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Q9NRA2 (S17A5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 106. 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·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Sialin
Alternative name(s):
H(+)/nitrate cotransporter
H(+)/sialic acid cotransporter
Short name=AST
Membrane glycoprotein HP59
Solute carrier family 17 member 5
Vesicular H(+)/Aspartate-glutamate cotransporter
Gene names
Name:SLC17A5
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length495 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Transports glucuronic acid and free sialic acid out of the lysosome after it is cleaved from sialoglycoconjugates undergoing degradation, this is required for normal CNS myelination. Mediates aspartate and glutamate membrane potential-dependent uptake into synaptic vesicles and synaptic-like microvesicles. Also functions as an electrogenic 2NO3-/H+ cotransporter in the plasma membrane of salivary gland acinar cells, mediating the physiological nitrate efflux, 25% of the circulating nitrate ions is typically removed and secreted in saliva. Ref.1 Ref.2 Ref.6 Ref.9 Ref.10

Subcellular location

Cell membrane; Multi-pass membrane protein. Cytoplasmic vesiclesecretory vesiclesynaptic vesicle membrane. Lysosome membrane; Multi-pass membrane protein Ref.7 Ref.9 Ref.10.

Tissue specificity

Found in fetal lung and small intestine, and at lower level in fetal skin and muscle. In the adult, detected in placenta, kidney and pancreas. Abundant in the endothelial cells of tumors from ovary, colon, breast and lung, but is not detected in endothelial cells from the corresponding normal tissues. Ref.1 Ref.2

Involvement in disease

Salla disease (SD) [MIM:604369]: Sialic acid storage disease (SASD). SASDs are autosomal recessive neurodegenerative disorders characterized by hypotonia, cerebellar ataxia and mental retardation. They are caused by a defect in the metabolism of sialic acid which results in increased urinary excretion of unconjugated sialic acid, specifically N-acetylneuraminic acid. Enlarged lysosomes are seen on electron microscopic studies. Clinical symptoms of SD present usually at age less than 1 year and progression is slow.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.2 Ref.9 Ref.11 Ref.12

Infantile sialic acid storage disorder (ISSD) [MIM:269920]: Severe form of sialic acid storage disease. Affected newborns exhibit visceromegaly, coarse features and failure to thrive immediately after birth. These patients have a shortened life span, usually less than 2 years.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.2 Ref.11

Infantile sialic acid storage disorder is associated with non-immune hydrops fetalis, a generalized edema of the fetus with fluid accumulation in the body cavities due to non-immune causes. Non-immune hydrops fetalis is not a diagnosis in itself but a symptom, a feature of many genetic disorders, and the end-stage of a wide variety of disorders.

Sequence similarities

Belongs to the major facilitator superfamily. Sodium/anion cotransporter family.

Sequence caution

The sequence AAF97769.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processAmino-acid transport
Symport
Transport
   Cellular componentCell junction
Cell membrane
Cytoplasmic vesicle
Lysosome
Membrane
Synapse
   Coding sequence diversityAlternative splicing
   DiseaseDisease mutation
   DomainTransmembrane
Transmembrane helix
   PTMGlycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processamino acid transport

Inferred from electronic annotation. Source: UniProtKB-KW

anion transport

Traceable author statement Ref.2. Source: ProtInc

ion transport

Traceable author statement. Source: Reactome

proton transport

Traceable author statement Ref.2. Source: GOC

sialic acid transport

Inferred from direct assay Ref.2. Source: MGI

transmembrane transport

Traceable author statement. Source: Reactome

   Cellular_componentcell junction

Inferred from electronic annotation. Source: UniProtKB-KW

cytoplasm

Inferred from direct assay. Source: HPA

integral component of plasma membrane

Traceable author statement Ref.2. Source: ProtInc

lysosomal membrane

Inferred from direct assay Ref.7. Source: UniProtKB

membrane

Traceable author statement Ref.2. Source: ProtInc

plasma membrane

Inferred from direct assay. Source: HPA

synaptic vesicle membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionsialic acid transmembrane transporter activity

Inferred from direct assay Ref.2. Source: MGI

sugar:hydrogen symporter activity

Traceable author statement Ref.2. Source: ProtInc

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9NRA2-1)

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 2 (identifier: Q9NRA2-2)

The sequence of this isoform differs from the canonical sequence as follows:
     274-276: LSS → AGV
     278-495: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 495495Sialin
PRO_0000220947

Regions

Topological domain1 – 4141Cytoplasmic Potential
Transmembrane42 – 6221Helical; Potential
Topological domain63 – 10947Lumenal Potential
Transmembrane110 – 13021Helical; Potential
Topological domain131 – 1366Cytoplasmic Potential
Transmembrane137 – 15721Helical; Potential
Topological domain1581Lumenal Potential
Transmembrane159 – 17921Helical; Potential
Topological domain180 – 20021Cytoplasmic Potential
Transmembrane201 – 22121Helical; Potential
Topological domain222 – 2276Lumenal Potential
Transmembrane228 – 24821Helical; Potential
Topological domain249 – 27931Cytoplasmic Potential
Transmembrane280 – 30021Helical; Potential
Topological domain301 – 32828Lumenal Potential
Transmembrane329 – 34921Helical; Potential
Topological domain350 – 36516Cytoplasmic Potential
Transmembrane366 – 38621Helical; Potential
Topological domain387 – 3915Lumenal Potential
Transmembrane392 – 41221Helical; Potential
Topological domain413 – 42311Cytoplasmic Potential
Transmembrane424 – 44421Helical; Potential
Topological domain445 – 45713Lumenal Potential
Transmembrane458 – 47821Helical; Potential
Topological domain479 – 49517Cytoplasmic Potential
Motif22 – 232Dileucine internalization motif

Amino acid modifications

Glycosylation711N-linked (GlcNAc...) Potential
Glycosylation771N-linked (GlcNAc...) Potential
Glycosylation951N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence274 – 2763LSS → AGV in isoform 2.
VSP_010482
Alternative sequence278 – 495218Missing in isoform 2.
VSP_010483
Natural variant391R → C in SD; completely devoid of aspartate and glutamate transport activity, but retains appreciable H(+)/sialic acid cotransport activity, frequent mutation in Finland. Ref.2 Ref.9 Ref.11 Ref.12
VAR_018684
Natural variant1361K → E in SD. Ref.11
VAR_018685
Natural variant1831H → R in ISSD. Ref.2 Ref.11
VAR_018686
Natural variant268 – 2725Missing in ISSD.
VAR_018687
Natural variant2961V → I.
Corresponds to variant rs16883930 [ dbSNP | Ensembl ].
VAR_034746
Natural variant3341P → R in ISSD. Ref.2 Ref.11
VAR_018688
Natural variant3711G → V in ISSD. Ref.11
VAR_018689

Experimental info

Mutagenesis22 – 232LL → GG: Targeted to plasma membrane; sialic acid uptake strongly activated at acidic pH. Ref.6
Mutagenesis1791F → C: 15 fold increase in affinity for glucuronic acid. Ref.8

Sequences

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

Last modified June 7, 2004. Version 2.
Checksum: 5C6C154B3E93A19E

FASTA49554,640
        10         20         30         40         50         60 
MRSPVRDLAR NDGEESTDRT PLLPGAPRAE AAPVCCSARY NLAILAFFGF FIVYALRVNL 

        70         80         90        100        110        120 
SVALVDMVDS NTTLEDNRTS KACPEHSAPI KVHHNQTGKK YQWDAETQGW ILGSFFYGYI 

       130        140        150        160        170        180 
ITQIPGGYVA SKIGGKMLLG FGILGTAVLT LFTPIAADLG VGPLIVLRAL EGLGEGVTFP 

       190        200        210        220        230        240 
AMHAMWSSWA PPLERSKLLS ISYAGAQLGT VISLPLSGII CYYMNWTYVF YFFGTIGIFW 

       250        260        270        280        290        300 
FLLWIWLVSD TPQKHKRISH YEKEYILSSL RNQLSSQKSV PWVPILKSLP LWAIVVAHFS 

       310        320        330        340        350        360 
YNWTFYTLLT LLPTYMKEIL RFNVQENGFL SSLPYLGSWL CMILSGQAAD NLRAKWNFST 

       370        380        390        400        410        420 
LCVRRIFSLI GMIGPAVFLV AAGFIGCDYS LAVAFLTIST TLGGFCSSGF SINHLDIAPS 

       430        440        450        460        470        480 
YAGILLGITN TFATIPGMVG PVIAKSLTPD NTVGEWQTVF YIAAAINVFG AIFFTLFAKG 

       490 
EVQNWALNDH HGHRH 

« Hide

Isoform 2 [UniParc].

Checksum: 1BF03EA560AB80DB
Show »

FASTA27730,667

References

« Hide 'large scale' references
[1]"Identification of a novel membrane protein, HP59, with therapeutic potential as a target of tumor angiogenesis."
Fu C., Bardhan S., Cetateanu N.D., Wamil B.D., Wang Y., Yan H.-P., Shi E., Carter C., Venkov C., Yakes F.M., Page D.L., Lloyd R.S., Mernaugh R.L., Hellerqvist C.G.
Clin. Cancer Res. 7:4182-4194(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY.
[2]"A new gene, encoding an anion transporter, is mutated in sialic acid storage diseases."
Verheijen F.W., Verbeek E., Aula N., Beerens C.E.M.T., Havelaar A.C., Joosse M., Peltonen L., Aula P., Galjaard H., Van der Spek P.J., Mancini G.M.S.
Nat. Genet. 23:462-465(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, VARIANT SD CYS-39, VARIANTS ISSD 268-SER--ASN-272 DEL; ARG-183 AND ARG-334.
[3]"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] (ISOFORM 2).
[4]"The DNA sequence and analysis of human chromosome 6."
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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 2).
Tissue: Colon.
[6]"Functional characterization of wild-type and mutant human sialin."
Morin P., Sagne C., Gasnier B.
EMBO J. 23:4560-4570(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DILEUCINE MOTIF, MUTAGENESIS OF 22-LEU--LEU-23.
[7]"Integral and associated lysosomal membrane proteins."
Schroeder B., Wrocklage C., Pan C., Jaeger R., Koesters B., Schaefer H., Elsaesser H.-P., Mann M., Hasilik A.
Traffic 8:1676-1686(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
Tissue: Placenta.
[8]"Structure-function studies of the SLC17 transporter sialin identify crucial residues and substrate-induced conformational changes."
Courville P., Quick M., Reimer R.J.
J. Biol. Chem. 285:19316-19323(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: TOPOLOGY, MUTAGENESIS OF PHE-179.
[9]"Functional characterization of vesicular excitatory amino acid transport by human sialin."
Miyaji T., Omote H., Moriyama Y.
J. Neurochem. 119:1-5(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, VARIANT SD CYS-39.
[10]"Sialin (SLC17A5) functions as a nitrate transporter in the plasma membrane."
Qin L., Liu X., Sun Q., Fan Z., Xia D., Ding G., Ong H.L., Adams D., Gahl W.A., Zheng C., Qi S., Jin L., Zhang C., Gu L., He J., Deng D., Ambudkar I.S., Wang S.
Proc. Natl. Acad. Sci. U.S.A. 109:13434-13439(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[11]"The spectrum of SLC17A5-gene mutations resulting in free sialic acid-storage diseases indicates some genotype-phenotype correlation."
Aula N., Salomaeki P., Timonen R., Verheijen F., Mancini G.M.S., Maensson J.-E., Aula P., Peltonen L.
Am. J. Hum. Genet. 67:832-840(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS SD CYS-39 AND GLU-136, VARIANTS ISSD 268-SER--ASN-272 DEL; ARG-183; ARG-334 AND VAL-371.
[12]"Sialic acid storage disease of the Salla phenotype in American monozygous twin female sibs."
Martin R.A., Slaugh R., Natowicz M., Pearlman K., Orvisky E., Krasnewich D., Kleta R., Huizing M., Gahl W.A.
Am. J. Med. Genet. A 120:23-27(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT SD CYS-39.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF244577 mRNA. Translation: AAF97769.1. Different initiation.
AJ387747 mRNA. Translation: CAB62540.1.
AK075320 mRNA. Translation: BAC11546.1.
AL590428, AL121972 Genomic DNA. Translation: CAI15635.1.
AL121972, AL590428 Genomic DNA. Translation: CAI20417.1.
BC020961 mRNA. Translation: AAH20961.1.
RefSeqNP_036566.1. NM_012434.4.
UniGeneHs.597422.

3D structure databases

ProteinModelPortalQ9NRA2.
SMRQ9NRA2. Positions 98-251, 286-356.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid117710. 2 interactions.
IntActQ9NRA2. 1 interaction.
STRING9606.ENSP00000348019.

Protein family/group databases

TCDB2.A.1.14.10. the major facilitator superfamily (mfs).

PTM databases

PhosphoSiteQ9NRA2.

Polymorphism databases

DMDM48428688.

Proteomic databases

PaxDbQ9NRA2.
PRIDEQ9NRA2.

Protocols and materials databases

DNASU26503.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000355773; ENSP00000348019; ENSG00000119899. [Q9NRA2-1]
GeneID26503.
KEGGhsa:26503.
UCSCuc003phn.4. human. [Q9NRA2-1]

Organism-specific databases

CTD26503.
GeneCardsGC06M074359.
HGNCHGNC:10933. SLC17A5.
HPAHPA044479.
MIM269920. phenotype.
604322. gene.
604369. phenotype.
neXtProtNX_Q9NRA2.
Orphanet309324. Free sialic acid storage disease, infantile form.
309331. Intermediate severe Salla disease.
309334. Salla disease.
PharmGKBPA35824.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0477.
HOGENOMHOG000230811.
HOVERGENHBG008834.
InParanoidQ9NRA2.
KOK12301.
OMAKHKRISH.
OrthoDBEOG789C9Z.
PhylomeDBQ9NRA2.
TreeFamTF313535.

Enzyme and pathway databases

ReactomeREACT_15518. Transmembrane transport of small molecules.
REACT_19419. Amino acid and oligopeptide SLC transporters.

Gene expression databases

ArrayExpressQ9NRA2.
BgeeQ9NRA2.
CleanExHS_SLC17A5.
GenevestigatorQ9NRA2.

Family and domain databases

InterProIPR011701. MFS.
IPR020846. MFS_dom.
IPR016196. MFS_dom_general_subst_transpt.
[Graphical view]
PfamPF07690. MFS_1. 1 hit.
[Graphical view]
SUPFAMSSF103473. SSF103473. 2 hits.
PROSITEPS50850. MFS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiHP59.
SLC17A5.
GenomeRNAi26503.
NextBio48778.
PROQ9NRA2.
SOURCESearch...

Entry information

Entry nameS17A5_HUMAN
AccessionPrimary (citable) accession number: Q9NRA2
Secondary accession number(s): Q5SZ76, Q8NBR5, Q9UGH0
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: June 7, 2004
Last modified: April 16, 2014
This is version 106 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

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 6

Human chromosome 6: entries, gene names and cross-references to MIM