ID H3BPH4_HUMAN Unreviewed; 142 AA. AC H3BPH4; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 24-JUL-2024, entry version 62. DE RecName: Full=Phosphomannomutase {ECO:0000256|ARBA:ARBA00012730, ECO:0000256|RuleBase:RU361118}; DE EC=5.4.2.8 {ECO:0000256|ARBA:ARBA00012730, ECO:0000256|RuleBase:RU361118}; DE Flags: Fragment; GN Name=PMM2 {ECO:0000313|Ensembl:ENSP00000455320.1}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000455320.1, ECO:0000313|Proteomes:UP000005640}; RN [1] {ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15616553; DOI=10.1038/nature03187; RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M., RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., RA Myers R.M., Rubin E.M., Pennacchio L.A.; RT "The sequence and analysis of duplication-rich human chromosome 16."; RL Nature 432:988-994(2004). RN [2] {ECO:0007829|PubMed:21269460} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Burckstummer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [3] {ECO:0007829|PubMed:24275569} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [4] {ECO:0000313|Ensembl:ENSP00000455320.1} RP IDENTIFICATION. RG Ensembl; RL Submitted (APR-2024) to UniProtKB. CC -!- FUNCTION: Involved in the synthesis of the GDP-mannose and dolichol- CC phosphate-mannose required for a number of critical mannosyl transfer CC reactions. {ECO:0000256|RuleBase:RU361118}. CC -!- CATALYTIC ACTIVITY: CC Reaction=alpha-D-mannose 1-phosphate = D-mannose 6-phosphate; CC Xref=Rhea:RHEA:11140, ChEBI:CHEBI:58409, ChEBI:CHEBI:58735; CC EC=5.4.2.8; Evidence={ECO:0000256|RuleBase:RU361118}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|PIRSR:PIRSR605002-3}; CC -!- PATHWAY: Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose CC biosynthesis; alpha-D-mannose 1-phosphate from D-fructose 6-phosphate: CC step 2/2. {ECO:0000256|ARBA:ARBA00004699, CC ECO:0000256|RuleBase:RU361118}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738, CC ECO:0000256|RuleBase:RU361118}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496, CC ECO:0000256|RuleBase:RU361118}. CC -!- SIMILARITY: Belongs to the eukaryotic PMM family. CC {ECO:0000256|ARBA:ARBA00009736, ECO:0000256|RuleBase:RU361118}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AC012173; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC022167; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR MassIVE; H3BPH4; -. DR PeptideAtlas; H3BPH4; -. DR ProteomicsDB; 41497; -. DR Ensembl; ENST00000564069.1; ENSP00000455320.1; ENSG00000140650.13. DR UCSC; uc059qpq.1; human. DR HGNC; HGNC:9115; PMM2. DR VEuPathDB; HostDB:ENSG00000140650; -. DR GeneTree; ENSGT00390000002918; -. DR HOGENOM; CLU_065642_1_0_1; -. DR UniPathway; UPA00126; UER00424. DR ChiTaRS; PMM2; human. DR Proteomes; UP000005640; Chromosome 16. DR Bgee; ENSG00000140650; Expressed in body of pancreas and 102 other cell types or tissues. DR ExpressionAtlas; H3BPH4; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004615; F:phosphomannomutase activity; IEA:UniProtKB-EC. DR GO; GO:0009298; P:GDP-mannose biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1. DR InterPro; IPR036412; HAD-like_sf. DR InterPro; IPR006379; HAD-SF_hydro_IIB. DR InterPro; IPR023214; HAD_sf. DR InterPro; IPR005002; PMM. DR NCBIfam; TIGR01484; HAD-SF-IIB; 1. DR PANTHER; PTHR10466; PHOSPHOMANNOMUTASE; 1. DR PANTHER; PTHR10466:SF2; PHOSPHOMANNOMUTASE 2; 1. DR Pfam; PF03332; PMM; 1. DR SUPFAM; SSF56784; HAD-like; 1. PE 1: Evidence at protein level; KW Cytoplasm {ECO:0000256|RuleBase:RU361118}; KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|RuleBase:RU361118}; KW Magnesium {ECO:0000256|PIRSR:PIRSR605002-3}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR605002-3}; KW Proteomics identification {ECO:0007829|PeptideAtlas:H3BPH4, KW ECO:0007829|ProteomicsDB:H3BPH4}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}. FT ACT_SITE 3 FT /note="Nucleophile" FT /evidence="ECO:0000256|PIRSR:PIRSR605002-1" FT ACT_SITE 5 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR605002-1" FT BINDING 3 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR605002-3" FT BINDING 5 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR605002-3" FT NON_TER 1 FT /evidence="ECO:0000313|Ensembl:ENSP00000455320.1" SQ SEQUENCE 142 AA; 16334 MW; A450D931404CC343 CRC64; XFDVDGTLTA PRQKITKEMD DFLQKLRQKI KIGVVGGSDF EKVQEQLGND VVEKYDYVFP ENGLVAYKDG KLLCRQNIQS HLGEALIQDL INYCLSYIAK IKLPKKRGTF IEFRNGMLNV SPIGRSCSQE ERIEFYELDK KI //