.S., Sarosi I., Nishina H., Lipkowitz S., Penninger J.M.; "Negative regulation of lymphocyte activation and autoimmunity by the molecular adaptor Cbl-b."; Nature 403:211-216(2000).
[17]	SUBCELLULAR LOCATION. PubMed=12218089 [NCBI, ExPASy, EBI, Israel, Japan] Yasuda K., Nagafuku M., Shima T., Okada M., Yagi T., Yamada T., Minaki Y., Kato A., Tani-Ichi S., Hamaoka T., Kosugi A.; "Fyn is essential for tyrosine phosphorylation of Csk-binding protein/phosphoprotein associated with glycolipid-enriched microdomains in lipid rafts in resting T cells."; J. Immunol. 169:2813-2817(2002).
[18]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-394, AND MASS SPECTROMETRY. DOI=10.1038/nbt1046; PubMed=15592455 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."; Nat. Biotechnol. 23:94-101(2005).

Comments

FUNCTION: Tyrosine kinase that plays an essential role for the selection and maturation of developing T-cell in the thymus and in mature T-cell function. Is constitutively associated with the cytoplasmic portions of the CD4 and CD8 surface receptors and plays a key role in T-cell antigen receptor(TCR)-linked signal transduction pathways. 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, and thereby recruits the associated LCK to the vicinity of the TCR/CD3 complex. LCK then phosphorylates tyrosines residues within the immunoreceptor tyrosines-based activation motifs (ITAMs) in the cytoplasmic tails of the TCRgamma chains and CD3 subunits, initiating the TCR/CD3 signaling pathway. In addition, contributes to signaling by other receptor molecules. Associates directly with the cytoplasmic tail of CD2, and upon engagement of the CD2 molecule, LCK undergoes hyperphosphorylation and activation. Also plays a role in the IL2 receptor-linked signaling pathway that controls 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 (By similarity).
CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.
ENZYME REGULATION: Inhibited by tyrosine phosphorylation (By similarity).
SUBUNIT: Binds to the cytoplasmic domain of cell surface receptors, such as 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 CDC2, 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. Interacts with SQSTM1. Interacts with phosphorylated LIME1. Interacts with CBLB and PTPRH (By similarity).
INTERACTION:
O92969:- (xeno); NbExp=2; IntAct=EBI-1401, EBI-710506;
P26660:- (xeno); NbExp=1; IntAct=EBI-1401, EBI-706322;
P27958:- (xeno); NbExp=3; IntAct=EBI-1401, EBI-706378;
P06332:Cd4; NbExp=2; IntAct=EBI-1401, EBI-1404;
P49710:Hcls1; NbExp=1; IntAct=EBI-1401, EBI-924601;
Q07666:KHDRBS1 (xeno); NbExp=1; IntAct=EBI-1401, EBI-1364;
Q9NP31:SH2D2A (xeno); NbExp=1; IntAct=EBI-1401, EBI-490630;
Q9QXK9:Sh2d2a; NbExp=1; IntAct=EBI-1401, EBI-1644;
SUBCELLULAR LOCATION: Cytoplasm. Cell membrane; Lipid-anchor; Cytoplasmic side. Note=Present in lipid rafts in an unactive form.
TISSUE SPECIFICITY: Present at a low level in most T-cells, and at an elevated level in LSTRA and THY 19 (T-cell lymphoma) cells.
DEVELOPMENTAL STAGE: Levels remain relatively constant throughout T-cell ontogeny.
DOMAIN: The SH2 domain mediates interaction with SQSTM1. Interaction is regulated by Ser-59 phosphorylation (By similarity).
PTM: Phosphorylated on Tyr-394, which increases enzymatic activity. Phosphorylated on Tyr-505, presumably by CSK, which decreases activity.
PTM: Myristoylation is required prior to palmitoylation.
SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein kinase family. SRC subfamily.
SIMILARITY: Contains 1 protein kinase domain.
SIMILARITY: Contains 1 SH2 domain.
SIMILARITY: Contains 1 SH3 domain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M12056; AAB59674.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X03533; CAA27234.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X03533; CAA27235.1; ALT_SEQ; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X03533; CAA27236.1; ALT_SEQ; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AK088001; BAC40086.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC011474; AAH11474.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M21511; AAA39422.1; ALT_SEQ; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M18098; AAA39421.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

I48845; I48845.

NP_034823.1; -.

3D structure databases

HSSP

P06239; 1H92. [HSSP ENTRY / SWISS-3DIMAGE / PDB]

SMR

P06240; 65-509.

ModBase

P06240.

Protein-protein interaction databases

IntAct

P06240; -.

PTM databases

PhosphoSite

P06240; -.

Organism-specific databases

MGI

MGI:96756; Lck.

Gene expression databases

ArrayExpress

P06240; -.

CleanEx

MM_LCK; -.

GermOnline

ENSMUSG00000000409; Mus musculus.

Ontologies

GO:0045121;	Cellular component: membrane raft (inferred from sequence or structural similarity from UniProtKB).
GO:0000242;	Cellular component: pericentriolar material (inferred from sequence or structural similarity from UniProtKB).
GO:0004722;	Molecular function: protein serine/threonine phosphatase activity (inferred from sequence or structural similarity from UniProtKB).
GO:0004713;	Molecular function: protein tyrosine kinase activity (inferred from sequence or structural similarity from UniProtKB).
GO:0042169;	Molecular function: SH2 domain binding (inferred from sequence or structural similarity from UniProtKB).
GO:0050853;	Biological process: B cell receptor signaling pathway (inferred from direct assay from MGI).
GO:0006919;	Biological process: caspase activation (inferred from sequence or structural similarity from UniProtKB).
GO:0006882;	Biological process: cellular zinc ion homeostasis (inferred from sequence or structural similarity from UniProtKB).
GO:0006917;	Biological process: induction of apoptosis (inferred from sequence or structural similarity from UniProtKB).
GO:0018108;	Biological process: peptidyl-tyrosine phosphorylation (inferred from direct assay from MGI).
GO:0045588;	Biological process: positive regulation of gamma-delta T cell differentiation (inferred from mutant phenotype from MGI).
GO:0046777;	Biological process: protein amino acid autophosphorylation (inferred from direct assay from MGI).
GO:0050856;	Biological process: regulation of T cell receptor signaling pathway (inferred from direct assay from MGI).
GO:0051209;	Biological process: release of sequestered calcium ion into cytosol (inferred from direct assay from UniProtKB).
GO:0042493;	Biological process: response to drug (inferred from sequence or structural similarity from UniProtKB).
QuickGo view.

Family and domain databases

InterPro

IPR000719; Prot_kinase_core.
IPR017441; Protein_kinase_ATP_bd_CS.
IPR000980; SH2.
IPR001452; SH3.
IPR001245; Tyr_pkinase.
IPR008266; Tyr_pkinase_AS.
Graphical view of domain structure.

Gene3D

G3DSA:3.30.505.10; SH2; 1.

Pfam

PF07714; Pkinase_Tyr; 1.
PF00017; SH2; 1.
PF00018; SH3_1; 1.
Pfam graphical view of domain structure.

ProDom

PD000001; Prot_kinase; 1.
PD000093; SH2; 1.
PD000066; SH3; 1.
[Domain structure / List of seq. sharing at least 1 domain]

SMART

SM00252; SH2; 1.
SM00326; SH3; 1.
SM00219; TyrKc; 1.
SMART graphical view of domain structure.

PROSITE

PS00107; PROTEIN_KINASE_ATP; 1.
PS50011; PROTEIN_KINASE_DOM; 1.
PS00109; PROTEIN_KINASE_TYR; 1.
PS50001; SH2; 1.
PS50002; SH3; 1.
PROSITE graphical view of domain structure (profiles).

Genome annotation databases

Ensembl

ENSMUSG00000000409; Mus musculus. [Contig view]

GeneID

16818; -.

KEGG

mmu:16818; -.

Phylogenomic databases

HOGENOM

P06240; -.

HOVERGEN

P06240; -.

Other

P06240; -.

290704; -.

Lck; Mus musculus.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

ATP-binding; Cell membrane; Cytoplasm; Kinase; Lipoprotein; Membrane; Myristate; Nucleotide-binding; Palmitate; Phosphoprotein; Proto-oncogene; SH2 domain; SH3 domain; Transferase; Tyrosine-protein kinase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed (Probable).`
`CHAIN`	`2 509`	`508`	`Proto-oncogene tyrosine-protein kinase LCK.`	`PRO_0000088125`
`DOMAIN`	`61 121`	`61`	`SH3.`
`DOMAIN`	`127 224`	`98`	`SH2.`
`DOMAIN`	`245 498`	`254`	`Protein kinase.`
`NP_BIND`	`251 259`	`9`	`ATP (By similarity).`
`REGION`	`2 72`	`71`	`Interactions with CD4 and CD8.`
`REGION`	`154 242`	`89`	`Interaction with PTPRH (By similarity).`
`ACT_SITE`	`364 364`		`Proton acceptor (By similarity).`
`BINDING`	`273 273`		`ATP (By similarity).`
`MOD_RES`	`162 162`		`Phosphoserine (By similarity).`
`MOD_RES`	`192 192`		`Phosphotyrosine (By similarity).`
`MOD_RES`	`213 213`		`Phosphoserine (By similarity).`
`MOD_RES`	`394 394`		`Phosphotyrosine; by autocatalysis.`
`MOD_RES`	`501 501`		`Phosphothreonine (By similarity).`
`MOD_RES`	`505 505`		`Phosphotyrosine (Probable).`
`LIPID`	`2 2`		`N-myristoyl glycine (Probable).`
`LIPID`	`3 3`		`S-palmitoyl cysteine.`
`LIPID`	`5 5`		`S-palmitoyl cysteine.`
`MUTAGEN`	`2 2`		`G->A: Abolishes myristoylation and palmitoylation.`
`MUTAGEN`	`3 5`		`CVC->SVK: Complete loss of interaction with CD4 or CD8.`
`MUTAGEN`	`3 3`		`C->S: Abolishes plasma membrane association; when associated with S-41. Reduced palmitoylation level.`
`MUTAGEN`	`5 5`		`C->K: Reduced palmitoylation level.`
`MUTAGEN`	`5 5`		`C->S: Abolishes plasma membrane association; when associated with S-21.`
`MUTAGEN`	`20 20`		`C->S: Complete loss of interaction with CD4 or CD8.`
`MUTAGEN`	`23 23`		`C->S: Complete loss of interaction with CD4 or CD8.`
`MUTAGEN`	`269 269`		`K->N: Reduced activity.`
`MUTAGEN`	`270 270`		`V->L: Reduced activity.`
`MUTAGEN`	`271 271`		`A->S: Reduced activity.`
`MUTAGEN`	`272 272`		`V->A: Reduced activity.`
`MUTAGEN`	`273 273`		`K->R: Loss of activity.`
`MUTAGEN`	`274 274`		`S->N: Reduced activity.`
`MUTAGEN`	`275 275`		`L->M: Reduced activity.`
`MUTAGEN`	`276 276`		`K->V: Reduced activity.`
`MUTAGEN`	`505 505`		`Y->F: Causes thymic tumors.`

Sequence information

Length: 509 AA [This is the length of the unprocessed precursor]

Molecular weight: 57943 Da [This is the MW of the unprocessed precursor]

CRC64: 3513102F49A7FD0B [This is a checksum on the sequence]

        10         20         30         40         50         60 
MGCVCSSNPE DDWMENIDVC ENCHYPIVPL DSKISLPIRN GSEVRDPLVT YEGSLPPASP 

        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 GLHDLVRHYT NASDGLCTKL SRPCQTQKPQ KPWWEDEWEV 

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

       310        320        330        340        350        360 
VRLYAVVTQE PIYIITEYME NGSLVDFLKT PSGIKLNVNK LLDMAAQIAE GMAFIEEQNY 

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

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

       490        500 
PEDRPTFDYL RSVLDDFFTA TEGQYQPQP

P06240 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools