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

P25092 (GUC2C_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 150. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Heat-stable enterotoxin receptor

Short name=STA receptor
Short name=hSTAR
EC=4.6.1.2
Alternative name(s):
Guanylyl cyclase C
Short name=GC-C
Intestinal guanylate cyclase
Gene names
Name:GUCY2C
Synonyms:GUC2C, STAR
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1073 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Receptor for the E.coli heat-stable enterotoxin (E.coli enterotoxin markedly stimulates the accumulation of cGMP in mammalian cells expressing GC-C). Also activated by the endogenous peptides guanylin and uroguanylin.

Catalytic activity

GTP = 3',5'-cyclic GMP + diphosphate.

Subunit structure

Homotrimer. Interacts via its C-terminal region with PDZK2. Interacts with the lectin chaperone VIP36. Ref.8 Ref.9 Ref.10

Subcellular location

Cell membrane; Single-pass type I membrane protein. Endoplasmic reticulum membrane; Single-pass type I membrane protein. Note: The 145 kDa plasma membrane form of GC-C contains sialic acid and galactose residues, while a differencially glycosylated 130 Kda form is a high mannose form that is resident in the endoplasmic reticulum and may serve as the precursor for the cell surface form. Ref.10

Domain

The protein kinase domain is predicted to be catalytically inactive.

Post-translational modification

Glycosylation at Asn-75 and/or Asn-79 is required for interaction with VIP36 while glycosylation at Asn-345 and Asn-402 modulates ligand-mediated GC-C activation.

Involvement in disease

Diarrhea 6 (DIAR6) [MIM:614616]: A relatively mild, early-onset chronic diarrhea that may be associated with increased susceptibility to inflammatory bowel disease, small bowel obstruction, and esophagitis.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.12

Meconium ileus (MECIL) [MIM:614665]: A condition characterized by a intestinal obstruction due to inspissated meconium in the distal ileum and cecum, which develops in utero and presents shortly after birth as a failure to pass meconium. Meconium ileus is a known clinical manifestation of cystic fibrosis.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.11

Sequence similarities

Belongs to the adenylyl cyclase class-4/guanylyl cyclase family.

Contains 1 guanylate cyclase domain.

Contains 1 protein kinase domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PDZD3Q86UT5-24EBI-2816795,EBI-8299496

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Potential
Chain24 – 10731050Heat-stable enterotoxin receptor
PRO_0000012376

Regions

Topological domain24 – 430407Extracellular Potential
Transmembrane431 – 45424Helical; Potential
Topological domain455 – 1073619Cytoplasmic Potential
Domain489 – 749261Protein kinase
Domain824 – 954131Guanylate cyclase

Sites

Site3571Not glycosylated

Amino acid modifications

Glycosylation321N-linked (GlcNAc...) Ref.10
Glycosylation751N-linked (GlcNAc...) Ref.10
Glycosylation791N-linked (GlcNAc...) Ref.10
Glycosylation1951N-linked (GlcNAc...) Ref.10
Glycosylation2841N-linked (GlcNAc...) Ref.10
Glycosylation3071N-linked (GlcNAc...) Ref.10
Glycosylation3451N-linked (GlcNAc...) Ref.10
Glycosylation4021N-linked (GlcNAc...) Ref.10

Natural variations

Natural variant301C → R. Ref.13
Corresponds to variant rs56142849 [ dbSNP | Ensembl ].
VAR_042221
Natural variant611G → R in a metastatic melanoma sample; somatic mutation. Ref.13
VAR_042222
Natural variant1141R → Q. Ref.13
Corresponds to variant rs56275235 [ dbSNP | Ensembl ].
VAR_042223
Natural variant2811F → L. Ref.1 Ref.2 Ref.4 Ref.5 Ref.7
Corresponds to variant rs1420635 [ dbSNP | Ensembl ].
VAR_049253
Natural variant3871D → G in MECIL; activation of guanylate cyclase activity is 60% lower than in wild-type. Ref.11
VAR_068174
Natural variant4641R → L. Ref.13
Corresponds to variant rs55684775 [ dbSNP | Ensembl ].
VAR_042224
Natural variant6101E → K. Ref.13
Corresponds to variant rs55897626 [ dbSNP | Ensembl ].
VAR_042225
Natural variant8401S → I in DIAR6; activating mutation; exposure of the mutant receptor to its ligands results in markedly increased production of cyclic guanosine monophosphate. Ref.12
VAR_067724
Natural variant8591I → V. Ref.13
Corresponds to variant rs34890806 [ dbSNP | Ensembl ].
VAR_042226
Natural variant10451Q → R. Ref.13
Corresponds to variant rs35617837 [ dbSNP | Ensembl ].
VAR_042227
Natural variant10721Y → C. Ref.13
Corresponds to variant rs35179392 [ dbSNP | Ensembl ].
VAR_042228

Experimental info

Sequence conflict3221A → R in AAB19934. Ref.1
Sequence conflict3311L → V in AAB19934. Ref.1
Sequence conflict5091D → V in AAB19934. Ref.1
Sequence conflict5431N → T in AAB19934. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P25092 [UniParc].

Last modified November 2, 2010. Version 2.
Checksum: 486A4DE6F9097E22

FASTA1,073123,403
        10         20         30         40         50         60 
MKTLLLDLAL WSLLFQPGWL SFSSQVSQNC HNGSYEISVL MMGNSAFAEP LKNLEDAVNE 

        70         80         90        100        110        120 
GLEIVRGRLQ NAGLNVTVNA TFMYSDGLIH NSGDCRSSTC EGLDLLRKIS NAQRMGCVLI 

       130        140        150        160        170        180 
GPSCTYSTFQ MYLDTELSYP MISAGSFGLS CDYKETLTRL MSPARKLMYF LVNFWKTNDL 

       190        200        210        220        230        240 
PFKTYSWSTS YVYKNGTETE DCFWYLNALE ASVSYFSHEL GFKVVLRQDK EFQDILMDHN 

       250        260        270        280        290        300 
RKSNVIIMCG GPEFLYKLKG DRAVAEDIVI ILVDLFNDQY FEDNVTAPDY MKNVLVLTLS 

       310        320        330        340        350        360 
PGNSLLNSSF SRNLSPTKRD FALAYLNGIL LFGHMLKIFL ENGENITTPK FAHAFRNLTF 

       370        380        390        400        410        420 
EGYDGPVTLD DWGDVDSTMV LLYTSVDTKK YKVLLTYDTH VNKTYPVDMS PTFTWKNSKL 

       430        440        450        460        470        480 
PNDITGRGPQ ILMIAVFTLT GAVVLLLLVA LLMLRKYRKD YELRQKKWSH IPPENIFPLE 

       490        500        510        520        530        540 
TNETNHVSLK IDDDKRRDTI QRLRQCKYDK KRVILKDLKH NDGNFTEKQK IELNKLLQID 

       550        560        570        580        590        600 
YYNLTKFYGT VKLDTMIFGV IEYCERGSLR EVLNDTISYP DGTFMDWEFK ISVLYDIAKG 

       610        620        630        640        650        660 
MSYLHSSKTE VHGRLKSTNC VVDSRMVVKI TDFGCNSILP PKKDLWTAPE HLRQANISQK 

       670        680        690        700        710        720 
GDVYSYGIIA QEIILRKETF YTLSCRDRNE KIFRVENSNG MKPFRPDLFL ETAEEKELEV 

       730        740        750        760        770        780 
YLLVKNCWEE DPEKRPDFKK IETTLAKIFG LFHDQKNESY MDTLIRRLQL YSRNLEHLVE 

       790        800        810        820        830        840 
ERTQLYKAER DRADRLNFML LPRLVVKSLK EKGFVEPELY EEVTIYFSDI VGFTTICKYS 

       850        860        870        880        890        900 
TPMEVVDMLN DIYKSFDHIV DHHDVYKVET IGDAYMVASG LPKRNGNRHA IDIAKMALEI 

       910        920        930        940        950        960 
LSFMGTFELE HLPGLPIWIR IGVHSGPCAA GVVGIKMPRY CLFGDTVNTA SRMESTGLPL 

       970        980        990       1000       1010       1020 
RIHVSGSTIA ILKRTECQFL YEVRGETYLK GRGNETTYWL TGMKDQKFNL PTPPTVENQQ 

      1030       1040       1050       1060       1070 
RLQAEFSDMI ANSLQKRQAA GIRSQKPRRV ASYKKGTLEY LQLNTTDKES TYF 

« Hide

References

« Hide 'large scale' references
[1]"Isolation and expression of a guanylate cyclase-coupled heat stable enterotoxin receptor cDNA from a human colonic cell line."
Singh S., Singh G., Heim J.-M., Gerzer R.
Biochem. Biophys. Res. Commun. 179:1455-1463(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT LEU-281.
[2]"Primary structure and functional expression of the human receptor for Escherichia coli heat-stable enterotoxin."
de Sauvage F.J., Camerato T.R., Goeddel D.V.
J. Biol. Chem. 266:17912-17918(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT LEU-281.
[3]"The finished DNA sequence of human chromosome 12."
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R. expand/collapse author list , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]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], VARIANT LEU-281.
[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], VARIANT LEU-281.
[6]"Cell line-specific transcriptional activation of the promoter of the human guanylyl cyclase C/heat-stable enterotoxin receptor gene."
Mann E.A., Jump M.L., Giannella R.A.
Biochim. Biophys. Acta 1305:7-10(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-72.
Tissue: Placenta.
[7]"Comparison of receptors for Escherichia coli heat-stable enterotoxin: novel receptor present in IEC-6 cells."
Mann E.A., Cohen M.B., Giannella R.A.
Am. J. Physiol. 264:G172-G178(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 24-1073, VARIANT LEU-281.
Tissue: Colon carcinoma.
[8]"Biochemical characterization of the intracellular domain of the human guanylyl cyclase C receptor provides evidence for a catalytically active homotrimer."
Vijayachandra K., Guruprasad M., Bhandari R., Manjunath U.H., Somesh B.P., Srinivasan N., Suguna K., Visweswariah S.S.
Biochemistry 39:16075-16083(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT.
[9]"A novel PDZ protein regulates the activity of guanylyl cyclase C, the heat-stable enterotoxin receptor."
Scott R.O., Thelin W.R., Milgram S.L.
J. Biol. Chem. 277:22934-22941(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PDZK2.
[10]"Site-specific N-linked glycosylation of receptor guanylyl cyclase C regulates ligand binding, ligand-mediated activation and interaction with vesicular integral membrane protein 36, VIP36."
Arshad N., Ballal S., Visweswariah S.S.
J. Biol. Chem. 288:3907-3917(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT ASN-32; ASN-75; ASN-79; ASN-195; ASN-284; ASN-307; ASN-345 AND ASN-402, ABSENCE OF GLYCOSYLATION AT ASN-357, INTERACTION WITH VIP36, SUBCELLULAR LOCATION.
[11]"Meconium ileus caused by mutations in GUCY2C, encoding the CFTR-activating guanylate cyclase 2C."
Romi H., Cohen I., Landau D., Alkrinawi S., Yerushalmi B., Hershkovitz R., Newman-Heiman N., Cutting G.R., Ofir R., Sivan S., Birk O.S.
Am. J. Hum. Genet. 90:893-899(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT MECIL GLY-387, CHARACTERIZATION OF VARIANT MECIL GLY-387.
[12]"Familial diarrhea syndrome caused by an activating GUCY2C mutation."
Fiskerstrand T., Arshad N., Haukanes B.I., Tronstad R.R., Pham K.D., Johansson S., Havik B., Tonder S.L., Levy S.E., Brackman D., Boman H., Biswas K.H., Apold J., Hovdenak N., Visweswariah S.S., Knappskog P.M.
N. Engl. J. Med. 366:1586-1595(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT DIAR6 ILE-840, CHARACTERIZATION OF VARIANT DIAR6 ILE-840.
[13]"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] ARG-30; ARG-61; GLN-114; LEU-464; LYS-610; VAL-859; ARG-1045 AND CYS-1072.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
S57551 mRNA. Translation: AAB19934.2.
M73489 mRNA. Translation: AAA36655.1.
AC007545 Genomic DNA. No translation available.
AC010168 Genomic DNA. No translation available.
CH471094 Genomic DNA. Translation: EAW96324.1.
BC136544 mRNA. Translation: AAI36545.1.
BC136545 mRNA. Translation: AAI36546.1.
U20230 Genomic DNA. Translation: AAC50381.1.
PIROYHUHX. A40940.
RefSeqNP_004954.2. NM_004963.3.
UniGeneHs.524278.

3D structure databases

ProteinModelPortalP25092.
SMRP25092. Positions 488-765, 815-1001.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109239. 1 interaction.
IntActP25092. 3 interactions.
MINTMINT-261763.
STRING9606.ENSP00000261170.

Chemistry

ChEMBLCHEMBL1795197.
GuidetoPHARMACOLOGY1750.

PTM databases

PhosphoSiteP25092.

Polymorphism databases

DMDM311033390.

Proteomic databases

PaxDbP25092.
PRIDEP25092.

Protocols and materials databases

DNASU2984.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000261170; ENSP00000261170; ENSG00000070019.
GeneID2984.
KEGGhsa:2984.
UCSCuc001rcd.3. human.

Organism-specific databases

CTD2984.
GeneCardsGC12M014765.
H-InvDBHIX0036867.
HGNCHGNC:4688. GUCY2C.
HPAHPA037655.
MIM601330. gene.
614616. phenotype.
614665. phenotype.
neXtProtNX_P25092.
Orphanet314373. Chronic diarrhea due to guanylate cyclase 2C overactivity.
314376. Intestinal obstruction in the newborn due to guanylate cyclase 2C deficiency.
PharmGKBPA29069.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000112833.
HOVERGENHBG106967.
InParanoidP25092.
KOK12320.
OMAAPDYMKN.
OrthoDBEOG72VH58.
PhylomeDBP25092.

Gene expression databases

BgeeP25092.
CleanExHS_GUCY2C.
HS_STAR.
GenevestigatorP25092.

Family and domain databases

Gene3D3.30.70.1230. 1 hit.
InterProIPR001054. A/G_cyclase.
IPR018297. A/G_cyclase_CS.
IPR001828. ANF_lig-bd_rcpt.
IPR011009. Kinase-like_dom.
IPR028082. Peripla_BP_I.
IPR000719. Prot_kinase_dom.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
[Graphical view]
PfamPF01094. ANF_receptor. 1 hit.
PF00211. Guanylate_cyc. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
SMARTSM00044. CYCc. 1 hit.
[Graphical view]
SUPFAMSSF53822. SSF53822. 1 hit.
SSF55073. SSF55073. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEPS00452. GUANYLATE_CYCLASE_1. 1 hit.
PS50125. GUANYLATE_CYCLASE_2. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiGuanylate_cyclase_2C.
GenomeRNAi2984.
NextBio11836.
PROP25092.
SOURCESearch...

Entry information

Entry nameGUC2C_HUMAN
AccessionPrimary (citable) accession number: P25092
Secondary accession number(s): B2RMY6
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: November 2, 2010
Last modified: March 19, 2014
This is version 150 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

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 12

Human chromosome 12: entries, gene names and cross-references to MIM