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Q8WWR8

- NEUR4_HUMAN

UniProt

Q8WWR8 - NEUR4_HUMAN

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Protein
Sialidase-4
Gene
NEU4, LP5125
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

May function in lysosomal catabolism of sialylated glycoconjugates. Has sialidase activity towards synthetic substrates, such as 2'-(4-methylumbelliferyl)-alpha-D-N-acetylneuraminic acid (4-MU-NANA or 4MU-NeuAc). Has a broad substrate specificity being active on glycoproteins, oligosaccharides and sialylated glycolipids.2 Publications

Catalytic activityi

Hydrolysis of alpha-(2->3)-, alpha-(2->6)-, alpha-(2->8)- glycosidic linkages of terminal sialic acid residues in oligosaccharides, glycoproteins, glycolipids, colominic acid and synthetic substrates.1 Publication

pH dependencei

Optimum pH is 3.2.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei23 – 231Substrate By similarity
Binding sitei43 – 431Substrate By similarity
Active sitei47 – 471Proton acceptor By similarity
Active sitei48 – 481Proton acceptor By similarity
Binding sitei177 – 1771Substrate By similarity
Binding sitei179 – 1791Substrate By similarity
Binding sitei222 – 2221Substrate By similarity
Binding sitei242 – 2421Substrate By similarity
Binding sitei389 – 3891Substrate By similarity
Active sitei419 – 4191Nucleophile By similarity
Active sitei440 – 4401 Reviewed prediction

GO - Molecular functioni

  1. exo-alpha-(2->3)-sialidase activity Source: UniProtKB-EC
  2. exo-alpha-(2->6)-sialidase activity Source: UniProtKB-EC
  3. exo-alpha-(2->8)-sialidase activity Source: UniProtKB-EC
  4. exo-alpha-sialidase activity Source: UniProtKB
  5. protein binding Source: IntAct

GO - Biological processi

  1. ganglioside catabolic process Source: UniProtKB
  2. glycoprotein catabolic process Source: UniProtKB
  3. glycosphingolipid metabolic process Source: Reactome
  4. oligosaccharide catabolic process Source: UniProtKB
  5. small molecule metabolic process Source: Reactome
  6. sphingolipid metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Lipid degradation, Lipid metabolism

Enzyme and pathway databases

BRENDAi3.2.1.18. 2681.
ReactomeiREACT_116105. Glycosphingolipid metabolism.
REACT_200874. Sialic acid metabolism.
SABIO-RKQ8WWR8.

Protein family/group databases

CAZyiGH33. Glycoside Hydrolase Family 33.

Names & Taxonomyi

Protein namesi
Recommended name:
Sialidase-4 (EC:3.2.1.18)
Alternative name(s):
N-acetyl-alpha-neuraminidase 4
Gene namesi
Name:NEU4
ORF Names:LP5125
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:21328. NEU4.

Subcellular locationi

Isoform 1 : Membrane; Peripheral membrane protein 2 Publications
Isoform 2 : Lysosome lumen
Note: According to 1 Publication, isoform 2 is soluble, N-glycosylated and found in the lumen of lysosomes. However, no signal sequence nor N-glycosylation site is predicted from the sequence.2 Publications

GO - Cellular componenti

  1. lysosomal lumen Source: Reactome
  2. lysosome Source: UniProtKB
  3. mitochondrion Source: Ensembl
  4. organelle inner membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Lysosome, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134917116.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 484484Sialidase-4
PRO_0000208906Add
BLAST

Post-translational modificationi

According to 1 Publication, phosphorylation of mannose residues may ensure efficient transport of isoform 2 to the lysosomes via the mannose 6-phosphate receptor.
Isoform 2 is glycosylated (1 Publication).1 Publication

Proteomic databases

PaxDbiQ8WWR8.
PRIDEiQ8WWR8.

PTM databases

PhosphoSiteiQ8WWR8.

Expressioni

Tissue specificityi

Ubiquitous with higher expression in heart, skeletal muscle, liver and placenta.1 Publication

Inductioni

Down-regulated during monocyte to macrophage differentiation.1 Publication

Gene expression databases

ArrayExpressiQ8WWR8.
BgeeiQ8WWR8.
CleanExiHS_NEU4.
GenevestigatoriQ8WWR8.

Organism-specific databases

HPAiHPA037394.
HPA037395.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
MDFIQ997504EBI-746964,EBI-724076
PLSCR1O151622EBI-746964,EBI-740019

Protein-protein interaction databases

BioGridi126209. 5 interactions.
IntActiQ8WWR8. 5 interactions.
MINTiMINT-1447950.
STRINGi9606.ENSP00000385149.

Structurei

3D structure databases

ProteinModelPortaliQ8WWR8.
SMRiQ8WWR8. Positions 22-344, 371-461.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati127 – 13812BNR 1
Add
BLAST
Repeati200 – 21112BNR 2
Add
BLAST
Repeati251 – 26212BNR 3
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi22 – 254FRIP motif

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi284 – 37592Pro-rich
Add
BLAST

Sequence similaritiesi

Contains 3 BNR repeats.

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG84455.
HOGENOMiHOG000233778.
HOVERGENiHBG052608.
InParanoidiQ8WWR8.
KOiK12357.
OMAiMNPCPVL.
OrthoDBiEOG7MSMNP.
PhylomeDBiQ8WWR8.
TreeFamiTF331063.

Family and domain databases

Gene3Di2.120.10.10. 2 hits.
InterProiIPR026946. Sialidase-4.
IPR026856. Sialidase_fam.
IPR011040. Sialidases.
[Graphical view]
PANTHERiPTHR10628. PTHR10628. 1 hit.
PTHR10628:SF8. PTHR10628:SF8. 1 hit.
SUPFAMiSSF50939. SSF50939. 2 hits.

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q8WWR8-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MGVPRTPSRT VLFERERTGL TYRVPSLLPV PPGPTLLAFV EQRLSPDDSH    50
AHRLVLRRGT LAGGSVRWGA LHVLGTAALA EHRSMNPCPV HDAGTGTVFL 100
FFIAVLGHTP EAVQIATGRN AARLCCVASR DAGLSWGSAR DLTEEAIGGA 150
VQDWATFAVG PGHGVQLPSG RLLVPAYTYR VDRRECFGKI CRTSPHSFAF 200
YSDDHGRTWR CGGLVPNLRS GECQLAAVDG GQAGSFLYCN ARSPLGSRVQ 250
ALSTDEGTSF LPAERVASLP ETAWGCQGSI VGFPAPAPNR PRDDSWSVGP 300
GSPLQPPLLG PGVHEPPEEA AVDPRGGQVP GGPFSRLQPR GDGPRQPGPR 350
PGVSGDVGSW TLALPMPFAA PPQSPTWLLY SHPVGRRARL HMGIRLSQSP 400
LDPRSWTEPW VIYEGPSGYS DLASIGPAPE GGLVFACLYE SGARTSYDEI 450
SFCTFSLREV LENVPASPKP PNLGDKPRGC CWPS 484
Length:484
Mass (Da):51,572
Last modified:March 7, 2006 - v3
Checksum:i14A878C2A9F18863
GO
Isoform 2 (identifier: Q8WWR8-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MMSSAAFPRWLSM

Show »
Length:496
Mass (Da):52,938
Checksum:i1DE1395862011A36
GO
Isoform 3 (identifier: Q8WWR8-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MMSSAAFPRWLQSM

Note: Gene prediction based on EST data.

Show »
Length:497
Mass (Da):53,066
Checksum:iC933EFAEC7383F69
GO

Sequence cautioni

The sequence AAP34475.1 differs from that shown. Reason: Frameshift at position 291.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti301 – 3011G → R.3 Publications
Corresponds to variant rs11545301 [ dbSNP | Ensembl ].
VAR_067458

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MMSSAAFPRWLSM in isoform 2.
VSP_037491
Alternative sequencei1 – 11M → MMSSAAFPRWLQSM in isoform 3.
VSP_047123

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti184 – 1841R → L in CAC81904. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ277883 mRNA. Translation: CAC81904.1.
AK289421 mRNA. Translation: BAF82110.1.
AY203952 mRNA. Translation: AAP34475.1. Frameshift.
AC114730 Genomic DNA. Translation: AAX82022.1.
CH471063 Genomic DNA. Translation: EAW71296.1.
BC012899 mRNA. Translation: AAH12899.2.
CCDSiCCDS2553.1. [Q8WWR8-2]
CCDS54441.1. [Q8WWR8-3]
CCDS54442.1. [Q8WWR8-1]
RefSeqiNP_001161071.1. NM_001167599.2. [Q8WWR8-3]
NP_001161072.1. NM_001167600.2. [Q8WWR8-1]
NP_001161073.1. NM_001167601.2. [Q8WWR8-1]
NP_001161074.1. NM_001167602.2. [Q8WWR8-1]
NP_542779.2. NM_080741.3. [Q8WWR8-2]
UniGeneiHs.551747.

Genome annotation databases

EnsembliENST00000325935; ENSP00000320318; ENSG00000204099. [Q8WWR8-3]
ENST00000391969; ENSP00000375830; ENSG00000204099. [Q8WWR8-1]
ENST00000404257; ENSP00000385149; ENSG00000204099. [Q8WWR8-2]
ENST00000405370; ENSP00000384804; ENSG00000204099. [Q8WWR8-1]
ENST00000407683; ENSP00000385402; ENSG00000204099. [Q8WWR8-1]
GeneIDi129807.
KEGGihsa:129807.
UCSCiuc002wcm.3. human. [Q8WWR8-1]
uc002wcn.2. human. [Q8WWR8-2]
uc002wcp.2. human.

Polymorphism databases

DMDMi90110434.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ277883 mRNA. Translation: CAC81904.1 .
AK289421 mRNA. Translation: BAF82110.1 .
AY203952 mRNA. Translation: AAP34475.1 . Frameshift.
AC114730 Genomic DNA. Translation: AAX82022.1 .
CH471063 Genomic DNA. Translation: EAW71296.1 .
BC012899 mRNA. Translation: AAH12899.2 .
CCDSi CCDS2553.1. [Q8WWR8-2 ]
CCDS54441.1. [Q8WWR8-3 ]
CCDS54442.1. [Q8WWR8-1 ]
RefSeqi NP_001161071.1. NM_001167599.2. [Q8WWR8-3 ]
NP_001161072.1. NM_001167600.2. [Q8WWR8-1 ]
NP_001161073.1. NM_001167601.2. [Q8WWR8-1 ]
NP_001161074.1. NM_001167602.2. [Q8WWR8-1 ]
NP_542779.2. NM_080741.3. [Q8WWR8-2 ]
UniGenei Hs.551747.

3D structure databases

ProteinModelPortali Q8WWR8.
SMRi Q8WWR8. Positions 22-344, 371-461.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 126209. 5 interactions.
IntActi Q8WWR8. 5 interactions.
MINTi MINT-1447950.
STRINGi 9606.ENSP00000385149.

Chemistry

BindingDBi Q8WWR8.
ChEMBLi CHEMBL4174.

Protein family/group databases

CAZyi GH33. Glycoside Hydrolase Family 33.

PTM databases

PhosphoSitei Q8WWR8.

Polymorphism databases

DMDMi 90110434.

Proteomic databases

PaxDbi Q8WWR8.
PRIDEi Q8WWR8.

Protocols and materials databases

DNASUi 129807.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000325935 ; ENSP00000320318 ; ENSG00000204099 . [Q8WWR8-3 ]
ENST00000391969 ; ENSP00000375830 ; ENSG00000204099 . [Q8WWR8-1 ]
ENST00000404257 ; ENSP00000385149 ; ENSG00000204099 . [Q8WWR8-2 ]
ENST00000405370 ; ENSP00000384804 ; ENSG00000204099 . [Q8WWR8-1 ]
ENST00000407683 ; ENSP00000385402 ; ENSG00000204099 . [Q8WWR8-1 ]
GeneIDi 129807.
KEGGi hsa:129807.
UCSCi uc002wcm.3. human. [Q8WWR8-1 ]
uc002wcn.2. human. [Q8WWR8-2 ]
uc002wcp.2. human.

Organism-specific databases

CTDi 129807.
GeneCardsi GC02P242770.
HGNCi HGNC:21328. NEU4.
HPAi HPA037394.
HPA037395.
MIMi 608527. gene.
neXtProti NX_Q8WWR8.
PharmGKBi PA134917116.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG84455.
HOGENOMi HOG000233778.
HOVERGENi HBG052608.
InParanoidi Q8WWR8.
KOi K12357.
OMAi MNPCPVL.
OrthoDBi EOG7MSMNP.
PhylomeDBi Q8WWR8.
TreeFami TF331063.

Enzyme and pathway databases

BRENDAi 3.2.1.18. 2681.
Reactomei REACT_116105. Glycosphingolipid metabolism.
REACT_200874. Sialic acid metabolism.
SABIO-RK Q8WWR8.

Miscellaneous databases

GeneWikii NEU4.
GenomeRNAii 129807.
NextBioi 35534929.
PROi Q8WWR8.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q8WWR8.
Bgeei Q8WWR8.
CleanExi HS_NEU4.
Genevestigatori Q8WWR8.

Family and domain databases

Gene3Di 2.120.10.10. 2 hits.
InterProi IPR026946. Sialidase-4.
IPR026856. Sialidase_fam.
IPR011040. Sialidases.
[Graphical view ]
PANTHERi PTHR10628. PTHR10628. 1 hit.
PTHR10628:SF8. PTHR10628:SF8. 1 hit.
SUPFAMi SSF50939. SSF50939. 2 hits.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and characterization of NEU4, the fourth member of the human sialidase gene family."
    Monti E., Bassi M.T., Bresciani R., Civini S., Croci G.L., Papini N., Riboni M., Zanchetti G., Ballabio A., Preti A., Tettamanti G., Venerando B., Borsani G.
    Genomics 83:445-453(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, VARIANT ARG-301.
    Tissue: Fibroblast.
  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.
    , 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], VARIANT ARG-301.
    Tissue: Mammary gland.
  3. "Large-scale cDNA transfection screening for genes related to cancer development and progression."
    Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.
    , Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.
    Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT ARG-301.
  4. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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 2).
    Tissue: Oligodendroglioma.
  7. "Neu4, a novel human lysosomal lumen sialidase, confers normal phenotype to sialidosis and galactosialidosis cells."
    Seyrantepe V., Landry K., Trudel S., Hassan J.A., Morales C.R., Pshezhetsky A.V.
    J. Biol. Chem. 279:37021-37029(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, ALTERNATIVE SPLICING (ISOFORM 2), CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, GLYCOSYLATION.
  8. "Differential expression of endogenous sialidases of human monocytes during cellular differentiation into macrophages."
    Stamatos N.M., Liang F., Nan X., Landry K., Cross A.S., Wang L.X., Pshezhetsky A.V.
    FEBS J. 272:2545-2556(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.

Entry informationi

Entry nameiNEUR4_HUMAN
AccessioniPrimary (citable) accession number: Q8WWR8
Secondary accession number(s): A8K056, J3KNJ5, Q96D64
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: March 7, 2006
Last modified: September 3, 2014
This is version 109 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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