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Q9H4G0 (E41L1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 129. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Band 4.1-like protein 1
Alternative name(s):
Neuronal protein 4.1
Short name=4.1N
Gene names
Name:EPB41L1
Synonyms:KIAA0338
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length881 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May function to confer stability and plasticity to neuronal membrane via multiple interactions, including the spectrin-actin-based cytoskeleton, integral membrane channels and membrane-associated guanylate kinases.

Subunit structure

Interacts with AGAP2. Ref.6

Subcellular location

Cytoplasmcytoskeleton.

Tissue specificity

Highest expression in brain, lower in heart, kidney, pancreas, placenta, lung and skeletal muscle.

Involvement in disease

Mental retardation, autosomal dominant 11 (MRD11) [MIM:614257]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.11

Sequence similarities

Contains 1 FERM domain.

Sequence caution

The sequence BAA20796.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9H4G0-1)

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: Q9H4G0-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-62: Missing.
     484-495: Missing.
     729-756: Missing.
Isoform 3 (identifier: Q9H4G0-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-62: Missing.
     115-149: Missing.
     484-495: Missing.
Note: No experimental confirmation available.
Isoform 4 (identifier: Q9H4G0-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-59: MTTETGPDSE...SQQDTRPAEQ → MVFLGRINEVEPAKGLAESLAPTERSVK
     484-495: Missing.
     556-692: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 881881Band 4.1-like protein 1
PRO_0000219395

Regions

Domain97 – 378282FERM
Region483 – 54159Spectrin--actin-binding
Region746 – 881136C-terminal (CTD)

Amino acid modifications

Modified residue751Phosphoserine Ref.8 Ref.9
Modified residue791Phosphothreonine Ref.8
Modified residue3431Phosphotyrosine By similarity
Modified residue4301Phosphoserine Ref.9
Modified residue4751Phosphothreonine Ref.8
Modified residue5101Phosphoserine Ref.9
Modified residue5401Phosphoserine Ref.8
Modified residue5411Phosphoserine Ref.8
Modified residue5441Phosphoserine Ref.8 Ref.9
Modified residue5461Phosphoserine Ref.8 Ref.9
Modified residue5501Phosphothreonine By similarity
Modified residue5641Phosphoserine Ref.9
Modified residue5781Phosphoserine Ref.8
Modified residue6481Phosphoserine Ref.8
Modified residue6501Phosphoserine Ref.8 Ref.9
Modified residue7841Phosphoserine Ref.8

Natural variations

Alternative sequence1 – 6262Missing in isoform 2 and isoform 3.
VSP_023958
Alternative sequence1 – 5959MTTET…RPAEQ → MVFLGRINEVEPAKGLAESL APTERSVK in isoform 4.
VSP_023959
Alternative sequence115 – 14935Missing in isoform 3.
VSP_023960
Alternative sequence484 – 49512Missing in isoform 2, isoform 3 and isoform 4.
VSP_023961
Alternative sequence556 – 692137Missing in isoform 4.
VSP_023962
Alternative sequence729 – 75628Missing in isoform 2.
VSP_023963
Natural variant8541P → S in MRD11; results in a 50% reduction of interaction of 4.1N protein to GRIA1 compared to wild-type. Ref.11
VAR_066600

Experimental info

Sequence conflict7281Missing in CAI95019. Ref.3
Sequence conflict7281Missing in CAI95025. Ref.3
Sequence conflict7281Missing in AAH40259. Ref.4
Sequence conflict7281Missing in AAL15446. Ref.5

Sequences

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

Last modified July 11, 2001. Version 2.
Checksum: D923CF554EDB41D3

FASTA88198,503
        10         20         30         40         50         60 
MTTETGPDSE VKKAQEEAPQ QPEAAAAVTT PVTPAGHGHP EANSNEKHPS QQDTRPAEQS 

        70         80         90        100        110        120 
LDMEEKDYSE ADGLSERTTP SKAQKSPQKI AKKYKSAICR VTLLDASEYE CEVEKHGRGQ 

       130        140        150        160        170        180 
VLFDLVCEHL NLLEKDYFGL TFCDADSQKN WLDPSKEIKK QIRSSPWNFA FTVKFYPPDP 

       190        200        210        220        230        240 
AQLTEDITRY YLCLQLRADI ITGRLPCSFV THALLGSYAV QAELGDYDAE EHVGNYVSEL 

       250        260        270        280        290        300 
RFAPNQTREL EERIMELHKT YRGMTPGEAE IHFLENAKKL SMYGVDLHHA KDSEGIDIML 

       310        320        330        340        350        360 
GVCANGLLIY RDRLRINRFA WPKILKISYK RSNFYIKIRP GEYEQFESTI GFKLPNHRSA 

       370        380        390        400        410        420 
KRLWKVCIEH HTFFRLVSPE PPPKGFLVMG SKFRYSGRTQ AQTRQASALI DRPAPFFERS 

       430        440        450        460        470        480 
SSKRYTMSRS LDGAEFSRPA SVSENHDAGP DGDKRDEDGE SGGQRSEAEE GEVRTPTKIK 

       490        500        510        520        530        540 
ELKPEQETTP RHKQEFLDKP EDVLLKHQAS INELKRTLKE PNSKLIHRDR DWERERRLPS 

       550        560        570        580        590        600 
SPASPSPKGT PEKANERAGL REGSEEKVKP PRPRAPESDT GDEDQDQERD TVFLKDNHLA 

       610        620        630        640        650        660 
IERKCSSITV SSTSSLEAEV DFTVIGDYHG SAFEDFSRSL PELDRDKSDS DTEGLLFSRD 

       670        680        690        700        710        720 
LNKGAPSQDD ESGGIEDSPD RGACSTPDMP QFEPVKTETM TVSSLAIRKK IEPEAVLQTR 

       730        740        750        760        770        780 
VSAMDNTQQV DGSASVGREF IATTPSITTE TISTTMENSL KSGKGAAAMI PGPQTVATEI 

       790        800        810        820        830        840 
RSLSPIIGKD VLTSTYGATA ETLSTSTTTH VTKTVKGGFS ETRIEKRIII TGDEDVDQDQ 

       850        860        870        880 
ALALAIKEAK LQHPDMLVTK AVVYRETDPS PEERDKKPQE S 

« Hide

Isoform 2 [UniParc].

Checksum: 144DEEB4E9174DF0
Show »

FASTA77987,645
Isoform 3 [UniParc].

Checksum: 3FD79DBAEB979E87
Show »

FASTA77286,506
Isoform 4 [UniParc].

Checksum: A1B6C60B3ABF611A
Show »

FASTA70178,831

References

« Hide 'large scale' references
[1]"Prediction of the coding sequences of unidentified human genes. VII. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
DNA Res. 4:141-150(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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] (ISOFORM 4).
Tissue: Amygdala.
[3]"The DNA sequence and comparative analysis of human chromosome 20."
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E. expand/collapse author list , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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] (ISOFORMS 1 AND 2).
Tissue: Brain and Pancreas.
[5]Liu J., Zhou Y., Zhang B., Peng X., Yuan J., Qiang B.
Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-873 (ISOFORM 1).
[6]"PIKE: a nuclear GTPase that enhances PI3kinase activity and is regulated by protein 4.1N."
Ye K., Hurt K.J., Wu F.Y., Fang M., Luo H.R., Hong J.J., Blackshaw S., Ferris C.D., Snyder S.H.
Cell 103:919-930(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH AGAP2.
[7]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75; THR-79; THR-475; SER-540; SER-541; SER-544; SER-546; SER-578; SER-648; SER-650 AND SER-784, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"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-75; SER-430; SER-510; SER-544; SER-546; SER-564 AND SER-650, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"Excess of de novo deleterious mutations in genes associated with glutamatergic systems in nonsyndromic intellectual disability."
Hamdan F.F., Gauthier J., Araki Y., Lin D.T., Yoshizawa Y., Higashi K., Park A.R., Spiegelman D., Dobrzeniecka S., Piton A., Tomitori H., Daoud H., Massicotte C., Henrion E., Diallo O., Shekarabi M., Marineau C., Shevell M. expand/collapse author list , Maranda B., Mitchell G., Nadeau A., D'Anjou G., Vanasse M., Srour M., Lafreniere R.G., Drapeau P., Lacaille J.C., Kim E., Lee J.R., Igarashi K., Huganir R.L., Rouleau G.A., Michaud J.L.
Am. J. Hum. Genet. 88:306-316(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT MRD11 SER-854, CHARACTERIZATION OF VARIANT MRD11 SER-854.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB002336 mRNA. Translation: BAA20796.1. Different initiation.
AK126875 mRNA. Translation: BAC86733.1.
AL121895 Genomic DNA. Translation: CAI95018.1.
AL121895 Genomic DNA. Translation: CAI95019.1.
AL121895 Genomic DNA. Translation: CAI95023.1.
AL121895 Genomic DNA. Translation: CAI95024.1.
AL121895 Genomic DNA. Translation: CAI95025.1.
AL121895 Genomic DNA. Translation: CAI95027.1.
BC013885 mRNA. Translation: AAH13885.1.
BC040259 mRNA. Translation: AAH40259.1.
AY049789 mRNA. Translation: AAL15446.1.
CCDSCCDS13271.1. [Q9H4G0-1]
CCDS13272.1. [Q9H4G0-2]
CCDS58770.1. [Q9H4G0-4]
RefSeqNP_001245258.1. NM_001258329.1.
NP_001245259.1. NM_001258330.1. [Q9H4G0-4]
NP_001245260.1. NM_001258331.1. [Q9H4G0-2]
NP_036288.2. NM_012156.2. [Q9H4G0-1]
NP_818932.1. NM_177996.2. [Q9H4G0-2]
XP_005260376.1. XM_005260319.1.
XP_006723799.1. XM_006723736.1. [Q9H4G0-1]
XP_006723800.1. XM_006723737.1. [Q9H4G0-1]
XP_006723801.1. XM_006723738.1. [Q9H4G0-1]
UniGeneHs.437422.

3D structure databases

ProteinModelPortalQ9H4G0.
SMRQ9H4G0. Positions 95-377.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108350. 37 interactions.
IntActQ9H4G0. 4 interactions.
MINTMINT-5005633.

PTM databases

PhosphoSiteQ9H4G0.

Polymorphism databases

DMDM14916561.

Proteomic databases

MaxQBQ9H4G0.
PaxDbQ9H4G0.
PRIDEQ9H4G0.

Protocols and materials databases

DNASU2036.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000202028; ENSP00000202028; ENSG00000088367. [Q9H4G0-2]
ENST00000338074; ENSP00000337168; ENSG00000088367. [Q9H4G0-1]
ENST00000373941; ENSP00000363052; ENSG00000088367.
ENST00000373946; ENSP00000363057; ENSG00000088367. [Q9H4G0-4]
ENST00000373950; ENSP00000363061; ENSG00000088367. [Q9H4G0-3]
ENST00000441639; ENSP00000399214; ENSG00000088367. [Q9H4G0-2]
GeneID2036.
KEGGhsa:2036.
UCSCuc002xeu.3. human. [Q9H4G0-2]
uc002xev.3. human. [Q9H4G0-1]
uc002xew.3. human. [Q9H4G0-3]
uc002xex.3. human. [Q9H4G0-4]

Organism-specific databases

CTD2036.
GeneCardsGC20P034679.
HGNCHGNC:3378. EPB41L1.
HPAHPA054104.
HPA056817.
MIM602879. gene.
614257. phenotype.
neXtProtNX_Q9H4G0.
Orphanet178469. Autosomal dominant nonsyndromic intellectual disability.
PharmGKBPA27811.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG242913.
HOVERGENHBG007777.
KOK06107.
OMASNEKHPS.
OrthoDBEOG7Z69BP.
PhylomeDBQ9H4G0.
TreeFamTF351626.

Enzyme and pathway databases

ReactomeREACT_13685. Neuronal System.

Gene expression databases

ArrayExpressQ9H4G0.
BgeeQ9H4G0.
GenevestigatorQ9H4G0.

Family and domain databases

Gene3D1.20.80.10. 1 hit.
2.30.29.30. 1 hit.
InterProIPR008379. Band_4.1_C.
IPR019749. Band_41_domain.
IPR019750. Band_41_fam.
IPR021187. Band_41_protein.
IPR000798. Ez/rad/moesin_like.
IPR014847. FERM-adjacent.
IPR014352. FERM/acyl-CoA-bd_prot_3-hlx.
IPR019748. FERM_central.
IPR019747. FERM_CS.
IPR000299. FERM_domain.
IPR018979. FERM_N.
IPR018980. FERM_PH-like_C.
IPR011993. PH_like_dom.
IPR007477. SAB_dom.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
PfamPF05902. 4_1_CTD. 1 hit.
PF08736. FA. 1 hit.
PF09380. FERM_C. 1 hit.
PF00373. FERM_M. 1 hit.
PF09379. FERM_N. 1 hit.
PF04382. SAB. 1 hit.
[Graphical view]
PIRSFPIRSF002304. Membrane_skeletal_4_1. 1 hit.
PRINTSPR00935. BAND41.
PR00661. ERMFAMILY.
SMARTSM00295. B41. 1 hit.
[Graphical view]
SUPFAMSSF47031. SSF47031. 1 hit.
SSF54236. SSF54236. 1 hit.
PROSITEPS00660. FERM_1. 1 hit.
PS00661. FERM_2. 1 hit.
PS50057. FERM_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSEPB41L1. human.
GeneWikiEPB41L1.
GenomeRNAi2036.
NextBio8267.
PROQ9H4G0.
SOURCESearch...

Entry information

Entry nameE41L1_HUMAN
AccessionPrimary (citable) accession number: Q9H4G0
Secondary accession number(s): O15046 expand/collapse secondary AC list , Q4VXM6, Q4VXM7, Q4VXM8, Q4VXN4, Q6ZT61, Q8IUU7, Q96CV5, Q96L65
Entry history
Integrated into UniProtKB/Swiss-Prot: July 11, 2001
Last sequence update: July 11, 2001
Last modified: July 9, 2014
This is version 129 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 20

Human chromosome 20: entries, gene names and cross-references to MIM