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P24604 (TEC_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 153. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tyrosine-protein kinase Tec

EC=2.7.10.2
Gene names
Name:Tec
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length630 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Non-receptor tyrosine kinase that contributes to signaling from many receptors and participates as a signal transducer in multiple downstream pathways, including regulation of the actin cytoskeleton. Plays a redundant role to ITK in regulation of the adaptive immune response. Regulates the development, function and differentiation of conventional T-cells and nonconventional NKT-cells. Required for TCR-dependent IL2 gene induction. Phosphorylates DOK1, one CD28-specific substrate, and contributes to CD28-signaling. Mediates signals that negatively regulate IL2RA expression induced by TCR cross-linking. Plays a redundant role to BTK in BCR-signaling for B-cell development and activation, especially by phosphorylating STAP1, a BCR-signaling protein. Required in mast cells for efficient cytokine production. Involved in both growth and differentiation mechanisms of myeloid cells through activation by the granulocyte colony-stimulating factor CSF3, a critical cytokine to promoting the growth, differentiation, and functional activation of myeloid cells. Participates in platelet signaling downstream of integrin activation. Cooperates with JAK2 through reciprocal phosphorylation to mediate cytokine-driven activation of FOS transcription. GRB10, a negative modifier of the FOS activation pathway, is another substrate of TEC. TEC is involved in G protein-coupled receptor- and integrin-mediated signalings in blood platelets. Plays a role in hepatocyte proliferation and liver regeneration and is involved in HGF-induced ERK signaling pathway. TEC regulates also FGF2 unconventional secretion (endoplasmic reticulum (ER)/Golgi-independent mechanism) under various physiological conditions through phosphorylation of FGF2 'Tyr-82'. May also be involved in the regulation of osteoclast differentiation. Ref.7 Ref.8 Ref.9 Ref.10 Ref.13 Ref.16

Catalytic activity

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

Cofactor

Binds 1 zinc ion per subunit By similarity.

Enzyme regulation

Activated by tyrosine phosphorylation by a wide range of cytokine stimulations. When T-cells or B-cells receptors are activated, a series of phosphorylation leads to the recruitment of TEC to the cell membrane, where it is phosphorylated at Tyr-518. Also activated in response to SCF. Integrin engagement induces tyrosine phosphorylation of TEC in platelets. STAP1 participates in a positive feedback loop by increasing the activity of TEC. SOCS1 is an inhibitor of TEC kinase activity. Ref.5 Ref.6 Ref.8 Ref.9

Subunit structure

Interacts with INPP5D/SHIP1 and INPPL1/SHIP2. Interacts with CD28, FASLG, FGF2, GRB10 and KIT By similarity. Interacts with VAV1 and JAK2. Interacts with LYN. Ref.5 Ref.9

Subcellular location

Cytoplasm. Cell membrane; Peripheral membrane protein. Cytoplasmcytoskeleton. Note: Following B-cell or T-cell receptors activation by antigen, translocates to the plasma membrane through its PH domain. Thrombin and integrin engagement induces translocation of TEC to the cytoskeleton during platelet activation. In cardiac myocytes, assumes a diffuse intracellular localization under basal conditions but is recruited to striated structures upon various stimuli, including ATP By similarity. Ref.10 Ref.11 Ref.15

Tissue specificity

Preferentially expressed in liver. Expression is also seen in the hematopoietic cells such as bone marrow, thymus and spleen. Lower expression is seen in the heart, kidney and ovary.

Domain

The PH domain mediates the binding to inositol polyphosphate and phosphoinositides, leading to its targeting to the plasma membrane. It is extended in the BTK kinase family by a region designated the TH (Tec homology) domain, which consists of about 80 residues preceding the SH3 domain. Ref.10

The SH3 domain is essential for its targeting to activated CD28 costimulatory molecule By similarity. Ref.10

Post-translational modification

Following B-cell or T-cell receptors engagement, translocates to the plasma membrane where it gets phosphorylated at Tyr-518. Undergoes also tyrosine phosphorylation during platelet activation. Ref.5 Ref.6 Ref.7

Sequence similarities

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

Contains 1 Btk-type zinc finger.

