SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q9UKM7

- MA1B1_HUMAN

UniProt

Q9UKM7 - MA1B1_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Endoplasmic reticulum mannosyl-oligosaccharide 1,2-alpha-mannosidase
Gene
MAN1B1, UNQ747/PRO1477
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Involved in glycoprotein quality control targeting of misfolded glycoproteins for degradation. It primarily trims a single alpha-1,2-linked mannose residue from Man9GlcNAc2 to produce Man8GlcNAc2, but at high enzyme concentrations, as found in the ER quality control compartment (ERQC), it further trims the carbohydrates to Man5-6GlcNAc2.2 Publications

Catalytic activityi

Hydrolysis of the terminal (1->2)-linked alpha-D-mannose residues in the oligo-mannose oligosaccharide Man9(GlcNAc)2.3 Publications

Cofactori

Calcium.

Enzyme regulationi

Inhibited by both 1-deoxymannojirimycin (dMNJ) and kifunensine.1 Publication

Kineticsi

  1. KM=0.4 mM for Man9GlcNAc21 Publication

pH dependencei

Optimum pH is between 6.5 and 6.9.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei330 – 3301Proton donor Inferred
Active sitei463 – 4631 Inferred
Active sitei599 – 5991 Inferred

GO - Molecular functioni

  1. calcium ion binding Source: UniProtKB
  2. mannosyl-oligosaccharide 1,2-alpha-mannosidase activity Source: UniProtKB

GO - Biological processi

  1. ER-associated ubiquitin-dependent protein catabolic process Source: UniProtKB
  2. cellular protein metabolic process Source: Reactome
  3. oligosaccharide metabolic process Source: ProtInc
  4. post-translational protein modification Source: Reactome
  5. protein N-linked glycosylation Source: UniProtKB
  6. protein N-linked glycosylation via asparagine Source: Reactome
  7. protein folding Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Ligandi

Calcium

Enzyme and pathway databases

BRENDAi3.2.1.113. 2681.
ReactomeiREACT_25091. ER Quality Control Compartment (ERQC).
UniPathwayiUPA00378.

Protein family/group databases

CAZyiGH47. Glycoside Hydrolase Family 47.

Names & Taxonomyi

Protein namesi
Recommended name:
Endoplasmic reticulum mannosyl-oligosaccharide 1,2-alpha-mannosidase (EC:3.2.1.113)
Alternative name(s):
ER alpha-1,2-mannosidase
ER mannosidase 1
Short name:
ERMan1
Man9GlcNAc2-specific-processing alpha-mannosidase
Mannosidase alpha class 1B member 1
Gene namesi
Name:MAN1B1
ORF Names:UNQ747/PRO1477
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 9

Organism-specific databases

HGNCiHGNC:6823. MAN1B1.

Subcellular locationi

Endoplasmic reticulum membrane; Single-pass type II membrane protein 1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 8484Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei85 – 10521Helical; Signal-anchor for type II membrane protein; Reviewed prediction
Add
BLAST
Topological domaini106 – 699594Lumenal Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum Source: UniProtKB
  2. endoplasmic reticulum membrane Source: UniProtKB-SubCell
  3. endoplasmic reticulum quality control compartment Source: Reactome
  4. integral component of membrane Source: UniProtKB
  5. membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Involvement in diseasei

Mental retardation, autosomal recessive 15 (MRT15) [MIM:614202]: 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.1 Publication
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti334 – 3341R → C in MRT15; results in about 1300-fold decrease in activity. 1 Publication
VAR_066592
Natural varianti397 – 3971E → K in MRT15; disrupts stable protein expression. 1 Publication
VAR_066593

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi330 – 3301E → Q: About 44-fold reduction in K(cat), slight reduction in K(m), about 100-fold increase in binding affinity for Man(9)GlcnAc(2) but no change in binding affinity for the inhibitor, dMNJ. Even further greater reduction in K(cat) and increase in K(m); when associated with Q-599. 1 Publication
Mutagenesisi463 – 4631D → N: Some reduction in K(cat) but no change in K(m), abolishes almost all binding to Man(9)GlcnAc(2) but reduced binding to the inhibitor dMNJ by about 73-fold. Further reduction in K(m) but slight increase in K(m); when associated with Q-599. 1 Publication
Mutagenesisi524 – 5241H → A: About 4-fold reduction in K(cat). 1 Publication
Mutagenesisi599 – 5991E → Q: Very significant reduction in K(cat), 4-fold weaker binding affinity for Man(9)GlcnAc(2) but about 1000-fold reduction in binding affinity for the inhibitor, dMNJ. Significant reductions in K(cat) and slight increase in K(m); when associated with E-330 or N-463. 1 Publication

Keywords - Diseasei

Disease mutation, Mental retardation

Organism-specific databases

MIMi614202. phenotype.
Orphaneti88616. Autosomal recessive nonsyndromic intellectual disability.
PharmGKBiPA30572.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 699699Endoplasmic reticulum mannosyl-oligosaccharide 1,2-alpha-mannosidase
PRO_0000210314Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi527 ↔ 5561 Publication

Keywords - PTMi

Disulfide bond

Proteomic databases

MaxQBiQ9UKM7.
PaxDbiQ9UKM7.
PRIDEiQ9UKM7.

PTM databases

PhosphoSiteiQ9UKM7.

Expressioni

Tissue specificityi

Widely expressed.2 Publications

Gene expression databases

ArrayExpressiQ9UKM7.
BgeeiQ9UKM7.
CleanExiHS_MAN1B1.
GenevestigatoriQ9UKM7.

Organism-specific databases

HPAiHPA051516.

Interactioni

Protein-protein interaction databases

BioGridi116414. 4 interactions.
IntActiQ9UKM7. 2 interactions.
MINTiMINT-6610355.
STRINGi9606.ENSP00000360645.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi244 – 2463
Helixi248 – 26720
Beta strandi271 – 2755
Turni276 – 2794
Beta strandi280 – 2823
Beta strandi284 – 2874
Helixi289 – 30012
Helixi304 – 31714
Beta strandi325 – 3273
Helixi328 – 34619
Helixi349 – 36214
Helixi363 – 3664
Beta strandi368 – 3703
Beta strandi375 – 3784
Turni379 – 3813
Beta strandi391 – 3944
Helixi395 – 3995
Helixi402 – 41211
Helixi416 – 42914
Beta strandi441 – 4444
Turni445 – 4473
Beta strandi450 – 4523
Turni460 – 4623
Helixi463 – 47513
Helixi481 – 49717
Beta strandi499 – 5013
Turni503 – 5053
Beta strandi508 – 5103
Beta strandi512 – 5143
Beta strandi517 – 5193
Beta strandi521 – 5233
Helixi524 – 5274
Helixi528 – 53811
Helixi543 – 56119
Beta strandi563 – 5664
Beta strandi570 – 5734
Beta strandi584 – 5863
Helixi589 – 5913
Helixi599 – 61113
Helixi615 – 63016
Helixi659 – 6624
Helixi664 – 6729
Turni676 – 6794
Turni681 – 6833
Beta strandi684 – 6863
Beta strandi692 – 6943

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FMIX-ray1.90A243-697[»]
1FO2X-ray2.38A243-699[»]
1FO3X-ray1.75A243-699[»]
1X9DX-ray1.41A172-699[»]
ProteinModelPortaliQ9UKM7.
SMRiQ9UKM7. Positions 243-697.

Miscellaneous databases

EvolutionaryTraceiQ9UKM7.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi39 – 457Poly-Pro

Sequence similaritiesi

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG300315.
HOGENOMiHOG000181987.
HOVERGENiHBG052389.
KOiK01230.
OMAiVHFNLHA.
OrthoDBiEOG7ZGX2S.
PhylomeDBiQ9UKM7.
TreeFamiTF354274.

Family and domain databases

Gene3Di1.50.10.50. 1 hit.
InterProiIPR001382. Glyco_hydro_47.
[Graphical view]
PANTHERiPTHR11742. PTHR11742. 1 hit.
PfamiPF01532. Glyco_hydro_47. 1 hit.
[Graphical view]
PRINTSiPR00747. GLYHDRLASE47.
SUPFAMiSSF48225. SSF48225. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9UKM7-1 [UniParc]FASTAAdd to Basket

« Hide

MAACEGRRSG ALGSSQSDFL TPPVGGAPWA VATTVVMYPP PPPPPHRDFI    50
SVTLSFGENY DNSKSWRRRS CWRKWKQLSR LQRNMILFLL AFLLFCGLLF 100
YINLADHWKA LAFRLEEEQK MRPEIAGLKP ANPPVLPAPQ KADTDPENLP 150
EISSQKTQRH IQRGPPHLQI RPPSQDLKDG TQEEATKRQE APVDPRPEGD 200
PQRTVISWRG AVIEPEQGTE LPSRRAEVPT KPPLPPARTQ GTPVHLNYRQ 250
KGVIDVFLHA WKGYRKFAWG HDELKPVSRS FSEWFGLGLT LIDALDTMWI 300
LGLRKEFEEA RKWVSKKLHF EKDVDVNLFE STIRILGGLL SAYHLSGDSL 350
FLRKAEDFGN RLMPAFRTPS KIPYSDVNIG TGVAHPPRWT SDSTVAEVTS 400
IQLEFRELSR LTGDKKFQEA VEKVTQHIHG LSGKKDGLVP MFINTHSGLF 450
THLGVFTLGA RADSYYEYLL KQWIQGGKQE TQLLEDYVEA IEGVRTHLLR 500
HSEPSKLTFV GELAHGRFSA KMDHLVCFLP GTLALGVYHG LPASHMELAQ 550
ELMETCYQMN RQMETGLSPE IVHFNLYPQP GRRDVEVKPA DRHNLLRPET 600
VESLFYLYRV TGDRKYQDWG WEILQSFSRF TRVPSGGYSS INNVQDPQKP 650
EPRDKMESFF LGETLKYLFL LFSDDPNLLS LDAYVFNTEA HPLPIWTPA 699
Length:699
Mass (Da):79,580
Last modified:March 7, 2006 - v2
Checksum:iB8BF3BE333D90261
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti59 – 591N → S.4 Publications
Corresponds to variant rs968733 [ dbSNP | Ensembl ].
VAR_055841
Natural varianti334 – 3341R → C in MRT15; results in about 1300-fold decrease in activity. 1 Publication
VAR_066592
Natural varianti397 – 3971E → K in MRT15; disrupts stable protein expression. 1 Publication
VAR_066593

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti204 – 2041T → A in AAD45504. 1 Publication
Sequence conflicti223 – 2231S → P in AAD45504. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF148509 mRNA. Translation: AAF03215.1.
AF145732 mRNA. Translation: AAD45504.1.
AY358465 mRNA. Translation: AAQ88830.1.
AL929554, AL807752 Genomic DNA. Translation: CAH72887.1.
AL807752, AL929554 Genomic DNA. Translation: CAI12781.1.
BC002953 mRNA. Translation: AAH02953.1.
BC006079 mRNA. Translation: AAH06079.1.
CCDSiCCDS7029.1.
RefSeqiNP_057303.2. NM_016219.4.
UniGeneiHs.279881.

Genome annotation databases

EnsembliENST00000371589; ENSP00000360645; ENSG00000177239.
GeneIDi11253.
KEGGihsa:11253.
UCSCiuc004cld.3. human.

Polymorphism databases

DMDMi93195043.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF148509 mRNA. Translation: AAF03215.1 .
AF145732 mRNA. Translation: AAD45504.1 .
AY358465 mRNA. Translation: AAQ88830.1 .
AL929554 , AL807752 Genomic DNA. Translation: CAH72887.1 .
AL807752 , AL929554 Genomic DNA. Translation: CAI12781.1 .
BC002953 mRNA. Translation: AAH02953.1 .
BC006079 mRNA. Translation: AAH06079.1 .
CCDSi CCDS7029.1.
RefSeqi NP_057303.2. NM_016219.4.
UniGenei Hs.279881.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1FMI X-ray 1.90 A 243-697 [» ]
1FO2 X-ray 2.38 A 243-699 [» ]
1FO3 X-ray 1.75 A 243-699 [» ]
1X9D X-ray 1.41 A 172-699 [» ]
ProteinModelPortali Q9UKM7.
SMRi Q9UKM7. Positions 243-697.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116414. 4 interactions.
IntActi Q9UKM7. 2 interactions.
MINTi MINT-6610355.
STRINGi 9606.ENSP00000360645.

Chemistry

BindingDBi Q9UKM7.
ChEMBLi CHEMBL2308.

Protein family/group databases

CAZyi GH47. Glycoside Hydrolase Family 47.

PTM databases

PhosphoSitei Q9UKM7.

Polymorphism databases

DMDMi 93195043.

Proteomic databases

MaxQBi Q9UKM7.
PaxDbi Q9UKM7.
PRIDEi Q9UKM7.

Protocols and materials databases

DNASUi 11253.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000371589 ; ENSP00000360645 ; ENSG00000177239 .
GeneIDi 11253.
KEGGi hsa:11253.
UCSCi uc004cld.3. human.

Organism-specific databases

CTDi 11253.
GeneCardsi GC09P139981.
H-InvDB HIX0035043.
HGNCi HGNC:6823. MAN1B1.
HPAi HPA051516.
MIMi 604346. gene.
614202. phenotype.
neXtProti NX_Q9UKM7.
Orphaneti 88616. Autosomal recessive nonsyndromic intellectual disability.
PharmGKBi PA30572.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG300315.
HOGENOMi HOG000181987.
HOVERGENi HBG052389.
KOi K01230.
OMAi VHFNLHA.
OrthoDBi EOG7ZGX2S.
PhylomeDBi Q9UKM7.
TreeFami TF354274.

Enzyme and pathway databases

UniPathwayi UPA00378 .
BRENDAi 3.2.1.113. 2681.
Reactomei REACT_25091. ER Quality Control Compartment (ERQC).

Miscellaneous databases

EvolutionaryTracei Q9UKM7.
GeneWikii MAN1B1.
GenomeRNAii 11253.
NextBioi 42822.
PROi Q9UKM7.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9UKM7.
Bgeei Q9UKM7.
CleanExi HS_MAN1B1.
Genevestigatori Q9UKM7.

Family and domain databases

Gene3Di 1.50.10.50. 1 hit.
InterProi IPR001382. Glyco_hydro_47.
[Graphical view ]
PANTHERi PTHR11742. PTHR11742. 1 hit.
Pfami PF01532. Glyco_hydro_47. 1 hit.
[Graphical view ]
PRINTSi PR00747. GLYHDRLASE47.
SUPFAMi SSF48225. SSF48225. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and expression of a specific human alpha1,2-mannosidase that trims Man9GlcNAc2 to Man8GlcNAc2 isomer B during N-glycan biosynthesis."
    Tremblay L.O., Herscovics A.
    Glycobiology 9:1073-1078(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, VARIANT SER-59.
    Tissue: Fetal brain, Liver, Placenta and Testis.
  2. "Identification, expression, and characterization of a cDNA encoding human endoplasmic reticulum mannosidase I, the enzyme that catalyzes the first mannose trimming step in mammalian Asn-linked oligosaccharide biosynthesis."
    Gonzalez D.S., Karaveg K., Vandersall-Nairn A.S., Lal A., Moremen K.W.
    J. Biol. Chem. 274:21375-21386(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 37-699, TISSUE SPECIFICITY, ENZYME ACTIVITY, ENZYME REGULATION, SUBCELLULAR LOCATION, VARIANT SER-59.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT SER-59.
  4. "DNA sequence and analysis of human chromosome 9."
    Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
    , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
    Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
    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], VARIANT SER-59.
    Tissue: Lung and Placenta.
  6. "The specificity of the yeast and human class I ER alpha 1,2-mannosidases involved in ER quality control is not as strict previously reported."
    Herscovics A., Romero P.A., Tremblay L.O.
    Glycobiology 12:14G-15G(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY.
  7. "Endoplasmic reticulum (ER) mannosidase I is compartmentalized and required for N-glycan trimming to Man5-6GlcNAc2 in glycoprotein ER-associated degradation."
    Avezov E., Frenkel Z., Ehrlich M., Herscovics A., Lederkremer G.Z.
    Mol. Biol. Cell 19:216-225(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "Structural basis for catalysis and inhibition of N-glycan processing class I alpha 1,2-mannosidases."
    Vallee F., Karaveg K., Herscovics A., Moremen K.W., Howell P.L.
    J. Biol. Chem. 275:41287-41298(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 243-699, DISULFIDE BOND.
  9. "Mechanism of class 1 (glycosylhydrolase family 47) {alpha}-mannosidases involved in N-glycan processing and endoplasmic reticulum quality control."
    Karaveg K., Siriwardena A., Tempel W., Liu Z.J., Glushka J., Wang B.C., Moremen K.W.
    J. Biol. Chem. 280:16197-16207(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.41 ANGSTROMS) OF 172-699 IN COMPLEX WITH A THIO-DISACCHARIDE SUBSTRATE ANALOG, ENZYME ACTIVITY, MUTAGENESIS OF GLU-330; ASP-463; HIS-524 AND GLU-599.
  10. Cited for: VARIANTS MRT15 CYS-334 AND LYS-397, CHARACTERIZATION OF VARIANTS MRT15 CYS-334 AND LYS-397.

Entry informationi

Entry nameiMA1B1_HUMAN
AccessioniPrimary (citable) accession number: Q9UKM7
Secondary accession number(s): Q5VSG3, Q9BRS9, Q9Y5K7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 16, 2001
Last sequence update: March 7, 2006
Last modified: September 3, 2014
This is version 141 of the entry and version 2 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

Caution

It is uncertain whether Met-1 or Met-37 is the initiator.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. Human chromosome 9
    Human chromosome 9: 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  7. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  8. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi