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O00754 (MA2B1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 148. 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·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Lysosomal alpha-mannosidase

Short name=Laman
EC=3.2.1.24
Alternative name(s):
Lysosomal acid alpha-mannosidase
Mannosidase alpha class 2B member 1
Mannosidase alpha-B
Gene names
Name:MAN2B1
Synonyms:LAMAN, MANB
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1011 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Necessary for the catabolism of N-linked carbohydrates released during glycoprotein turnover. Cleaves all known types of alpha-mannosidic linkages.

Catalytic activity

Hydrolysis of terminal, non-reducing alpha-D-mannose residues in alpha-D-mannosides.

Cofactor

Binds 1 zinc ion per subunit By similarity.

Subcellular location

Lysosome.

Post-translational modification

First processed into 3 peptides of 70 kDa, 42 kDa (D) and 13/15 kDa (E). The 70 kDa peptide is further processed into three peptides (A, B and C). The A, B and C peptides are disulfide-linked.

Heavily glycosylated. Ref.9

Involvement in disease

Mannosidosis, alpha B, lysosomal (MANSA) [MIM:248500]: A lysosomal storage disease characterized by accumulation of unbranched oligosaccharide chains. This accumulation is expressed histologically as cytoplasmic vacuolation predominantly in the CNS and parenchymatous organs. Depending on the clinical findings at the age of onset, a severe infantile (type I) and a mild juvenile (type II) form of alpha-mannosidosis are recognized. There is considerable variation in the clinical expression with mental retardation, recurrent infections, impaired hearing and Hurler-like skeletal changes being the most consistent abnormalities.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.2 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16

Sequence similarities

Belongs to the glycosyl hydrolase 38 family.

Sequence caution

The sequence AAB03816.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence AAC50812.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O00754-1)

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: O00754-2)

The sequence of this isoform differs from the canonical sequence as follows:
     343-343: Missing.
Note: Gene prediction based on EST data.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 4949
Chain50 – 1011962Lysosomal alpha-mannosidase
PRO_0000012069
Chain50 – 345296Lysosomal alpha-mannosidase A peptide
PRO_0000012070
Chain346 – 42984Lysosomal alpha-mannosidase B peptide
PRO_0000012071
Chain430 – 601172Lysosomal alpha-mannosidase C peptide
PRO_0000012072
Chain602 – 882281Lysosomal alpha-mannosidase D peptide
PRO_0000012073
Chain883 – 1011129Lysosomal alpha-mannosidase E peptide
PRO_0000012074

Sites

Active site1961Nucleophile By similarity
Metal binding721Zinc By similarity
Metal binding741Zinc By similarity
Metal binding1961Zinc By similarity
Metal binding4461Zinc By similarity

Amino acid modifications

Glycosylation1331N-linked (GlcNAc...) Potential
Glycosylation3101N-linked (GlcNAc...) Potential
Glycosylation3671N-linked (GlcNAc...) Ref.10
Glycosylation4971N-linked (GlcNAc...) Potential
Glycosylation6451N-linked (GlcNAc...) Potential
Glycosylation6511N-linked (GlcNAc...) Potential
Glycosylation6921N-linked (GlcNAc...) Potential
Glycosylation7661N-linked (GlcNAc...) Ref.10
Glycosylation8321N-linked (GlcNAc...) Potential
Glycosylation9301N-linked (GlcNAc...) Ref.9
Glycosylation9891N-linked (GlcNAc...) Potential
Disulfide bond55 ↔ 358 By similarity
Disulfide bond268 ↔ 273 By similarity
Disulfide bond412 ↔ 472 By similarity
Disulfide bond493 ↔ 501 By similarity

Natural variations

Alternative sequence3431Missing in isoform 2.
VSP_047391
Natural variant551C → F in MANSA; results in less than 20% of wild-type enzyme activity. Ref.16
VAR_068034
Natural variant721H → L in MANSA; type II. Ref.2 Ref.12
VAR_003338
Natural variant741D → E in MANSA; results in less than 20% of wild-type enzyme activity. Ref.16
VAR_068035
Natural variant951A → P in MANSA; results in less than 20% of wild-type enzyme activity. Ref.16
VAR_068036
Natural variant991Y → H in MANSA; results in less than 20% of wild-type enzyme activity. Ref.16
VAR_068037
Natural variant1591D → N in MANSA; results in less than 20% of wild-type enzyme activity. Ref.16
VAR_068038
Natural variant1971P → R in MANSA; results in less than 20% of wild-type enzyme activity. Ref.16
VAR_068039
Natural variant2001H → L in MANSA; no residual enzyme activity. Ref.15 Ref.16
VAR_026412
Natural variant2001H → N in MANSA; reduced enzyme activity. Ref.16
VAR_068040
Natural variant2021R → P in MANSA; reduced enzyme activity. Ref.16
VAR_068041
Natural variant2291R → W in MANSA; reduced enzyme activity. Ref.16
VAR_068042
Natural variant2481P → L. Ref.16
Corresponds to variant rs117843968 [ dbSNP | Ensembl ].
VAR_068043
Natural variant2501A → S.
Corresponds to variant rs3745650 [ dbSNP | Ensembl ].
VAR_049209
Natural variant2631P → L in MANSA; results in less than 20% of wild-type enzyme activity. Ref.16
VAR_068044
Natural variant2781L → V. Ref.13 Ref.16
Corresponds to variant rs1054486 [ dbSNP | Ensembl ].
VAR_003339
Natural variant2821P → S. Ref.16
Corresponds to variant rs45576136 [ dbSNP | Ensembl ].
VAR_068045
Natural variant3121T → I. Ref.13 Ref.16
Corresponds to variant rs1054487 [ dbSNP | Ensembl ].
VAR_003340
Natural variant3181S → L in MANSA; reduced enzyme activity. Ref.16
VAR_068046
Natural variant3371R → Q. Ref.13 Ref.16
Corresponds to variant rs1133330 [ dbSNP | Ensembl ].
VAR_003341
Natural variant339 – 3424Missing in MANSA.
VAR_068047
Natural variant3521L → P in MANSA; results in less than 20% of wild-type enzyme activity. Ref.16
VAR_068048
Natural variant3551T → P in MANSA. Ref.13
VAR_003342
Natural variant3561P → R in MANSA; type I. Ref.12
VAR_003343
Natural variant3791P → L in MANSA; reduced enzyme activity. Ref.16
VAR_068049
Natural variant3901G → C in MANSA; results in less than 20% of wild-type enzyme activity. Ref.16
VAR_068050
Natural variant4021E → K in MANSA; unknown pathological significance. Ref.13 Ref.16
VAR_003344
Natural variant4131N → S. Ref.13 Ref.16
Corresponds to variant rs35836657 [ dbSNP | Ensembl ].
VAR_003345
Natural variant4201G → V in MANSA; results in less than 20% of wild-type enzyme activity. Ref.16
VAR_068051
Natural variant4451H → Y in MANSA; results in less than 20% of wild-type enzyme activity. Ref.16
VAR_068052
Natural variant4511G → C in MANSA; reduced enzyme activity. Ref.16
VAR_068053
Natural variant4531S → F in MANSA; reduced enzyme activity. Ref.16
VAR_068054
Natural variant4531S → Y in MANSA. Ref.14 Ref.16
VAR_026413
Natural variant4571V → E in MANSA; reduced enzyme activity. Ref.16
VAR_068055
Natural variant4811A → S. Ref.16
Corresponds to variant rs34544747 [ dbSNP | Ensembl ].
VAR_049210
Natural variant5011C → S in MANSA; reduced enzyme activity. Ref.16
VAR_068056
Natural variant5651L → P in MANSA; results in less than 20% of wild-type enzyme activity. Ref.16
VAR_068057
Natural variant6691P → L. Ref.16
Corresponds to variant rs75029862 [ dbSNP | Ensembl ].
VAR_068058
Natural variant7141W → R in MANSA. Ref.13
VAR_003346
Natural variant7451T → R in MANSA; results in less than 20% of wild-type enzyme activity. Ref.16
VAR_068059
Natural variant7501R → W in MANSA; type II. Ref.12
VAR_003347
Natural variant8001G → R in MANSA; results in less than 20% of wild-type enzyme activity. Ref.16
VAR_068060
Natural variant8001G → W in MANSA; results in less than 20% of wild-type enzyme activity. Ref.16
VAR_068061
Natural variant8011G → D in MANSA; no residual enzyme activity. Ref.15
VAR_026414
Natural variant8091L → P in MANSA. Ref.13
VAR_003348
Natural variant8151R → RHR in MANSA; results in less than 20% of wild-type enzyme activity.
VAR_068062
Natural variant8911G → R in MANSA; results in less than 20% of wild-type enzyme activity. Ref.16
VAR_068063
Natural variant8921L → P in MANSA; results in less than 20% of wild-type enzyme activity. Ref.16
VAR_068064
Natural variant9161R → C in MANSA; results in less than 20% of wild-type enzyme activity. Ref.16
VAR_068065
Natural variant9161R → H in MANSA; results in less than 20% of wild-type enzyme activity. Ref.16
VAR_068066
Natural variant9501R → P in MANSA; results in less than 20% of wild-type enzyme activity. Ref.16
VAR_068067
Natural variant9561L → R in MANSA; results in less than 20% of wild-type enzyme activity. Ref.16
VAR_068068
Natural variant10001F → S in MANSA; results in less than 20% of wild-type enzyme activity. Ref.16
VAR_068069

Experimental info

Sequence conflict31Missing in AAC51362. Ref.3
Sequence conflict1861D → V in AAC34130. Ref.2
Sequence conflict3841P → H in AAC50812. Ref.7

Sequences

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

Last modified October 31, 2006. Version 3.
Checksum: E11C77C19D8BD88C

FASTA1,011113,744
        10         20         30         40         50         60 
MGAYARASGV CARGCLDSAG PWTMSRALRP PLPPLCFFLL LLAAAGARAG GYETCPTVQP 

        70         80         90        100        110        120 
NMLNVHLLPH THDDVGWLKT VDQYFYGIKN DIQHAGVQYI LDSVISALLA DPTRRFIYVE 

       130        140        150        160        170        180 
IAFFSRWWHQ QTNATQEVVR DLVRQGRLEF ANGGWVMNDE AATHYGAIVD QMTLGLRFLE 

       190        200        210        220        230        240 
DTFGNDGRPR VAWHIDPFGH SREQASLFAQ MGFDGFFFGR LDYQDKWVRM QKLEMEQVWR 

       250        260        270        280        290        300 
ASTSLKPPTA DLFTGVLPNG YNPPRNLCWD VLCVDQPLVE DPRSPEYNAK ELVDYFLNVA 

       310        320        330        340        350        360 
TAQGRYYRTN HTVMTMGSDF QYENANMWFK NLDKLIRLVN AQQAKGSSVH VLYSTPACYL 

       370        380        390        400        410        420 
WELNKANLTW SVKHDDFFPY ADGPHQFWTG YFSSRPALKR YERLSYNFLQ VCNQLEALVG 

       430        440        450        460        470        480 
LAANVGPYGS GDSAPLNEAM AVLQHHDAVS GTSRQHVAND YARQLAAGWG PCEVLLSNAL 

       490        500        510        520        530        540 
ARLRGFKDHF TFCQQLNISI CPLSQTAARF QVIVYNPLGR KVNWMVRLPV SEGVFVVKDP 

       550        560        570        580        590        600 
NGRTVPSDVV IFPSSDSQAH PPELLFSASL PALGFSTYSV AQVPRWKPQA RAPQPIPRRS 

       610        620        630        640        650        660 
WSPALTIENE HIRATFDPDT GLLMEIMNMN QQLLLPVRQT FFWYNASIGD NESDQASGAY 

       670        680        690        700        710        720 
IFRPNQQKPL PVSRWAQIHL VKTPLVQEVH QNFSAWCSQV VRLYPGQRHL ELEWSVGPIP 

       730        740        750        760        770        780 
VGDTWGKEVI SRFDTPLETK GRFYTDSNGR EILERRRDYR PTWKLNQTEP VAGNYYPVNT 

       790        800        810        820        830        840 
RIYITDGNMQ LTVLTDRSQG GSSLRDGSLE LMVHRRLLKD DGRGVSEPLM ENGSGAWVRG 

       850        860        870        880        890        900 
RHLVLLDTAQ AAAAGHRLLA EQEVLAPQVV LAPGGGAAYN LGAPPRTQFS GLRRDLPPSV 

       910        920        930        940        950        960 
HLLTLASWGP EMVLLRLEHQ FAVGEDSGRN LSAPVTLNLR DLFSTFTITR LQETTLVANQ 

       970        980        990       1000       1010 
LREAASRLKW TTNTGPTPHQ TPYQLDPANI TLEPMEIRTF LASVQWKEVD G 

« Hide

Isoform 2 [UniParc].

