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Q15382 (RHEB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 153. 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·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
GTP-binding protein Rheb
Alternative name(s):
Ras homolog enriched in brain
Gene names
Name:RHEB
Synonyms:RHEB2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length184 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Stimulates the phosphorylation of S6K1 and EIF4EBP1 through activation of mTORC1 signaling. Activates the protein kinase activity of mTORC1. Has low intrinsic GTPase activity. Ref.10 Ref.11 Ref.12 Ref.14 Ref.15 Ref.16

Enzyme regulation

Alternates between an inactive form bound to GDP and an active form bound to GTP. Inactivated by TSC1-TSC2 via the GTPase activating protein (GAP) domain of TSC2.

Subunit structure

Binds to mTORC1 in a guanyl nucleotide-independent manner. Interacts directly with MTOR, MLST8 and RPTOR. Interacts with TSC2. Ref.14 Ref.15

Subcellular location

Cell membrane; Lipid-anchor; Cytoplasmic side Potential.

Tissue specificity

Ubiquitous. Highest levels observed in skeletal and cardiac muscle.

Post-translational modification

Farnesylation is important for efficiently activating mTORC1-mediated signaling.

Phosphorylation by MAPKAPK5 impairs GTP-binding and inactivation By similarity.

Miscellaneous

The conserved catalytic Gln-64 found in other Ras-like GTPases seems not to be involved in GTP hydrolysis in RHEB.

Sequence similarities

Belongs to the small GTPase superfamily. Rheb family.

Ontologies

Keywords
   Cellular componentCell membrane
Membrane
   Coding sequence diversityPolymorphism
   LigandGTP-binding
Magnesium
Metal-binding
Nucleotide-binding
   PTMLipoprotein
Methylation
Phosphoprotein
Prenylation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell cycle arrest

Traceable author statement. Source: Reactome

insulin receptor signaling pathway

Traceable author statement. Source: Reactome

positive regulation of TOR signaling

Inferred from mutant phenotype Ref.16. Source: UniProtKB

small GTPase mediated signal transduction

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

dendrite

Inferred from electronic annotation. Source: Ensembl

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 20458337. Source: UniProt

membrane

Traceable author statement PubMed 8206940. Source: ProtInc

neuronal cell body

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

spliceosomal complex

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionGDP binding

Inferred from electronic annotation. Source: Ensembl

GTP binding

Inferred from sequence or structural similarity. Source: UniProtKB

GTPase activity

Traceable author statement PubMed 8206940. Source: ProtInc

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PDE6DO439245EBI-6860739,EBI-712685

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 181181GTP-binding protein Rheb
PRO_0000082708
Propeptide182 – 1843Removed in mature form
PRO_0000281365

Regions

Nucleotide binding16 – 216GTP
Nucleotide binding32 – 387GTP
Nucleotide binding119 – 1224GTP
Nucleotide binding149 – 1502GTP
Motif35 – 439Effector region

Sites

Metal binding201Magnesium
Metal binding381Magnesium

Amino acid modifications

Modified residue1301Phosphoserine; by MAPKAPK5 By similarity
Modified residue1811Cysteine methyl ester Probable
Lipidation1811S-farnesyl cysteine Ref.13

Natural variations

Natural variant1391E → K in a colorectal cancer sample; somatic mutation. Ref.19
VAR_036310

Experimental info

Mutagenesis151R → G: Partially resistant to inactivation by TSC1-TSC2. Ref.12
Mutagenesis201S → N: Deficient in guanine nucleotide binding. Unable to rescue S6K1 from inactivation by amino-acid withdrawal. Ref.12 Ref.14
Mutagenesis381T → M: Slightly impairs signaling through mTORC1, but still binds guanine nucleotides normally. Ref.14 Ref.15
Mutagenesis391I → K: Impairs S6K1 activation, but still binds guanine nucleotides normally. Ref.14
Mutagenesis401E → G: No effect. Ref.15
Mutagenesis411N → A: Impairs interaction with MTOR. Impairs signaling through mTORC1, but still binds guanine nucleotides normally. Ref.14 Ref.15
Mutagenesis431F → C: No effect. Ref.15
Mutagenesis461L → A: Causes slight reduction in S6K1 activation. Ref.15
Mutagenesis481T → A: Causes slightly reduced phosphorylation of EIF4EBP1. Ref.15
Mutagenesis491V → A: Causes slightly reduced phosphorylation of EIF4EBP1. Ref.15
Mutagenesis531E → A: Causes slightly reduced phosphorylation of EIF4EBP1. Ref.15
Mutagenesis541Y → A: Partially deficient in guanine nucleotide binding. Fully impairs EIF4EBP1 phosphorylation and S6K1 activation. Ref.15
Mutagenesis561L → A: Partially deficient in guanine nucleotide binding. Fully impairs EIF4EBP1 phosphorylation and S6K1 activation. Ref.15
Mutagenesis601D → I: Deficient in guanine nucleotide binding. Unable to rescue S6K1 from inactivation by amino-acid withdrawal. Ref.12
Mutagenesis641Q → L: Has a higher basal GTPase level, however, is still sensitive to TSC2 GAP activity. Ref.12
Mutagenesis1811C → S: Reduces the ability to rescue S6K1 from inactivation by amino-acid withdrawal. Ref.12
Sequence conflict1181G → W in BAA11211. Ref.2

Secondary structure

............................ 184
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q15382 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 8F4C8080BDF928FD

FASTA18420,497
        10         20         30         40         50         60 
MPQSKSRKIA ILGYRSVGKS SLTIQFVEGQ FVDSYDPTIE NTFTKLITVN GQEYHLQLVD 

        70         80         90        100        110        120 
TAGQDEYSIF PQTYSIDING YILVYSVTSI KSFEVIKVIH GKLLDMVGKV QIPIMLVGNK 

       130        140        150        160        170        180 
KDLHMERVIS YEEGKALAES WNAAFLESSA KENQTAVDVF RRIILEAEKM DGAASQGKSS 


CSVM 

« Hide

References

« Hide 'large scale' references
[1]"A novel approach for expression cloning of small GTPases: identification, tissue distribution and chromosome mapping of the human homolog of rheb."
Gromov P.S., Madsen P., Tomerup N., Celis J.E.
FEBS Lett. 377:221-226(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Psoriatic skin.
[2]"Isolation of cDNA and genomic clones of a human Ras-related GTP-binding protein gene and its chromosomal localization to the long arm of chromosome 7, 7q36."
Mizuki N., Kimura M., Ohno S., Miyata S., Sato M., Ando H., Ishihara M., Goto K., Watanabe S., Yamazaki M., Ono A., Taguchi S., Okumura K., Nogami M., Taguchi H., Ando A., Inoko H.
Genomics 34:114-118(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Skin.
[3]"Detection of membrane-associated proteins using serum of mice immunized with membrane fractions of breast carcinoma cells."
Weidenmueller U., Tur M.K., Tawadros S., Engert A., Barth S.
Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Mammary carcinoma.
[4]"cDNA clones of human proteins involved in signal transduction sequenced by the Guthrie cDNA resource center (www.cdna.org)."
Puhl H.L. III, Ikeda S.R., Aronstam R.S.
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[5]"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: Brain.
[6]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[7]"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].
[8]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].
[9]"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: Muscle and Testis.
[10]"Tuberous sclerosis complex-1 and -2 gene products function together to inhibit mammalian target of rapamycin (mTOR)-mediated downstream signaling."
Tee A.R., Fingar D.C., Manning B.D., Kwiatkowski D.J., Cantley L.C., Blenis J.
Proc. Natl. Acad. Sci. U.S.A. 99:13571-13576(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[11]"Rheb GTPase is a direct target of TSC2 GAP activity and regulates mTOR signaling."
Inoki K., Li Y., Xu T., Guan K.-L.
Genes Dev. 17:1829-1834(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[12]"Biochemical and functional characterizations of small GTPase Rheb and TSC2 GAP activity."
Li Y., Inoki K., Guan K.-L.
Mol. Cell. Biol. 24:7965-7975(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF ARG-15; SER-20; ASP-60; GLN-64 AND CYS-181.
[13]"A tagging-via-substrate technology for detection and proteomics of farnesylated proteins."
Kho Y., Kim S.C., Jiang C., Barma D., Kwon S.W., Cheng J., Jaunbergs J., Weinbaum C., Tamanoi F., Falck J., Zhao Y.
Proc. Natl. Acad. Sci. U.S.A. 101:12479-12484(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: ISOPRENYLATION AT CYS-181.
[14]"Rheb binds and regulates the mTOR kinase."
Long X., Lin Y., Ortiz-Vega S., Yonezawa K., Avruch J.
Curr. Biol. 15:702-713(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH MTOR; MLST8; RPTOR AND TSC2, MUTAGENESIS OF SER-20; THR-38; ILE-39 AND ASN-41.
[15]"Analysis of mTOR signaling by the small G-proteins, Rheb and RhebL1."
Tee A.R., Blenis J., Proud C.G.
FEBS Lett. 579:4763-4768(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF THR-38; GLU-40; ASN-41; PHE-43; LEU-46; THR-48; VAL-49; GLU-53; TYR-54 AND LEU-56, INTERACTION WITH MTOR.
[16]"Ragulator-Rag complex targets mTORC1 to the lysosomal surface and is necessary for its activation by amino acids."
Sancak Y., Bar-Peled L., Zoncu R., Markhard A.L., Nada S., Sabatini D.M.
Cell 141:290-303(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[17]"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].
[18]"Structural basis for the unique biological function of small GTPase RHEB."
Yu Y., Li S., Xu X., Li Y., Guan K., Arnold E., Ding J.
J. Biol. Chem. 280:17093-17100(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-169 IN COMPLEX WITH GDP AND GTP.
[19]"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] LYS-139.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z29677 mRNA. Translation: CAA82774.1.
D78132 mRNA. Translation: BAA11211.1.
AF148645 mRNA. Translation: AAF73125.1.
AF493921 mRNA. Translation: AAM12635.1.
AK125446 mRNA. Translation: BAG54198.1.
BT006958 mRNA. Translation: AAP35604.1.
AC005996 Genomic DNA. Translation: AAD15548.1.
CH471173 Genomic DNA. Translation: EAW53989.1.
BC016155 mRNA. Translation: AAH16155.1.
BC107705 mRNA. Translation: AAI07706.1.
PIRS41960. S68419.
RefSeqNP_005605.1. NM_005614.3.
UniGeneHs.283521.
Hs.568850.
Hs.647068.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1XTQX-ray2.00A1-169[»]
1XTRX-ray2.65A1-169[»]
1XTSX-ray2.80A1-169[»]
3SEAX-ray2.00A/B3-169[»]
3T5GX-ray1.70A1-181[»]
DisProtDP00364.
ProteinModelPortalQ15382.
SMRQ15382. Positions 3-169.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111941. 27 interactions.
DIPDIP-42816N.
IntActQ15382. 12 interactions.
MINTMINT-1365334.
STRING9606.ENSP00000262187.

PTM databases

PhosphoSiteQ15382.

Polymorphism databases

DMDM6919957.

Proteomic databases

PaxDbQ15382.
PRIDEQ15382.

Protocols and materials databases

DNASU6009.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000262187; ENSP00000262187; ENSG00000106615.
GeneID6009.
KEGGhsa:6009.
UCSCuc003wkh.1. human.

Organism-specific databases

CTD6009.
GeneCardsGC07M151163.
HGNCHGNC:10011. RHEB.
HPACAB019436.
HPA054743.
MIM601293. gene.
neXtProtNX_Q15382.
PharmGKBPA34389.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1100.
HOGENOMHOG000233973.
HOVERGENHBG009351.
InParanoidQ15382.
KOK07208.
OMATILNSKH.
OrthoDBEOG7Q2N6K.
PhylomeDBQ15382.
TreeFamTF314986.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
SignaLinkQ15382.

Gene expression databases

ArrayExpressQ15382.
BgeeQ15382.
CleanExHS_RHEB.
GenevestigatorQ15382.

Family and domain databases

InterProIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR020849. Small_GTPase_Ras.
[Graphical view]
PANTHERPTHR24070. PTHR24070. 1 hit.
PfamPF00071. Ras. 1 hit.
[Graphical view]
PRINTSPR00449. RASTRNSFRMNG.
SMARTSM00173. RAS. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR00231. small_GTP. 1 hit.
PROSITEPS51421. RAS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRHEB. human.
EvolutionaryTraceQ15382.
GeneWikiRHEB.
GenomeRNAi6009.
NextBio23445.
PROQ15382.
SOURCESearch...

Entry information

Entry nameRHEB_HUMAN
AccessionPrimary (citable) accession number: Q15382
Secondary accession number(s): B3KWN6 expand/collapse secondary AC list , D3DX13, Q53Y56, Q99444
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1996
Last modified: March 19, 2014
This is version 153 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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