Contains 1 PH domain.

Contains 1 protein kinase domain.

Contains 1 SH2 domain.

Contains 1 SH3 domain.

Alternative products

This entry describes 6 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P24604-1)

Also known as: TecIV;

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: P24604-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-94: MNFNTILEEI...DANTLYIFAP → MMVSFPVKINFHS
     224-245: Missing.
Isoform 3 (identifier: P24604-3)

Also known as: TecIIb;

The sequence of this isoform differs from the canonical sequence as follows:
     604-630: RPEGRPSLEDLLRTIDELVECEETFGR → ESCLCRVAQDLSSKNLIGSRF
Isoform 4 (identifier: P24604-4)

Also known as: TecIIa;

The sequence of this isoform differs from the canonical sequence as follows:
     224-245: Missing.
     604-630: RPEGRPSLEDLLRTIDELVECEETFGR → ESCLCRVAQDLSSKNLIGSRF
Isoform 5 (identifier: P24604-5)

Also known as: TecIII;

The sequence of this isoform differs from the canonical sequence as follows:
     224-245: Missing.
Isoform 6 (identifier: P24604-6)

Also known as: TecI;

The sequence of this isoform differs from the canonical sequence as follows:
     82-100: VVHDANTLYIFAPSPQSRD → STKQGPMGEEVKRRNKEQQ
     101-630: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 630630Tyrosine-protein kinase Tec
PRO_0000088171

Regions

Domain4 – 111108PH
Domain178 – 23861SH3
Domain246 – 34499SH2
Domain369 – 622254Protein kinase
Zinc finger113 – 14937Btk-type
Nucleotide binding375 – 3839ATP By similarity

Sites

Active site4881Proton acceptor By similarity
Metal binding1211Zinc By similarity
Metal binding1321Zinc By similarity
Metal binding1331Zinc By similarity
Metal binding1431Zinc By similarity
Binding site3971ATP By similarity

Amino acid modifications

Modified residue2051Phosphotyrosine; by autocatalysis By similarity
Modified residue2271Phosphotyrosine By similarity
Modified residue5181Phosphotyrosine; by autocatalysis, LYN and JAK2 Ref.7 Ref.12 Ref.14

Natural variations

Alternative sequence1 – 9494MNFNT…YIFAP → MMVSFPVKINFHS in isoform 2.
VSP_005012
Alternative sequence82 – 10019VVHDA…PQSRD → STKQGPMGEEVKRRNKEQQ in isoform 6.
VSP_005013
Alternative sequence101 – 630530Missing in isoform 6.
VSP_005014
Alternative sequence224 – 24522Missing in isoform 2, isoform 4 and isoform 5.
VSP_005015
Alternative sequence604 – 63027RPEGR…ETFGR → ESCLCRVAQDLSSKNLIGSR F in isoform 3 and isoform 4.
VSP_005016

Experimental info

Mutagenesis3971K → M: Impairs kinase activity. Ref.6
Sequence conflict231L → P in AAD43404. Ref.2
Sequence conflict231L → P in AAD43402. Ref.2
Sequence conflict231L → P in AAD43405. Ref.2
Sequence conflict231L → P in AAD43406. Ref.2
Sequence conflict231L → P in AAD43407. Ref.2
Sequence conflict311C → F in AAD43404. Ref.2
Sequence conflict311C → F in AAD43402. Ref.2
Sequence conflict311C → F in AAD43405. Ref.2
Sequence conflict311C → F in AAD43406. Ref.2
Sequence conflict311C → F in AAD43407. Ref.2
Sequence conflict341P → T in AAD43404. Ref.2
Sequence conflict341P → T in AAD43402. Ref.2
Sequence conflict341P → T in AAD43405. Ref.2
Sequence conflict341P → T in AAD43406. Ref.2
Sequence conflict341P → T in AAD43407. Ref.2
Sequence conflict5351V → E in AAA40018. Ref.4
Sequence conflict550 – 5534FGVL → YGIP in AAA40018. Ref.4
Sequence conflict5901T → S in AAD43402. Ref.2
Sequence conflict5901T → S in AAD43405. Ref.2
Sequence conflict5901T → S in AAD43406. Ref.2
Sequence conflict5901T → S in AAD43407. Ref.2
Sequence conflict6111L → F in AAD43404. Ref.2
Sequence conflict6111L → F in AAD43402. Ref.2
Sequence conflict6111L → F in AAD43405. Ref.2
Sequence conflict6111L → F in AAD43406. Ref.2
Sequence conflict6111L → F in AAD43407. Ref.2
Sequence conflict6111L → F in CAA39196. Ref.3

