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P42680 (TEC_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 142. 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·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
Synonyms:PSCTK4
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length631 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-215'. May also be involved in the regulation of osteoclast differentiation. Ref.8 Ref.10 Ref.15 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-519. 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.7 Ref.9 Ref.10

Subunit structure

Interacts with INPP5D/SHIP1 and INPPL1/SHIP2. Interacts with CD28, FASLG, FGF2, GRB10, LYN and KIT. Interacts with VAV1 and JAK2 By similarity. Ref.5 Ref.8 Ref.11 Ref.12 Ref.16

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.6 Ref.9

Tissue specificity

Expressed in a wide range of cells, including hematopoietic cell lines like myeloid, B-, and T-cell lineages.

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.

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

Post-translational modification

Following B-cell or T-cell receptors engagement, translocates to the plasma membrane where it gets phosphorylated at Tyr-519. Undergoes also tyrosine phosphorylation during platelet activation. Ref.4 Ref.5 Ref.6 Ref.9

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.

Caution

It is uncertain whether Met-1 is the initiator.

Ontologies

Keywords
   Biological processAdaptive immunity
Immunity
   Cellular componentCell membrane
Cytoplasm
Cytoskeleton
Membrane
   Coding sequence diversityPolymorphism
   DomainSH2 domain
SH3 domain
Zinc-finger
   LigandATP-binding
Lipid-binding
Metal-binding
Nucleotide-binding
Zinc
   Molecular functionKinase
Transferase
Tyrosine-protein kinase
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processB cell receptor signaling pathway

Inferred from direct assay Ref.10. Source: UniProtKB

Fc-epsilon receptor signaling pathway

Traceable author statement. Source: Reactome

innate immune response

Traceable author statement. Source: Reactome

integrin-mediated signaling pathway

Inferred from direct assay Ref.9. Source: UniProtKB

intracellular signal transduction

Traceable author statement Ref.1. Source: ProtInc

peptidyl-tyrosine phosphorylation

Inferred from direct assay Ref.10. Source: GOC

protein phosphorylation

Traceable author statement Ref.1. Source: ProtInc

regulation of platelet activation

Inferred from direct assay Ref.6Ref.9. Source: UniProtKB

tissue regeneration

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcytoskeleton

Inferred from direct assay Ref.6Ref.9. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

lipid binding

Inferred from electronic annotation. Source: UniProtKB-KW

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

non-membrane spanning protein tyrosine kinase activity

Inferred from direct assay Ref.10. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 631631Tyrosine-protein kinase Tec
PRO_0000088170

Regions

Domain4 – 111108PH
Domain179 – 23961SH3
Domain247 – 34599SH2
Domain370 – 623254Protein kinase
Zinc finger113 – 14937Btk-type
Nucleotide binding376 – 3849ATP By similarity

Sites

Active site4891Proton acceptor By similarity
Metal binding1211Zinc By similarity
Metal binding1321Zinc By similarity
Metal binding1331Zinc By similarity
Metal binding1431Zinc By similarity
Binding site3981ATP By similarity

Amino acid modifications

Modified residue2061Phosphotyrosine; by autocatalysis Ref.4 Ref.13
Modified residue2281Phosphotyrosine Ref.13
Modified residue5191Phosphotyrosine; by autocatalysis, LYN and JAK2 Ref.14

Natural variations

Natural variant441R → Q. Ref.17
Corresponds to variant rs35374286 [ dbSNP | Ensembl ].
VAR_041850
Natural variant5631R → K in a lung adenocarcinoma sample; somatic mutation. Ref.17
VAR_041851

Experimental info

Sequence conflict5141V → F in BAA06171. Ref.1

Secondary structure

.............................. 631
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P42680 [UniParc].

Last modified September 11, 2007. Version 2.
Checksum: F55DECBF9916E1F9

FASTA63173,581
        10         20         30         40         50         60 
MNFNTILEEI LIKRSQQKKK TSPLNYKERL FVLTKSMLTY YEGRAEKKYR KGFIDVSKIK 

        70         80         90        100        110        120 
CVEIVKNDDG VIPCQNKYPF QVVHDANTLY IFAPSPQSRD LWVKKLKEEI KNNNNIMIKY 

       130        140        150        160        170        180 
HPKFWTDGSY QCCRQTEKLA PGCEKYNLFE SSIRKALPPA PETKKRRPPP PIPLEEEDNS 

       190        200        210        220        230        240 
EEIVVAMYDF QAAEGHDLRL ERGQEYLILE KNDVHWWRAR DKYGNEGYIP SNYVTGKKSN 

       250        260        270        280        290        300 
NLDQYEWYCR NMNRSKAEQL LRSEDKEGGF MVRDSSQPGL YTVSLYTKFG GEGSSGFRHY 

       310        320        330        340        350        360 
HIKETTTSPK KYYLAEKHAF GSIPEIIEYH KHNAAGLVTR LRYPVSVKGK NAPTTAGFSY 

       370        380        390        400        410        420 
EKWEINPSEL TFMRELGSGL FGVVRLGKWR AQYKVAIKAI REGAMCEEDF IEEAKVMMKL 

       430        440        450        460        470        480 
THPKLVQLYG VCTQQKPIYI VTEFMERGCL LNFLRQRQGH FSRDVLLSMC QDVCEGMEYL 

       490        500        510        520        530        540 
ERNSFIHRDL AARNCLVSEA GVVKVSDFGM ARYVLDDQYT SSSGAKFPVK WCPPEVFNYS 

       550        560        570        580        590        600 
RFSSKSDVWS FGVLMWEVFT EGRMPFEKYT NYEVVTMVTR GHRLYQPKLA SNYVYEVMLR 

       610        620        630 
CWQEKPEGRP SFEDLLRTID ELVECEETFG R 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning and analysis of the human Tec protein-tyrosine kinase."
Sato K., Mano H., Ariyama T., Inazawa J., Yazaki Y., Hirai H.
Leukemia 8:1663-1672(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Blood.
[2]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 (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"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].
Tissue: Liver.
[4]"Identification of phosphorylation sites within the SH3 domains of Tec family tyrosine kinases."
Nore B.F., Mattsson P.T., Antonsson P., Backesjo C.-M., Westlund A., Lennartsson J., Hansson H., Low P., Ronnstrand L., Smith C.I.E.
Biochim. Biophys. Acta 1645:123-132(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 203-206, PHOSPHORYLATION AT TYR-206.
[5]"Tec kinase associates with c-kit and is tyrosine phosphorylated and activated following stem cell factor binding."
Tang B., Mano H., Yi T., Ihle J.N.
Mol. Cell. Biol. 14:8432-8437(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION, INTERACTION WITH KIT, ENZYME REGULATION.
[6]"Integrin-dependent tyrosine phosphorylation and cytoskeletal translocation of Tec in thrombin-activated platelets."
Laffargue M., Monnereau L., Tuech J., Ragab A., Ragab-Thomas J., Payrastre B., Raynal P., Chap H.
Biochem. Biophys. Res. Commun. 238:247-251(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION, SUBCELLULAR LOCATION.
[7]"SOCS-1/JAB/SSI-1 can bind to and suppress Tec protein-tyrosine kinase."
Ohya K., Kajigaya S., Yamashita Y., Miyazato A., Hatake K., Miura Y., Ikeda U., Shimada K., Ozawa K., Mano H.
J. Biol. Chem. 272:27178-27182(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYME REGULATION.
[8]"Grb10/GrbIR as an in vivo substrate of Tec tyrosine kinase."
Mano H., Ohya K., Miyazato A., Yamashita Y., Ogawa W., Inazawa J., Ikeda U., Shimada K., Hatake K., Kasuga M., Ozawa K., Kajigaya S.
Genes Cells 3:431-441(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH GRB10, FUNCTION IN PHOSPHORYLATION OF GRB10.
[9]"Tec is involved in G protein-coupled receptor- and integrin-mediated signalings in human blood platelets."
Hamazaki Y., Kojima H., Mano H., Nagata Y., Todokoro K., Abe T., Nagasawa T.
Oncogene 16:2773-2779(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION, ENZYME REGULATION, SUBCELLULAR LOCATION.
[10]"Molecular cloning of a docking protein, BRDG1, that acts downstream of the Tec tyrosine kinase."
Ohya K., Kajigaya S., Kitanaka A., Yoshida K., Miyazato A., Yamashita Y., Yamanaka T., Ikeda U., Shimada K., Ozawa K., Mano H.
Proc. Natl. Acad. Sci. U.S.A. 96:11976-11981(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF STAP1, ENZYME REGULATION.
[11]"SHIP family inositol phosphatases interact with and negatively regulate the Tec tyrosine kinase."
Tomlinson M.G., Heath V.L., Turck C.W., Watson S.P., Weiss A.
J. Biol. Chem. 279:55089-55096(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH INPP5D AND INPPL1.
[12]"Identification of SH3 domain interaction partners of human FasL (CD178) by phage display screening."
Voss M., Lettau M., Janssen O.
BMC Immunol. 10:53-53(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FASLG.
[13]"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-206 AND TYR-228, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-519, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[15]"Tec protein tyrosine kinase inhibits CD25 expression in human T-lymphocyte."
Susaki K., Kitanaka A., Dobashi H., Kubota Y., Kittaka K., Kameda T., Yamaoka G., Mano H., Mihara K., Ishida T.
Immunol. Lett. 127:135-142(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[16]"Tec-kinase-mediated phosphorylation of fibroblast growth factor 2 is essential for unconventional secretion."
Ebert A.D., Laussmann M., Wegehingel S., Kaderali L., Erfle H., Reichert J., Lechner J., Beer H.D., Pepperkok R., Nickel W.
Traffic 11:813-826(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF FGF2, INTERACTION WITH FGF2.
[17]"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] [Europe PMC] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] GLN-44 AND LYS-563.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D29767 mRNA. Translation: BAA06171.1.
CH471069 Genomic DNA. Translation: EAW93055.1.
BC101711 mRNA. Translation: AAI01712.1.
BC101713 mRNA. Translation: AAI01714.1.
BC143487 mRNA. Translation: AAI43488.1.
PIRI38268.
I56997.
RefSeqNP_003206.2. NM_003215.2.
UniGeneHs.479670.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2LULNMR-A1-154[»]
ProteinModelPortalP42680.
SMRP42680. Positions 1-154, 182-624.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112865. 23 interactions.
IntActP42680. 13 interactions.
MINTMINT-1498364.
STRING9606.ENSP00000370912.

Chemistry

BindingDBP42680.
ChEMBLCHEMBL4246.
GuidetoPHARMACOLOGY2238.

PTM databases

PhosphoSiteP42680.

Polymorphism databases

DMDM158518392.

Proteomic databases

PaxDbP42680.
PRIDEP42680.

Protocols and materials databases

DNASU7006.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000381501; ENSP00000370912; ENSG00000135605.
GeneID7006.
KEGGhsa:7006.
UCSCuc003gxz.3. human.

Organism-specific databases

CTD7006.
GeneCardsGC04M048137.
HGNCHGNC:11719. TEC.
HPAHPA005733.
MIM600583. gene.
neXtProtNX_P42680.
PharmGKBPA36436.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000233859.
HOVERGENHBG008761.
InParanoidP42680.
KOK07364.
OMACTQQKPI.
OrthoDBEOG7KM5SC.
PhylomeDBP42680.
TreeFamTF351634.

Enzyme and pathway databases

BRENDA2.7.10.2. 2681.
ReactomeREACT_111102. Signal Transduction.
REACT_6900. Immune System.
SignaLinkP42680.

Gene expression databases

ArrayExpressP42680.
BgeeP42680.
CleanExHS_TEC.
GenevestigatorP42680.

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

GeneWikiTEC_(gene).
GenomeRNAi7006.
NextBio27366.
PROP42680.
SOURCESearch...

Entry information

Entry nameTEC_HUMAN
AccessionPrimary (citable) accession number: P42680
Secondary accession number(s): B7ZKZ6, Q3MIS5
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: September 11, 2007
Last modified: April 16, 2014
This is version 142 of the entry and version 2 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 4

Human chromosome 4: entries, gene names and cross-references to MIM