Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q13424 (SNTA1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 132. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Alpha-1-syntrophin
Alternative name(s):
59 kDa dystrophin-associated protein A1 acidic component 1
Pro-TGF-alpha cytoplasmic domain-interacting protein 1
Short name=TACIP1
Syntrophin-1
Gene names
Name:SNTA1
Synonyms:SNT1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length505 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Adapter protein that binds to and probably organizes the subcellular localization of a variety of membrane proteins. May link various receptors to the actin cytoskeleton and the extracellular matrix via the dystrophin glycoprotein complex. Plays an important role in synapse formation and in the organization of UTRN and acetylcholine receptors at the neuromuscular synapse. Binds to phosphatidylinositol 4,5-bisphosphate By similarity.

Subunit structure

Monomer and homodimer. Interacts with the other members of the syntrophin family SNTB1 and SNTB2; SGCG and SGCA of the dystrophin glycoprotein complex; NOS1; GRB2; the sodium channel proteins SCN4A and SCN5A; F-actin and calmodulin By similarity. Interacts with dystrophin protein DMD and related proteins DTNA and UTRN and with MAPK12, TGFA and GA. Interacts with MYOC; regulates muscle hypertrophy By similarity. Ref.1 Ref.2 Ref.3 Ref.8 Ref.9

Subcellular location

Cell membranesarcolemma; Peripheral membrane protein; Cytoplasmic side By similarity. Cell junction By similarity. Cytoplasmcytoskeleton By similarity. Note: In skeletal muscle, it localizes at the cytoplasmic side of the sarcolemmal membrane and at neuromuscular junctions By similarity.

Tissue specificity

High expression in skeletal muscle and heart. Low expression in brain, pancreas, liver, kidney and lung. Not detected in placenta.

Domain

The PH 1 domain mediates the oligomerization in a calcium dependent manner, and the association with the phosphatidylinositol 4,5-bisphosphate By similarity.

The PDZ domain binds to the last three or four amino acids of ion channels and receptor proteins. The association with dystrophin or related proteins probably leaves the PDZ domain available to recruit proteins to the membrane By similarity.

The SU domain binds calmodulin in a calcium-dependent manner By similarity.

Post-translational modification

Phosphorylated by CaM-kinase II. Phosphorylation may inhibit the interaction with DMD By similarity.

Involvement in disease

Long QT syndrome 12 (LQT12) [MIM:612955]: A heart disorder characterized by a prolonged QT interval on the ECG and polymorphic ventricular arrhythmias. They cause syncope and sudden death in response to exercise or emotional stress, and can present with a sentinel event of sudden cardiac death in infancy.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.14 Ref.15

Sequence similarities

Belongs to the syntrophin family.

Contains 1 PDZ (DHR) domain.

Contains 2 PH domains.

Contains 1 SU (syntrophin unique) domain.

Ontologies

Keywords
   Cellular componentCell junction
Cell membrane
Cytoplasm
Cytoskeleton
Membrane
   Coding sequence diversityPolymorphism
   DiseaseDisease mutation
Long QT syndrome
   DomainRepeat
   LigandActin-binding
Calcium
Calmodulin-binding
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processmuscle contraction

Traceable author statement Ref.1. Source: ProtInc

negative regulation of peptidyl-cysteine S-nitrosylation

Inferred from mutant phenotype Ref.15. Source: BHF-UCL

neuromuscular junction development

Inferred from electronic annotation. Source: Ensembl

regulation of heart rate

Inferred from mutant phenotype Ref.15. Source: BHF-UCL

regulation of sodium ion transmembrane transport

Inferred from mutant phenotype Ref.15. Source: BHF-UCL

regulation of vasoconstriction by circulating norepinephrine

Inferred from electronic annotation. Source: Ensembl

regulation of ventricular cardiac muscle cell membrane repolarization

Inferred from mutant phenotype Ref.15. Source: BHF-UCL

ventricular cardiac muscle cell action potential

Inferred from mutant phenotype Ref.15. Source: BHF-UCL

   Cellular_componentcell junction

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoplasm

Inferred from electronic annotation. Source: UniProtKB-KW

cytoskeleton

Inferred from electronic annotation. Source: UniProtKB-SubCell

intracellular

Inferred from direct assay PubMed 17628813. Source: UniProtKB

neuromuscular junction

Inferred from electronic annotation. Source: Ensembl

postsynaptic membrane

Inferred from electronic annotation. Source: Ensembl

protein complex

Inferred from direct assay Ref.15. Source: BHF-UCL

sarcolemma

Inferred from electronic annotation. Source: UniProtKB-SubCell

syntrophin complex

Traceable author statement PubMed 21164104. Source: BHF-UCL

   Molecular_functionATPase binding

Inferred from physical interaction Ref.15. Source: BHF-UCL

ion channel binding

Inferred from physical interaction Ref.15. Source: BHF-UCL

nitric-oxide synthase binding

Inferred from physical interaction Ref.15. Source: BHF-UCL

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ABCA1O954772EBI-717191,EBI-784112
Mapk12Q635385EBI-717191,EBI-783937From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 505505Alpha-1-syntrophin
PRO_0000184006

