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Q9H9S5 (FKRP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

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

Names and origin

Protein namesRecommended name:
Fukutin-related protein

EC=2.-.-.-
Gene names
Name:FKRP
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

Could be a transferase involved in the modification of glycan moieties of alpha-dystroglycan (DAG1).

Subunit structure

May interact with the dystrophin-glycoprotein complex (DGC) By similarity. Homodimer; disulfide-linked. Exists also as large multimeric protein complexes. Ref.9

Subcellular location

Golgi apparatus membrane; Single-pass type II membrane protein. Secreted. Cell membranesarcolemma By similarity. Rough endoplasmic reticulum. Note: According to some studies the N-terminal hydrophobic domain is cleaved after translocation to the Golgi apparatus and the protein is secreted. Localization at the cell membrane may require the presence of dystroglycan. At the Golgi apparatus localizes to the middle-to-trans-cisternae, as assessed by MG160 colocalization. Detected in rough endoplasmic reticulum in myocytes. In general, mutants associated with severe clinical phenotypes are retained within the endoplasmic reticulum. Ref.6 Ref.7 Ref.8 Ref.9

Tissue specificity

Expressed predominantly in skeletal muscle, placenta, and heart and relatively weakly in brain, lung, liver kidney and pancreas.

Post-translational modification

N-glycosylated. Ref.8 Ref.9

Involvement in disease

Muscular dystrophy-dystroglycanopathy congenital with brain and eye anomalies A5 (MDDGA5) [MIM:613153]: An autosomal recessive disorder characterized by congenital muscular dystrophy associated with cobblestone lissencephaly and other brain anomalies, eye malformations, profound mental retardation, and death usually in the first years of life. Included diseases are the more severe Walker-Warburg syndrome and the slightly less severe muscle-eye-brain disease.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.16

Muscular dystrophy-dystroglycanopathy congenital with or without mental retardation B5 (MDDGB5) [MIM:606612]: A congenital muscular dystrophy characterized by a severe phenotype with inability to walk, muscle hypertrophy, marked elevation of serum creatine kinase, secondary deficiency of laminin alpha2, and a marked reduction in alpha-dystroglycan expression. Only a subset of affected individuals have brain involvements.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.1 Ref.12 Ref.14 Ref.17 Ref.18

Muscular dystrophy-dystroglycanopathy limb-girdle C5 (MDDGC5) [MIM:607155]: An autosomal recessive degenerative myopathy with age of onset ranging from childhood to adult life, and variable severity. Clinical features include proximal muscle weakness, waddling gait, calf hypertrophy, cardiomyopathy and respiratory insufficiency. A reduction of alpha-dystroglycan and laminin alpha-2 expression can be observed on skeletal muscle biopsy from MDDGC5 patients.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.10 Ref.11 Ref.12 Ref.13 Ref.15

Sequence similarities

Belongs to the LicD transferase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 495495Fukutin-related protein
PRO_0000204723

Regions

Topological domain1 – 66Cytoplasmic Potential
Transmembrane7 – 2923Helical; Potential
Topological domain30 – 495466Lumenal Potential

Amino acid modifications

Glycosylation1721N-linked (GlcNAc...) Ref.9
Glycosylation2091N-linked (GlcNAc...) Ref.9
Disulfide bond6Interchain Ref.9