Secondary structure

................ 630
Helix Strand Turn

Details...

Sequences

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

Last modified November 1, 1995. Version 2.
Checksum: 262640EE90D4A6D2

FASTA63073,426
        10         20         30         40         50         60 
MNFNTILEEI LIKRSQQKKK TSLLNYKERL CVLPKSVLSY YEGRAEKKYR KGVIDISKIK 

        70         80         90        100        110        120 
CVEIVKNDDG VIPCQNKFPF QVVHDANTLY IFAPSPQSRD RWVKKLKEEI KNNNNIMIKY 

       130        140        150        160        170        180 
HPKFWADGSY QCCRQTEKLA PGCEKYNLFE SSIRKTLPPA PEIKKRRPPP PIPPEEENTE 

       190        200        210        220        230        240 
EIVVAMYDFQ ATEAHDLRLE RGQEYIILEK NDLHWWRARD KYGSEGYIPS NYVTGKKSNN 

       250        260        270        280        290        300 
LDQYEWYCRN TNRSKAEQLL RTEDKEGGFM VRDSSQPGLY TVSLYTKFGG EGSSGFRHYH 

       310        320        330        340        350        360 
IKETATSPKK YYLAEKHAFG SIPEIIEYHK HNAAGLVTRL RYPVSTKGKN APTTAGFSYD 

       370        380        390        400        410        420 
KWEINPSELT FMRELGSGLF GVVRLGKWRA QYKVAIKAIR EGAMCEEDFI EEAKVMMKLT 

       430        440        450        460        470        480 
HPKLVQLYGV CTQQKPIYIV TEFMERGCLL NFLRQRQGHF SRDMLLSMCQ DVCEGMEYLE 

       490        500        510        520        530        540 
RNSFIHRDLA ARNCLVNEAG VVKVSDFGMA RYVLDDQYTS SSGAKFPVKW CPPEVFNYSR 

       550        560        570        580        590        600 
FSSKSDVWSF GVLMWEIFTE GRMPFEKNTN YEVVTMVTRG HRLHRPKLAT KYLYEVMLRC 

       610        620        630 
WQERPEGRPS LEDLLRTIDE LVECEETFGR 

« Hide

Isoform 2 [UniParc].

Checksum: 72819611523F0872
Show »

FASTA52761,523
Isoform 3 (TecIIb) [UniParc].

Checksum: 196018BC9EC862A5
Show »

FASTA62472,592
Isoform 4 (TecIIa) [UniParc].

Checksum: B213B18A8519E4F5
Show »

FASTA60270,104
Isoform 5 (TecIII) [UniParc].

Checksum: C43EF410FD030DA1
Show »

FASTA60870,938
Isoform 6 (TecI) [UniParc].

Checksum: 32AB0BC0567F2CEC
Show »

FASTA10011,723

References

« Hide 'large scale' references
[1]"Expression of a novel form of Tec kinase in hematopoietic cells and mapping of the gene to chromosome 5 near Kit."
Mano H., Mano K., Tang B., Koehler M., Yi T., Gilbert D.J., Jenkins N.A., Copeland N.G., Ihle J.N.
Oncogene 8:417-424(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"Splice variants of the mouse Tec gene are differentially expressed in vivo."
Merkel A.L., Atmosukarto I.I.C., Stevens K., Rathjen P.D., Booker G.W.
Cytogenet. Cell Genet. 84:132-139(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1; 3; 4; 5 AND 6).
Strain: 129.
[3]"A novel protein-tyrosine kinase, tec, is preferentially expressed in liver."
Mano H., Ishikawa F., Nishida J., Hirai H., Takaku F.
Oncogene 5:1781-1786(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 82-630 (ISOFORM 2).
Strain: BALB/c.
Tissue: Liver.
[4]"The application of the polymerase chain reaction to cloning members of the protein tyrosine kinase family."
Wilks A.F., Kurban R.R., Hovens C.M., Ralph S.J.
Gene 85:67-74(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 485-553.
[5]"Tec protein tyrosine kinase is involved in the signaling mechanism of granulocyte colony-stimulating factor receptor."
Miyazato A., Yamashita Y., Hatake K., Miura Y., Ozawa K., Mano H.
Cell Growth Differ. 7:1135-1139(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION, ENZYME REGULATION, INTERACTION WITH VAV1.
[6]"Tec protein-tyrosine kinase is an effector molecule of Lyn protein-tyrosine kinase."
Mano H., Yamashita Y., Miyazato A., Miura Y., Ozawa K.
FASEB J. 10:637-642(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION BY LYN, ENZYME REGULATION, MUTAGENESIS OF LYS-397.
[7]"Tec and Jak2 kinases cooperate to mediate cytokine-driven activation of c-fos transcription."
Yamashita Y., Watanabe S., Miyazato A., Ohya K., Ikeda U., Shimada K., Komatsu N., Hatake K., Miura Y., Ozawa K., Mano H.
Blood 91:1496-1507(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, PHOSPHORYLATION OF JAK2, PHOSPHORYLATION AT TYR-518.
[8]"Tec kinase is involved in transcriptional regulation of IL-2 and IL-4 in the CD28 pathway."
Yang W.C., Olive D.
Eur. J. Immunol. 29:1842-1849(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYME REGULATION, FUNCTION IN THE CD28 SIGNALING PATHWAY.
[9]"The role of Tec protein-tyrosine kinase in T cell signaling."
Yang W.C., Ghiotto M., Barbarat B., Olive D.
J. Biol. Chem. 274:607-617(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CD28, ENZYME REGULATION, FUNCTION IN PHOSPHORYLATION OF DOK1.
[10]"The SH3 domain of Tec kinase is essential for its targeting to activated CD28 costimulatory molecule."
Garcon F., Ghiotto M., Gerard A., Yang W.C., Olive D., Nunes J.A.
Eur. J. Immunol. 34:1972-1980(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, DOMAIN.
[11]"Dynamic regulation of Tec kinase localization in membrane-proximal vesicles of a T cell clone revealed by total internal reflection fluorescence and confocal microscopy."
Kane L.P., Watkins S.C.
J. Biol. Chem. 280:21949-21954(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[12]"Quantitative time-resolved phosphoproteomic analysis of mast cell signaling."
Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R.
J. Immunol. 179:5864-5876(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-518, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Mast cell.
[13]"The protein tyrosine kinase Tec regulates mast cell function."
Schmidt U., Abramova A., Boucheron N., Eckelhart E., Schebesta A., Bilic I., Kneidinger M., Unger B., Hammer M., Sibilia M., Valent P., Ellmeier W.
Eur. J. Immunol. 39:3228-3238(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[14]"The phagosomal proteome in interferon-gamma-activated macrophages."
Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-518, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"Stress signaling by Tec tyrosine kinase in the ischemic myocardium."
Zhang M.J., Franklin S., Li Y., Wang S., Ru X., Mitchell-Jordan S.A., Mano H., Stefani E., Ping P., Vondriska T.M.
Am. J. Physiol. 299:H713-H722(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[16]"TEC protein tyrosine kinase is involved in the Erk signaling pathway induced by HGF."
Li F., Jiang Y., Zheng Q., Yang X., Wang S.
Biochem. Biophys. Res. Commun. 404:79-85(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN THE HGF-INDUCED ERK SIGNALING PATHWAY.
[17]"The solution structure and intramolecular associations of the Tec kinase SRC homology 3 domain."
Pursglove S.E., Mulhern T.D., Mackay J.P., Hinds M.G., Booker G.W.
J. Biol. Chem. 277:755-762(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 179-245.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
S53716 mRNA. Translation: AAA13515.2.
AF071938, AF071936, AF071937 Genomic DNA. Translation: AAD43404.1.
AF071946 expand/collapse EMBL AC list , AF071936, AF071937, AF071938, AF071939, AF071940, AF071941, AF071942, AF071943, AF071944, AF071945 Genomic DNA. Translation: AAD43402.1.
AF071946 expand/collapse EMBL AC list , AF071936, AF071937, AF071938, AF071939, AF071940, AF071941, AF071942, AF071943, AF071944, AF071945 Genomic DNA. Translation: AAD43405.1.
AF071946 expand/collapse EMBL AC list , AF071936, AF071937, AF071938, AF071940, AF071941, AF071942, AF071943, AF071944, AF071945 Genomic DNA. Translation: AAD43406.1.
AF071946 expand/collapse EMBL AC list , AF071936, AF071937, AF071938, AF071940, AF071941, AF071942, AF071943, AF071944, AF071945 Genomic DNA. Translation: AAD43407.1.
X55663 mRNA. Translation: CAA39196.1.
M33427 mRNA. Translation: AAA40018.1.
CCDSCCDS51515.1. [P24604-5]
CCDS51516.1. [P24604-1]
PIRJU0215.
S13763.
T01380.
RefSeqNP_001106931.1. NM_001113460.2.
NP_001106932.1. NM_001113461.2.
NP_001106935.1. NM_001113464.2.
XP_006503908.1. XM_006503845.1.
XP_006503909.1. XM_006503846.1.
UniGeneMm.319581.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1GL5NMR-A181-244[»]
ProteinModelPortalP24604.
SMRP24604. Positions 1-623.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid204103. 2 interactions.
IntActP24604. 1 interaction.
MINTMINT-5167157.

PTM databases

PhosphoSiteP24604.

Proteomic databases

PRIDEP24604.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000138842; ENSMUSP00000120155; ENSMUSG00000029217.
ENSMUST00000149533; ENSMUSP00000123258; ENSMUSG00000029217.
GeneID21682.
KEGGmmu:21682.

Organism-specific databases

CTD7006.
MGIMGI:98662. Tec.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00640000091251.
HOGENOMHOG000233859.
HOVERGENHBG008761.
InParanoidP24604.
KOK07364.
OrthoDBEOG7KM5SC.
PhylomeDBP24604.

Enzyme and pathway databases

BRENDA2.7.10.2. 3474.

Gene expression databases

ArrayExpressP24604.
BgeeP24604.
GenevestigatorP24604.

Family and domain databases

Gene3D2.30.29.30. 1 hit.
3.30.505.10. 1 hit.
InterProIPR011009. Kinase-like_dom.
IPR011993. PH_like_dom.
IPR001849. Pleckstrin_homology.
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.
IPR001562. Znf_Btk_motif.
[Graphical view]
PfamPF00779. BTK. 1 hit.
PF00169. PH. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
PF00017. SH2. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
PRINTSPR00401. SH2DOMAIN.
PR00452. SH3DOMAIN.
PR00402. TECBTKDOMAIN.
PR00109. TYRKINASE.
SMARTSM00107. BTK. 1 hit.
SM00233. PH. 1 hit.
SM00252. 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.
PROSITEPS50003. PH_DOMAIN. 1 hit.
PS00107. 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.
PS51113. ZF_BTK. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP24604.
NextBio300992.
PROP24604.
SOURCESearch...

Entry information

Entry nameTEC_MOUSE
AccessionPrimary (citable) accession number: P24604
Secondary accession number(s): Q9R1M9 expand/collapse secondary AC list , Q9WVN0, Q9WVN1, Q9WVN2, Q9WVN3
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: November 1, 1995
Last modified: July 9, 2014
This is version 153 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

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

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot