Q15124 (PGM5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Phosphoglucomutase-like protein 5

Alternative name(s):
Aciculin
Phosphoglucomutase-related protein
Short name=PGM-RP

Gene names

Name:	PGM5
Synonyms:	PGMRP

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	567 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Component of adherens-type cell-cell and cell-matrix junctions. Lacks phosphoglucomutase activity.
Cofactor	Binds 1 magnesium ion per subunit Potential.
Subunit structure	Interacts with cytoskeletal proteins dystrophin and utrophin.
Subcellular location	Cell junction › adherens junction. Cytoplasm › cytoskeleton. Note: Adherens-type cellular junctions. Concentrated in focal contacts at the ends of actin bundles, and associated with actin filaments. Ref.7
Tissue specificity	Detected in smooth and cardiac muscle at high levels and in skeletal muscle at low level. Present in other tissues due to vascular or other smooth muscle component. Low levels are present in liver, kidney, skin and brain (at protein level). Ref.6 Ref.7
Developmental stage	In the developing aorta, expressed at low levels in 10-12 week old fetuses. Levels increase progressively in 24 week fetus, 6 month old child and 1.5 year old child aortic smooth muscle, reaching a maximum at maturity. Ref.7
Sequence similarities	Belongs to the phosphohexose mutase family.
Sequence caution	The sequence AAC41948.1 differs from that shown. Reason: Erroneous initiation. The sequence AAH33073.1 differs from that shown. Reason: Erroneous initiation. The sequence CAA73882.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Cell adhesion Glucose metabolism
Cellular component	Cell junction Cytoplasm Cytoskeleton
Coding sequence diversity	Alternative splicing
Ligand	Magnesium Metal-binding
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cell adhesion Inferred from electronic annotation. Source: UniProtKB-KW glucose metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	Z disc Inferred from Biological aspect of Ancestor. Source: RefGenome costamere Inferred from direct assay Ref.7. Source: UniProtKB dystrophin-associated glycoprotein complex Inferred from sequence or structural similarity. Source: UniProtKB focal adhesion Inferred from direct assay Ref.7. Source: UniProtKB intercalated disc Inferred from direct assay Ref.7. Source: UniProtKB internal side of plasma membrane Inferred from direct assay PubMed 10867799. Source: UniProtKB sarcolemma Inferred from direct assay PubMed 10867799. Source: UniProtKB spot adherens junction Inferred from direct assay Ref.7. Source: UniProtKB stress fiber Inferred from direct assay Ref.7. Source: UniProtKB
Molecular_function	intramolecular transferase activity, phosphotransferases Inferred from electronic annotation. Source: InterPro magnesium ion binding Inferred from electronic annotation. Source: InterPro structural molecule activity Non-traceable author statement Ref.6. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q15124-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q15124-2)

The sequence of this isoform differs from the canonical sequence as follows:
     387-387: G → V
     388-567: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 567	567	Phosphoglucomutase-like protein 5		PRO_0000147787
Regions
	Compositional bias	510 – 513	4	Poly-Ser
Sites
	Metal binding	293	1	Magnesium Potential
	Metal binding	295	1	Magnesium Potential
	Metal binding	297	1	Magnesium Potential
Amino acid modifications
	Modified residue	120	1	Phosphothreonine By similarity
	Modified residue	122	1	Phosphoserine By similarity
Natural variations
	Alternative sequence	387	1	G → V in isoform 2.		VSP_030014
	Alternative sequence	388 – 567	180	Missing in isoform 2.		VSP_030015
Experimental info
	Sequence conflict	22	1	A → S in CAA73882. Ref.4
	Sequence conflict	244	1	D → E AA sequence Ref.7
	Sequence conflict	260 – 261	2	ED → DE AA sequence Ref.7

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified July 10, 2007. Version 2. Checksum: 00583A442977A025	FASTA	567	62,225
	10 20 30 40 50 60 MEGSPIPVLT VPTAPYEDQR PAGGGGLRRP TGLFEGQRNY LPNFIQSVLS SIDLRDRQGC 70 80 90 100 110 120 TMVVGSDGRY FSRTAIEIVV QMAAANGIGR LIIGQNGILS TPAVSCIIRK IKAAGGIILT 130 140 150 160 170 180 ASHCPGGPGG EFGVKFNVAN GGPAPDVVSD KIYQISKTIE EYAICPDLRI DLSRLGRQEF 190 200 210 220 230 240 DLENKFKPFR VEIVDPVDIY LNLLRTIFDF HAIKGLLTGP SQLKIRIDAM HGVMGPYVRK 250 260 270 280 290 300 VLCDELGAPA NSAINCVPLE DFGGQHPDPN LTYATTLLEA MKGGEYGFGA AFDADGDRYM 310 320 330 340 350 360 ILGQNGFFVS PSDSLAIIAA NLSCIPYFRQ MGVRGFGRSM PTSMALDRVA KSMKVPVYET 370 380 390 400 410 420 PAGWRFFSNL MDSGRCNLCG EESFGTGSDH LREKDGLWAV LVWLSIIAAR KQSVEEIVRD 430 440 450 460 470 480 HWAKFGRHYY CRFDYEGLDP KTTYYIMRDL EALVTDKSFI GQQFAVGSHV YSVAKTDSFE 490 500 510 520 530 540 YVDPVDGTVT KKQGLRIIFS DASRLIFRLS SSSGVRATLR LYAESYERDP SGHDQEPQAV 550 560 LSPLIAIALK ISQIHERTGR RGPTVIT
	Isoform 2 [UniParc]. Checksum: 31FF5EACAFB47DC4	FASTA	387	41,790
	10 20 30 40 50 60 MEGSPIPVLT VPTAPYEDQR PAGGGGLRRP TGLFEGQRNY LPNFIQSVLS SIDLRDRQGC 70 80 90 100 110 120 TMVVGSDGRY FSRTAIEIVV QMAAANGIGR LIIGQNGILS TPAVSCIIRK IKAAGGIILT 130 140 150 160 170 180 ASHCPGGPGG EFGVKFNVAN GGPAPDVVSD KIYQISKTIE EYAICPDLRI DLSRLGRQEF 190 200 210 220 230 240 DLENKFKPFR VEIVDPVDIY LNLLRTIFDF HAIKGLLTGP SQLKIRIDAM HGVMGPYVRK 250 260 270 280 290 300 VLCDELGAPA NSAINCVPLE DFGGQHPDPN LTYATTLLEA MKGGEYGFGA AFDADGDRYM 310 320 330 340 350 360 ILGQNGFFVS PSDSLAIIAA NLSCIPYFRQ MGVRGFGRSM PTSMALDRVA KSMKVPVYET 370 380 PAGWRFFSNL MDSGRCNLCG EESFGTV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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] (ISOFORM 1).
[2]	"DNA sequence and analysis of human chromosome 9." Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I. Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"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] (ISOFORM 2). Tissue: Muscle.
[4]	"Characterisation of the promoter which regulates expression of a phosphoglucomutase-related protein, a component of the dystrophin/utrophin cytoskeleton predominantly expressed in smooth muscle." Moiseeva E.P., Critchley D.R. Eur. J. Biochem. 248:634-643(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 2-87.
[5]	Parker K. Submitted (JUN-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 29-55; 158-169; 191-224; 227-239; 355-375; 433-492 AND 497-504, MASS SPECTROMETRY.
[6]	"A novel dystrophin/utrophin-associated protein is an enzymatically inactive member of the phosphoglucomutase superfamily." Moiseeva E.P., Belkin A.M., Spurr N.K., Koteliansky V.E., Critchley D.R. Eur. J. Biochem. 235:103-113(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 32-567, TISSUE SPECIFICITY. Tissue: Uterus.
[7]	"A novel phosphoglucomutase-related protein is concentrated in adherens junctions of muscle and nonmuscle cells." Belkin A.M., Klimanskaya I.V., Lukashev M.E., Lilley K., Critchley D.R., Koteliansky V.E. J. Cell Sci. 107:159-173(1994) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 82-104; 234-262 AND 447-467, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE. Tissue: Uterus.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AK297108 mRNA. Translation: BAG59618.1. AL161457, AL353608, AL353616 Genomic DNA. Translation: CAI16959.2. AL353608, AL161457, AL353616 Genomic DNA. Translation: CAI41169.2. AL353616, AL161457, AL353608 Genomic DNA. Translation: CAH71906.2. AL353608, AL161457 Genomic DNA. Translation: CAO03528.1. AL161457, AL353608 Genomic DNA. Translation: CAO03529.1. BC033073 mRNA. Translation: AAH33073.1. Different initiation. Y13478 Genomic DNA. Translation: CAA73882.1. Different initiation. L40933 Genomic DNA. Translation: AAC41948.1. Different initiation.
IPI	IPI00014852. IPI00852717.
PIR	S62629.
RefSeq	NP_068800.2. NM_021965.3.
UniGene	Hs.307835.
3D structure databases
ProteinModelPortal	Q15124.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000379678.
PTM databases
PhosphoSite	Q15124.
Polymorphism databases
DMDM	152031655.
Proteomic databases
PaxDb	Q15124.
PRIDE	Q15124.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000396392; ENSP00000379674; ENSG00000154330. ENST00000396396; ENSP00000379678; ENSG00000154330. ENST00000579791; ENSP00000464667; ENSG00000266607. ENST00000579948; ENSP00000463663; ENSG00000266607.
GeneID	5239.
KEGG	hsa:5239.
UCSC	uc004agr.3. human.
Organism-specific databases
CTD	5239.
GeneCards	GC09P070971.
H-InvDB	HIX0020782.
HGNC	HGNC:8908. PGM5.
HPA	CAB034397.
MIM	600981. gene.
neXtProt	NX_Q15124.
PharmGKB	PA33245.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0033.
HOGENOM	HOG000009550.
HOVERGEN	HBG001599.
InParanoid	Q15124.
KO	K15636.
OMA	LEEYAIC.
Gene expression databases
ArrayExpress	Q15124.
Bgee	Q15124.
CleanEx	HS_PGM5.
Genevestigator	Q15124.
GermOnline	ENSG00000154330. Homo sapiens.
Family and domain databases
Gene3D	3.40.120.10. 3 hits.
InterPro	IPR005844. A-D-PHexomutase_a/b/a-I. IPR016055. A-D-PHexomutase_a/b/a-I/II/III. IPR005845. A-D-PHexomutase_a/b/a-II. IPR005846. A-D-PHexomutase_a/b/a-III. IPR016066. A-D-PHexomutase_CS. IPR005841. Alpha-D-phosphohexomutase_SF. [Graphical view]
Pfam	PF02878. PGM_PMM_I. 1 hit. PF02879. PGM_PMM_II. 1 hit. PF02880. PGM_PMM_III. 1 hit. [Graphical view]
PRINTS	PR00509. PGMPMM.
SUPFAM	SSF53738. A-D-PHexomutase_a/b/a-I/II/III. 2 hits.
PROSITE	PS00710. PGM_PMM. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	PGM5. human.
GenomeRNAi	5239.
NextBio	20240.
SOURCE	Search...

Entry information

Entry name

PGM5_HUMAN

Accession

Primary (citable) accession number: Q15124
Secondary accession number(s): B1AM46 , B4DLQ6, Q5VYV3, Q8N527, Q9UDH4

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 24, 2001
Last sequence update:	July 10, 2007
Last modified:	May 1, 2013
This is version 115 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.