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UniProtKB - P98160 (PGBM_HUMAN)

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Protein

Basement membrane-specific heparan sulfate proteoglycan core protein

Gene

HSPG2

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

Functioni

Integral component of basement membranes. Component of the glomerular basement membrane (GBM), responsible for the fixed negative electrostatic membrane charge, and which provides a barrier which is both size- and charge-selective. It serves as an attachment substrate for cells. Plays essential roles in vascularization. Critical for normal heart development and for regulating the vascular response to injury. Also required for avascular cartilage development.
Endorepellin in an anti-angiogenic and anti-tumor peptide that inhibits endothelial cell migration, collagen-induced endothelial tube morphogenesis and blood vessel growth in the chorioallantoic membrane. Blocks endothelial cell adhesion to fibronectin and type I collagen. Anti-tumor agent in neovascularization. Interaction with its ligand, integrin alpha2/beta1, is required for the anti-angiogenic properties. Evokes a reduction in phosphorylation of receptor tyrosine kinases via alpha2/beta1 integrin-mediated activation of the tyrosine phosphatase, PTPN6.
The LG3 peptide has anti-angiogenic properties that require binding of calcium ions for full activity.

Miscellaneous

The LG3 peptide has been found in the urine of patients with end-stage renal disease and in the amniotic fluid of pregnant women with premature rupture of fetal membranes.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi4258Calcium1
Metal bindingi4275Calcium; via carbonyl oxygen1
Metal bindingi4325Calcium; via carbonyl oxygen1
Metal bindingi4327Calcium1

GO - Molecular functioni

  • calcium ion binding Source: InterPro
  • extracellular matrix structural constituent conferring compression resistance Source: BHF-UCL
  • integrin binding Source: ARUK-UCL
  • low-density lipoprotein particle receptor binding Source: ARUK-UCL
  • protein C-terminus binding Source: UniProtKB
View the complete GO annotation on QuickGO ...

GO - Biological processi

  • angiogenesis Source: UniProtKB-KW
  • brain development Source: ARUK-UCL
  • cardiovascular system development Source: ARUK-UCL
  • cell differentiation Source: ARUK-UCL
  • cellular protein metabolic process Source: Reactome
  • extracellular matrix organization Source: Reactome
  • glycosaminoglycan biosynthetic process Source: Reactome
  • glycosaminoglycan catabolic process Source: Reactome
  • inflammatory response Source: ARUK-UCL
  • lipid metabolic process Source: ARUK-UCL
  • negative regulation of amyloid fibril formation Source: ARUK-UCL
  • negative regulation of angiogenesis Source: ARUK-UCL
  • negative regulation of cell death Source: ARUK-UCL
  • receptor-mediated endocytosis Source: ARUK-UCL
  • retinoid metabolic process Source: Reactome
View the complete GO annotation on QuickGO ...

Keywordsi

Biological processAngiogenesis
LigandCalcium, Metal-binding

Enzyme and pathway databases

ReactomeiR-HSA-1474228 Degradation of the extracellular matrix
R-HSA-1971475 A tetrasaccharide linker sequence is required for GAG synthesis
R-HSA-2022928 HS-GAG biosynthesis
R-HSA-2024096 HS-GAG degradation
R-HSA-216083 Integrin cell surface interactions
R-HSA-3000157 Laminin interactions
R-HSA-3000171 Non-integrin membrane-ECM interactions
R-HSA-3000178 ECM proteoglycans
R-HSA-3560783 Defective B4GALT7 causes EDS, progeroid type
R-HSA-3560801 Defective B3GAT3 causes JDSSDHD
R-HSA-3656237 Defective EXT2 causes exostoses 2
R-HSA-3656253 Defective EXT1 causes exostoses 1, TRPS2 and CHDS
R-HSA-4420332 Defective B3GALT6 causes EDSP2 and SEMDJL1
R-HSA-975634 Retinoid metabolism and transport
R-HSA-977225 Amyloid fiber formation
SIGNORiP98160

Names & Taxonomyi

Protein namesi
Recommended name:
Basement membrane-specific heparan sulfate proteoglycan core protein
Short name:
HSPG
Alternative name(s):
Perlecan
Short name:
PLC
Cleaved into the following 2 chains:
Endorepellin
LG3 peptide
Gene namesi
Name:HSPG2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

EuPathDBiHostDB:ENSG00000142798.17
HGNCiHGNC:5273 HSPG2
MIMi142461 gene
neXtProtiNX_P98160

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Basement membrane, Extracellular matrix, Secreted

Pathology & Biotechi

Involvement in diseasei

Schwartz-Jampel syndrome (SJS1)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionRare autosomal recessive disorder characterized by permanent myotonia (prolonged failure of muscle relaxation) and skeletal dysplasia, resulting in reduced stature, kyphoscoliosis, bowing of the diaphyses and irregular epiphyses.
See also OMIM:255800
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0141221532C → Y in SJS1. 1 PublicationCorresponds to variant dbSNP:rs137853248EnsemblClinVar.1
Dyssegmental dysplasia Silverman-Handmaker type (DDSH)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionThe dyssegmental dysplasias are rare, autosomal recessive skeletal dysplasias with anisospondyly and micromelia. There are two recognized types: the severe, lethal DDSH and the milder Rolland-Desbuquois form. Individuals with DDSH also have a flat face, micrognathia, cleft palate and reduced joint mobility, and frequently have an encephalocoele. The endochondral growth plate is short, the calcospherites (which are spherical calcium-phosphorus crystals produced by hypertrophic chondrocytes) are unfused, and there is mucoid degeneration of the resting cartilage.
See also OMIM:224410

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi4197D → I: Abolishes BMP1-mediated cleavage of endorepellin. 1 Publication1
Mutagenesisi4258D → A: Retains proper folding. Reduced calcium ion binding. 1 Publication1
Mutagenesisi4327N → A: Retains proper folding. Reduced calcium ion binding. 1 Publication1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi3339
MalaCardsiHSPG2
MIMi224410 phenotype
255800 phenotype
OpenTargetsiENSG00000142798
Orphaneti1865 Dyssegmental dysplasia, Silverman-Handmaker type
800 Schwartz-Jampel syndrome
PharmGKBiPA29537

Chemistry databases

DrugBankiDB00039 Palifermin

Polymorphism and mutation databases

BioMutaiHSPG2
DMDMi317373536

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 21Sequence analysisAdd BLAST21
ChainiPRO_000002669622 – 4391Basement membrane-specific heparan sulfate proteoglycan core proteinAdd BLAST4370
ChainiPRO_00003916213687 – 4391EndorepellinAdd BLAST705
ChainiPRO_00003916224197 – 4391LG3 peptideAdd BLAST195

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi42O-linked (GalNAc...) threonine1 Publication1
Glycosylationi65O-linked (Xyl...) (heparan sulfate) serineSequence analysis1
Glycosylationi71O-linked (Xyl...) (heparan sulfate) serineSequence analysis1
Glycosylationi76O-linked (Xyl...) (heparan sulfate) serineSequence analysis1
Glycosylationi89N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi199 ↔ 212By similarity
Disulfide bondi206 ↔ 225By similarity
Disulfide bondi219 ↔ 234By similarity
Disulfide bondi285 ↔ 297By similarity
Disulfide bondi292 ↔ 310By similarity
Disulfide bondi304 ↔ 319By similarity
Disulfide bondi325 ↔ 337By similarity
Disulfide bondi332 ↔ 350By similarity
Disulfide bondi344 ↔ 359By similarity
Disulfide bondi368 ↔ 381By similarity
Disulfide bondi375 ↔ 394By similarity
Disulfide bondi388 ↔ 403By similarity
Glycosylationi554N-linked (GlcNAc...) asparagine1 Publication1
Disulfide bondi764 ↔ 773By similarity
Disulfide bondi766 ↔ 780By similarity
Disulfide bondi783 ↔ 792By similarity
Disulfide bondi795 ↔ 811By similarity
Disulfide bondi814 ↔ 829By similarity
Disulfide bondi816 ↔ 839By similarity
Disulfide bondi842 ↔ 851By similarity
Disulfide bondi854 ↔ 869By similarity
Disulfide bondi879 ↔ 892By similarity
Disulfide bondi894 ↔ 903By similarity
Disulfide bondi906 ↔ 921By similarity
Disulfide bondi1159 ↔ 1168By similarity
Disulfide bondi1161 ↔ 1175By similarity
Disulfide bondi1178 ↔ 1187By similarity
Disulfide bondi1190 ↔ 1206By similarity
Disulfide bondi1209 ↔ 1224By similarity
Disulfide bondi1211 ↔ 1234By similarity
Disulfide bondi1237 ↔ 1246By similarity
Disulfide bondi1249 ↔ 1263By similarity
Disulfide bondi1275 ↔ 1287By similarity
Disulfide bondi1277 ↔ 1293By similarity
Disulfide bondi1295 ↔ 1304By similarity
Disulfide bondi1307 ↔ 1322By similarity
Disulfide bondi1563 ↔ 1572By similarity
Disulfide bondi1565 ↔ 1579By similarity
Disulfide bondi1582 ↔ 1591By similarity
Disulfide bondi1594 ↔ 1610By similarity
Disulfide bondi1613 ↔ 1628By similarity
Disulfide bondi1615 ↔ 1638By similarity
Disulfide bondi1641 ↔ 1650By similarity
Disulfide bondi1653 ↔ 1668By similarity
Glycosylationi1755N-linked (GlcNAc...) asparagine2 Publications1
Glycosylationi2121N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi2995O-linked (Xyl...) (chondroitin sulfate) serineSequence analysis1
Glycosylationi3072N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi3105N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi3279N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi3780N-linked (GlcNAc...) asparagine1 Publication1
Disulfide bondi3819 ↔ 3845By similarity
Glycosylationi3836N-linked (GlcNAc...) asparagine1 Publication1
Disulfide bondi3848 ↔ 3859By similarity
Disulfide bondi3853 ↔ 3869By similarity
Disulfide bondi3871 ↔ 3880By similarity
Disulfide bondi3888 ↔ 3899By similarity
Disulfide bondi3893 ↔ 3910By similarity
Disulfide bondi3912 ↔ 3921By similarity
Glycosylationi3933O-linked (Xyl...) (chondroitin sulfate) serineSequence analysis1
Glycosylationi4068N-linked (GlcNAc...) asparagine1 Publication1
Disulfide bondi4076 ↔ 4102By similarity
Disulfide bondi4108 ↔ 4119By similarity
Disulfide bondi4113 ↔ 4129By similarity
Disulfide bondi4131 ↔ 4140By similarity
Disulfide bondi4147 ↔ 4159By similarity
Disulfide bondi4153 ↔ 4164By similarity
Disulfide bondi4166 ↔ 4175By similarity
Glycosylationi4179O-linked (Xyl...) (chondroitin sulfate) serineSequence analysis1
Disulfide bondi4355 ↔ 43891 Publication

Post-translational modificationi

Proteolytic processing produces the C-terminal angiogenic peptide, endorepellin. This peptide can be further processed to produce the LG3 peptide.2 Publications
N- and O-glycosylated. O-glycosylated with core 1 or possibly core 8 glycans. Perlecan contains three heparan sulfate chains. The LG3 peptide contains at least three and up to five potential O-glycosylation sites but no N-glycosylation.5 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei4196 – 4197Cleavage; by BMP12

Keywords - PTMi

Disulfide bond, Glycoprotein, Heparan sulfate, Proteoglycan

Proteomic databases

EPDiP98160
MaxQBiP98160
PaxDbiP98160
PeptideAtlasiP98160
PRIDEiP98160
ProteomicsDBi57796

2D gel databases

DOSAC-COBS-2DPAGEiP98160

PTM databases

CarbonylDBiP98160
GlyConnecti653
iPTMnetiP98160
PhosphoSitePlusiP98160
UniCarbKBiP98160

Expressioni

Tissue specificityi

Found in the basement membranes.

Gene expression databases

BgeeiENSG00000142798
CleanExiHS_HSPG2
ExpressionAtlasiP98160 baseline and differential
GenevisibleiP98160 HS

Organism-specific databases

HPAiCAB009820
CAB020718
HPA018892

Interactioni

Subunit structurei

Purified perlecan has a strong tendency to aggregate in dimers or stellate structures. It interacts with other basement membrane components such as laminin, prolargin and collagen type IV. Interacts with COL13A1, FGFBP1 and VWA1. Interacts (via C-terminus) with ECM1 (via C-terminus).3 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • integrin binding Source: ARUK-UCL
  • low-density lipoprotein particle receptor binding Source: ARUK-UCL
  • protein C-terminus binding Source: UniProtKB
View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridi109571, 36 interactors
IntActiP98160, 30 interactors
MINTiP98160
STRINGi9606.ENSP00000363827

Structurei

Secondary structure

14391
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni4199 – 4202Combined sources4
Beta strandi4203 – 4214Combined sources12
Helixi4216 – 4219Combined sources4
Beta strandi4228 – 4236Combined sources9
Beta strandi4239 – 4246Combined sources8
Beta strandi4259 – 4265Combined sources7
Beta strandi4268 – 4274Combined sources7
Beta strandi4279 – 4283Combined sources5
Beta strandi4290 – 4292Combined sources3
Beta strandi4294 – 4301Combined sources8
Beta strandi4304 – 4309Combined sources6
Beta strandi4315 – 4318Combined sources4
Beta strandi4320 – 4322Combined sources3
Beta strandi4332 – 4335Combined sources4
Helixi4340 – 4343Combined sources4
Turni4344 – 4346Combined sources3
Beta strandi4353 – 4363Combined sources11
Beta strandi4366 – 4368Combined sources3
Turni4376 – 4378Combined sources3
Beta strandi4381 – 4388Combined sources8

3D structure databases

ProteinModelPortaliP98160
SMRiP98160
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini80 – 191SEAPROSITE-ProRule annotationAdd BLAST112
Domaini198 – 235LDL-receptor class A 1PROSITE-ProRule annotationAdd BLAST38
Domaini284 – 320LDL-receptor class A 2PROSITE-ProRule annotationAdd BLAST37
Domaini324 – 360LDL-receptor class A 3PROSITE-ProRule annotationAdd BLAST37
Domaini367 – 404LDL-receptor class A 4PROSITE-ProRule annotationAdd BLAST38
Domaini405 – 504Ig-like C2-type 1Add BLAST100
Domaini521 – 530Laminin EGF-like 1; first partPROSITE-ProRule annotation10
Domaini538 – 730Laminin IV type A 1PROSITE-ProRule annotationAdd BLAST193
Domaini731 – 763Laminin EGF-like 1; second partPROSITE-ProRule annotationAdd BLAST33
Domaini764 – 813Laminin EGF-like 2PROSITE-ProRule annotationAdd BLAST50
Domaini814 – 871Laminin EGF-like 3PROSITE-ProRule annotationAdd BLAST58
Domaini879 – 923Laminin EGF-like 4; truncatedPROSITE-ProRule annotationAdd BLAST45
Domaini924 – 933Laminin EGF-like 5; first partPROSITE-ProRule annotation10
Domaini941 – 1125Laminin IV type A 2PROSITE-ProRule annotationAdd BLAST185
Domaini1126 – 1158Laminin EGF-like 5; second partPROSITE-ProRule annotationAdd BLAST33
Domaini1159 – 1208Laminin EGF-like 6PROSITE-ProRule annotationAdd BLAST50
Domaini1209 – 1265Laminin EGF-like 7PROSITE-ProRule annotationAdd BLAST57
Domaini1275 – 1324Laminin EGF-like 8PROSITE-ProRule annotationAdd BLAST50
Domaini1325 – 1334Laminin EGF-like 9; first partPROSITE-ProRule annotation10
Domaini1344 – 1529Laminin IV type A 3PROSITE-ProRule annotationAdd BLAST186
Domaini1530 – 1562Laminin EGF-like 9; second partPROSITE-ProRule annotationAdd BLAST33
Domaini1563 – 1612Laminin EGF-like 10PROSITE-ProRule annotationAdd BLAST50
Domaini1613 – 1670Laminin EGF-like 11PROSITE-ProRule annotationAdd BLAST58
Domaini1677 – 1771Ig-like C2-type 2Add BLAST95
Domaini1772 – 1865Ig-like C2-type 3Add BLAST94
Domaini1866 – 1955Ig-like C2-type 4Add BLAST90
Domaini1956 – 2051Ig-like C2-type 5Add BLAST96
Domaini2052 – 2151Ig-like C2-type 6Add BLAST100
Domaini2152 – 2244Ig-like C2-type 7Add BLAST93
Domaini2245 – 2340Ig-like C2-type 8Add BLAST96
Domaini2341 – 2436Ig-like C2-type 9Add BLAST96
Domaini2437 – 2533Ig-like C2-type 10Add BLAST97
Domaini2534 – 2629Ig-like C2-type 11Add BLAST96
Domaini2630 – 2726Ig-like C2-type 12Add BLAST97
Domaini2727 – 2826Ig-like C2-type 13Add BLAST100
Domaini2827 – 2924Ig-like C2-type 14Add BLAST98
Domaini2925 – 3021Ig-like C2-type 15Add BLAST97
Domaini3022 – 3112Ig-like C2-type 16Add BLAST91
Domaini3113 – 3211Ig-like C2-type 17Add BLAST99
Domaini3212 – 3298Ig-like C2-type 18Add BLAST87
Domaini3299 – 3399Ig-like C2-type 19Add BLAST101
Domaini3400 – 3488Ig-like C2-type 20Add BLAST89
Domaini3489 – 3574Ig-like C2-type 21Add BLAST86
Domaini3575 – 3662Ig-like C2-type 22Add BLAST88
Domaini3663 – 3843Laminin G-like 1PROSITE-ProRule annotationAdd BLAST181
Domaini3844 – 3881EGF-like 1PROSITE-ProRule annotationAdd BLAST38
Domaini3884 – 3922EGF-like 2PROSITE-ProRule annotationAdd BLAST39
Domaini3928 – 4103Laminin G-like 2PROSITE-ProRule annotationAdd BLAST176
Domaini4104 – 4141EGF-like 3PROSITE-ProRule annotationAdd BLAST38
Domaini4143 – 4176EGF-like 4PROSITE-ProRule annotationAdd BLAST34
Domaini4201 – 4389Laminin G-like 3PROSITE-ProRule annotationAdd BLAST189

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni4149 – 4151Mediates motor neuron attachmentSequence analysis3
Regioni4299 – 4301Mediates motor neuron attachmentSequence analysis3

Keywords - Domaini

EGF-like domain, Immunoglobulin domain, Laminin EGF-like domain, Repeat, Signal

Phylogenomic databases

eggNOGiKOG3509 Eukaryota
ENOG410XTD2 LUCA
GeneTreeiENSGT00530000063501
HOGENOMiHOG000049276
HOVERGENiHBG008174
InParanoidiP98160
KOiK06255
OMAiTEGPQCN
OrthoDBiEOG091G048M
PhylomeDBiP98160
TreeFamiTF326548

Family and domain databases

CDDicd00112 LDLa, 4 hits
Gene3Di2.60.40.10, 22 hits
InterProiView protein in InterPro
IPR013320 ConA-like_dom_sf
IPR001881 EGF-like_Ca-bd_dom
IPR013032 EGF-like_CS
IPR000742 EGF-like_dom
IPR007110 Ig-like_dom
IPR036179 Ig-like_dom_sf
IPR013783 Ig-like_fold
IPR013098 Ig_I-set
IPR003599 Ig_sub
IPR003598 Ig_sub2
IPR013106 Ig_V-set
IPR002049 Laminin_EGF
IPR001791 Laminin_G
IPR000034 Laminin_IV
IPR036055 LDL_receptor-like_sf
IPR023415 LDLR_class-A_CS
IPR002172 LDrepeatLR_classA_rpt
IPR000082 SEA_dom
PfamiView protein in Pfam
PF00008 EGF, 2 hits
PF07679 I-set, 9 hits
PF13895 Ig_2, 1 hit
PF00052 Laminin_B, 3 hits
PF00053 Laminin_EGF, 9 hits
PF00054 Laminin_G_1, 3 hits
PF00057 Ldl_recept_a, 4 hits
PRINTSiPR00261 LDLRECEPTOR
SMARTiView protein in SMART
SM00181 EGF, 11 hits
SM00179 EGF_CA, 5 hits
SM00180 EGF_Lam, 9 hits
SM00409 IG, 22 hits
SM00408 IGc2, 22 hits
SM00406 IGv, 8 hits
SM00281 LamB, 3 hits
SM00282 LamG, 3 hits
SM00192 LDLa, 4 hits
SM00200 SEA, 1 hit
SUPFAMiSSF48726 SSF48726, 22 hits
SSF49899 SSF49899, 3 hits
SSF57424 SSF57424, 4 hits
PROSITEiView protein in PROSITE
PS00022 EGF_1, 9 hits
PS01186 EGF_2, 6 hits
PS50026 EGF_3, 4 hits
PS01248 EGF_LAM_1, 11 hits
PS50027 EGF_LAM_2, 8 hits
PS50835 IG_LIKE, 22 hits
PS50025 LAM_G_DOMAIN, 3 hits
PS51115 LAMININ_IVA, 3 hits
PS01209 LDLRA_1, 4 hits
PS50068 LDLRA_2, 4 hits
PS50024 SEA, 1 hit

Sequencei

Sequence statusi: Complete.

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

P98160-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGWRAAGALL LALLLHGRLL AVTHGLRAYD GLSLPEDIET VTASQMRWTH 
        60         70         80         90        100
SYLSDDEDML ADSISGDDLG SGDLGSGDFQ MVYFRALVNF TRSIEYSPQL 
       110        120        130        140        150
EDAGSREFRE VSEAVVDTLE SEYLKIPGDQ VVSVVFIKEL DGWVFVELDV 
       160        170        180        190        200
GSEGNADGAQ IQEMLLRVIS SGSVASYVTS PQGFQFRRLG TVPQFPRACT 
       210        220        230        240        250
EAEFACHSYN ECVALEYRCD RRPDCRDMSD ELNCEEPVLG ISPTFSLLVE 
       260        270        280        290        300
TTSLPPRPET TIMRQPPVTH APQPLLPGSV RPLPCGPQEA ACRNGHCIPR 
       310        320        330        340        350
DYLCDGQEDC EDGSDELDCG PPPPCEPNEF PCGNGHCALK LWRCDGDFDC 
       360        370        380        390        400
EDRTDEANCP TKRPEEVCGP TQFRCVSTNM CIPASFHCDE ESDCPDRSDE 
       410        420        430        440        450
FGCMPPQVVT PPRESIQASR GQTVTFTCVA IGVPTPIINW RLNWGHIPSH 
       460        470        480        490        500
PRVTVTSEGG RGTLIIRDVK ESDQGAYTCE AMNARGMVFG IPDGVLELVP 
       510        520        530        540        550
QRGPCPDGHF YLEHSAACLP CFCFGITSVC QSTRRFRDQI RLRFDQPDDF 
       560        570        580        590        600
KGVNVTMPAQ PGTPPLSSTQ LQIDPSLHEF QLVDLSRRFL VHDSFWALPE 
       610        620        630        640        650
QFLGNKVDSY GGSLRYNVRY ELARGMLEPV QRPDVVLMGA GYRLLSRGHT 
       660        670        680        690        700
PTQPGALNQR QVQFSEEHWV HESGRPVQRA ELLQVLQSLE AVLIQTVYNT 
       710        720        730        740        750
KMASVGLSDI AMDTTVTHAT SHGRAHSVEE CRCPIGYSGL SCESCDAHFT 
       760        770        780        790        800
RVPGGPYLGT CSGCNCNGHA SSCDPVYGHC LNCQHNTEGP QCNKCKAGFF 
       810        820        830        840        850
GDAMKATATS CRPCPCPYID ASRRFSDTCF LDTDGQATCD ACAPGYTGRR 
       860        870        880        890        900
CESCAPGYEG NPIQPGGKCR PVNQEIVRCD ERGSMGTSGE ACRCKNNVVG 
       910        920        930        940        950
RLCNECADGS FHLSTRNPDG CLKCFCMGVS RHCTSSSWSR AQLHGASEEP 
       960        970        980        990       1000
GHFSLTNAAS THTTNEGIFS PTPGELGFSS FHRLLSGPYF WSLPSRFLGD 
      1010       1020       1030       1040       1050
KVTSYGGELR FTVTQRSQPG STPLHGQPLV VLQGNNIILE HHVAQEPSPG 
      1060       1070       1080       1090       1100
QPSTFIVPFR EQAWQRPDGQ PATREHLLMA LAGIDTLLIR ASYAQQPAES 
      1110       1120       1130       1140       1150
RVSGISMDVA VPEETGQDPA LEVEQCSCPP GYRGPSCQDC DTGYTRTPSG 
      1160       1170       1180       1190       1200
LYLGTCERCS CHGHSEACEP ETGACQGCQH HTEGPRCEQC QPGYYGDAQR 
      1210       1220       1230       1240       1250
GTPQDCQLCP CYGDPAAGQA AHTCFLDTDG HPTCDACSPG HSGRHCERCA 
      1260       1270       1280       1290       1300
PGYYGNPSQG QPCQRDSQVP GPIGCNCDPQ GSVSSQCDAA GQCQCKAQVE 
      1310       1320       1330       1340       1350
GLTCSHCRPH HFHLSASNPD GCLPCFCMGI TQQCASSAYT RHLISTHFAP 
      1360       1370       1380       1390       1400
GDFQGFALVN PQRNSRLTGE FTVEPVPEGA QLSFGNFAQL GHESFYWQLP 
      1410       1420       1430       1440       1450
ETYQGDKVAA YGGKLRYTLS YTAGPQGSPL SDPDVQITGN NIMLVASQPA 
      1460       1470       1480       1490       1500
LQGPERRSYE IMFREEFWRR PDGQPATREH LLMALADLDE LLIRATFSSV 
      1510       1520       1530       1540       1550
PLAASISAVS LEVAQPGPSN RPRALEVEEC RCPPGYIGLS CQDCAPGYTR 
      1560       1570       1580       1590       1600
TGSGLYLGHC ELCECNGHSD LCHPETGACS QCQHNAAGEF CELCAPGYYG 
      1610       1620       1630       1640       1650
DATAGTPEDC QPCACPLTNP ENMFSRTCES LGAGGYRCTA CEPGYTGQYC 
      1660       1670       1680       1690       1700
EQCGPGYVGN PSVQGGQCLP ETNQAPLVVE VHPARSIVPQ GGSHSLRCQV 
      1710       1720       1730       1740       1750
SGSPPHYFYW SREDGRPVPS GTQQRHQGSE LHFPSVQPSD AGVYICTCRN 
      1760       1770       1780       1790       1800
LHQSNTSRAE LLVTEAPSKP ITVTVEEQRS QSVRPGADVT FICTAKSKSP 
      1810       1820       1830       1840       1850
AYTLVWTRLH NGKLPTRAMD FNGILTIRNV QLSDAGTYVC TGSNMFAMDQ 
      1860       1870       1880       1890       1900
GTATLHVQAS GTLSAPVVSI HPPQLTVQPG QLAEFRCSAT GSPTPTLEWT 
      1910       1920       1930       1940       1950
GGPGGQLPAK AQIHGGILRL PAVEPTDQAQ YLCRAHSSAG QQVARAVLHV 
      1960       1970       1980       1990       2000
HGGGGPRVQV SPERTQVHAG RTVRLYCRAA GVPSATITWR KEGGSLPPQA 
      2010       2020       2030       2040       2050
RSERTDIATL LIPAITTADA GFYLCVATSP AGTAQARIQV VVLSASDASP 
      2060       2070       2080       2090       2100
PPVKIESSSP SVTEGQTLDL NCVVAGSAHA QVTWYRRGGS LPPHTQVHGS 
      2110       2120       2130       2140       2150
RLRLPQVSPA DSGEYVCRVE NGSGPKEASI TVSVLHGTHS GPSYTPVPGS 
      2160       2170       2180       2190       2200
TRPIRIEPSS SHVAEGQTLD LNCVVPGQAH AQVTWHKRGG SLPARHQTHG 
      2210       2220       2230       2240       2250
SLLRLHQVTP ADSGEYVCHV VGTSGPLEAS VLVTIEASVI PGPIPPVRIE 
      2260       2270       2280       2290       2300
SSSSTVAEGQ TLDLSCVVAG QAHAQVTWYK RGGSLPARHQ VRGSRLYIFQ 
      2310       2320       2330       2340       2350
ASPADAGQYV CRASNGMEAS ITVTVTGTQG ANLAYPAGST QPIRIEPSSS 
      2360       2370       2380       2390       2400
QVAEGQTLDL NCVVPGQSHA QVTWHKRGGS LPVRHQTHGS LLRLYQASPA 
      2410       2420       2430       2440       2450
DSGEYVCRVL GSSVPLEASV LVTIEPAGSV PALGVTPTVR IESSSSQVAE 
      2460       2470       2480       2490       2500
GQTLDLNCLV AGQAHAQVTW HKRGGSLPAR HQVHGSRLRL LQVTPADSGE 
      2510       2520       2530       2540       2550
YVCRVVGSSG TQEASVLVTI QQRLSGSHSQ GVAYPVRIES SSASLANGHT 
      2560       2570       2580       2590       2600
LDLNCLVASQ APHTITWYKR GGSLPSRHQI VGSRLRIPQV TPADSGEYVC 
      2610       2620       2630       2640       2650
HVSNGAGSRE TSLIVTIQGS GSSHVPSVSP PIRIESSSPT VVEGQTLDLN 
      2660       2670       2680       2690       2700
CVVARQPQAI ITWYKRGGSL PSRHQTHGSH LRLHQMSVAD SGEYVCRANN 
      2710       2720       2730       2740       2750
NIDALEASIV ISVSPSAGSP SAPGSSMPIR IESSSSHVAE GETLDLNCVV 
      2760       2770       2780       2790       2800
PGQAHAQVTW HKRGGSLPSH HQTRGSRLRL HHVSPADSGE YVCRVMGSSG 
      2810       2820       2830       2840       2850
PLEASVLVTI EASGSSAVHV PAPGGAPPIR IEPSSSRVAE GQTLDLKCVV 
      2860       2870       2880       2890       2900
PGQAHAQVTW HKRGGNLPAR HQVHGPLLRL NQVSPADSGE YSCQVTGSSG 
      2910       2920       2930       2940       2950
TLEASVLVTI EPSSPGPIPA PGLAQPIYIE ASSSHVTEGQ TLDLNCVVPG 
      2960       2970       2980       2990       3000
QAHAQVTWYK RGGSLPARHQ THGSQLRLHL VSPADSGEYV CRAASGPGPE 
      3010       3020       3030       3040       3050
QEASFTVTVP PSEGSSYRLR SPVISIDPPS STVQQGQDAS FKCLIHDGAA 
      3060       3070       3080       3090       3100
PISLEWKTRN QELEDNVHIS PNGSIITIVG TRPSNHGTYR CVASNAYGVA 
      3110       3120       3130       3140       3150
QSVVNLSVHG PPTVSVLPEG PVWVKVGKAV TLECVSAGEP RSSARWTRIS 
      3160       3170       3180       3190       3200
STPAKLEQRT YGLMDSHAVL QISSAKPSDA GTYVCLAQNA LGTAQKQVEV 
      3210       3220       3230       3240       3250
IVDTGAMAPG APQVQAEEAE LTVEAGHTAT LRCSATGSPA PTIHWSKLRS 
      3260       3270       3280       3290       3300
PLPWQHRLEG DTLIIPRVAQ QDSGQYICNA TSPAGHAEAT IILHVESPPY 
      3310       3320       3330       3340       3350
ATTVPEHASV QAGETVQLQC LAHGTPPLTF QWSRVGSSLP GRATARNELL 
      3360       3370       3380       3390       3400
HFERAAPEDS GRYRCRVTNK VGSAEAFAQL LVQGPPGSLP ATSIPAGSTP 
      3410       3420       3430       3440       3450
TVQVTPQLET KSIGASVEFH CAVPSDRGTQ LRWFKEGGQL PPGHSVQDGV 
      3460       3470       3480       3490       3500
LRIQNLDQSC QGTYICQAHG PWGKAQASAQ LVIQALPSVL INIRTSVQTV 
      3510       3520       3530       3540       3550
VVGHAVEFEC LALGDPKPQV TWSKVGGHLR PGIVQSGGVV RIAHVELADA 
      3560       3570       3580       3590       3600
GQYRCTATNA AGTTQSHVLL LVQALPQISM PQEVRVPAGS AAVFPCIASG 
      3610       3620       3630       3640       3650
YPTPDISWSK LDGSLPPDSR LENNMLMLPS VRPQDAGTYV CTATNRQGKV 
      3660       3670       3680       3690       3700
KAFAHLQVPE RVVPYFTQTP YSFLPLPTIK DAYRKFEIKI TFRPDSADGM 
      3710       3720       3730       3740       3750
LLYNGQKRVP GSPTNLANRQ PDFISFGLVG GRPEFRFDAG SGMATIRHPT 
      3760       3770       3780       3790       3800
PLALGHFHTV TLLRSLTQGS LIVGDLAPVN GTSQGKFQGL DLNEELYLGG 
      3810       3820       3830       3840       3850
YPDYGAIPKA GLSSGFIGCV RELRIQGEEI VFHDLNLTAH GISHCPTCRD 
      3860       3870       3880       3890       3900
RPCQNGGQCH DSESSSYVCV CPAGFTGSRC EHSQALHCHP EACGPDATCV 
      3910       3920       3930       3940       3950
NRPDGRGYTC RCHLGRSGLR CEEGVTVTTP SLSGAGSYLA LPALTNTHHE 
      3960       3970       3980       3990       4000
LRLDVEFKPL APDGVLLFSG GKSGPVEDFV SLAMVGGHLE FRYELGSGLA 
      4010       4020       4030       4040       4050
VLRSAEPLAL GRWHRVSAER LNKDGSLRVN GGRPVLRSSP GKSQGLNLHT 
      4060       4070       4080       4090       4100
LLYLGGVEPS VPLSPATNMS AHFRGCVGEV SVNGKRLDLT YSFLGSQGIG 
      4110       4120       4130       4140       4150
QCYDSSPCER QPCQHGATCM PAGEYEFQCL CRDGFKGDLC EHEENPCQLR 
      4160       4170       4180       4190       4200
EPCLHGGTCQ GTRCLCLPGF SGPRCQQGSG HGIAESDWHL EGSGGNDAPG 
      4210       4220       4230       4240       4250
QYGAYFHDDG FLAFPGHVFS RSLPEVPETI ELEVRTSTAS GLLLWQGVEV 
      4260       4270       4280       4290       4300
GEAGQGKDFI SLGLQDGHLV FRYQLGSGEA RLVSEDPIND GEWHRVTALR 
      4310       4320       4330       4340       4350
EGRRGSIQVD GEELVSGRSP GPNVAVNAKG SVYIGGAPDV ATLTGGRFSS 
      4360       4370       4380       4390 
GITGCVKNLV LHSARPGAPP PQPLDLQHRA QAGANTRPCP S
Length:4,391
Mass (Da):468,830
Last modified:January 11, 2011 - v4
Checksum:iC587660E24C83324
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti6A → P in CAA44373 (PubMed:1730768).Curated1
Sequence conflicti6A → P in AAA52700 (PubMed:1569102).Curated1
Sequence conflicti58D → Y in AAA52700 (PubMed:1569102).Curated1
Sequence conflicti435 – 437TPI → APFL in CAA44373 (PubMed:1730768).Curated3
Sequence conflicti450H → Q in CAA44373 (PubMed:1730768).Curated1
Sequence conflicti502R → RA in CAA44373 (PubMed:1730768).Curated1
Sequence conflicti793N → K in CAA44373 (PubMed:1730768).Curated1
Sequence conflicti890 – 891EA → RT in AAB21121 (PubMed:1685141).Curated2
Sequence conflicti909G → R in CAA44373 (PubMed:1730768).Curated1
Sequence conflicti909G → R in AAB21121 (PubMed:1685141).Curated1
Sequence conflicti1102V → L in AAB21121 (PubMed:1685141).Curated1
Sequence conflicti1133R → L in AAB21121 (PubMed:1685141).Curated1
Sequence conflicti1222H → L in AAB21121 (PubMed:1685141).Curated1
Sequence conflicti1406D → G in AAA52699 (PubMed:1679749).Curated1
Sequence conflicti1410A → G in AAA52699 (PubMed:1679749).Curated1
Sequence conflicti1466 – 1470EFWRR → LNLRQ in AAA52699 (PubMed:1679749).Curated5
Sequence conflicti1703 – 1704SP → RG in CAA44373 (PubMed:1730768).Curated2
Sequence conflicti1753Q → R in CAA44373 (PubMed:1730768).Curated1
Sequence conflicti2038I → M in AAA52700 (PubMed:1569102).Curated1
Sequence conflicti2050P → Q in CAA44373 (PubMed:1730768).Curated1
Sequence conflicti2052P → G in AAA52700 (PubMed:1569102).Curated1
Sequence conflicti2093P → H in CAA44373 (PubMed:1730768).Curated1
Sequence conflicti2627S → R in CAA44373 (PubMed:1730768).Curated1
Sequence conflicti2770H → Y in CAA44373 (PubMed:1730768).Curated1
Sequence conflicti3241P → R in CAA44373 (PubMed:1730768).Curated1
Sequence conflicti3427R → Q in AAA52700 (PubMed:1569102).Curated1
Sequence conflicti4004S → T in CAA44373 (PubMed:1730768).Curated1
Sequence conflicti4135F → I in CAA44373 (PubMed:1730768).Curated1
Sequence conflicti4332V → I in CAA44373 (PubMed:1730768).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_04797968D → E. Corresponds to variant dbSNP:rs1869780EnsemblClinVar.1
Natural variantiVAR_057051303L → H. Corresponds to variant dbSNP:rs17460381Ensembl.1
Natural variantiVAR_047980638M → V3 PublicationsCorresponds to variant dbSNP:rs1874792EnsemblClinVar.1
Natural variantiVAR_047981765N → S3 PublicationsCorresponds to variant dbSNP:rs989994EnsemblClinVar.1
Natural variantiVAR_0479821186R → Q. Corresponds to variant dbSNP:rs2229481EnsemblClinVar.1
Natural variantiVAR_0570521323L → V. Corresponds to variant dbSNP:rs10917058Ensembl.1
Natural variantiVAR_0479831503A → V3 PublicationsCorresponds to variant dbSNP:rs897471EnsemblClinVar.1
Natural variantiVAR_0141221532C → Y in SJS1. 1 PublicationCorresponds to variant dbSNP:rs137853248EnsemblClinVar.1
Natural variantiVAR_0479841758R → Q. Corresponds to variant dbSNP:rs2229483Ensembl.1
Natural variantiVAR_0479851919R → C. Corresponds to variant dbSNP:rs2229474EnsemblClinVar.1
Natural variantiVAR_0479861967V → I. Corresponds to variant dbSNP:rs2229475EnsemblClinVar.1
Natural variantiVAR_0479872980L → H1 PublicationCorresponds to variant dbSNP:rs2229489EnsemblClinVar.1
Natural variantiVAR_0479882981V → I. Corresponds to variant dbSNP:rs2229490EnsemblClinVar.1
Natural variantiVAR_0479892995S → G1 PublicationCorresponds to variant dbSNP:rs2229491EnsemblClinVar.1
Natural variantiVAR_0479903168A → T1 PublicationCorresponds to variant dbSNP:rs2228349EnsemblClinVar.1
Natural variantiVAR_0479913256H → Y. Corresponds to variant dbSNP:rs2291827EnsemblClinVar.1
Natural variantiVAR_0479923530R → W. Corresponds to variant dbSNP:rs2270699Ensembl.1
Natural variantiVAR_0479933632R → Q1 PublicationCorresponds to variant dbSNP:rs2229493EnsemblClinVar.1
Natural variantiVAR_0479943640V → I. Corresponds to variant dbSNP:rs17459097EnsemblClinVar.1
Natural variantiVAR_0479954331S → N. Corresponds to variant dbSNP:rs3736360EnsemblClinVar.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M85289 mRNA Translation: AAA52700.1
X62515 mRNA Translation: CAA44373.1
AL590556 Genomic DNA No translation available.
AL590103 Genomic DNA No translation available.
L22078 Genomic DNA No translation available.
AL445795 Genomic DNA Translation: CAC18534.1
S76436 mRNA Translation: AAB21121.2
M64283 mRNA Translation: AAA52699.1
CCDSiCCDS30625.1
PIRiA38096
RefSeqiNP_001278789.1, NM_001291860.1
NP_005520.4, NM_005529.6
UniGeneiHs.562227

Genome annotation databases

EnsembliENST00000374695; ENSP00000363827; ENSG00000142798
GeneIDi3339
KEGGihsa:3339
UCSCiuc001bfj.4 human

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Entry informationi

Entry nameiPGBM_HUMAN
AccessioniPrimary (citable) accession number: P98160
Secondary accession number(s): Q16287, Q5SZI3, Q9H3V5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 11, 2011
Last modified: July 18, 2018
This is version 212 of the entry and version 4 of the sequence. See 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

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