UniProt Accession

 PMM2_HUMAN; O15305; A8K672; D3DUF3 

Genbank Protein ID

 U85773; AF157796; AF157790; AF157791; AF157792; AF157793; AF157794; AF157795; AK291537; CH471112; CH471112; BC008310 

Genbank Nucleotide ID

 AAC51368.1; AAD45895.1; AAD45895.1; AAD45895.1; AAD45895.1; AAD45895.1; AAD45895.1; AAD45895.1; BAF84226.1; EAW85202.1; EAW85203.1; AAH08310.1 

Protein Name

 Phosphomannomutase 2 

Protein Synonyms/Alias

 PMM 2 

Gene Name

 PMM2 

Gene Synonyms/Alias

  

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
34	EMDDFLQKLRQKIKI	ubiquitination	[1]
51	VGGSDFEKVQEQLGN	ubiquitination	[2]
77	ENGLVAYKDGKLLCR	ubiquitination	[2]
149	IEFYELDKKENIRQK	acetylation	[3]
202	HVENDGYKTIYFFGD	ubiquitination	[4]

Reference

 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [2] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [3] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [4] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473] 

Functional Description

 Involved in the synthesis of the GDP-mannose and dolichol-phosphate-mannose required for a number of critical mannosyl transfer reactions (By similarity). 

Sequence Annotation

 ACT_SITE 12 12 Nucleophile (By similarity).
 ACT_SITE 14 14 By similarity.
 ACT_SITE 47 47 By similarity.
 ACT_SITE 189 189 By similarity.
 BINDING 21 21 Substrate (By similarity).
 BINDING 123 123 Substrate (By similarity).
 BINDING 134 134 Substrate (By similarity).
 BINDING 141 141 Substrate (By similarity).
 BINDING 179 179 Substrate (By similarity).
 BINDING 181 181 Substrate (By similarity).  

Keyword

 3D-structure; Complete proteome; Congenital disorder of glycosylation; Cytoplasm; Disease mutation; Isomerase; Polymorphism; Reference proteome. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 246 AA 

Protein Sequence

Gene Ontology

 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0043025; C:neuronal cell body; IEA:Compara.
 GO:0004615; F:phosphomannomutase activity; TAS:ProtInc.
 GO:0006488; P:dolichol-linked oligosaccharide biosynthetic process; TAS:Reactome.
 GO:0009298; P:GDP-mannose biosynthetic process; TAS:Reactome.
 GO:0019307; P:mannose biosynthetic process; IEA:InterPro.
 GO:0043687; P:post-translational protein modification; TAS:Reactome.
 GO:0018279; P:protein N-linked glycosylation via asparagine; TAS:Reactome. 

Interpro

 IPR023214; HAD-like_dom.
 IPR006379; HAD-SF_hydro_IIB.
 IPR005002; PMM. 

Pfam

 PF03332; PMM 

SMART

  

PROSITE

  

PRINTS