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Q8IY81 (SPB1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 109. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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:
pre-rRNA processing protein FTSJ3

EC=2.1.1.-
Alternative name(s):
2'-O-ribose RNA methyltransferase SPB1 homolog
Protein ftsJ homolog 3
Putative rRNA methyltransferase 3
Gene names
Name:FTSJ3
ORF Names:SB92
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length847 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Probable methyltransferase involved in the processing of the 34S pre-rRNA to 18S rRNA and in 40S ribosomal subunit formation. Ref.17

Catalytic activity

S-adenosyl-L-methionine + rRNA = S-adenosyl-L-homocysteine + rRNA containing 2'-O-methylnucleoside. HAMAP-Rule MF_03163

Subunit structure

Interacts with NIP7. Ref.17

Subcellular location

Nucleusnucleolus Ref.7 Ref.17.

Post-translational modification

Citrullinated by PADI4 By similarity. HAMAP-Rule MF_03163

Sequence similarities

Belongs to the methyltransferase superfamily. RlmE family. SPB1 subfamily.

Sequence caution

The sequence BAA90924.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
   Biological processRibosome biogenesis
rRNA processing
   Cellular componentNucleus
   Coding sequence diversityPolymorphism
   DomainCoiled coil
   LigandS-adenosyl-L-methionine
   Molecular functionMethyltransferase
Transferase
   PTMCitrullination
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Cellular_componentnucleolus

Inferred from direct assay. Source: HPA

nucleus

Inferred from direct assay. Source: HPA

   Molecular_functionpoly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

rRNA methyltransferase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

EIF2AK2P195252EBI-744088,EBI-640775
OAS3Q9Y6K52EBI-744088,EBI-6115729

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 847847pre-rRNA processing protein FTSJ3 HAMAP-Rule MF_03163
PRO_0000155577

Regions

Coiled coil355 – 40753 Potential
Coiled coil739 – 77739 Potential

Sites

Active site1571Proton acceptor By similarity
Binding site561S-adenosyl-L-methionine; via amide nitrogen By similarity
Binding site581S-adenosyl-L-methionine; via amide nitrogen By similarity
Binding site761S-adenosyl-L-methionine By similarity
Binding site921S-adenosyl-L-methionine By similarity
Binding site1171S-adenosyl-L-methionine By similarity

Amino acid modifications

Modified residue3331Phosphoserine Ref.11 Ref.13 Ref.18
Modified residue3351Phosphoserine Ref.11 Ref.13 Ref.18
Modified residue3361Phosphoserine Ref.11 Ref.13 Ref.15 Ref.18
Modified residue3471Phosphoserine Ref.11
Modified residue3561Phosphoserine Ref.13
Modified residue3711Phosphothreonine Ref.13
Modified residue3921Citrulline By similarity
Modified residue5491Phosphoserine Ref.13
Modified residue5841Phosphoserine Ref.13 Ref.15 Ref.18
Modified residue6441Phosphoserine Ref.13 Ref.15 Ref.18
Modified residue6761Phosphoserine Ref.15
Modified residue6881Phosphoserine Ref.15
Modified residue7831Citrulline By similarity

Natural variations

Natural variant911Q → E. Ref.1 Ref.2 Ref.5
Corresponds to variant rs2584625 [ dbSNP | Ensembl ].
VAR_023284
Natural variant4241S → C. Ref.1 Ref.2 Ref.5 Ref.6
Corresponds to variant rs2727288 [ dbSNP | Ensembl ].
VAR_023285

Experimental info

Sequence conflict2781E → I in AAL56015. Ref.1
Sequence conflict2781E → I in BAA90924. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q8IY81 [UniParc].

Last modified May 18, 2010. Version 2.
Checksum: 06B2F4D28A48026F

FASTA84796,558
        10         20         30         40         50         60 
MGKKGKVGKS RRDKFYHLAK ETGYRSRSAF KLIQLNRRFQ FLQKARALLD LCAAPGGWLQ 

        70         80         90        100        110        120 
VAAKFMPVSS LIVGVDLVPI KPLPNVVTLQ QDITTERCRQ ALRKELKTWK VDVVLNDGAP 

       130        140        150        160        170        180 
NVGASWVHDA YSQAHLTLMA LRLACDFLAR GGSFITKVFR SRDYQPLLWI FQQLFRRVQA 

       190        200        210        220        230        240 
TKPQASRHES AEIFVVCQGF LAPDKVDSKF FDPKFAFKEV EVQAKTVTEL VTKKKPKAEG 

       250        260        270        280        290        300 
YAEGDLTLYH RTSVTDFLRA ANPVDFLSKA SEIMVDDEEL AQHPATTEDI RVCCQDIRVL 

       310        320        330        340        350        360 
GRKELRSLLN WRTKLRRYVA KKLKEQAKAL DISLSSGEED EGDEEDSTAG TTKQPSKEEE 

       370        380        390        400        410        420 
EEEEEEQLNQ TLAEMKAQEV AELKRKKKKL LREQRKQRER VELKMDLPGV SIADEGETGM 

       430        440        450        460        470        480 
FSLSTIRGHQ LLEEVTQGDM SAADTFLSDL PRDDIYVSDV EDDGDDTSLD SDLDPEELAG 

       490        500        510        520        530        540 
VRGHQGLRDQ KRMRLTEVQD DKEEEEEENP LLVPLEEKAV LQEEQANLWF SKGSFAGIED 

       550        560        570        580        590        600 
DADEALEISQ AQLLFENRRK GRQQQQKQQL PQTPPSCLKT EIMSPLYQDE APKGTEASSG 

       610        620        630        640        650        660 
TEAATGLEGE EKDGISDSDS STSSEEEESW EPLRGKKRSR GPKSDDDGFE IVPIEDPAKH 

       670        680        690        700        710        720 
RILDPEGLAL GAVIASSKKA KRDLIDNSFN RYTFNEDEGE LPEWFVQEEK QHRIRQLPVG 

       730        740        750        760        770        780 
KKEVEHYRKR WREINARPIK KVAEAKARKK RRMLKRLEQT RKKAEAVVNT VDISEREKVA 

       790        800        810        820        830        840 
QLRSLYKKAG LGKEKRHVTY VVAKKGVGRK VRRPAGVRGH FKVVDSRMKK DQRAQQRKEQ 


KKKHKRK 

« Hide

References

« Hide 'large scale' references
[1]Zhang W., Li N., Wan T., Chen T., Cao T.
Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS GLU-91 AND CYS-424.
[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], VARIANTS GLU-91 AND CYS-424.
Tissue: Colon and Placenta.
[3]"DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L. expand/collapse author list , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
Nature 440:1045-1049(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 (SEP-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], VARIANTS GLU-91 AND CYS-424.
Tissue: Placenta and Skin.
[6]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 157-847, VARIANT CYS-424.
Tissue: Melanoma.
[7]"Functional proteomic analysis of human nucleolus."
Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C., Greco A., Hochstrasser D.F., Diaz J.-J.
Mol. Biol. Cell 13:4100-4109(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"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.
[9]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"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-333; SER-335; SER-336 AND SER-347, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"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].
[13]"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-333; SER-335; SER-336; SER-356; THR-371; SER-549; SER-584 AND SER-644, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[14]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"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-336; SER-584; SER-644; SER-676 AND SER-688, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"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].
[17]"The human nucleolar protein FTSJ3 associates with NIP7 and functions in pre-rRNA processing."
Morello L.G., Coltri P.P., Quaresma A.J., Simabuco F.M., Silva T.C., Singh G., Nickerson J.A., Oliveira C.C., Moore M.J., Zanchin N.I.
PLoS ONE 6:E29174-E29174(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH NIP7, SUBCELLULAR LOCATION.
[18]"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-333; SER-335; SER-336; SER-584 AND SER-644, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]"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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF327355 mRNA. Translation: AAL56015.1.
AK000069 mRNA. Translation: BAA90924.1. Different initiation.
AK315010 mRNA. Translation: BAG37502.1.
AC015651 Genomic DNA. No translation available.
CH471109 Genomic DNA. Translation: EAW94273.1.
CH471109 Genomic DNA. Translation: EAW94274.1.
CH471109 Genomic DNA. Translation: EAW94275.1.
BC000131 mRNA. Translation: AAH00131.2.
BC036710 mRNA. Translation: AAH36710.1.
AL834482 mRNA. Translation: CAD39141.1.
RefSeqNP_060117.3. NM_017647.3.
UniGeneHs.463785.

3D structure databases

ProteinModelPortalQ8IY81.
SMRQ8IY81. Positions 24-184.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid125581. 41 interactions.
IntActQ8IY81. 12 interactions.
MINTMINT-1468947.
STRING9606.ENSP00000337518.

PTM databases

PhosphoSiteQ8IY81.

Polymorphism databases

DMDM296452883.

2D gel databases

SWISS-2DPAGEQ8IY81.

Proteomic databases

PaxDbQ8IY81.
PRIDEQ8IY81.

Protocols and materials databases

DNASU117246.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000427159; ENSP00000396673; ENSG00000108592.
GeneID117246.
KEGGhsa:117246.
UCSCuc002jbz.3. human.

Organism-specific databases

CTD117246.
GeneCardsGC17M061896.
HGNCHGNC:17136. FTSJ3.
HPAHPA055544.
neXtProtNX_Q8IY81.
PharmGKBPA28419.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0293.
HOVERGENHBG075246.
InParanoidQ8IY81.
KOK14857.
OMALIWVFNQ.
OrthoDBEOG7WX07S.
PhylomeDBQ8IY81.
TreeFamTF106102.

Gene expression databases

ArrayExpressQ8IY81.
BgeeQ8IY81.
CleanExHS_FTSJ3.
GenevestigatorQ8IY81.

Family and domain databases

HAMAPMF_01547. RNA_methyltr_E.
MF_03163. RNA_methyltr_E_SPB1.
InterProIPR015507. rRNA-MeTfrase_E.
IPR012920. rRNA_MeTfrase_Spb1_C.
IPR024576. rRNA_MeTfrase_Spb1_DUF3381.
IPR002877. rRNA_MeTrfase_FtsJ_dom.
IPR028589. Spb1.
[Graphical view]
PANTHERPTHR10920. PTHR10920. 1 hit.
PTHR10920:SF13. PTHR10920:SF13. 1 hit.
PfamPF11861. DUF3381. 1 hit.
PF01728. FtsJ. 1 hit.
PF07780. Spb1_C. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSFTSJ3. human.
GeneWikiFTSJ3.
GenomeRNAi117246.
NextBio80174.
PROQ8IY81.

Entry information

Entry nameSPB1_HUMAN
AccessionPrimary (citable) accession number: Q8IY81
Secondary accession number(s): B2RCA5 expand/collapse secondary AC list , D3DU22, Q8N3A3, Q8WXX1, Q9BWM4, Q9NXT6
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2005
Last sequence update: May 18, 2010
Last modified: April 16, 2014
This is version 109 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 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 17

Human chromosome 17: entries, gene names and cross-references to MIM