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

O00592 (PODXL_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 105. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Podocalyxin
Alternative name(s):
GCTM-2 antigen
Gp200
Podocalyxin-like protein 1
Short name=PC
Short name=PCLP-1
Gene names
Name:PODXL
Synonyms:PCLP, PCLP1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length558 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in the regulation of both adhesion and cell morphology and cancer progression. Function as an anti-adhesive molecule that maintains an open filtration pathway between neighboring foot processes in the podocyte by charge repulsion. Acts as a pro-adhesive molecule, enhancing the adherence of cells to immobilized ligands, increasing the rate of migration and cell-cell contacts in an integrin-dependent manner. Induces the formation of apical actin-dependent microvilli. Involved in the formation of a preapical plasma membrane subdomain to set up inital epithelial polarization and the apical lumen formation during renal tubulogenesis. Plays a role in cancer development and aggressiveness by inducing cell migration and invasion through its interaction with the actin-binding protein EZR. Affects EZR-dependent signaling events, leading to increased activities of the MAPK and PI3K pathways in cancer cells. Ref.9 Ref.10

Subunit structure

Monomer; when associated with the membrane raft. Oligomer; when integrated in the apical membrane. Interacts (via the C-terminal PDZ-binding motif DTHL) with SLC9A3R1 (via the PDZ domains); the interaction is not detected in glomerular epithelium cells, take place early in the secretory pathway and is necessary for its apical membrane sorting. Found in a complex with EZR, PODXL and SLC9A3R2. Associates with the actin cytoskeleton through complex formation with EZR and SLC9A3R2. Interacts (via the C-terminal PDZ-binding motif DTHL) with SLC9A3R2 (via the PDZ 1 domain); interaction is detected in glomerular epithelium cells By similarity. Interacts with EZR. Ref.9

Subcellular location

Apical cell membrane. Cell projectionlamellipodium. Cell projectionfilopodium. Cell projectionruffle. Cell projectionmicrovillus By similarity. Membrane raft By similarity. Membrane; Single-pass type I membrane protein Potential. Note: In single attached epithelial cells is restricted to a preapical pole on the free plasma membrane whereas other apical and basolateral proteins are not yet polarized. Colocalizes with SLC9A3R2 at the apical plasma membrane during epithelial polarization. Colocalizes with SLC9A3R1 at the trans-Golgi network (transiently) and at the apical plasma membrane. Its association with the membrane raft is transient. Colocalizes with actin filaments, EZR and SLC9A3R1 in a punctate pattern at the apical cell surface where microvilli form. Colocalizes with EZR and SLC9A3R2 at the apical cell membrane of glomerular epithelium cells By similarity. Forms granular, punctuated pattern, forming patches, preferentially adopting a polar distribution, located on the migrating poles of the cell or forming clusters along the terminal ends of filipodia establishing contact with the endothelial cells. Colocalizes with the submembrane actin of lamellipodia, particularly associated with ruffles. Colocalizes with vinculin at protrusions of cells. Colocalizes with ITGB1. Colocalizes with PARD3, PRKCI, EXOC5, OCLN, RAB11A and RAB8A in apical membrane initiation sites (AMIS) during the generation of apical surface and luminogenesis By similarity. Ref.9 Ref.10

Tissue specificity

Glomerular epithelium cell (podocyte).

Domain

Both the O-glycan-rich domain of the extracellular domain and the C-terminus PDZ-binding motif (DTHL) in the cytoplasmic tail harbor an apical sorting signal. The cytoplasmic domain is necessary for the apical membrane targeting and renal tubulogenesis. The cytoplasmic C-terminus PDZ-binding motif (DTHL) is essential for interaction with SLC9A3R1 and for targeting SLC9A3R1 to the apical cell membrane. The extracellular domain is necessary for microvillus formation By similarity. The large highly anionic extracellular domain allows to maintain open filtration pathways between neighboring podocyte foot processes.

Post-translational modification

N- and O-linked glycosylated. Sialoglycoprotein By similarity.

Sequence similarities

Belongs to the podocalyxin family.

Ontologies

Keywords
   Biological processCell adhesion
   Cellular componentCell membrane
Cell projection
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainSignal
Transmembrane
Transmembrane helix
   PTMGlycoprotein
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcell adhesion

Inferred from electronic annotation. Source: UniProtKB-KW

cell migration

Inferred from sequence or structural similarity. Source: UniProtKB

epithelial tube formation

Inferred from sequence or structural similarity. Source: UniProtKB

glomerular visceral epithelial cell development

Inferred from sequence or structural similarity. Source: UniProtKB

leukocyte migration

Inferred from electronic annotation. Source: Ensembl

negative regulation of cell adhesion

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of cell-cell adhesion

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of cell migration

Inferred from direct assay Ref.10. Source: UniProtKB

positive regulation of cell-cell adhesion mediated by integrin

Inferred from direct assay Ref.10. Source: UniProtKB

regulation of microvillus assembly

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentapical plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

cell body

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from direct assay Ref.10. Source: UniProtKB

extracellular vesicular exosome

Inferred from direct assay PubMed 15326289PubMed 19056867PubMed 23376485. Source: UniProt

filopodium

Inferred from direct assay Ref.10. Source: UniProtKB

integral component of plasma membrane

Traceable author statement Ref.1. Source: ProtInc

lamellipodium

Inferred from direct assay Ref.10. Source: UniProtKB

membrane raft

Inferred from electronic annotation. Source: UniProtKB-SubCell

microvillus membrane

Inferred from sequence or structural similarity. Source: UniProtKB

plasma membrane

Inferred from direct assay Ref.10. Source: UniProtKB

ruffle

Inferred from direct assay Ref.10. Source: UniProtKB

slit diaphragm

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionprotein binding

Inferred from physical interaction PubMed 22662192. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

IQGAP1P469404EBI-6897823,EBI-297509

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O00592-1)

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: O00592-2)

The sequence of this isoform differs from the canonical sequence as follows:
     236-268: LETVFHHVSQAGLELLTSGDLPTLASQSAGITA → P

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Potential
Chain23 – 558536Podocalyxin
PRO_0000024754

Regions

Topological domain23 – 461439Extracellular Potential
Transmembrane462 – 48221Helical; Potential
Topological domain483 – 55876Cytoplasmic Potential
Compositional bias35 – 334300Thr-rich

Amino acid modifications

Modified residue5291Phosphoserine Ref.14
Modified residue5371Phosphoserine Ref.12
Modified residue5561Phosphothreonine Ref.14
Glycosylation331N-linked (GlcNAc...) Potential
Glycosylation431N-linked (GlcNAc...) Potential
Glycosylation1041N-linked (GlcNAc...) Potential
Glycosylation1441N-linked (GlcNAc...) Potential
Glycosylation3601N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence236 – 26833LETVF…AGITA → P in isoform 2.
VSP_037220
Natural variant601T → R.
VAR_012236
Natural variant1121G → S.
Corresponds to variant rs3735035 [ dbSNP | Ensembl ].
VAR_055237
Natural variant1261T → P.
Corresponds to variant rs55698400 [ dbSNP | Ensembl ].
VAR_062136
Natural variant1941S → L. Ref.1
Corresponds to variant rs12670788 [ dbSNP | Ensembl ].
VAR_012237
Natural variant2981P → A.
Corresponds to variant rs35893129 [ dbSNP | Ensembl ].
VAR_060090
Natural variant3581V → I. Ref.2
Corresponds to variant rs3212298 [ dbSNP | Ensembl ].
VAR_055238

Experimental info

Sequence conflict311S → SPS in AAB61574. Ref.1
Sequence conflict4041G → Q AA sequence Ref.8

Sequences

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

Last modified May 5, 2009. Version 2.
Checksum: 8B1CF30D14D51691

FASTA55858,635
        10         20         30         40         50         60 
MRCALALSAL LLLLSTPPLL PSSPSPSPSP SQNATQTTTD SSNKTAPTPA SSVTIMATDT 

        70         80         90        100        110        120 
AQQSTVPTSK ANEILASVKA TTLGVSSDSP GTTTLAQQVS GPVNTTVARG GGSGNPTTTI 

       130        140        150        160        170        180 
ESPKSTKSAD TTTVATSTAT AKPNTTSSQN GAEDTTNSGG KSSHSVTTDL TSTKAEHLTT 

       190        200        210        220        230        240 
PHPTSPLSPR QPTSTHPVAT PTSSGHDHLM KISSSSSTVA IPGYTFTSPG MTTTLLETVF 

       250        260        270        280        290        300 
HHVSQAGLEL LTSGDLPTLA SQSAGITASS VISQRTQQTS SQMPASSTAP SSQETVQPTS 

       310        320        330        340        350        360 
PATALRTPTL PETMSSSPTA ASTTHRYPKT PSPTVAHESN WAKCEDLETQ TQSEKQLVLN 

       370        380        390        400        410        420 
LTGNTLCAGG ASDEKLISLI CRAVKATFNP AQDKCGIRLA SVPGSQTVVV KEITIHTKLP 

       430        440        450        460        470        480 
AKDVYERLKD KWDELKEAGV SDMKLGDQGP PEEAEDRFSM PLIITIVCMA SFLLLVAALY 

       490        500        510        520        530        540 
GCCHQRLSQR KDQQRLTEEL QTVENGYHDN PTLEVMETSS EMQEKKVVSL NGELGDSWIV 

       550 
PLDNLTKDDL DEEEDTHL 

« Hide

Isoform 2 [UniParc].

Checksum: 3F14C259BDB3AC76
Show »

FASTA52655,386

References

« Hide 'large scale' references
[1]"Molecular cloning and characterization of human podocalyxin-like protein. Orthologous relationship to rabbit PCLP1 and rat podocalyxin."
Kershaw D.B., Beck S.G., Wharram B.L., Wiggins J.E., Goyal M., Thomas P.E., Wiggins R.C.
J. Biol. Chem. 272:15708-15714(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANT LEU-194.
[2]Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANT ILE-358.
Tissue: Heart.
[3]"The DNA sequence of human chromosome 7."
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L. expand/collapse author list , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"Human chromosome 7: DNA sequence and biology."
Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S. expand/collapse author list , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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 (JUL-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] (ISOFORM 2).
Tissue: Liver.
[7]Suzuki Y., Yamashita R., Shirota M., Sakakibara Y., Chiba J., Nakai K., Sugano S.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 120-310 (ISOFORM 1).
[8]"Human embryonal carcinoma tumor antigen, Gp200/GCTM-2, is podocalyxin."
Schopperle W.M., Kershaw D.B., DeWolf W.C.
Biochem. Biophys. Res. Commun. 300:285-290(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 399-411 AND 445-372.
[9]"Podocalyxin increases the aggressive phenotype of breast and prostate cancer cells in vitro through its interaction with ezrin."
Sizemore S., Cicek M., Sizemore N., Ng K.P., Casey G.
Cancer Res. 67:6183-6191(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH EZR, SUBCELLULAR LOCATION.
[10]"Expression of podocalyxin enhances the adherence, migration, and intercellular communication of cells."
Larrucea S., Butta N., Arias-Salgado E.G., Alonso-Martin S., Ayuso M.S., Parrilla R.
Exp. Cell Res. 314:2004-2015(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"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-537, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-529 AND THR-556, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U97519 mRNA. Translation: AAB61574.1.
AK223573 mRNA. Translation: BAD97293.1.
AC008264 Genomic DNA. No translation available.
CH236950 Genomic DNA. Translation: EAL24080.1.
CH471070 Genomic DNA. Translation: EAW83786.1.
BC093730 mRNA. Translation: AAH93730.1.
BC112035 mRNA. Translation: AAI12036.1.
BP234810 mRNA. No translation available.
CCDSCCDS34755.1. [O00592-1]
CCDS47714.1. [O00592-2]
RefSeqNP_001018121.1. NM_001018111.2. [O00592-1]
NP_005388.2. NM_005397.3. [O00592-2]
UniGeneHs.744213.

3D structure databases

ProteinModelPortalO00592.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111416. 4 interactions.
DIPDIP-58638N.
IntActO00592. 1 interaction.
MINTMINT-5000334.
STRING9606.ENSP00000367817.

PTM databases

PhosphoSiteO00592.

Proteomic databases

MaxQBO00592.
PaxDbO00592.
PRIDEO00592.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000322985; ENSP00000319782; ENSG00000128567. [O00592-2]
ENST00000378555; ENSP00000367817; ENSG00000128567. [O00592-1]
GeneID5420.
KEGGhsa:5420.
UCSCuc003vqw.4. human. [O00592-1]
uc003vqx.4. human. [O00592-2]

Organism-specific databases

CTD5420.
GeneCardsGC07M131185.
H-InvDBHIX0007089.
HGNCHGNC:9171. PODXL.
HPACAB016169.
CAB062558.
HPA002110.
HPA045507.
MIM602632. gene.
neXtProtNX_O00592.
PharmGKBPA33493.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG47672.
HOVERGENHBG053629.
KOK06817.
OrthoDBEOG7CVQ0P.
PhylomeDBO00592.
TreeFamTF333564.

Gene expression databases

ArrayExpressO00592.
BgeeO00592.
CleanExHS_PODXL.
GenevestigatorO00592.

Family and domain databases

InterProIPR013836. CD34/Podocalyxin.
IPR017403. Podocalyxin-like_p1.
[Graphical view]
PfamPF06365. CD34_antigen. 1 hit.
[Graphical view]
PIRSFPIRSF038143. Podocalyxin-like_p1. 1 hit.
ProtoNetSearch...

Other

ChiTaRSPODXL. human.
GeneWikiPODXL.
GenomeRNAi5420.
NextBio20969.
PROO00592.
SOURCESearch...

Entry information

Entry namePODXL_HUMAN
AccessionPrimary (citable) accession number: O00592
Secondary accession number(s): A6NHX8, Q52LZ7, Q53ER6
Entry history
Integrated into UniProtKB/Swiss-Prot: December 13, 2001
Last sequence update: May 5, 2009
Last modified: July 9, 2014
This is version 105 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 7

Human chromosome 7: entries, gene names and cross-references to MIM