Regions

Domain6 – 269264PH 1
Domain87 – 17084PDZ
Domain293 – 401109PH 2
Domain449 – 50557SU
Region483 – 50523Calmodulin-binding By similarity

Amino acid modifications

Modified residue1891Phosphoserine Ref.10 Ref.11 Ref.13
Modified residue1931Phosphoserine Ref.10 Ref.11

Natural variations

Natural variant2571A → G in LQT12; leads to a gain of function of the voltage dependent sodium channel. Ref.14
Corresponds to variant rs56157422 [ dbSNP | Ensembl ].
VAR_062399
Natural variant3641L → F.
Corresponds to variant rs1046815 [ dbSNP | Ensembl ].
VAR_014075
Natural variant3901A → V in LQT12; results in released inhibition of nNOS, S-nitrosylation of SCN5A and increased late sodium current. Ref.15
VAR_062400

Experimental info

Sequence conflict61R → P in AAB36398. Ref.2
Sequence conflict251G → A in AAB36398. Ref.2
Sequence conflict32 – 332LL → PV in AAB36398. Ref.2
Sequence conflict661G → D in AAB36398. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q13424 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: C07DA5F21C775CF8

FASTA50553,895
        10         20         30         40         50         60 
MASGRRAPRT GLLELRAGAG SGAGGERWQR VLLSLAEDVL TVSPADGDPG PEPGAPREQE 

        70         80         90        100        110        120 
PAQLNGAAEP GAGPPQLPEA LLLQRRRVTV RKADAGGLGI SIKGGRENKM PILISKIFKG 

       130        140        150        160        170        180 
LAADQTEALF VGDAILSVNG EDLSSATHDE AVQVLKKTGK EVVLEVKYMK DVSPYFKNST 

       190        200        210        220        230        240 
GGTSVGWDSP PASPLQRQPS SPGPTPRNFS EAKHMSLKMA YVSKRCTPND PEPRYLEICS 

       250        260        270        280        290        300 
ADGQDTLFLR AKDEASARSW ATAIQAQVNT LTPRVKDELQ ALLAATSTAG SQDIKQIGWL 

       310        320        330        340        350        360 
TEQLPSGGTA PTLALLTEKE LLLYLSLPET REALSRPART APLIATRLVH SGPSKGSVPY 

       370        380        390        400        410        420 
DAELSFALRT GTRHGVDTHL FSVESPQELA AWTRQLVDGC HRAAEGVQEV STACTWNGRP 

       430        440        450        460        470        480 
CSLSVHIDKG FTLWAAEPGA ARAVLLRQPF EKLQMSSDDG ASLLFLDFGG AEGEIQLDLH 

       490        500 
SCPKTIVFII HSFLSAKVTR LGLLA 

« Hide

References

« Hide 'large scale' references
[1]"The three human syntrophin genes are expressed in diverse tissues, have distinct chromosomal locations, and each bind to dystrophin and its relatives."
Ahn A.H., Feener C.A., Gussoni E., Yoshida M., Ozawa E., Kunkel L.M.
J. Biol. Chem. 271:2724-2730(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH DMD; DTNA AND UTRN.
Tissue: Muscle.
[2]"Characterization of the dystrophin-syntrophin interaction using the two-hybrid system in yeast."
Castello A., Brocheriou V., Chafey P., Kahn A., Gilgenkrantz H.
FEBS Lett. 383:124-128(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH DMD.
Tissue: Heart.
[3]"Stress-activated protein kinase-3 interacts with the PDZ domain of alpha1-syntrophin. A mechanism for specific substrate recognition."
Hasegawa M., Cuenda A., Spillantini M.G., Thomas G.M., Buee-Scherrer V., Cohen P., Goedert M.
J. Biol. Chem. 274:12626-12631(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH MAPK12.
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Small intestine.
[5]"The DNA sequence and comparative analysis of human chromosome 20."
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E. expand/collapse author list , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]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].
[7]"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.
[8]"A role for a PDZ protein in the early secretory pathway for the targeting of proTGF-alpha to the cell surface."
Fernandez-Larrea J., Merlos-Suarez A., Urena J.M., Baselga J., Arribas J.
Mol. Cell 3:423-433(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TGFA.
[9]"The C-terminus of human glutaminase L mediates association with PDZ domain-containing proteins."
Olalla L., Aledo J.C., Bannenberg G., Marquez J.
FEBS Lett. 488:116-122(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH GA.
[10]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-189 AND SER-193, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-189 AND SER-193, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-189, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"alpha-1-syntrophin mutation and the long-QT syndrome: a disease of sodium channel disruption."
Wu G., Ai T., Kim J.J., Mohapatra B., Xi Y., Li Z., Abbasi S., Purevjav E., Samani K., Ackerman M.J., Qi M., Moss A.J., Shimizu W., Towbin J.A., Cheng J., Vatta M.
Circ. Arrhythm. Electrophysiol. 1:193-201(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT LQT12 GLY-257, CHARACTERIZATION OF VARIANT LQT12 GLY-257.
[15]"Syntrophin mutation associated with long QT syndrome through activation of the nNOS-SCN5A macromolecular complex."
Ueda K., Valdivia C., Medeiros-Domingo A., Tester D.J., Vatta M., Farrugia G., Ackerman M.J., Makielski J.C.
Proc. Natl. Acad. Sci. U.S.A. 105:9355-9360(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT LQT12 VAL-390, CHARACTERIZATION OF VARIANT LQT12 VAL-390.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U40571 mRNA. Translation: AAC50448.1.
S81737 mRNA. Translation: AAB36398.1.
AL355392 Genomic DNA. Translation: CAC15884.1.
AK291994 mRNA. Translation: BAF84683.1.
CH471077 Genomic DNA. Translation: EAW76316.1.
CH471077 Genomic DNA. Translation: EAW76317.1.
BC026215 mRNA. Translation: AAH26215.1.
PIRS62894.
RefSeqNP_003089.1. NM_003098.2.
UniGeneHs.31121.

3D structure databases

ProteinModelPortalQ13424.
SMRQ13424. Positions 2-270.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112523. 78 interactions.
DIPDIP-966N.
IntActQ13424. 5 interactions.
MINTMINT-90249.
STRING9606.ENSP00000217381.

PTM databases

PhosphoSiteQ13424.

Polymorphism databases

DMDM23822157.

Proteomic databases

PaxDbQ13424.
PRIDEQ13424.

Protocols and materials databases

DNASU6640.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000217381; ENSP00000217381; ENSG00000101400.
GeneID6640.
KEGGhsa:6640.
UCSCuc002wzd.1. human.

Organism-specific databases

CTD6640.
GeneCardsGC20M031995.
HGNCHGNC:11167. SNTA1.
HPACAB037059.
MIM601017. gene.
612955. phenotype.
neXtProtNX_Q13424.
Orphanet101016. Romano-Ward syndrome.
PharmGKBPA36007.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG318350.
HOGENOMHOG000231596.
HOVERGENHBG054204.
InParanoidQ13424.
OMAKMAYVSK.
OrthoDBEOG7R56VZ.
PhylomeDBQ13424.
TreeFamTF317932.

Gene expression databases

ArrayExpressQ13424.
BgeeQ13424.
CleanExHS_SNTA1.
GenevestigatorQ13424.

Family and domain databases

Gene3D2.30.42.10. 1 hit.
InterProIPR001478. PDZ.
IPR001849. Pleckstrin_homology.
IPR028552. SNTA1.
IPR015482. Syntrophin.
[Graphical view]
PANTHERPTHR10554. PTHR10554. 1 hit.
PTHR10554:SF6. PTHR10554:SF6. 1 hit.
PfamPF00595. PDZ. 1 hit.
[Graphical view]
SMARTSM00228. PDZ. 1 hit.
SM00233. PH. 2 hits.
[Graphical view]
SUPFAMSSF50156. SSF50156. 1 hit.
PROSITEPS50106. PDZ. 1 hit.
PS50003. PH_DOMAIN. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSNTA1. human.
GeneWikiSyntrophin,_alpha_1.
GenomeRNAi6640.
NextBio25873.
PROQ13424.
SOURCESearch...

Entry information

Entry nameSNTA1_HUMAN
AccessionPrimary (citable) accession number: Q13424
Secondary accession number(s): A8K7H9, E1P5N1, Q16438
Entry history
Integrated into UniProtKB/Swiss-Prot: October 10, 2002
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 132 of the entry and version 1 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

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 20

Human chromosome 20: entries, gene names and cross-references to MIM