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Q9GZU1 (MCLN1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 117. 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·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Mucolipin-1
Alternative name(s):
MG-2
Mucolipidin
Gene names
Name:MCOLN1
Synonyms:ML4
ORF Names:MSTP080
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length580 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Cation channel probably playing a role in the endocytic pathway and in the control of membrane trafficking of proteins and lipids. Could play a major role in Ca2+ transport regulating lysosomal exocytosis. Ref.1 Ref.8 Ref.10

Enzyme regulation

Channel function is transiently modulated by changes in Ca2+, and inhibited by a reduction of pH; pH changes modify the aggregation state of unitary channels.

Subunit structure

Forms multimeric complexes. Interacts with PDCD6. Ref.10 Ref.12

Subcellular location

Cell membrane; Multi-pass membrane protein. Late endosome membrane; Multi-pass membrane protein. Lysosome membrane; Multi-pass membrane protein Ref.1 Ref.8 Ref.9 Ref.11.

Tissue specificity

Widely expressed in adult and fetal tissues. Ref.1 Ref.2 Ref.3

Involvement in disease

Mucolipidosis type IV (MLIV) [MIM:252650]: Autosomal recessive lysosomal storage disorder characterized by severe psychomotor retardation and ophthalmologic abnormalities, including corneal opacity, retinal degeneration and strabismus. Storage bodies of lipids and water-soluble substances are seen by electron microscopy in almost every cell type of the patients. Most patients are unable to speak or walk independently and reach a maximal developmental level of 1-2 years. All patients have constitutive achlorhydia associated with a secondary elevation of serum gastrin levels. MLIV may be due to a defect in sorting and/or transport along the late endocytic pathway. MLIV is found at relatively high frequency among Ashkenazi Jews.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.2 Ref.9 Ref.10 Ref.14 Ref.15 Ref.16

Sequence similarities

Belongs to the transient receptor (TC 1.A.4) family. Polycystin subfamily. MCOLN1 sub-subfamily. [View classification]

Sequence caution

The sequence AAQ13604.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence CAC07813.1 differs from that shown. Reason: Probable cloning artifact.

The sequence EAW69031.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence EAW69034.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Biological processCalcium transport
Ion transport
Transport
   Cellular componentCell membrane
Endosome
Lysosome
Membrane
   Coding sequence diversityPolymorphism
   DiseaseDisease mutation
Mucolipidosis
   DomainTransmembrane
Transmembrane helix
   LigandCalcium
   Molecular functionIon channel
   PTMGlycoprotein
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcalcium ion transmembrane transport

Traceable author statement. Source: Reactome

cation transport

Non-traceable author statement Ref.2. Source: UniProtKB

cellular iron ion homeostasis

Traceable author statement. Source: Reactome

ion transmembrane transport

Traceable author statement. Source: Reactome

release of sequestered calcium ion into cytosol

Inferred from electronic annotation. Source: Ensembl

transferrin transport

Traceable author statement. Source: Reactome

transmembrane transport

Traceable author statement. Source: Reactome

   Cellular_componentcytoplasm

Inferred from direct assay. Source: HPA

endosome membrane

Traceable author statement. Source: Reactome

integral component of membrane

Non-traceable author statement Ref.2. Source: UniProtKB

integral component of plasma membrane

Non-traceable author statement Ref.1. Source: UniProtKB

late endosome membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

lysosomal membrane

Inferred from direct assay Ref.11. Source: UniProtKB

plasma membrane

Inferred from direct assay. Source: HPA

receptor complex

Inferred from direct assay PubMed 23382219. Source: MGI

   Molecular_functionNAADP-sensitive calcium-release channel activity

Inferred from electronic annotation. Source: Ensembl

cation channel activity

Non-traceable author statement Ref.2. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 580580Mucolipin-1
PRO_0000215362

Regions

Transmembrane66 – 8621Helical; Potential
Transmembrane297 – 31721Helical; Potential
Transmembrane350 – 37021Helical; Potential
Transmembrane388 – 40821Helical; Potential
Transmembrane428 – 44821Helical; Potential
Transmembrane497 – 51721Helical; Potential

Amino acid modifications

Modified residue101Phosphoserine By similarity
Glycosylation2301N-linked (GlcNAc...) Ref.13

Natural variations

Natural variant1061L → P in MLIV. Ref.15
VAR_019369
Natural variant2321T → P in MLIV; fails to localize to late endosomes. Ref.9 Ref.14
VAR_019370
Natural variant3311V → L in a breast cancer sample; somatic mutation. Ref.17
VAR_036453
Natural variant3621D → Y in MLIV; affects channel activity. Ref.2 Ref.10 Ref.15
VAR_019371
Natural variant4031R → C in MLIV. Ref.16
VAR_038380
Natural variant4081Missing in MLIV; mild psychomotor involvement; does not affect channel activity; affects channel inhibition by low pH; still localizes to late endosomes. Ref.2 Ref.9 Ref.10 Ref.14 Ref.15
VAR_019372
Natural variant4461V → L in MLIV; does not affect channel activity; affects channel inhibition by low pH. Ref.2 Ref.10
VAR_019373
Natural variant4471L → P in MLIV. Ref.15
VAR_019374
Natural variant4651F → L in MLIV; still localizes to late endosomes. Ref.9 Ref.14
VAR_019375

Experimental info

Mutagenesis44 – 463RLK → AAA: Abolishes interaction with PDCD6 and decreases formation of aberrant endosomes upon overexpression. Ref.12
Mutagenesis441R → A: Abolishes interaction with PDCD6. Ref.12
Mutagenesis451L → A: Abolishes interaction with PDCD6. Ref.12
Mutagenesis47 – 493YFF → AAA: Abolishes interaction with PDCD6. Ref.12
Sequence conflict164 – 19128ALCQR…MVVTD → LSASGTTTEATWTRPTTHLT LIRWWLLVN in AAG42242. Ref.3
Sequence conflict2031P → S in CAC08215. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9GZU1 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 7E7691F58D01C804

FASTA58065,022
        10         20         30         40         50         60 
MTAPAGPRGS ETERLLTPNP GYGTQAGPSP APPTPPEEED LRRRLKYFFM SPCDKFRAKG 

        70         80         90        100        110        120 
RKPCKLMLQV VKILVVTVQL ILFGLSNQLA VTFREENTIA FRHLFLLGYS DGADDTFAAY 

       130        140        150        160        170        180 
TREQLYQAIF HAVDQYLALP DVSLGRYAYV RGGGDPWTNG SGLALCQRYY HRGHVDPAND 

       190        200        210        220        230        240 
TFDIDPMVVT DCIQVDPPER PPPPPSDDLT LLESSSSYKN LTLKFHKLVN VTIHFRLKTI 

       250        260        270        280        290        300 
NLQSLINNEI PDCYTFSVLI TFDNKAHSGR IPISLETQAH IQECKHPSVF QHGDNSFRLL 

       310        320        330        340        350        360 
FDVVVILTCS LSFLLCARSL LRGFLLQNEF VGFMWRQRGR VISLWERLEF VNGWYILLVT 

       370        380        390        400        410        420 
SDVLTISGTI MKIGIEAKNL ASYDVCSILL GTSTLLVWVG VIRYLTFFHN YNILIATLRV 

       430        440        450        460        470        480 
ALPSVMRFCC CVAVIYLGYC FCGWIVLGPY HVKFRSLSMV SECLFSLING DDMFVTFAAM 

       490        500        510        520        530        540 
QAQQGRSSLV WLFSQLYLYS FISLFIYMVL SLFIALITGA YDTIKHPGGA GAEESELQAY 

       550        560        570        580 
IAQCQDSPTS GKFRRGSGSA CSLLCCCGRD PSEEHSLLVN 

« Hide

References

« Hide 'large scale' references
[1]"Cloning of the gene encoding a novel integral membrane protein, mucolipidin, and identification of the two major founder mutations causing mucolipidosis type IV."
Bassi M.T., Manzoni M., Monti E., Pizzo M.T., Ballabio A., Borsani G.
Am. J. Hum. Genet. 67:1110-1120(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROBABLE FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INVOLVEMENT IN MUCOLIPIDOSIS IV.
[2]"Mucolipidosis type IV is caused by mutations in a gene encoding a novel transient receptor potential channel."
Sun M., Goldin E., Stahl S., Falardeau J.L., Kennedy J.C., Acierno J.S. Jr., Bove C., Kaneski C.R., Nagle J., Bromley M.C., Colman M., Schiffmann R., Slaugenhaupt S.A.
Hum. Mol. Genet. 9:2471-2478(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], TISSUE SPECIFICITY, VARIANTS MLIV TYR-362; PHE-408 DEL AND LEU-446.
[3]"Identification of the gene causing mucolipidosis type IV."
Bargal R., Avidan N., Ben-Asher E., Olender Z., Zeigler M., Frumkin A., Raas-Rothschild A., Glusman G., Lancet D., Bach G.
Nat. Genet. 26:118-123(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INVOLVEMENT IN MUCOLIPIDOSIS IV.
[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].
[5]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].
[6]"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: Brain.
[7]Xu H.S., Sheng H., Qin B.M., Liu Y.Q., Zhao B., Liu B., Wang X.Y., Zhang Q., Song L., Gao Y., Zhang C.L., Ye J., Ji X.J., Liu B.H., Lu H., Chen J.Z., Cai M.Q., Zheng W.Y. expand/collapse author list , Teng C.Y., Liu Q., Yu L.T., Lin J., Gong Q., Zhang A.M., Gao R.L., Hui R.T.
Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 391-580.
Tissue: Aorta.
[8]"Identification and characterization of the single channel function of human mucolipin-1 implicated in mucolipidosis type IV, a disorder affecting the lysosomal pathway."
LaPlante J.M., Falardeau J., Sun M., Kanazirska M., Brown E.M., Slaugenhaupt S.A., Vassilev P.M.
FEBS Lett. 532:183-187(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTIONAL CHARACTERIZATION, REGULATION BY CALCIUM, SUBCELLULAR LOCATION.
[9]"Overexpression of wild-type and mutant mucolipin proteins in mammalian cells: effects on the late endocytic compartment organization."
Manzoni M., Monti E., Bresciani R., Bozzato A., Barlati S., Bassi M.T., Borsani G.
FEBS Lett. 567:219-224(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANTS MLIV PRO-232; PHE-408 DEL AND LEU-465.
[10]"Molecular pathophysiology of mucolipidosis type IV: pH dysregulation of the mucolipin-1 cation channel."
Raychowdhury M.K., Gonzalez-Perrett S., Montalbetti N., Timpanaro G.A., Chasan B., Goldmann W.H., Stahl S., Cooney A., Goldin E., Cantiello H.F.
Hum. Mol. Genet. 13:617-627(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTIONAL CHARACTERIZATION, SUBUNIT, CHARACTERIZATION OF VARIANTS MLIV TYR-362; PHE-408 DEL AND LEU-446.
[11]"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.
[12]"Identification of the penta-EF-hand protein ALG-2 as a Ca2+-dependent interactor of mucolipin-1."
Vergarajauregui S., Martina J.A., Puertollano R.
J. Biol. Chem. 284:36357-36366(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PDCD6, MUTAGENESIS OF ARG-44; LEU-45; 44-ARG--LYS-46 AND 47-TYR--PHE-49.
[13]"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-230.
Tissue: Liver.
[14]"Mucolipidosis type IV: novel MCOLN1 mutations in Jewish and non-Jewish patients and the frequency of the disease in the Ashkenazi Jewish population."
Bargal R., Avidan N., Olender Z., Ben-Asher E., Zeigler M., Raas-Rothschild A., Frumkin A., Ben-Yoseph O., Friedlender Y., Lancet D., Bach G.
Hum. Mutat. 17:397-402(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS MLIV PRO-232; PHE-408 DEL AND LEU-465.
[15]"The neurogenetics of mucolipidosis type IV."
Altarescu G., Sun M., Moore D.F., Smith J.A., Wiggs E.A., Solomon B.I., Patronas N.J., Frei K.P., Gupta S., Kaneski C.R., Quarrell O.W., Slaugenhaupt S.A., Goldin E., Schiffmann R.
Neurology 59:306-313(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS MLIV PRO-106; TYR-362; PHE-408 DEL AND PRO-447.
[16]"Transfer of a mitochondrial DNA fragment to MCOLN1 causes an inherited case of mucolipidosis IV."
Goldin E., Stahl S., Cooney A.M., Kaneski C.R., Gupta S., Brady R.O., Ellis J.R., Schiffmann R.
Hum. Mutat. 24:460-465(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT MLIV CYS-403.
[17]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] LEU-331.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ293659 mRNA. Translation: CAC07813.1. Sequence problems.
AJ293970 mRNA. Translation: CAC08215.1.
AF287269 mRNA. Translation: AAG00797.1.
AF287270 Genomic DNA. Translation: AAG00798.1.
AF249319 mRNA. Translation: AAG10422.1.
AF305579 expand/collapse EMBL AC list , AF305572, AF305573, AF305574, AF305575, AF305576, AF305577, AF305578 Genomic DNA. Translation: AAG42242.1.
AK026102 mRNA. Translation: BAB15360.1.
CH471139 Genomic DNA. Translation: EAW69031.1. Sequence problems.
CH471139 Genomic DNA. Translation: EAW69034.1. Sequence problems.
BC005149 mRNA. Translation: AAH05149.1.
AF171088 mRNA. Translation: AAQ13604.1. Different initiation.
RefSeqNP_065394.1. NM_020533.2.
UniGeneHs.631858.

3D structure databases

ProteinModelPortalQ9GZU1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid121441. 2 interactions.
IntActQ9GZU1. 2 interactions.
MINTMINT-1409368.
STRING9606.ENSP00000264079.

Chemistry

GuidetoPHARMACOLOGY501.

Protein family/group databases

TCDB1.A.5.3.1. the polycystin cation channel (pcc) family.

PTM databases

PhosphoSiteQ9GZU1.

Polymorphism databases

DMDM50401163.

Proteomic databases

PaxDbQ9GZU1.
PRIDEQ9GZU1.

Protocols and materials databases

DNASU57192.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000264079; ENSP00000264079; ENSG00000090674.
GeneID57192.
KEGGhsa:57192.
UCSCuc002mgo.3. human.

Organism-specific databases

CTD57192.
GeneCardsGC19P007587.
H-InvDBHIX0023287.
HGNCHGNC:13356. MCOLN1.
HPAHPA031763.
MIM252650. phenotype.
605248. gene.
neXtProtNX_Q9GZU1.
Orphanet578. Mucolipidosis type 4.
PharmGKBPA30699.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG149591.
HOGENOMHOG000232158.
HOVERGENHBG052430.
InParanoidQ9GZU1.
KOK04992.
OMAAIFHAVD.
OrthoDBEOG7V1FQ9.
PhylomeDBQ9GZU1.
TreeFamTF317783.

Enzyme and pathway databases

ReactomeREACT_15518. Transmembrane transport of small molecules.

Gene expression databases

ArrayExpressQ9GZU1.
BgeeQ9GZU1.
CleanExHS_MCOLN1.
GenevestigatorQ9GZU1.

Family and domain databases

InterProIPR013122. PKD1_2_channel.
[Graphical view]
PfamPF08016. PKD_channel. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiMCOLN1.
GenomeRNAi57192.
NextBio63278.
PROQ9GZU1.
SOURCESearch...

Entry information

Entry nameMCLN1_HUMAN
AccessionPrimary (citable) accession number: Q9GZU1
Secondary accession number(s): D6W647 expand/collapse secondary AC list , Q7Z4F7, Q9H292, Q9H4B3, Q9H4B5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: March 1, 2001
Last modified: April 16, 2014
This is version 117 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 19

Human chromosome 19: entries, gene names and cross-references to MIM