Q92871 (PMM1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Phosphomannomutase 1
Short name=PMM 1
EC=5.4.2.8

Alternative name(s):
PMMH-22

Gene names

Name:	PMM1
Synonyms:	PMMH22

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	262 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Involved in the synthesis of the GDP-mannose and dolichol-phosphate-mannose required for a number of critical mannosyl transfer reactions. In addition, may be responsible for the degradation of glucose-1,6-bisphosphate in ischemic brain. Ref.9
Catalytic activity	Alpha-D-mannose 1-phosphate = D-mannose 6-phosphate.
Cofactor	Magnesium. Ref.9
Enzyme regulation	IMP, a metabolite whose concentration is elevated in anoxia, inhibits phosphomannomutase and phosphoglucomutase activities and strongly enhances glucose-1,6-bisphosphatase activity By similarity.
Pathway	Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose biosynthesis; alpha-D-mannose 1-phosphate from D-fructose 6-phosphate: step 2/2.
Subunit structure	Homodimer. Ref.9
Subcellular location	Cytoplasm.
Tissue specificity	Strong expression in liver, heart, brain, and pancreas; lower expression in skeletal muscle.
Sequence similarities	Belongs to the eukaryotic PMM family.
Biophysicochemical properties	Kinetic parameters: KM=54 µM for alpha-D-mannose 1-phosphate Ref.9 KM=7.5 µM for alpha-D-glucose 1-phosphate

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	Magnesium Metal-binding
Molecular function	Isomerase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	GDP-mannose biosynthetic process Traceable author statement. Source: Reactome dolichol-linked oligosaccharide biosynthetic process Traceable author statement. Source: Reactome mannose biosynthetic process Inferred from electronic annotation. Source: InterPro mannose metabolic process Traceable author statement Ref.1. Source: ProtInc post-translational protein modification Traceable author statement. Source: Reactome protein N-linked glycosylation via asparagine Traceable author statement. Source: Reactome
Cellular_component	cytosol Traceable author statement. Source: Reactome neuronal cell body Inferred from electronic annotation. Source: Compara
Molecular_function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW phosphomannomutase activity Traceable author statement Ref.1. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 262

262

Phosphomannomutase 1

PRO_0000199692

Sites

Active site

19

1

Nucleophile

Active site

21

1

Active site

54

1

Active site

198

1

Metal binding

218

1

Magnesium

Binding site

28

1

Substrate

Binding site

132

1

Substrate

Binding site

143

1

Substrate

Binding site

150

1

Substrate

Binding site

186

1

Substrate

Binding site

188

1

Substrate

Binding site

190

1

Substrate

Experimental info

Sequence conflict

11

1

K → R in AAC51117. Ref.1

Sequence conflict

169

1

A → D in AAC51117. Ref.1

Secondary structure

1

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262

Helix Strand Turn

Details...

Beta strand

14 – 21

8

Turn

22 – 24

3

Helix

33 – 42

10

Turn

43 – 45

3

Beta strand

46 – 51

6

Helix

56 – 63

8

Turn

66 – 68

3

Helix

69 – 72

4

Beta strand

74 – 78

5

Helix

79 – 81

3

Beta strand

83 – 86

4

Beta strand

89 – 91

3

Helix

96 – 100

5

Helix

102 – 117

16

Beta strand

128 – 131

4

Beta strand

136 – 138

3

Helix

147 – 160

14

Helix

162 – 173

12

Turn

174 – 176

3

Beta strand

179 – 182

4

Beta strand

185 – 187

3

Beta strand

189 – 193

5

Helix

198 – 201

4

Helix

202 – 205

4

Turn

206 – 209

4

Beta strand

211 – 218

8

Helix

227 – 231

5

Beta strand

235 – 239

5

Helix

243 – 254

12

Sequences

	Sequence		Length	Mass (Da)
	Q92871 [UniParc]. Last modified November 1, 1997. Version 2. Checksum: 1FBA7BFC9C3BB0BB	FASTA	262	29,747
	10 20 30 40 50 60 MAVTAQAARR KERVLCLFDV DGTLTPARQK IDPEVAAFLQ KLRSRVQIGV VGGSDYCKIA 70 80 90 100 110 120 EQLGDGDEVI EKFDYVFAEN GTVQYKHGRL LSKQTIQNHL GEELLQDLIN FCLSYMALLR 130 140 150 160 170 180 LPKKRGTFIE FRNGMLNISP IGRSCTLEER IEFSELDKKE KIREKFVEAL KTEFAGKGLR 190 200 210 220 230 240 FSRGGMISFD VFPEGWDKRY CLDSLDQDSF DTIHFFGNET SPGGNDFEIF ADPRTVGHSV 250 260 VSPQDTVQRC REIFFPETAH EA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"PMM (PMM1), the human homologue of SEC53 or yeast phosphomannomutase, is localized on chromosome 22q13." Matthijs G., Schollen E., Pirard M., Budarf M.L., van Schaftingen E., Cassiman J.-J. Genomics 40:41-47(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.
[2]	"Isolation of the human phosphomannomutase gene (PMM1) and assignment to chromosome 22q13." Wada Y., Sakamoto M. Genomics 39:416-417(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	Hansen S.H., Frank S.R., Casanova J.E. Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Brain.
[4]	"A genome annotation-driven approach to cloning the human ORFeome." Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., Beare D.M., Dunham I. Genome Biol. 5:R84.1-R84.11(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]	"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]. Tissue: Skeletal muscle.
[6]	"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].
[7]	Mural R.J., Istrail S., Sutton 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. , 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].
[8]	"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]. Tissue: Brain and Pancreas.
[9]	"The X-ray crystal structures of human alpha-phosphomannomutase 1 reveal the structural basis of congenital disorder of glycosylation type 1a." Silvaggi N.R., Zhang C., Lu Z., Dai J., Dunaway-Mariano D., Allen K.N. J. Biol. Chem. 281:14918-14926(2006) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS), FUNCTION, COFACTOR, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U62526 mRNA. Translation: AAC51117.1.
D87810 mRNA. Translation: BAA13460.1.
U86070 mRNA. Translation: AAC00023.1.
CR456544 mRNA. Translation: CAG30430.1.
AK289368 mRNA. Translation: BAF82057.1.
AK316580 mRNA. Translation: BAG38168.1.
AL023553 Genomic DNA. Translation: CAB46025.1.
CH471095 Genomic DNA. Translation: EAW60443.1.
BC010855 mRNA. Translation: AAH10855.1.
BC016818 mRNA. Translation: AAH16818.1.

IPI

IPI00294903.

RefSeq

NP_002667.2. NM_002676.2.

UniGene

Hs.75835.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2FUC	X-ray	2.10	A	1-262	[»]
2FUE	X-ray	1.75	A	1-262	[»]

ProteinModelPortal

Q92871.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q92871. 3 interactions.

MINT

MINT-1482037.

STRING

9606.ENSP00000216259.

PTM databases

PhosphoSite

Q92871.

Polymorphism databases

DMDM

2499519.

Proteomic databases

PaxDb

Q92871.

PRIDE

Q92871.

Protocols and materials databases

DNASU

5372.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000216259; ENSP00000216259; ENSG00000100417.

GeneID

5372.

KEGG

hsa:5372.

UCSC

uc003bal.2. human.

Organism-specific databases

CTD

5372.

GeneCards

GC22M041972.

HGNC

HGNC:9114. PMM1.

HPA

HPA030712.

MIM

601786. gene.

neXtProt

NX_Q92871.

PharmGKB

PA33440.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0561.

HOGENOM

HOG000181843.

HOVERGEN

HBG009971.

InParanoid

Q92871.

KO

K01840.

OMA

NDYEIYD.

OrthoDB

EOG4894NB.

Enzyme and pathway databases

BRENDA

5.4.2.8. 2681.

Reactome

REACT_17015. Metabolism of proteins.

UniPathway

UPA00126; UER00424.

Gene expression databases

ArrayExpress

Q92871.

Bgee

Q92871.

CleanEx

HS_PMM1.

Genevestigator

Q92871.

GermOnline

ENSG00000100417. Homo sapiens.

Family and domain databases

Gene3D

3.40.50.1000. 2 hits.

InterPro

IPR023214. HAD-like_dom.
IPR006379. HAD-SF_hydro_IIB.
IPR005002. PMM.
[Graphical view]

PANTHER

PTHR10466. PTHR10466. 1 hit.

Pfam

PF03332. PMM. 1 hit.
[Graphical view]

SUPFAM

SSF56784. HAD-like_dom. 1 hit.

TIGRFAMs

TIGR01484. HAD-SF-IIB. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

Q92871.

GenomeRNAi

5372.

NextBio

20842.

SOURCE

Search...

Entry information

Entry name

PMM1_HUMAN

Accession

Primary (citable) accession number: Q92871
Secondary accession number(s): A8K003, Q92586

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1997
Last modified:	May 1, 2013
This is version 124 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.