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Protein

Dol-P-Man:Man(7)GlcNAc(2)-PP-Dol alpha-1,6-mannosyltransferase

Gene

ALG12

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Adds the eighth mannose residue in an alpha-1,6 linkage onto the dolichol-PP-oligosaccharide precursor (dolichol-PP-Man7GlcNAc2) required for protein glycosylation.

Catalytic activityi

Dolichyl beta-D-mannosyl phosphate + D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-(D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-D-Man-alpha-(1->6))-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol = D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-(D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-(D-Man-alpha-(1->6))-D-Man-alpha-(1->6))-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol + dolichyl phosphate.

Pathwayi

GO - Molecular functioni

  1. alpha-1,6-mannosyltransferase activity Source: UniProtKB
  2. dol-P-Man:Man(7)GlcNAc(2)-PP-Dol alpha-1,6-mannosyltransferase activity Source: UniProtKB-EC
  3. mannosyltransferase activity Source: GO_Central

GO - Biological processi

  1. cellular protein metabolic process Source: Reactome
  2. dolichol-linked oligosaccharide biosynthetic process Source: MGI
  3. mannosylation Source: GOC
  4. post-translational protein modification Source: Reactome
  5. protein folding Source: UniProtKB
  6. protein N-linked glycosylation Source: UniProtKB
  7. protein N-linked glycosylation via asparagine Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Enzyme and pathway databases

BRENDAi2.4.1.260. 2681.
ReactomeiREACT_22433. Biosynthesis of the N-glycan precursor (dolichol lipid-linked oligosaccharide, LLO) and transfer to a nascent protein.
REACT_267773. Defective ALG12 causes ALG12-CDG (CDG-1g).
UniPathwayiUPA00378.

Protein family/group databases

CAZyiGT22. Glycosyltransferase Family 22.

Names & Taxonomyi

Protein namesi
Recommended name:
Dol-P-Man:Man(7)GlcNAc(2)-PP-Dol alpha-1,6-mannosyltransferase (EC:2.4.1.260)
Alternative name(s):
Asparagine-linked glycosylation protein 12 homolog
Short name:
hALG12
Dolichyl-P-Man:Man(7)GlcNAc(2)-PP-dolichyl-alpha-1,6-mannosyltransferase
Mannosyltransferase ALG12 homolog
Membrane protein SB87
Gene namesi
Name:ALG12
ORF Names:PP14673
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 22

Organism-specific databases

HGNCiHGNC:19358. ALG12.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei11 – 3121HelicalSequence AnalysisAdd
BLAST
Transmembranei68 – 8821HelicalSequence AnalysisAdd
BLAST
Transmembranei93 – 11321HelicalSequence AnalysisAdd
BLAST
Transmembranei122 – 14221HelicalSequence AnalysisAdd
BLAST
Transmembranei145 – 16521HelicalSequence AnalysisAdd
BLAST
Transmembranei177 – 19721HelicalSequence AnalysisAdd
BLAST
Transmembranei212 – 23221HelicalSequence AnalysisAdd
BLAST
Transmembranei264 – 28421HelicalSequence AnalysisAdd
BLAST
Transmembranei290 – 31021HelicalSequence AnalysisAdd
BLAST
Transmembranei312 – 33221HelicalSequence AnalysisAdd
BLAST
Transmembranei346 – 36621HelicalSequence AnalysisAdd
BLAST
Transmembranei423 – 44321HelicalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum Source: UniProtKB
  2. endoplasmic reticulum membrane Source: Reactome
  3. integral component of membrane Source: UniProtKB-KW
  4. membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Involvement in diseasei

Congenital disorder of glycosylation 1G (CDG1G)3 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA multisystem disorder caused by a defect in glycoprotein biosynthesis and characterized by under-glycosylated serum glycoproteins. Congenital disorders of glycosylation result in a wide variety of clinical features, such as defects in the nervous system development, psychomotor retardation, dysmorphic features, hypotonia, coagulation disorders, and immunodeficiency. The broad spectrum of features reflects the critical role of N-glycoproteins during embryonic development, differentiation, and maintenance of cell functions.

See also OMIM:607143
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti67 – 671T → M in CDG1G. 1 Publication
VAR_017904
Natural varianti101 – 1011G → R in CDG1G. 1 Publication
VAR_038428
Natural varianti142 – 1421F → V in CDG1G. 1 Publication
Corresponds to variant rs28942090 [ dbSNP | Ensembl ].
VAR_017905
Natural varianti146 – 1461R → Q in CDG1G. 2 Publications
VAR_017906
Natural varianti158 – 1581L → P in CDG1G. 1 Publication
VAR_017907

Keywords - Diseasei

Congenital disorder of glycosylation, Disease mutation

Organism-specific databases

MIMi607143. phenotype.
Orphaneti79324. ALG12-CDG.
PharmGKBiPA134987771.

Polymorphism and mutation databases

BioMutaiALG12.
DMDMi45476971.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 488488Dol-P-Man:Man(7)GlcNAc(2)-PP-Dol alpha-1,6-mannosyltransferasePRO_0000215781Add
BLAST

Proteomic databases

MaxQBiQ9BV10.
PaxDbiQ9BV10.
PRIDEiQ9BV10.

PTM databases

PhosphoSiteiQ9BV10.

Expressioni

Tissue specificityi

Expressed in fibroblasts.

Gene expression databases

BgeeiQ9BV10.
CleanExiHS_ALG12.
ExpressionAtlasiQ9BV10. baseline and differential.
GenevestigatoriQ9BV10.

Organism-specific databases

HPAiHPA051665.

Interactioni

Protein-protein interaction databases

BioGridi122535. 4 interactions.
IntActiQ9BV10. 2 interactions.
STRINGi9606.ENSP00000333813.

Structurei

3D structure databases

ProteinModelPortaliQ9BV10.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyltransferase 22 family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG256776.
GeneTreeiENSGT00550000075005.
HOGENOMiHOG000265945.
HOVERGENiHBG050486.
InParanoidiQ9BV10.
KOiK03847.
OMAiSYTHILM.
OrthoDBiEOG7ZGX2X.
PhylomeDBiQ9BV10.
TreeFamiTF314453.

Family and domain databases

InterProiIPR005599. GPI_mannosylTrfase.
[Graphical view]
PANTHERiPTHR22760. PTHR22760. 1 hit.
PfamiPF03901. Glyco_transf_22. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9BV10-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGKGSSGRR PLLLGLLVAV ATVHLVICPY TKVEESFNLQ ATHDLLYHWQ
60 70 80 90 100
DLEQYDHLEF PGVVPRTFLG PVVIAVFSSP AVYVLSLLEM SKFYSQLIVR
110 120 130 140 150
GVLGLGVIFG LWTLQKEVRR HFGAMVATMF CWVTAMQFHL MFYCTRTLPN
160 170 180 190 200
VLALPVVLLA LAAWLRHEWA RFIWLSAFAI IVFRVELCLF LGLLLLLALG
210 220 230 240 250
NRKVSVVRAL RHAVPAGILC LGLTVAVDSY FWRQLTWPEG KVLWYNTVLN
260 270 280 290 300
KSSNWGTSPL LWYFYSALPR GLGCSLLFIP LGLVDRRTHA PTVLALGFMA
310 320 330 340 350
LYSLLPHKEL RFIIYAFPML NITAARGCSY LLNNYKKSWL YKAGSLLVIG
360 370 380 390 400
HLVVNAAYSA TALYVSHFNY PGGVAMQRLH QLVPPQTDVL LHIDVAAAQT
410 420 430 440 450
GVSRFLQVNS AWRYDKREDV QPGTGMLAYT HILMEAAPGL LALYRDTHRV
460 470 480
LASVVGTTGV SLNLTQLPPF NVHLQTKLVL LERLPRPS
Length:488
Mass (Da):54,655
Last modified:June 1, 2001 - v1
Checksum:i8D4F921C21CBC8B6
GO

Sequence cautioni

The sequence AAM94900.1 differs from that shown. Reason: Frameshift at position 468. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti267 – 2671A → T in AAM94900 (Ref. 2) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti67 – 671T → M in CDG1G. 1 Publication
VAR_017904
Natural varianti101 – 1011G → R in CDG1G. 1 Publication
VAR_038428
Natural varianti142 – 1421F → V in CDG1G. 1 Publication
Corresponds to variant rs28942090 [ dbSNP | Ensembl ].
VAR_017905
Natural varianti146 – 1461R → Q in CDG1G. 2 Publications
VAR_017906
Natural varianti158 – 1581L → P in CDG1G. 1 Publication
VAR_017907
Natural varianti393 – 3931I → V.1 Publication
Corresponds to variant rs3922872 [ dbSNP | Ensembl ].
VAR_024466

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ290427 mRNA. Translation: CAC83681.1.
AJ303120 mRNA. Translation: CAC67488.1.
AF311904 mRNA. Translation: AAM94900.1. Frameshift.
AF318343 mRNA. Translation: AAL55850.1.
CR456369 mRNA. Translation: CAG30255.1.
AL671710 Genomic DNA. Translation: CAO72064.1.
CH471138 Genomic DNA. Translation: EAW73480.1.
BC001729 mRNA. Translation: AAH01729.1.
BC098562 mRNA. Translation: AAH98562.1.
CCDSiCCDS14081.1.
RefSeqiNP_077010.1. NM_024105.3.
UniGeneiHs.526711.

Genome annotation databases

EnsembliENST00000330817; ENSP00000333813; ENSG00000182858.
GeneIDi79087.
KEGGihsa:79087.
UCSCiuc003biy.3. human.

Polymorphism and mutation databases

BioMutaiALG12.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

GGDB

GlycoGene database

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ290427 mRNA. Translation: CAC83681.1.
AJ303120 mRNA. Translation: CAC67488.1.
AF311904 mRNA. Translation: AAM94900.1. Frameshift.
AF318343 mRNA. Translation: AAL55850.1.
CR456369 mRNA. Translation: CAG30255.1.
AL671710 Genomic DNA. Translation: CAO72064.1.
CH471138 Genomic DNA. Translation: EAW73480.1.
BC001729 mRNA. Translation: AAH01729.1.
BC098562 mRNA. Translation: AAH98562.1.
CCDSiCCDS14081.1.
RefSeqiNP_077010.1. NM_024105.3.
UniGeneiHs.526711.

3D structure databases

ProteinModelPortaliQ9BV10.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi122535. 4 interactions.
IntActiQ9BV10. 2 interactions.
STRINGi9606.ENSP00000333813.

Protein family/group databases

CAZyiGT22. Glycosyltransferase Family 22.

PTM databases

PhosphoSiteiQ9BV10.

Polymorphism and mutation databases

BioMutaiALG12.
DMDMi45476971.

Proteomic databases

MaxQBiQ9BV10.
PaxDbiQ9BV10.
PRIDEiQ9BV10.

Protocols and materials databases

DNASUi79087.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000330817; ENSP00000333813; ENSG00000182858.
GeneIDi79087.
KEGGihsa:79087.
UCSCiuc003biy.3. human.

Organism-specific databases

CTDi79087.
GeneCardsiGC22M050297.
GeneReviewsiALG12.
H-InvDBHIX0175449.
HGNCiHGNC:19358. ALG12.
HPAiHPA051665.
MIMi607143. phenotype.
607144. gene.
neXtProtiNX_Q9BV10.
Orphaneti79324. ALG12-CDG.
PharmGKBiPA134987771.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG256776.
GeneTreeiENSGT00550000075005.
HOGENOMiHOG000265945.
HOVERGENiHBG050486.
InParanoidiQ9BV10.
KOiK03847.
OMAiSYTHILM.
OrthoDBiEOG7ZGX2X.
PhylomeDBiQ9BV10.
TreeFamiTF314453.

Enzyme and pathway databases

UniPathwayiUPA00378.
BRENDAi2.4.1.260. 2681.
ReactomeiREACT_22433. Biosynthesis of the N-glycan precursor (dolichol lipid-linked oligosaccharide, LLO) and transfer to a nascent protein.
REACT_267773. Defective ALG12 causes ALG12-CDG (CDG-1g).

Miscellaneous databases

ChiTaRSiALG12. human.
GeneWikiiALG12.
GenomeRNAii79087.
NextBioi67909.
PROiQ9BV10.
SOURCEiSearch...

Gene expression databases

BgeeiQ9BV10.
CleanExiHS_ALG12.
ExpressionAtlasiQ9BV10. baseline and differential.
GenevestigatoriQ9BV10.

Family and domain databases

InterProiIPR005599. GPI_mannosylTrfase.
[Graphical view]
PANTHERiPTHR22760. PTHR22760. 1 hit.
PfamiPF03901. Glyco_transf_22. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Congenital disorders of glycosylation type Ig is defined by a deficiency in dolichyl-P-mannose:Man7GlcNAc2-PP-dolichyl mannosyltransferase."
    Chantret I., Dupre T., Delenda C., Bucher S., Dancourt J., Barnier A., Charollais A., Heron D., Bader-Meunier B., Danos O., Seta N., Durand G., Oriol R., Codogno P., Moore S.E.H.
    J. Biol. Chem. 277:25815-25822(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT CDG1G VAL-142.
    Tissue: Skin.
  2. "Identification of novel membrane proteins."
    Zhang W., Li N., Wan T., Cao X.
    Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  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].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  5. "The DNA sequence of human chromosome 22."
    Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
    , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
    Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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 VAL-393.
    Tissue: Eye.
  8. "ALG12 mannosyltransferase defect in congenital disorder of glycosylation type Ig."
    Grubenmann C.E., Frank C.G., Kjaergaard S., Berger E.G., Aebi M., Hennet T.
    Hum. Mol. Genet. 11:2331-2339(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF VARIANTS CDG1G MET-67 AND GLN-146.
  9. "Deficiency of dolichyl-P-Man:Man7GlcNAc2-PP-dolichyl mannosyltransferase causes congenital disorder of glycosylation type Ig."
    Thiel C., Schwarz M., Hasilik M., Grieben U., Hanefeld F., Lehle L., von Figura K., Koerner C.
    Biochem. J. 367:195-201(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF VARIANT CDG1G PRO-158.
  10. "Abnormal glycosylation of red cell membrane band 3 in the congenital disorder of glycosylation Ig."
    Zdebska E., Bader-Meunier B., Schischmanoff P.-O., Dupre T., Seta N., Tchernia G., Koscielak J., Delaunay J.
    Pediatr. Res. 54:224-229(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN CDG1G.
  11. "Expanding spectrum of congenital disorder of glycosylation Ig (CDG-Ig): sibs with a unique skeletal dysplasia, hypogammaglobulinemia, cardiomyopathy, genital malformations, and early lethality."
    Kranz C., Basinger A.A., Guecsavas-Calikoglu M., Sun L., Powell C.M., Henderson F.W., Aylsworth A.S., Freeze H.H.
    Am. J. Med. Genet. A 143:1371-1378(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS CDG1G ARG-101 AND GLN-146.

Entry informationi

Entry nameiALG12_HUMAN
AccessioniPrimary (citable) accession number: Q9BV10
Secondary accession number(s): A6PWM1
, Q4KMH4, Q8NG10, Q96AA4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 15, 2004
Last sequence update: June 1, 2001
Last modified: April 29, 2015
This is version 128 of the entry and version 1 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. Human chromosome 22
    Human chromosome 22: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.