Natural variations

Natural variant541R → W in MDDGC5. Ref.15
Corresponds to variant rs28937905 [ dbSNP | Ensembl ].
VAR_019272
Natural variant791V → M in MDDGC5. Ref.13
Corresponds to variant rs104894683 [ dbSNP | Ensembl ].
VAR_065055
Natural variant1141A → G in MDDGB5; unknown pathological significance. Ref.1
Corresponds to variant rs143793528 [ dbSNP | Ensembl ].
VAR_018280
Natural variant1341R → W in MDDGC5. Ref.13
VAR_065056
Natural variant143 – 1464Missing in MDDGC5.
VAR_018281
Natural variant1431R → S in MDDGC5. Ref.11
Corresponds to variant rs148206382 [ dbSNP | Ensembl ].
VAR_018282
Natural variant1601V → F in MDDGC5. Ref.13
VAR_065057
Natural variant1821Y → C in MDDGC5. Ref.13
VAR_065058
Natural variant2171P → T in MDDGB5. Ref.1
VAR_018283
Natural variant2211S → R in MDDGB5; severe form; brain involvement; mental retardation and cerebellar cysts on cranial MRI. Ref.14
Corresponds to variant rs28937902 [ dbSNP | Ensembl ].
VAR_018284
Natural variant2761L → I in MDDGC5; reduced secretion to the medium; localizes mainly to the Golgi apparatus. Ref.7 Ref.8 Ref.11 Ref.12 Ref.13
Corresponds to variant rs28937900 [ dbSNP | Ensembl ].
VAR_018285
Natural variant2931T → I in MDDGC5. Ref.13
VAR_065059
Natural variant3001V → A in MDDGC5. Ref.13
VAR_065060
Natural variant3001V → M in MDDGC5. Ref.13
VAR_065061
Natural variant3071Y → N in MDDGC5 and MDDGA5; muscle-eye-brain disease. Ref.12 Ref.16
VAR_022850
Natural variant3091Y → C in MDDGB5. Ref.1 Ref.12
VAR_018286
Natural variant3121R → C in MDDGC5. Ref.11
VAR_018287
Natural variant3151P → T in MDDGB5; severe form; brain involvement; mental retardation and cerebellar cysts on cranial MRI. Ref.14
VAR_018288
Natural variant3161P → R in MDDGB5 and MDDGC5. Ref.1 Ref.11
VAR_018289
Natural variant3161P → S in MDDGC5. Ref.12
VAR_022851
Natural variant3181C → Y in MDDGA5; severe Walker-Warburg syndrome. Ref.16
VAR_022852
Natural variant3281Y → S in MDDGB5. Ref.1
VAR_018290
Natural variant3391R → H in MDDGB5. Ref.1 Ref.12
VAR_018292
Natural variant3391R → L in MDDGC5. Ref.11
VAR_018291
Natural variant3581P → L in MDDGC5. Ref.13
VAR_065062
Natural variant3601D → N in MDDGC5. Ref.12
VAR_022853
Natural variant4011D → N in MDDGB5. Ref.1
VAR_018293
Natural variant4051V → L in MDDGB5; severe form; brain involvement; mental retardation and cerebellar cysts on cranial MRI. Ref.17
Corresponds to variant rs28937904 [ dbSNP | Ensembl ].
VAR_022854
Natural variant4481P → L in MDDGB5; strongly reduced secretion to the medium; localizes mainly to the ER compartment. Ref.1 Ref.7 Ref.8 Ref.12
VAR_018294
Natural variant4551A → D in MDDGB5; severe form; brain involvement; mental retardation and cerebellar cysts on cranial MRI. Ref.17
Corresponds to variant rs28937903 [ dbSNP | Ensembl ].
VAR_022855
Natural variant4621P → S in MDDGC5. Ref.12
VAR_022856
Natural variant4631N → D in MDDGB5. Ref.18
VAR_065063
Natural variant4651Y → S in MDDGB5. Ref.1
VAR_018295

Sequences

Sequence LengthMass (Da)Tools
Q9H9S5 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 8D47756C28C6F578

FASTA49554,568
        10         20         30         40         50         60 
MRLTRCQAAL AAAITLNLLV LFYVSWLQHQ PRNSRARGPR RASAAGPRVT VLVREFEAFD 

        70         80         90        100        110        120 
NAVPELVDSF LQQDPAQPVV VAADTLPYPP LALPRIPNVR LALLQPALDR PAAASRPETY 

       130        140        150        160        170        180 
VATEFVALVP DGARAEAPGL LERMVEALRA GSARLVAAPV ATANPARCLA LNVSLREWTA 

       190        200        210        220        230        240 
RYGAAPAAPR CDALDGDAVV LLRARDLFNL SAPLARPVGT SLFLQTALRG WAVQLLDLTF 

       250        260        270        280        290        300 
AAARQPPLAT AHARWKAERE GRARRAALLR ALGIRLVSWE GGRLEWFGCN KETTRCFGTV 

       310        320        330        340        350        360 
VGDTPAYLYE ERWTPPCCLR ALRETARYVV GVLEAAGVRY WLEGGSLLGA ARHGDIIPWD 

       370        380        390        400        410        420 
YDVDLGIYLE DVGNCEQLRG AEAGSVVDER GFVWEKAVEG DFFRVQYSES NHLHVDLWPF 

       430        440        450        460        470        480 
YPRNGVMTKD TWLDHRQDVE FPEHFLQPLV PLPFAGFVAQ APNNYRRFLE LKFGPGVIEN 

       490 
PQYPNPALLS LTGSG 

« Hide

References

« Hide 'large scale' references
[1]"Mutations in the fukutin-related protein gene (FKRP) cause a form of congenital muscular dystrophy with secondary laminin alpha2 deficiency and abnormal glycosylation of alpha-dystroglycan."
Brockington M., Blake D.J., Prandini P., Brown S.C., Torelli S., Benson M.A., Ponting C.P., Estournet B., Romero N.B., Mercuri E., Voit T., Sewry C.A., Guicheney P., Muntoni F.
Am. J. Hum. Genet. 69:1198-1209(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS MDDGB5 GLY-114; THR-217; CYS-309; ARG-316; SER-328; HIS-339; ASN-401; LEU-448 AND SER-465.
Tissue: Brain.
[2]"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.
[3]"The DNA sequence and biology of human chromosome 19."
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V. expand/collapse author list , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
Nature 428:529-535(2004) [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].
[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].
Tissue: Brain.
[6]"Subcellular localization of fukutin and fukutin-related protein in muscle cells."
Matsumoto H., Noguchi S., Sugie K., Ogawa M., Murayama K., Hayashi Y.K., Nishino I.
J. Biochem. 135:709-712(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[7]"Fukutin-related protein localizes to the Golgi apparatus and mutations lead to mislocalization in muscle in vivo."
Keramaris-Vrantsis E., Lu P.J., Doran T., Zillmer A., Ashar J., Esapa C.T., Benson M.A., Blake D.J., Rosenfeld J., Lu Q.L.
Muscle Nerve 36:455-465(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANTS ILE-276 AND LEU-448.
[8]"Mutations alter secretion of fukutin-related protein."
Lu P.J., Zillmer A., Wu X., Lochmuller H., Vachris J., Blake D., Chan Y.M., Lu Q.L.
Biochim. Biophys. Acta 1802:253-258(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, GLYCOSYLATION, CHARACTERIZATION OF VARIANTS ILE-276 AND LEU-448.
[9]"Fukutin-related protein resides in the Golgi cisternae of skeletal muscle fibres and forms disulfide-linked homodimers via an N-Terminal interaction."
Alhamidi M., Kjeldsen Buvang E., Fagerheim T., Brox V., Lindal S., Van Ghelue M., Nilssen O.
PLoS ONE 6:E22968-E22968(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, GLYCOSYLATION AT ASN-172 AND ASN-209, SUBUNIT, DISULFIDE BOND.
[10]"Limb-girdle muscular dystrophy type 2I is not rare in Taiwan."
Liang W.C., Hayashi Y.K., Ogawa M., Wang C.H., Huang W.T., Nishino I., Jong Y.J.
Neuromuscul. Disord. 23:675-681(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN MDDGC5.
[11]"Mutations in the fukutin-related protein gene (FKRP) identify limb girdle muscular dystrophy 2I as a milder allelic variant of congenital muscular dystrophy MDC1C."
Brockington M., Yuva Y., Prandini P., Brown S.C., Torelli S., Benson M.A., Herrmann R., Anderson L.V.B., Bashir R., Burgunder J.-M., Fallet S., Romero N., Fardeau M., Straub V., Storey G., Pollitt C., Richard I., Sewry C.A. expand/collapse author list , Bushby K., Voit T., Blake D.J., Muntoni F.
Hum. Mol. Genet. 10:2851-2859(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS MDDGC5 143-ARG--GLU-146 DEL; SER-143; ILE-276; CYS-312; ARG-316 AND LEU-339.
[12]"Phenotypic spectrum associated with mutations in the fukutin-related protein gene."
Mercuri E., Brockington M., Straub V., Quijano-Roy S., Yuva Y., Herrmann R., Brown S.C., Torelli S., Dubowitz V., Blake D.J., Romero N.B., Estournet B., Sewry C.A., Guicheney P., Voit T., Muntoni F.
Ann. Neurol. 53:537-542(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS MDDGB5 CYS-309; HIS-339 AND LEU-448, VARIANTS MDDGC5 ILE-276; ASN-307; SER-316; ASN-360 AND SER-462.
[13]"Asymptomatic carriers for homozygous novel mutations in the FKRP gene: the other end of the spectrum."
de Paula F., Vieira N., Starling A., Yamamoto L.U., Lima B., de Cassia Pavanello R., Vainzof M., Nigro V., Zatz M.
Eur. J. Hum. Genet. 11:923-930(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS MDDGC5 MET-79; TRP-134; PHE-160; CYS-182; ILE-276; ILE-293; ALA-300; MET-300 AND LEU-358.
[14]"FKRP gene mutations cause congenital muscular dystrophy, mental retardation, and cerebellar cysts."
Topaloglu H., Brockington M., Yuva Y., Talim B., Haliloglu G., Blake D.J., Torelli S., Brown S.C., Muntoni F.
Neurology 60:988-992(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS MDDGB5 ARG-221 AND THR-315.
[15]"Limb-girdle muscular dystrophy 2I: phenotypic variability within a large consanguineous Bedouin family associated with a novel FKRP mutation."
Harel T., Goldberg Y., Shalev S.A., Chervinski I., Ofir R., Birk O.S.
Eur. J. Hum. Genet. 12:38-43(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT MDDGC5 TRP-54.
[16]"Mutations in the FKRP gene can cause muscle-eye-brain disease and Walker-Warburg syndrome."
Beltran-Valero de Bernabe D., Voit T., Longman C., Steinbrecher A., Straub V., Yuva Y., Herrmann R., Sperner J., Korenke C., Diesen C., Dobyns W.B., Brunner H.G., van Bokhoven H., Brockington M., Muntoni F.
J. Med. Genet. 41:E61-E61(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS MDDGA5 ASN-307 AND TYR-318.
[17]"New FKRP mutations causing congenital muscular dystrophy associated with mental retardation and central nervous system abnormalities. Identification of a founder mutation in Tunisian families."
Louhichi N., Triki C., Quijano-Roy S., Richard P., Makri S., Meziou M., Estournet B., Mrad S., Romero N.B., Ayadi H., Guicheney P., Fakhfakh F.
Neurogenetics 5:27-34(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS MDDGB5 LEU-405 AND ASP-455.
[18]"A novel FKRP mutation in congenital muscular dystrophy disrupts the dystrophin glycoprotein complex."
MacLeod H., Pytel P., Wollmann R., Chelmicka-Schorr E., Silver K., Anderson R.B., Waggoner D., McNally E.M.
Neuromuscul. Disord. 17:285-289(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT MDDGB5 ASP-463.
+Additional computationally mapped references.

Web resources

GeneReviews
GGDB

GlycoGene database

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ314847 mRNA. Translation: CAC85633.1.
AK022638 mRNA. Translation: BAB14146.1.
AK095497 mRNA. Translation: BAG53071.1.
AK291282 mRNA. Translation: BAF83971.1.
AC008622 Genomic DNA. No translation available.
CH471126 Genomic DNA. Translation: EAW57444.1.
BC002612 mRNA. Translation: AAH02612.1.
RefSeqNP_001034974.1. NM_001039885.2.
NP_077277.1. NM_024301.4.
XP_005259304.1. XM_005259247.1.
XP_005259305.1. XM_005259248.1.
XP_005259306.1. XM_005259249.2.
XP_005259307.1. XM_005259250.2.
UniGeneHs.515493.

3D structure databases

ProteinModelPortalQ9H9S5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid122565. 1 interaction.
STRING9606.ENSP00000326570.

PTM databases

PhosphoSiteQ9H9S5.

Polymorphism databases

DMDM46395992.

Proteomic databases

PaxDbQ9H9S5.
PRIDEQ9H9S5.

Protocols and materials databases

DNASU79147.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000318584; ENSP00000326570; ENSG00000181027.
ENST00000391909; ENSP00000375776; ENSG00000181027.
GeneID79147.
KEGGhsa:79147.
UCSCuc002pfn.2. human.

Organism-specific databases

CTD79147.
GeneCardsGC19P047249.
HGNCHGNC:17997. FKRP.
HPAHPA060454.
MIM606596. gene.
606612. phenotype.
607155. phenotype.
613153. phenotype.
neXtProtNX_Q9H9S5.
Orphanet34515. Autosomal recessive limb-girdle muscular dystrophy type 2I.
370959. Congenital muscular dystrophy with cerebellar involvement.
370968. Congenital muscular dystrophy with intellectual disability.
370980. Congenital muscular dystrophy without intellectual disability.
588. Muscle-eye-brain disease.
899. Walker-Warburg syndrome.
PharmGKBPA134976709.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG3475.
HOGENOMHOG000007172.
HOVERGENHBG048950.
InParanoidQ9H9S5.
OMATAHARWK.
PhylomeDBQ9H9S5.
TreeFamTF324064.

Gene expression databases

ArrayExpressQ9H9S5.
BgeeQ9H9S5.
CleanExHS_FKRP.
GenevestigatorQ9H9S5.

Family and domain databases

InterProIPR007074. LicD.
[Graphical view]
PfamPF04991. LicD. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi79147.
NextBio68051.
PROQ9H9S5.
SOURCESearch...

Entry information

Entry nameFKRP_HUMAN
AccessionPrimary (citable) accession number: Q9H9S5
Secondary accession number(s): A8K5G7
Entry history
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: March 1, 2001
Last modified: April 16, 2014
This is version 105 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