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Protein

Phosphomannomutase 1

Gene

PMM1

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

Functioni

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.1 Publication

Catalytic activityi

Alpha-D-mannose 1-phosphate = D-mannose 6-phosphate.

Cofactori

Mg2+1 Publication

Enzyme regulationi

IMP, a metabolite whose concentration is elevated in anoxia, inhibits phosphomannomutase and phosphoglucomutase activities and strongly enhances glucose-1,6-bisphosphatase activity.By similarity

Kineticsi

  1. KM=54 µM for alpha-D-mannose 1-phosphate1 Publication
  2. KM=7.5 µM for alpha-D-glucose 1-phosphate1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei19 – 191Nucleophile1 Publication
Metal bindingi19 – 191Magnesium
Active sitei21 – 211Proton donor/acceptorSequence Analysis
Metal bindingi21 – 211Magnesium; via carbonyl oxygen
Binding sitei28 – 281Substrate
Binding sitei132 – 1321Substrate
Binding sitei143 – 1431Substrate
Binding sitei150 – 1501Substrate
Binding sitei186 – 1861Substrate; via amide nitrogen
Binding sitei188 – 1881Substrate
Binding sitei190 – 1901Substrate
Metal bindingi218 – 2181Magnesium

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. phosphomannomutase activity Source: UniProtKB

GO - Biological processi

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

Keywords - Molecular functioni

Isomerase

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BRENDAi5.4.2.8. 2681.
ReactomeiREACT_22423. Synthesis of GDP-mannose.
UniPathwayiUPA00126; UER00424.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphomannomutase 1 (EC:5.4.2.8)
Short name:
PMM 1
Alternative name(s):
PMMH-22
Gene namesi
Name:PMM1
Synonyms:PMMH22
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 22

Organism-specific databases

HGNCiHGNC:9114. PMM1.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. neuronal cell body Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33440.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 262261Phosphomannomutase 1PRO_0000199692Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ92871.
PaxDbiQ92871.
PRIDEiQ92871.

PTM databases

DEPODiQ92871.
PhosphoSiteiQ92871.

Expressioni

Tissue specificityi

Strong expression in liver, heart, brain, and pancreas; lower expression in skeletal muscle.

Gene expression databases

BgeeiQ92871.
CleanExiHS_PMM1.
ExpressionAtlasiQ92871. baseline and differential.
GenevestigatoriQ92871.

Organism-specific databases

HPAiHPA030712.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

BioGridi111385. 13 interactions.
IntActiQ92871. 4 interactions.
MINTiMINT-1482037.
STRINGi9606.ENSP00000216259.

Structurei

Secondary structure

1
262
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi14 – 218Combined sources
Turni22 – 243Combined sources
Helixi33 – 4210Combined sources
Turni43 – 453Combined sources
Beta strandi46 – 516Combined sources
Helixi56 – 638Combined sources
Turni66 – 683Combined sources
Helixi69 – 724Combined sources
Beta strandi74 – 785Combined sources
Helixi79 – 813Combined sources
Beta strandi83 – 864Combined sources
Beta strandi89 – 913Combined sources
Helixi96 – 1005Combined sources
Helixi102 – 11716Combined sources
Beta strandi128 – 1314Combined sources
Beta strandi136 – 1383Combined sources
Helixi147 – 16014Combined sources
Helixi162 – 17312Combined sources
Turni174 – 1763Combined sources
Beta strandi179 – 1824Combined sources
Beta strandi185 – 1873Combined sources
Beta strandi189 – 1935Combined sources
Helixi198 – 2014Combined sources
Helixi202 – 2054Combined sources
Turni206 – 2094Combined sources
Beta strandi211 – 2188Combined sources
Helixi227 – 2315Combined sources
Beta strandi235 – 2395Combined sources
Helixi243 – 25412Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2FUCX-ray2.10A1-262[»]
2FUEX-ray1.75A1-262[»]
ProteinModelPortaliQ92871.
SMRiQ92871. Positions 13-258.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ92871.

Family & Domainsi

Sequence similaritiesi

Belongs to the eukaryotic PMM family.Curated

Phylogenomic databases

eggNOGiCOG0561.
GeneTreeiENSGT00390000002918.
HOGENOMiHOG000181843.
HOVERGENiHBG009971.
InParanoidiQ92871.
KOiK17497.
OMAiNDYEIYD.
OrthoDBiEOG773XH0.
PhylomeDBiQ92871.
TreeFamiTF300874.

Family and domain databases

Gene3Di3.40.50.1000. 2 hits.
InterProiIPR023214. HAD-like_dom.
IPR006379. HAD-SF_hydro_IIB.
IPR005002. PMM.
[Graphical view]
PANTHERiPTHR10466. PTHR10466. 1 hit.
PfamiPF03332. PMM. 1 hit.
[Graphical view]
SUPFAMiSSF56784. SSF56784. 1 hit.
TIGRFAMsiTIGR01484. HAD-SF-IIB. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q92871-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAVTAQAARR KERVLCLFDV DGTLTPARQK IDPEVAAFLQ KLRSRVQIGV
60 70 80 90 100
VGGSDYCKIA EQLGDGDEVI EKFDYVFAEN GTVQYKHGRL LSKQTIQNHL
110 120 130 140 150
GEELLQDLIN FCLSYMALLR LPKKRGTFIE FRNGMLNISP IGRSCTLEER
160 170 180 190 200
IEFSELDKKE KIREKFVEAL KTEFAGKGLR FSRGGMISFD VFPEGWDKRY
210 220 230 240 250
CLDSLDQDSF DTIHFFGNET SPGGNDFEIF ADPRTVGHSV VSPQDTVQRC
260
REIFFPETAH EA
Length:262
Mass (Da):29,747
Last modified:November 1, 1997 - v2
Checksum:i1FBA7BFC9C3BB0BB
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti11 – 111K → R in AAC51117. (PubMed:9070917)Curated
Sequence conflicti169 – 1691A → D in AAC51117. (PubMed:9070917)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS14020.1.
RefSeqiNP_002667.2. NM_002676.2.
UniGeneiHs.75835.

Genome annotation databases

EnsembliENST00000216259; ENSP00000216259; ENSG00000100417.
GeneIDi5372.
KEGGihsa:5372.
UCSCiuc003bal.2. human.

Polymorphism databases

DMDMi2499519.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS14020.1.
RefSeqiNP_002667.2. NM_002676.2.
UniGeneiHs.75835.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2FUCX-ray2.10A1-262[»]
2FUEX-ray1.75A1-262[»]
ProteinModelPortaliQ92871.
SMRiQ92871. Positions 13-258.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111385. 13 interactions.
IntActiQ92871. 4 interactions.
MINTiMINT-1482037.
STRINGi9606.ENSP00000216259.

PTM databases

DEPODiQ92871.
PhosphoSiteiQ92871.

Polymorphism databases

DMDMi2499519.

Proteomic databases

MaxQBiQ92871.
PaxDbiQ92871.
PRIDEiQ92871.

Protocols and materials databases

DNASUi5372.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000216259; ENSP00000216259; ENSG00000100417.
GeneIDi5372.
KEGGihsa:5372.
UCSCiuc003bal.2. human.

Organism-specific databases

CTDi5372.
GeneCardsiGC22M041972.
HGNCiHGNC:9114. PMM1.
HPAiHPA030712.
MIMi601786. gene.
neXtProtiNX_Q92871.
PharmGKBiPA33440.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0561.
GeneTreeiENSGT00390000002918.
HOGENOMiHOG000181843.
HOVERGENiHBG009971.
InParanoidiQ92871.
KOiK17497.
OMAiNDYEIYD.
OrthoDBiEOG773XH0.
PhylomeDBiQ92871.
TreeFamiTF300874.

Enzyme and pathway databases

UniPathwayiUPA00126; UER00424.
BRENDAi5.4.2.8. 2681.
ReactomeiREACT_22423. Synthesis of GDP-mannose.

Miscellaneous databases

EvolutionaryTraceiQ92871.
GeneWikiiPMM1.
GenomeRNAii5372.
NextBioi20842.
PROiQ92871.
SOURCEiSearch...

Gene expression databases

BgeeiQ92871.
CleanExiHS_PMM1.
ExpressionAtlasiQ92871. baseline and differential.
GenevestigatoriQ92871.

Family and domain databases

Gene3Di3.40.50.1000. 2 hits.
InterProiIPR023214. HAD-like_dom.
IPR006379. HAD-SF_hydro_IIB.
IPR005002. PMM.
[Graphical view]
PANTHERiPTHR10466. PTHR10466. 1 hit.
PfamiPF03332. PMM. 1 hit.
[Graphical view]
SUPFAMiSSF56784. SSF56784. 1 hit.
TIGRFAMsiTIGR01484. HAD-SF-IIB. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  10. "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 (1.75 ANGSTROMS) IN COMPLEX WITH MAGNESIUM IONS AND MANNOSE 1-PHOSPHATE, FUNCTION, ACTIVE SITE, COFACTOR, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES.

Entry informationi

Entry nameiPMM1_HUMAN
AccessioniPrimary (citable) accession number: Q92871
Secondary accession number(s): A8K003, Q92586
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: January 7, 2015
This is version 140 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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 22
    Human chromosome 22: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. 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.