Checksum: BCCA165E4D5D46CA
Show »

FASTA1,010113,616

References

« Hide 'large scale' references
[1]"Human lysosomal alpha-mannosidase: isolation and nucleotide sequence of the full-length cDNA."
Nebes V.L., Schmidt M.C.
Biochem. Biophys. Res. Commun. 200:239-245(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"Alpha-mannosidosis: functional cloning of the lysosomal alpha-mannosidase cDNA and identification of a mutation in two affected siblings."
Nilssen O., Berg T., Riise H.M.F., Ramachandran U., Evjen G., Hansen G.M., Malm D., Tranebjaerg L., Tollersrud O.-K.
Hum. Mol. Genet. 6:717-726(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, VARIANT MANSA LEU-72.
Tissue: Lung and Skin.
[3]"Genomic structure of the human lysosomal alpha-mannosidase gene (MANB)."
Riise H.M.F., Berg T., Nilssen O., Romeo G., Tollersrud O.-K., Ceccherini I.
Genomics 42:200-207(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
[4]"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].
[5]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].
[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 1).
Tissue: Placenta.
[7]"Cloning, expression, purification, and characterization of the human broad specificity lysosomal acid alpha-mannosidase."
Liao Y.-F., Lal A., Moremen K.W.
J. Biol. Chem. 271:28348-28358(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 9-1010 (ISOFORM 1).
Tissue: Spleen.
[8]"Partial sequence of the purified protein confirms the identity of cDNA coding for human lysosomal alpha-mannosidase B."
Emiliani C., Martino S., Stirling J.L., Maras B., Orlacchio A.
Biochem. J. 305:363-366(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE.
[9]"Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry."
Zhang H., Li X.-J., Martin D.B., Aebersold R.
Nat. Biotechnol. 21:660-666(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT ASN-930.
[10]"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-367 AND ASN-766.
Tissue: Liver.
[11]"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].
[12]"Missense and nonsense mutations in the lysosomal alpha-mannosidase gene (MANB) in severe and mild forms of alpha-mannosidosis."
Gotoda Y., Wakamatsu N., Kawai H., Nishida Y., Matsumoto T.
Am. J. Hum. Genet. 63:1015-1024(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS MANSA LEU-72; ARG-356 AND TRP-750.
[13]"Spectrum of mutations in alpha-mannosidosis."
Berg T., Riise H.M.F., Hansen G.M., Malm D., Tranebjaerg L., Tollersrud O.-K., Nilssen O.
Am. J. Hum. Genet. 64:77-88(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS MANSA PRO-355; LYS-402; ARG-714 AND PRO-809, VARIANTS VAL-278; ILE-312; GLN-337 AND SER-413.
[14]"Alpha-mannosidosis and mutational analysis in a Turkish patient."
Oelmez A., Nilssen O., Coskun T., Klenow H.
Turk. J. Pediatr. 45:46-50(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT MANSA TYR-453.
[15]"Identification and characterization of five novel MAN2B1 mutations in Italian patients with alpha-mannosidosis."
Sbaragli M., Bibi L., Pittis M.G., Balducci C., Heikinheimo P., Ricci R., Antuzzi D., Parini R., Spaccini L., Bembi B., Beccari T.
Hum. Mutat. 25:320-320(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS MANSA LEU-200 AND ASP-801, CHARACTERIZATION OF VARIANTS MANSA LEU-200 AND ASP-801.
[16]"Identification of 83 novel alpha-mannosidosis-associated sequence variants: functional analysis of MAN2B1 missense mutations."
Riise Stensland H.M., Klenow H.B., Van Nguyen L., Hansen G.M., Malm D., Nilssen O.
Hum. Mutat. 33:511-520(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS MANSA PHE-55; GLU-74; PRO-95; HIS-99; ASN-159; ARG-197; ASN-200; LEU-200; PRO-202; TRP-229; LEU-263; LEU-318; 339-VAL--GLN-342 DEL; PRO-352; LEU-379; CYS-390; LYS-402; VAL-420; TYR-445; CYS-451; TYR-453; PHE-453; GLU-457; SER-501; PRO-565; ARG-745; ARG-800; TRP-800; HIS-ARG-815 INS; ARG-891; PRO-892; CYS-916; HIS-916; PRO-950; ARG-956 AND SER-1000, VARIANTS LEU-248; VAL-278; SER-282; ILE-312; GLN-337; SER-413; SER-481 AND LEU-669, CHARACTERIZATION OF VARIANTS MANSA PHE-55; GLU-74; PRO-95; HIS-99; ASN-159; ARG-197; ASN-200; LEU-200; PRO-202; TRP-229; LEU-263; LEU-318; PRO-352; LEU-379; CYS-390; LYS-402; VAL-420; TYR-445; CYS-451; TYR-453; PHE-453; GLU-457; SER-501; PRO-565; ARG-745; ARG-800; TRP-800; HIS-ARG-815 INS; ARG-891; PRO-892; CYS-916; HIS-916; PRO-950; ARG-956 AND SER-1000.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U05572 mRNA. Translation: AAB03816.1. Different initiation.
U60266 mRNA. Translation: AAC34130.1.
U60899 expand/collapse EMBL AC list , U60885, U60886, U60887, U60888, U60889, U60890, U60891, U60892, U60893, U60894, U60895, U60896, U60897, U60898 Genomic DNA. Translation: AAC51362.1.
AC010422 Genomic DNA. No translation available.
CH471106 Genomic DNA. Translation: EAW84279.1.
BC000736 mRNA. Translation: AAH00736.1.
U68567 mRNA. Translation: AAC50812.1. Different initiation.
CCDSCCDS32919.1. [O00754-1]
CCDS54224.1. [O00754-2]
RefSeqNP_000519.2. NM_000528.3. [O00754-1]
NP_001166969.1. NM_001173498.1. [O00754-2]
UniGeneHs.356769.
Hs.657204.

