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

O95671 (ASML_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 124. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
N-acetylserotonin O-methyltransferase-like protein

Short name=ASMTL
EC=2.1.1.-
Gene names
Name:ASMTL
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length621 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Unknown. The presence of the putative catalytic domain of S-adenosyl-L-methionine binding argues for a methyltransferase activity. HAMAP-Rule MF_00528

Tissue specificity

Widely expressed. In adult, highly expressed in pancreas, placenta, fibroblast, thymus, prostate, testis, ovary and colon. Expressed at lower levels in spleen, small intestine and leukocytes. In fetus, expressed at high levels in the lung and kidney and at lower level in brain and liver.

Miscellaneous

The gene coding for this protein is located in the pseudoautosomal region 1 (PAR1) of X and Y chromosomes. It represents a unique fusion product of 2 different genes of different evolutionary origin and function. The N-terminus is homologous to the bacterial maf/orfE genes and the C-terminus is homologous to ASMT. Exon duplication, exon shuffling and gene fusion seem to be common characteristics of the PAR1 region.

Sequence similarities

Belongs to the class I-like SAM-binding methyltransferase superfamily. Cation-independent O-methyltransferase family.

In the N-terminal section; belongs to the maf family.

Sequence caution

The sequence CAA75675.1 differs from that shown. Reason: Frameshift at position 616.

The sequence CAA75676.1 differs from that shown. Reason: Frameshift at position 616.

Ontologies

Keywords
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandS-adenosyl-L-methionine
   Molecular functionMethyltransferase
Transferase
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Cellular_componentcytoplasm

Inferred from direct assay. Source: HPA

   Molecular_functionO-methyltransferase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O95671-1)

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: O95671-2)

The sequence of this isoform differs from the canonical sequence as follows:
     76-91: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: O95671-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-58: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 621621N-acetylserotonin O-methyltransferase-like protein HAMAP-Rule MF_00528
PRO_0000064702

Regions

Region11 – 223213MAF-like HAMAP-Rule MF_00528
Region277 – 621345ASMT-like HAMAP-Rule MF_00528
Region508 – 5103S-adenosyl-L-methionine binding By similarity

Sites

Active site441 Potential
Binding site4821S-adenosyl-L-methionine By similarity
Binding site5251S-adenosyl-L-methionine By similarity

Amino acid modifications

Modified residue2391Phosphoserine Ref.5 Ref.6 Ref.7 Ref.8 Ref.10 Ref.11 Ref.13

Natural variations

Alternative sequence1 – 5858Missing in isoform 3.
VSP_047412
Alternative sequence76 – 9116Missing in isoform 2.
VSP_007213
Natural variant4581V → M. Ref.4
Corresponds to variant rs4503285 [ dbSNP | Ensembl ].
VAR_054802
Natural variant5411R → K. Ref.1 Ref.4
Corresponds to variant rs1127297 [ dbSNP | Ensembl ].
VAR_054803

Experimental info

Sequence conflict2281S → P in BAG63287. Ref.2
Sequence conflict3641Y → H in BAG63287. Ref.2
Sequence conflict4341G → S in BAG63287. Ref.2

Secondary structure

.................................. 621
Helix Strand Turn

Details...

Sequences

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

Last modified October 3, 2006. Version 3.
Checksum: 564C2D538F4919EC

FASTA62168,857
        10         20         30         40         50         60 
MVLCPVIGKL LHKRVVLASA SPRRQEILSN AGLRFEVVPS KFKEKLDKAS FATPYGYAME 

        70         80         90        100        110        120 
TAKQKALEVA NRLYQKDLRA PDVVIGADTI VTVGGLILEK PVDKQDAYRM LSRLSGREHS 

       130        140        150        160        170        180 
VFTGVAIVHC SSKDHQLDTR VSEFYEETKV KFSELSEELL WEYVHSGEPM DKAGGYGIQA 

       190        200        210        220        230        240 
LGGMLVESVH GDFLNVVGFP LNHFCKQLVK LYYPPRPEDL RRSVKHDSIP AADTFEDLSD 

       250        260        270        280        290        300 
VEGGGSEPTQ RDAGSRDEKA EAGEAGQATA EAECHRTRET LPPFPTRLLE LIEGFMLSKG 

       310        320        330        340        350        360 
LLTACKLKVF DLLKDEAPQK AADIASKVDA SACGMERLLD ICAAMGLLEK TEQGYSNTET 

       370        380        390        400        410        420 
ANVYLASDGE YSLHGFIMHN NDLTWNLFTY LEFAIREGTN QHHRALGKKA EDLFQDAYYQ 

       430        440        450        460        470        480 
SPETRLRFMR AMHGMTKLTA CQVATAFNLS RFSSACDVGG CTGALARELA REYPRMQVTV 

       490        500        510        520        530        540 
FDLPDIIELA AHFQPPGPQA VQIHFAAGDF FRDPLPSAEL YVLCRILHDW PDDKVHKLLS 

       550        560        570        580        590        600 
RVAESCKPGA GLLLVETLLD EEKRVAQRAL MQSLNMLVQT EGKERSLGEY QCLLELHGFH 

       610        620 
QVQVVHLGGV LDAILATKVA P 

« Hide

Isoform 2 [UniParc].

Checksum: 68D9C963275E9A36
Show »

FASTA60567,193
Isoform 3 [UniParc].

Checksum: 5AC40CB68911EF40
Show »

FASTA56362,443

References

« Hide 'large scale' references
[1]"Gene duplications as a recurrent theme in the evolution of the human pseudoautosomal region 1: isolation of the gene ASMTL."
Ried K., Rao E., Schiebel K., Rappold G.A.
Hum. Mol. Genet. 7:1771-1778(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT LYS-541.
Tissue: Bone marrow, Colon, Fetal brain, Pancreas and Placenta.
[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] (ISOFORMS 2 AND 3).
Tissue: Adrenal gland and Testis.
[3]"The DNA sequence of the human X chromosome."
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. expand/collapse author list , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
Nature 434:325-337(2005) [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] (ISOFORM 1), VARIANTS MET-458 AND LYS-541.
Tissue: Colon adenocarcinoma.
[5]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-239, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[6]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-239, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[7]"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-239, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-239, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[9]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-239, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[11]"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-239, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"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].
[13]"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-239, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"Crystal structure of maf domain of human N-acetylserotonin O-methyltransferase-like protein."
Structural genomics consortium (SGC)
Submitted (MAR-2007) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 10-239.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y15521 Genomic DNA. Translation: CAA75675.1. Frameshift.
Y15521 Genomic DNA. Translation: CAA75676.1. Frameshift.
AK090498 mRNA. Translation: BAC03468.1.
AK301844 mRNA. Translation: BAG63287.1.
AL683870 Genomic DNA. Translation: CAI39847.1.
AL683870 Genomic DNA. Translation: CAI39848.1.
BC002508 mRNA. Translation: AAH02508.1.
BC010089 mRNA. Translation: AAH10089.1.
RefSeqNP_001166944.1. NM_001173473.1.
NP_001166945.1. NM_001173474.1.
NP_004183.2. NM_004192.3.
XP_005274491.1. XM_005274434.1.
XP_005274840.1. XM_005274783.1.
UniGeneHs.533514.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2P5XX-ray2.00A/B10-239[»]
ProteinModelPortalO95671.
SMRO95671. Positions 10-213, 287-618.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114178. 6 interactions.
IntActO95671. 2 interactions.
STRING9606.ENSP00000370718.

PTM databases

PhosphoSiteO95671.

Proteomic databases

PaxDbO95671.
PRIDEO95671.

Protocols and materials databases

DNASU8623.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000381317; ENSP00000370718; ENSG00000169093. [O95671-1]
ENST00000381333; ENSP00000370734; ENSG00000169093. [O95671-2]
ENST00000534940; ENSP00000446410; ENSG00000169093. [O95671-3]
GeneID8623.
KEGGhsa:8623.
UCSCuc004cpx.2. human. [O95671-1]
uc004cpy.2. human. [O95671-2]

Organism-specific databases

CTD8623.
GeneCardsGC0XM001522.
H-InvDBHIX0176513.
HIX0177590.
HGNCHGNC:751. ASMTL.
HPAHPA003630.
HPA021865.
MIM300162. gene.
400011. gene.
neXtProtNX_O95671.
PharmGKBPA25050.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0500.
HOGENOMHOG000034104.
HOVERGENHBG036737.
InParanoidO95671.
OMAWEYINSG.
OrthoDBEOG7W1557.
PhylomeDBO95671.
TreeFamTF314574.

Gene expression databases

ArrayExpressO95671.
BgeeO95671.
CleanExHS_ASMTL.
GenevestigatorO95671.

Family and domain databases

Gene3D1.10.10.10. 1 hit.
HAMAPMF_00528. Maf.
InterProIPR025772. ASMT-like.
IPR003697. Maf.
IPR001077. O_MeTrfase_2.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamPF02545. Maf. 1 hit.
PF00891. Methyltransf_2. 1 hit.
[Graphical view]
TIGRFAMsTIGR00172. maf. 1 hit.
PROSITEPS51683. SAM_OMT_II. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceO95671.
GeneWikiASMTL.
GenomeRNAi8623.
NextBio32321.
PROO95671.
SOURCESearch...

Entry information

Entry nameASML_HUMAN
AccessionPrimary (citable) accession number: O95671
Secondary accession number(s): B4DX75 expand/collapse secondary AC list , F5GXH4, J3JS33, Q5JQ53, Q8NBH5, Q96G02, Q9BUL6
Entry history
Integrated into UniProtKB/Swiss-Prot: April 23, 2003
Last sequence update: October 3, 2006
Last modified: April 16, 2014
This is version 124 of the entry and version 3 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 X

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