3D structure databases

ProteinModelPortalO00754.
SMRO00754. Positions 51-341, 349-420, 431-584, 605-874, 885-1006.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110298. 6 interactions.
IntActO00754. 1 interaction.
MINTMINT-253662.
STRING9606.ENSP00000395473.

Chemistry

BindingDBO00754.
ChEMBLCHEMBL4059.

Protein family/group databases

CAZyGH38. Glycoside Hydrolase Family 38.

PTM databases

PhosphoSiteO00754.

Proteomic databases

MaxQBO00754.
PaxDbO00754.
PRIDEO00754.

Protocols and materials databases

DNASU4125.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000221363; ENSP00000221363; ENSG00000104774. [O00754-2]
ENST00000456935; ENSP00000395473; ENSG00000104774. [O00754-1]
GeneID4125.
KEGGhsa:4125.
UCSCuc002mub.2. human. [O00754-1]
uc010dyv.1. human.

Organism-specific databases

CTD4125.
GeneCardsGC19M012757.
GeneReviewsMAN2B1.
HGNCHGNC:6826. MAN2B1.
HPAHPA041530.
MIM248500. phenotype.
609458. gene.
neXtProtNX_O00754.
Orphanet309288. Alpha-mannosidosis, adult form.
309282. Alpha-mannosidosis, infantile form.
PharmGKBPA30575.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG306356.
HOGENOMHOG000007676.
HOVERGENHBG052391.
InParanoidO00754.
KOK12311.
OMANMQLTVL.
OrthoDBEOG786H2P.
PhylomeDBO00754.
TreeFamTF313840.

Enzyme and pathway databases

BRENDA3.2.1.24. 2681.

Gene expression databases

ArrayExpressO00754.
BgeeO00754.
CleanExHS_MAN2B1.
GenevestigatorO00754.

Family and domain databases

Gene3D1.20.1270.50. 1 hit.
2.60.40.1180. 1 hit.
3.20.110.10. 1 hit.
InterProIPR011013. Gal_mutarotase_SF_dom.
IPR011330. Glyco_hydro/deAcase_b/a-brl.
IPR013780. Glyco_hydro_13_b.
IPR027291. Glyco_hydro_38/57_N.
IPR011682. Glyco_hydro_38_C.
IPR015341. Glyco_hydro_38_cen.
IPR000602. Glyco_hydro_38_N.
IPR028995. Glyco_hydro_57/38_cen.
[Graphical view]
PfamPF09261. Alpha-mann_mid. 1 hit.
PF01074. Glyco_hydro_38. 1 hit.
PF07748. Glyco_hydro_38C. 1 hit.
[Graphical view]
SMARTSM00872. Alpha-mann_mid. 1 hit.
[Graphical view]
SUPFAMSSF74650. SSF74650. 1 hit.
SSF88688. SSF88688. 1 hit.
SSF88713. SSF88713. 1 hit.
ProtoNetSearch...

Other

ChiTaRSMAN2B1. human.
GenomeRNAi4125.
NextBio16196.
PROO00754.
SOURCESearch...

Entry information

Entry nameMA2B1_HUMAN
AccessionPrimary (citable) accession number: O00754
Secondary accession number(s): G5E928 expand/collapse secondary AC list , O15330, Q16680, Q93094, Q9BW13
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: October 31, 2006
Last modified: July 9, 2014
This is version 148 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

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

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries