Basement membrane-specific heparan sulfate proteoglycan core protein precursor

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P98160 (PGBM_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 156. History...

Clusters with 100%, 90%, 50% identity |

Documents (6) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Basement membrane-specific heparan sulfate proteoglycan core protein
Short name=HSPG

Alternative name(s):
Perlecan
Short name=PLC

Gene names

Name:

HSPG2

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	4391 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.9 Ref.10 Ref.17 Ref.18 Ref.19 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. Ref.9 Ref.10 Ref.17 Ref.18 Ref.19 The LG3 peptide has anti-angiogenic properties that require binding of calcium ions for full activity. Ref.9 Ref.10 Ref.17 Ref.18 Ref.19
Subunit structure	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). Ref.11 Ref.13 Ref.14
Subcellular location	Secreted › extracellular space › extracellular matrix › basement membrane.
Tissue specificity	Found in the basement membranes.
Post-translational modification	Proteolytic processing produces the C-terminal angiogenic peptide, endorepellin. This peptide can be further processed to produce the LG3 peptide. 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. Ref.9 Ref.15 Ref.21
Involvement in disease	Schwartz-Jampel syndrome (SJS1) [MIM:255800]: Rare 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. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.5 Dyssegmental dysplasia Silverman-Handmaker type (DDSH) [MIM:224410]: The 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. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.12
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.
Sequence similarities	Contains 4 EGF-like domains. Contains 22 Ig-like C2-type (immunoglobulin-like) domains. Contains 11 laminin EGF-like domains. Contains 3 laminin G-like domains. Contains 3 laminin IV type A domains. Contains 4 LDL-receptor class A domains. Contains 1 SEA domain.

Ontologies

Keywords
Biological process	Angiogenesis
Cellular component	Basement membrane Extracellular matrix Secreted
Coding sequence diversity	Polymorphism
Disease	Disease mutation
Domain	EGF-like domain Immunoglobulin domain Laminin EGF-like domain Repeat Signal
Ligand	Calcium Metal-binding
PTM	Disulfide bond Glycoprotein Heparan sulfate Proteoglycan
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	angiogenesis Inferred from electronic annotation. Source: UniProtKB-KW brain development Inferred from electronic annotation. Source: Compara carbohydrate metabolic process Traceable author statement. Source: Reactome cardiac muscle tissue development Inferred from electronic annotation. Source: Compara cartilage development involved in endochondral bone morphogenesis Inferred from electronic annotation. Source: Compara chondrocyte differentiation Inferred from electronic annotation. Source: Compara chondroitin sulfate metabolic process Traceable author statement. Source: Reactome embryonic skeletal system morphogenesis Inferred from electronic annotation. Source: Compara endochondral ossification Inferred from electronic annotation. Source: Compara extracellular matrix organization Inferred from electronic annotation. Source: Compara glycosaminoglycan biosynthetic process Traceable author statement. Source: Reactome glycosaminoglycan catabolic process Traceable author statement. Source: Reactome lipoprotein metabolic process Traceable author statement. Source: Reactome phototransduction, visible light Traceable author statement. Source: Reactome protein localization Inferred from electronic annotation. Source: Compara retinoid metabolic process Traceable author statement. Source: Reactome
Cellular_component	Golgi lumen Traceable author statement. Source: Reactome basal lamina Inferred from electronic annotation. Source: Compara extracellular space Inferred from direct assay PubMed 20551380. Source: BHF-UCL extracellular vesicular exosome Inferred from direct assay PubMed 21362503. Source: UniProtKB lysosomal lumen Traceable author statement. Source: Reactome plasma membrane Traceable author statement. Source: Reactome
Molecular_function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 21

Potential

Chain

22 – 4391

4370

Basement membrane-specific heparan sulfate proteoglycan core protein

PRO_0000026696

Chain

3687 – 4391

705

Endorepellin

PRO_0000391621

Chain

4197 – 4391

195

LG3 peptide

PRO_0000391622

Regions

Domain

80 – 194

115

SEA

Domain

198 – 235

LDL-receptor class A 1

Domain

284 – 320

LDL-receptor class A 2

Domain

324 – 360

LDL-receptor class A 3

Domain

367 – 404

LDL-receptor class A 4

Domain

405 – 504

100

Ig-like C2-type 1

Domain

521 – 530

Laminin EGF-like 1; first part

Domain

538 – 730

193

Laminin IV type A 1

Domain

731 – 763

Laminin EGF-like 1; second part

Domain

764 – 813

Laminin EGF-like 2

Domain

814 – 871

Laminin EGF-like 3

Domain

879 – 923

Laminin EGF-like 4; truncated

Domain

924 – 933

Laminin EGF-like 5; first part

Domain

941 – 1125

185

Laminin IV type A 2

Domain

1126 – 1158

Laminin EGF-like 5; second part

Domain

1159 – 1208

Laminin EGF-like 6

Domain

1209 – 1265

Laminin EGF-like 7

Domain

1275 – 1324

Laminin EGF-like 8

Domain

1325 – 1334

Laminin EGF-like 9; first part

Domain

1344 – 1529

186

Laminin IV type A 3

Domain

1530 – 1562

Laminin EGF-like 9; second part

Domain

1563 – 1612

Laminin EGF-like 10

Domain

1613 – 1670

Laminin EGF-like 11

Domain

1677 – 1771

Ig-like C2-type 2

Domain

1772 – 1865

Ig-like C2-type 3

Domain

1866 – 1955

Ig-like C2-type 4

Domain

1956 – 2051

Ig-like C2-type 5

Domain

2052 – 2151

100

Ig-like C2-type 6

Domain

2152 – 2244

Ig-like C2-type 7

Domain

2245 – 2340

Ig-like C2-type 8

Domain

2341 – 2436

Ig-like C2-type 9

Domain

2437 – 2533

Ig-like C2-type 10

Domain

2534 – 2629

Ig-like C2-type 11

Domain

2630 – 2726

Ig-like C2-type 12

Domain

2727 – 2826

100

Ig-like C2-type 13

Domain

2827 – 2924

Ig-like C2-type 14

Domain

2925 – 3021

Ig-like C2-type 15

Domain

3022 – 3112

Ig-like C2-type 16

Domain

3113 – 3211

Ig-like C2-type 17

Domain

3212 – 3298

Ig-like C2-type 18

Domain

3299 – 3399

101

Ig-like C2-type 19

Domain

3400 – 3488

Ig-like C2-type 20

Domain

3489 – 3574

Ig-like C2-type 21

Domain

3575 – 3662

Ig-like C2-type 22

Domain

3663 – 3843

181

Laminin G-like 1

Domain

3844 – 3881

EGF-like 1

Domain

3884 – 3922

EGF-like 2

Domain

3928 – 4103

176

Laminin G-like 2

Domain

4104 – 4141

EGF-like 3

Domain

4143 – 4176

EGF-like 4

Domain

4201 – 4389

189

Laminin G-like 3

Region

4149 – 4151

Mediates motor neuron attachment Potential

Region

4299 – 4301

Mediates motor neuron attachment Potential

Sites

Metal binding

4258

Calcium

Metal binding

4275

Calcium; via carbonyl oxygen

Metal binding

4325

Calcium; via carbonyl oxygen

Metal binding

4327

Calcium

Site

4196 – 4197

Cleavage; by BMP1

Amino acid modifications

Glycosylation

O-linked (GalNAc...) Ref.21

Glycosylation

O-linked (Xyl...) (heparan sulfate) Potential

Glycosylation

O-linked (Xyl...) (heparan sulfate) Potential

Glycosylation

O-linked (Xyl...) (heparan sulfate) Potential

Glycosylation

N-linked (GlcNAc...) Potential

Glycosylation

554

N-linked (GlcNAc...) Ref.20

Glycosylation

1755

N-linked (GlcNAc...) Ref.16 Ref.20

Glycosylation

2121

N-linked (GlcNAc...) Ref.15

Glycosylation

2995

O-linked (Xyl...) (chondroitin sulfate) Potential

Glycosylation

3072

N-linked (GlcNAc...) Ref.20

Glycosylation

3105

N-linked (GlcNAc...) Potential

Glycosylation

3279

N-linked (GlcNAc...) Potential

Glycosylation

3780

N-linked (GlcNAc...) Ref.20

Glycosylation

3836

N-linked (GlcNAc...) Ref.20

Glycosylation

3933

O-linked (Xyl...) (chondroitin sulfate) Potential

Glycosylation

4068

N-linked (GlcNAc...) Ref.20

Glycosylation

4179

O-linked (Xyl...) (chondroitin sulfate) Potential

Disulfide bond

199 ↔ 212

By similarity

Disulfide bond

206 ↔ 225

By similarity

Disulfide bond

219 ↔ 234

By similarity

Disulfide bond

285 ↔ 297

By similarity

Disulfide bond

292 ↔ 310

By similarity

Disulfide bond

304 ↔ 319

By similarity

Disulfide bond

325 ↔ 337

By similarity

Disulfide bond

332 ↔ 350

By similarity

Disulfide bond

344 ↔ 359

By similarity

Disulfide bond

368 ↔ 381

By similarity

Disulfide bond

375 ↔ 394

By similarity

Disulfide bond

388 ↔ 403

By similarity

Disulfide bond

764 ↔ 773

By similarity

Disulfide bond

766 ↔ 780

By similarity

Disulfide bond

783 ↔ 792

By similarity

Disulfide bond

795 ↔ 811

By similarity

Disulfide bond

814 ↔ 829

By similarity

Disulfide bond

816 ↔ 839

By similarity

Disulfide bond

842 ↔ 851

By similarity

Disulfide bond

854 ↔ 869

By similarity

Disulfide bond

879 ↔ 892

By similarity

Disulfide bond

894 ↔ 903

By similarity

Disulfide bond

906 ↔ 921

By similarity

Disulfide bond

1159 ↔ 1168

By similarity

Disulfide bond

1161 ↔ 1175

By similarity

Disulfide bond

1178 ↔ 1187

By similarity

Disulfide bond

1190 ↔ 1206

By similarity

Disulfide bond

1209 ↔ 1224

By similarity

Disulfide bond

1211 ↔ 1234

By similarity

Disulfide bond

1237 ↔ 1246

By similarity

Disulfide bond

1249 ↔ 1263

By similarity

Disulfide bond

1275 ↔ 1287

By similarity

Disulfide bond

1277 ↔ 1293

By similarity

Disulfide bond

1295 ↔ 1304

By similarity

Disulfide bond

1307 ↔ 1322

By similarity

Disulfide bond

1563 ↔ 1572

By similarity

Disulfide bond

1565 ↔ 1579

By similarity

Disulfide bond

1582 ↔ 1591

By similarity

Disulfide bond

1594 ↔ 1610

By similarity

Disulfide bond

1613 ↔ 1628

By similarity

Disulfide bond

1615 ↔ 1638

By similarity

Disulfide bond

1641 ↔ 1650

By similarity

Disulfide bond

1653 ↔ 1668

By similarity

Disulfide bond

3819 ↔ 3845

By similarity

Disulfide bond

3848 ↔ 3859

By similarity

Disulfide bond

3853 ↔ 3869

By similarity

Disulfide bond

3871 ↔ 3880

By similarity

Disulfide bond

3888 ↔ 3899

By similarity

Disulfide bond

3893 ↔ 3910

By similarity

Disulfide bond

3912 ↔ 3921

By similarity

Disulfide bond

4076 ↔ 4102

By similarity

Disulfide bond

4108 ↔ 4119

By similarity

Disulfide bond

4113 ↔ 4129

By similarity

Disulfide bond

4131 ↔ 4140

By similarity

Disulfide bond

4147 ↔ 4159

By similarity

Disulfide bond

4153 ↔ 4164

By similarity

Disulfide bond

4166 ↔ 4175

By similarity

Disulfide bond

4355 ↔ 4389

Ref.22

Natural variations

Natural variant

D → E.
Corresponds to variant rs1869780 [ dbSNP | Ensembl ].

VAR_047979

Natural variant

303

L → H.
Corresponds to variant rs17460381 [ dbSNP | Ensembl ].

VAR_057051

Natural variant

638

M → V. Ref.1 Ref.2 Ref.5
Corresponds to variant rs1874792 [ dbSNP | Ensembl ].

VAR_047980

Natural variant

765

N → S. Ref.1 Ref.2 Ref.5
Corresponds to variant rs989994 [ dbSNP | Ensembl ].

VAR_047981

Natural variant

1186

R → Q.
Corresponds to variant rs2229481 [ dbSNP | Ensembl ].

VAR_047982

Natural variant

1323

L → V.
Corresponds to variant rs10917058 [ dbSNP | Ensembl ].

VAR_057052

Natural variant

1503

A → V. Ref.1 Ref.2 Ref.5
Corresponds to variant rs897471 [ dbSNP | Ensembl ].

VAR_047983

Natural variant

1532

C → Y in SJS1. Ref.5

VAR_014122

Natural variant

1758

R → Q.
Corresponds to variant rs2229483 [ dbSNP | Ensembl ].

VAR_047984

Natural variant

1919

R → C.
Corresponds to variant rs2229474 [ dbSNP | Ensembl ].

VAR_047985

Natural variant

1967

V → I.
Corresponds to variant rs2229475 [ dbSNP | Ensembl ].

VAR_047986

Natural variant

2980

L → H. Ref.2
Corresponds to variant rs2229489 [ dbSNP | Ensembl ].

VAR_047987

Natural variant

2981

V → I.
Corresponds to variant rs2229490 [ dbSNP | Ensembl ].

VAR_047988

Natural variant

2995

S → G. Ref.2
Corresponds to variant rs2229491 [ dbSNP | Ensembl ].

VAR_047989

Natural variant

3168

A → T. Ref.2
Corresponds to variant rs2228349 [ dbSNP | Ensembl ].

VAR_047990

Natural variant

3256

H → Y.
Corresponds to variant rs2291827 [ dbSNP | Ensembl ].

VAR_047991

Natural variant

3530

R → W.
Corresponds to variant rs2270699 [ dbSNP | Ensembl ].

VAR_047992

Natural variant

3632

R → Q. Ref.2
Corresponds to variant rs2229493 [ dbSNP | Ensembl ].

VAR_047993

Natural variant

3640

V → I.
Corresponds to variant rs17459097 [ dbSNP | Ensembl ].

VAR_047994

Natural variant

4331

S → N.
Corresponds to variant rs3736360 [ dbSNP | Ensembl ].

VAR_047995

Experimental info

Mutagenesis

4197

D → I: Abolishes BMP1-mediated cleavage of endorepellin. Ref.9

Mutagenesis

4258

D → A: Retains proper folding. Reduced calcium ion binding. Ref.9

Mutagenesis

4327

N → A: Retains proper folding. Reduced calcium ion binding. Ref.9

Sequence conflict

A → P in CAA44373. Ref.2

Sequence conflict

A → P in AAA52700. Ref.1

Sequence conflict

D → Y in AAA52700. Ref.1

Sequence conflict

435 – 437

TPI → APFL in CAA44373. Ref.2

Sequence conflict

450

H → Q in CAA44373. Ref.2

Sequence conflict

502

R → RA in CAA44373. Ref.2

Sequence conflict

793

N → K in CAA44373. Ref.2

Sequence conflict

890 – 891

EA → RT in AAB21121. Ref.6

Sequence conflict

909

G → R in CAA44373. Ref.2

Sequence conflict

909

G → R in AAB21121. Ref.6

Sequence conflict

1102

V → L in AAB21121. Ref.6

Sequence conflict

1133

R → L in AAB21121. Ref.6

Sequence conflict

1222

H → L in AAB21121. Ref.6

Sequence conflict

1406

D → G in AAA52699. Ref.7

Sequence conflict

1410

A → G in AAA52699. Ref.7

Sequence conflict

1466 – 1470

EFWRR → LNLRQ in AAA52699. Ref.7

Sequence conflict

1703 – 1704

SP → RG in CAA44373. Ref.2

Sequence conflict

1753

Q → R in CAA44373. Ref.2

Sequence conflict

2038

I → M in AAA52700. Ref.1

Sequence conflict

2050

P → Q in CAA44373. Ref.2

Sequence conflict

2052

P → G in AAA52700. Ref.1

Sequence conflict

2093

P → H in CAA44373. Ref.2

Sequence conflict

2627

S → R in CAA44373. Ref.2

Sequence conflict

2770

H → Y in CAA44373. Ref.2

Sequence conflict

3241

P → R in CAA44373. Ref.2

Sequence conflict

3427

R → Q in AAA52700. Ref.1

Sequence conflict

4004

S → T in CAA44373. Ref.2

Sequence conflict

4135

F → I in CAA44373. Ref.2

Sequence conflict

4332

V → I in CAA44373. Ref.2

Secondary structure

4391

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P98160 [UniParc].

Last modified January 11, 2011. Version 4.
Checksum: C587660E24C83324
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FASTA

4,391

468,830

        10         20         30         40         50         60 
MGWRAAGALL LALLLHGRLL AVTHGLRAYD GLSLPEDIET VTASQMRWTH SYLSDDEDML 

        70         80         90        100        110        120 
ADSISGDDLG SGDLGSGDFQ MVYFRALVNF TRSIEYSPQL EDAGSREFRE VSEAVVDTLE 

       130        140        150        160        170        180 
SEYLKIPGDQ VVSVVFIKEL DGWVFVELDV GSEGNADGAQ IQEMLLRVIS SGSVASYVTS 

       190        200        210        220        230        240 
PQGFQFRRLG TVPQFPRACT EAEFACHSYN ECVALEYRCD RRPDCRDMSD ELNCEEPVLG 

       250        260        270        280        290        300 
ISPTFSLLVE TTSLPPRPET TIMRQPPVTH APQPLLPGSV RPLPCGPQEA ACRNGHCIPR 

       310        320        330        340        350        360 
DYLCDGQEDC EDGSDELDCG PPPPCEPNEF PCGNGHCALK LWRCDGDFDC EDRTDEANCP 

       370        380        390        400        410        420 
TKRPEEVCGP TQFRCVSTNM CIPASFHCDE ESDCPDRSDE FGCMPPQVVT PPRESIQASR 

       430        440        450        460        470        480 
GQTVTFTCVA IGVPTPIINW RLNWGHIPSH PRVTVTSEGG RGTLIIRDVK ESDQGAYTCE 

       490        500        510        520        530        540 
AMNARGMVFG IPDGVLELVP QRGPCPDGHF YLEHSAACLP CFCFGITSVC QSTRRFRDQI 

       550        560        570        580        590        600 
RLRFDQPDDF KGVNVTMPAQ PGTPPLSSTQ LQIDPSLHEF QLVDLSRRFL VHDSFWALPE 

       610        620        630        640        650        660 
QFLGNKVDSY GGSLRYNVRY ELARGMLEPV QRPDVVLMGA GYRLLSRGHT PTQPGALNQR 

       670        680        690        700        710        720 
QVQFSEEHWV HESGRPVQRA ELLQVLQSLE AVLIQTVYNT KMASVGLSDI AMDTTVTHAT 

       730        740        750        760        770        780 
SHGRAHSVEE CRCPIGYSGL SCESCDAHFT RVPGGPYLGT CSGCNCNGHA SSCDPVYGHC 

       790        800        810        820        830        840 
LNCQHNTEGP QCNKCKAGFF GDAMKATATS CRPCPCPYID ASRRFSDTCF LDTDGQATCD 

       850        860        870        880        890        900 
ACAPGYTGRR CESCAPGYEG NPIQPGGKCR PVNQEIVRCD ERGSMGTSGE ACRCKNNVVG 

       910        920        930        940        950        960 
RLCNECADGS FHLSTRNPDG CLKCFCMGVS RHCTSSSWSR AQLHGASEEP GHFSLTNAAS 

       970        980        990       1000       1010       1020 
THTTNEGIFS PTPGELGFSS FHRLLSGPYF WSLPSRFLGD KVTSYGGELR FTVTQRSQPG 

      1030       1040       1050       1060       1070       1080 
STPLHGQPLV VLQGNNIILE HHVAQEPSPG QPSTFIVPFR EQAWQRPDGQ PATREHLLMA 

      1090       1100       1110       1120       1130       1140 
LAGIDTLLIR ASYAQQPAES RVSGISMDVA VPEETGQDPA LEVEQCSCPP GYRGPSCQDC 

      1150       1160       1170       1180       1190       1200 
DTGYTRTPSG LYLGTCERCS CHGHSEACEP ETGACQGCQH HTEGPRCEQC QPGYYGDAQR 

      1210       1220       1230       1240       1250       1260 
GTPQDCQLCP CYGDPAAGQA AHTCFLDTDG HPTCDACSPG HSGRHCERCA PGYYGNPSQG 

      1270       1280       1290       1300       1310       1320 
QPCQRDSQVP GPIGCNCDPQ GSVSSQCDAA GQCQCKAQVE GLTCSHCRPH HFHLSASNPD 

      1330       1340       1350       1360       1370       1380 
GCLPCFCMGI TQQCASSAYT RHLISTHFAP GDFQGFALVN PQRNSRLTGE FTVEPVPEGA 

      1390       1400       1410       1420       1430       1440 
QLSFGNFAQL GHESFYWQLP ETYQGDKVAA YGGKLRYTLS YTAGPQGSPL SDPDVQITGN 

      1450       1460       1470       1480       1490       1500 
NIMLVASQPA LQGPERRSYE IMFREEFWRR PDGQPATREH LLMALADLDE LLIRATFSSV 

      1510       1520       1530       1540       1550       1560 
PLAASISAVS LEVAQPGPSN RPRALEVEEC RCPPGYIGLS CQDCAPGYTR TGSGLYLGHC 

      1570       1580       1590       1600       1610       1620 
ELCECNGHSD LCHPETGACS QCQHNAAGEF CELCAPGYYG DATAGTPEDC QPCACPLTNP 

      1630       1640       1650       1660       1670       1680 
ENMFSRTCES LGAGGYRCTA CEPGYTGQYC EQCGPGYVGN PSVQGGQCLP ETNQAPLVVE 

      1690       1700       1710       1720       1730       1740 
VHPARSIVPQ GGSHSLRCQV SGSPPHYFYW SREDGRPVPS GTQQRHQGSE LHFPSVQPSD 

      1750       1760       1770       1780       1790       1800 
AGVYICTCRN LHQSNTSRAE LLVTEAPSKP ITVTVEEQRS QSVRPGADVT FICTAKSKSP 

      1810       1820       1830       1840       1850       1860 
AYTLVWTRLH NGKLPTRAMD FNGILTIRNV QLSDAGTYVC TGSNMFAMDQ GTATLHVQAS 

      1870       1880       1890       1900       1910       1920 
GTLSAPVVSI HPPQLTVQPG QLAEFRCSAT GSPTPTLEWT GGPGGQLPAK AQIHGGILRL 

      1930       1940       1950       1960       1970       1980 
PAVEPTDQAQ YLCRAHSSAG QQVARAVLHV HGGGGPRVQV SPERTQVHAG RTVRLYCRAA 

      1990       2000       2010       2020       2030       2040 
GVPSATITWR KEGGSLPPQA RSERTDIATL LIPAITTADA GFYLCVATSP AGTAQARIQV 

      2050       2060       2070       2080       2090       2100 
VVLSASDASP PPVKIESSSP SVTEGQTLDL NCVVAGSAHA QVTWYRRGGS LPPHTQVHGS 

      2110       2120       2130       2140       2150       2160 
RLRLPQVSPA DSGEYVCRVE NGSGPKEASI TVSVLHGTHS GPSYTPVPGS TRPIRIEPSS 

      2170       2180       2190       2200       2210       2220 
SHVAEGQTLD LNCVVPGQAH AQVTWHKRGG SLPARHQTHG SLLRLHQVTP ADSGEYVCHV 

      2230       2240       2250       2260       2270       2280 
VGTSGPLEAS VLVTIEASVI PGPIPPVRIE SSSSTVAEGQ TLDLSCVVAG QAHAQVTWYK 

      2290       2300       2310       2320       2330       2340 
RGGSLPARHQ VRGSRLYIFQ ASPADAGQYV CRASNGMEAS ITVTVTGTQG ANLAYPAGST 

      2350       2360       2370       2380       2390       2400 
QPIRIEPSSS QVAEGQTLDL NCVVPGQSHA QVTWHKRGGS LPVRHQTHGS LLRLYQASPA 

      2410       2420       2430       2440       2450       2460 
DSGEYVCRVL GSSVPLEASV LVTIEPAGSV PALGVTPTVR IESSSSQVAE GQTLDLNCLV 

      2470       2480       2490       2500       2510       2520 
AGQAHAQVTW HKRGGSLPAR HQVHGSRLRL LQVTPADSGE YVCRVVGSSG TQEASVLVTI 

      2530       2540       2550       2560       2570       2580 
QQRLSGSHSQ GVAYPVRIES SSASLANGHT LDLNCLVASQ APHTITWYKR GGSLPSRHQI 

      2590       2600       2610       2620       2630       2640 
VGSRLRIPQV TPADSGEYVC HVSNGAGSRE TSLIVTIQGS GSSHVPSVSP PIRIESSSPT 

      2650       2660       2670       2680       2690       2700 
VVEGQTLDLN CVVARQPQAI ITWYKRGGSL PSRHQTHGSH LRLHQMSVAD SGEYVCRANN 

      2710       2720       2730       2740       2750       2760 
NIDALEASIV ISVSPSAGSP SAPGSSMPIR IESSSSHVAE GETLDLNCVV PGQAHAQVTW 

      2770       2780       2790       2800       2810       2820 
HKRGGSLPSH HQTRGSRLRL HHVSPADSGE YVCRVMGSSG PLEASVLVTI EASGSSAVHV 

      2830       2840       2850       2860       2870       2880 
PAPGGAPPIR IEPSSSRVAE GQTLDLKCVV PGQAHAQVTW HKRGGNLPAR HQVHGPLLRL 

      2890       2900       2910       2920       2930       2940 
NQVSPADSGE YSCQVTGSSG TLEASVLVTI EPSSPGPIPA PGLAQPIYIE ASSSHVTEGQ 

      2950       2960       2970       2980       2990       3000 
TLDLNCVVPG QAHAQVTWYK RGGSLPARHQ THGSQLRLHL VSPADSGEYV CRAASGPGPE 

      3010       3020       3030       3040       3050       3060 
QEASFTVTVP PSEGSSYRLR SPVISIDPPS STVQQGQDAS FKCLIHDGAA PISLEWKTRN 

      3070       3080       3090       3100       3110       3120 
QELEDNVHIS PNGSIITIVG TRPSNHGTYR CVASNAYGVA QSVVNLSVHG PPTVSVLPEG 

      3130       3140       3150       3160       3170       3180 
PVWVKVGKAV TLECVSAGEP RSSARWTRIS STPAKLEQRT YGLMDSHAVL QISSAKPSDA 

      3190       3200       3210       3220       3230       3240 
GTYVCLAQNA LGTAQKQVEV IVDTGAMAPG APQVQAEEAE LTVEAGHTAT LRCSATGSPA 

      3250       3260       3270       3280       3290       3300 
PTIHWSKLRS PLPWQHRLEG DTLIIPRVAQ QDSGQYICNA TSPAGHAEAT IILHVESPPY 

      3310       3320       3330       3340       3350       3360 
ATTVPEHASV QAGETVQLQC LAHGTPPLTF QWSRVGSSLP GRATARNELL HFERAAPEDS 

      3370       3380       3390       3400       3410       3420 
GRYRCRVTNK VGSAEAFAQL LVQGPPGSLP ATSIPAGSTP TVQVTPQLET KSIGASVEFH 

      3430       3440       3450       3460       3470       3480 
CAVPSDRGTQ LRWFKEGGQL PPGHSVQDGV LRIQNLDQSC QGTYICQAHG PWGKAQASAQ 

      3490       3500       3510       3520       3530       3540 
LVIQALPSVL INIRTSVQTV VVGHAVEFEC LALGDPKPQV TWSKVGGHLR PGIVQSGGVV 

      3550       3560       3570       3580       3590       3600 
RIAHVELADA GQYRCTATNA AGTTQSHVLL LVQALPQISM PQEVRVPAGS AAVFPCIASG 

      3610       3620       3630       3640       3650       3660 
YPTPDISWSK LDGSLPPDSR LENNMLMLPS VRPQDAGTYV CTATNRQGKV KAFAHLQVPE 

      3670       3680       3690       3700       3710       3720 
RVVPYFTQTP YSFLPLPTIK DAYRKFEIKI TFRPDSADGM LLYNGQKRVP GSPTNLANRQ 

      3730       3740       3750       3760       3770       3780 
PDFISFGLVG GRPEFRFDAG SGMATIRHPT PLALGHFHTV TLLRSLTQGS LIVGDLAPVN 

      3790       3800       3810       3820       3830       3840 
GTSQGKFQGL DLNEELYLGG YPDYGAIPKA GLSSGFIGCV RELRIQGEEI VFHDLNLTAH 

      3850       3860       3870       3880       3890       3900 
GISHCPTCRD RPCQNGGQCH DSESSSYVCV CPAGFTGSRC EHSQALHCHP EACGPDATCV 

      3910       3920       3930       3940       3950       3960 
NRPDGRGYTC RCHLGRSGLR CEEGVTVTTP SLSGAGSYLA LPALTNTHHE LRLDVEFKPL 

      3970       3980       3990       4000       4010       4020 
APDGVLLFSG GKSGPVEDFV SLAMVGGHLE FRYELGSGLA VLRSAEPLAL GRWHRVSAER 

      4030       4040       4050       4060       4070       4080 
LNKDGSLRVN GGRPVLRSSP GKSQGLNLHT LLYLGGVEPS VPLSPATNMS AHFRGCVGEV 

      4090       4100       4110       4120       4130       4140 
SVNGKRLDLT YSFLGSQGIG QCYDSSPCER QPCQHGATCM PAGEYEFQCL CRDGFKGDLC 

      4150       4160       4170       4180       4190       4200 
EHEENPCQLR EPCLHGGTCQ GTRCLCLPGF SGPRCQQGSG HGIAESDWHL EGSGGNDAPG 

      4210       4220       4230       4240       4250       4260 
QYGAYFHDDG FLAFPGHVFS RSLPEVPETI ELEVRTSTAS GLLLWQGVEV GEAGQGKDFI 

      4270       4280       4290       4300       4310       4320 
SLGLQDGHLV FRYQLGSGEA RLVSEDPIND GEWHRVTALR EGRRGSIQVD GEELVSGRSP 

      4330       4340       4350       4360       4370       4380 
GPNVAVNAKG SVYIGGAPDV ATLTGGRFSS GITGCVKNLV LHSARPGAPP PQPLDLQHRA 

      4390 
QAGANTRPCP S

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Primary structure of the human heparan sulfate proteoglycan from basement membrane (HSPG2/perlecan). A chimeric molecule with multiple domains homologous to the low density lipoprotein receptor, laminin, neural cell adhesion molecules, and epidermal growth factor." Murdoch A.D., Dodge G.R., Cohen I., Tuan R.S., Iozzo R.V. J. Biol. Chem. 267:8544-8557(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS VAL-638; SER-765 AND VAL-1503. Tissue: Colon and Skin.
[2]	"Human basement membrane heparan sulfate proteoglycan core protein: a 467-kD protein containing multiple domains resembling elements of the low density lipoprotein receptor, laminin, neural cell adhesion molecules, and epidermal growth factor." Kallunki P., Tryggvason K. J. Cell Biol. 116:559-571(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS VAL-638; SER-765; VAL-1503; HIS-2980; GLY-2995; THR-3168 AND GLN-3632.
[3]	"The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. Bentley D.R. Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"Structural characterization of the complete human perlecan gene and its promoter." Cohen I.R., Graessel S., Murdoch A.D., Iozzo R.V. Proc. Natl. Acad. Sci. U.S.A. 90:10404-10408(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21.
[5]	"Perlecan, the major proteoglycan of basement membranes, is altered in patients with Schwartz-Jampel syndrome (chondrodystrophic myotonia)." Nicole S., Davoine C.-S., Topaloglu H., Cattolico L., Barral D., Beighton P., Ben-Hamida C., Hammouda H., Cruaud C., White P.S., Samson D., Urtizberea J.A., Lehmann-Horn F., Weissenbach J., Hentati F., Fontaine B. Nat. Genet. 26:480-483(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 22-4391, VARIANTS VAL-638 AND SJS1 TYR-1532, VARIANTS SER-765 AND VAL-1503.
[6]	"Cloning of human heparan sulfate proteoglycan core protein, assignment of the gene (HSPG2) to 1p36.1-->p35 and identification of a BamHI restriction fragment length polymorphism." Kallunki P., Eddy R.L., Byers M.G., Kestila M., Shows T.B., Tryggvason K. Genomics 11:389-396(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 890-1396. Tissue: Fibrosarcoma.
[7]	"Heparan sulfate proteoglycan of human colon: partial molecular cloning, cellular expression, and mapping of the gene (HSPG2) to the short arm of human chromosome 1." Dodge G.R., Kovalszky I., Chu M.-L., Hassell J.R., McBride O.W., Yi H.F., Iozzo R.V. Genomics 10:673-680(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1016-1470. Tissue: Colon.
[8]	"Matrix-associated heparan sulfate proteoglycan: core protein-specific monoclonal antibodies decorate the pericellular matrix of connective tissue cells and the stromal side of basement membranes." Heremans A., van der Schueren B., de Cock B., Paulsson M., Cassiman J.-J., van den Berghe H., David G. J. Cell Biol. 109:3199-3211(1989) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 1379-1398 AND 2259-2278.
[9]	"BMP-1/Tolloid-like metalloproteases process endorepellin, the angiostatic C-terminal fragment of perlecan." Gonzalez E.M., Reed C.C., Bix G., Fu J., Zhang Y., Gopalakrishnan B., Greenspan D.S., Iozzo R.V. J. Biol. Chem. 280:7080-7087(2005) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 4197-4208, PROTEOLYTIC PROCESSING AT ASN-4196, FUNCTION OF LG3 PEPTIDE, GLYCOSYLATION, MUTAGENESIS OF ASP-4197; ASP-4258 AND ASN-4327.
[10]	"Endorepellin, a novel inhibitor of angiogenesis derived from the C terminus of perlecan." Mongiat M., Sweeney S.M., San Antonio J.D., Fu J., Iozzo R.V. J. Biol. Chem. 278:4238-4249(2003) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 4197-4203, PROTEOLYTIC PROCESSING AT ASN-4196, FUNCTION OF ENDOREPELLIN AND LG3 PEPTIDE.
[11]	"Fibroblast growth factor-binding protein is a novel partner for perlecan protein core." Mongiat M., Otto J., Oldershaw R., Ferrer F., Sato J.D., Iozzo R.V. J. Biol. Chem. 276:10263-10271(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH FGFBP1.
[12]	"Dyssegmental dysplasia, Silverman-Handmaker type, is caused by functional null mutations of the perlecan gene." Arikawa-Hirasawa E., Wilcox W.R., Le A.H., Silverman N., Govindraj P., Hassell J.R., Yamada Y. Nat. Genet. 27:431-434(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INVOLVEMENT IN DDSH.
[13]	"The type XIII collagen ectodomain is a 150-nm rod and capable of binding to fibronectin, nidogen-2, perlecan, and heparin." Tu H., Sasaki T., Snellman A., Gohring W., Pirila P., Timpl R., Pihlajaniemi T. J. Biol. Chem. 277:23092-23099(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH COL13A1.
[14]	"Perlecan protein core interacts with extracellular matrix protein 1 (ECM1), a glycoprotein involved in bone formation and angiogenesis." Mongiat M., Fu J., Oldershaw R., Greenhalgh R., Gown A.M., Iozzo R.V. J. Biol. Chem. 278:17491-17499(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ECM1.
[15]	"Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry." Zhang H., Li X.-J., Martin D.B., Aebersold R. Nat. Biotechnol. 21:660-666(2003) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION AT ASN-2121.
[16]	"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry." Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D. J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1755, MASS SPECTROMETRY. Tissue: Plasma.
[17]	"Endorepellin in vivo: targeting the tumor vasculature and retarding cancer growth and metabolism." Bix G., Castello R., Burrows M., Zoeller J.J., Weech M., Iozzo R.A., Cardi C., Thakur M.L., Barker C.A., Camphausen K., Iozzo R.V. J. Natl. Cancer Inst. 98:1634-1646(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION OF ENDOREPELLIN.
[18]	"Integrin alpha2beta1 is the required receptor for endorepellin angiostatic activity." Woodall B.P., Nystroem A., Iozzo R.A., Eble J.A., Niland S., Krieg T., Eckes B., Pozzi A., Iozzo R.V. J. Biol. Chem. 283:2335-2343(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION OF ENDOREPELLIN, IDENTIFICATION OF RECEPTOR.
[19]	"Role of tyrosine phosphatase SHP-1 in the mechanism of endorepellin angiostatic activity." Nystrom A., Shaik Z.P., Gullberg D., Krieg T., Eckes B., Zent R., Pozzi A., Iozzo R.V. Blood 114:4897-4906(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[20]	"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry." Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H. J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-554; ASN-1755; ASN-3072; ASN-3780; ASN-3836 AND ASN-4068, MASS SPECTROMETRY. Tissue: Liver.
[21]	"Human urinary glycoproteomics; attachment site specific analysis of N-and O-linked glycosylations by CID and ECD." Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G. Mol. Cell. Proteomics 0:0-0(2011) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION AT THR-42, STRUCTURE OF CARBOHYDRATES, MASS SPECTROMETRY.
[22]	"Crystal structure of the LG3 domain of endorepellin, an angiogenesis inhibitor." Le B.V., Kim H., Choi J., Kim J.H., Hahn M.J., Lee C., Kim K.K., Hwang H.Y. J. Mol. Biol. 414:231-242(2011) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 4197-4391, DISULFIDE BOND, CALCIUM-BINDING SITES.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Wikipedia

Perlecan entry

GeneReviews

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M85289 mRNA. Translation: AAA52700.1.
X62515 mRNA. Translation: CAA44373.1.
AL590556, AL590103 Genomic DNA. Translation: CAH71870.1.
AL590103, AL590556 Genomic DNA. Translation: CAI12125.1.
L22078 Genomic DNA. No translation available.
AL445795 Genomic DNA. Translation: CAC18534.1.
S76436 mRNA. Translation: AAB21121.2.
M64283 mRNA. Translation: AAA52699.1.

IPI

IPI00024284.

PIR

A38096.

RefSeq

NP_005520.4. NM_005529.5.

UniGene

Hs.562227.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3SH4	X-ray	1.50	A	4197-4391	[»]
3SH5	X-ray	2.80	A	4197-4391	[»]

ProteinModelPortal

P98160.

SMR

P98160. Positions 1770-1858, 4197-4391.

ModBase

Search...

Protein-protein interaction databases

IntAct

P98160. 8 interactions.

MINT

MINT-123304.

STRING

9606.ENSP00000363827.

PTM databases

PhosphoSite

P98160.

Polymorphism databases

DMDM

218512120.

2D gel databases

DOSAC-COBS-2DPAGE

P98160.

Proteomic databases

PaxDb

P98160.

PRIDE

P98160.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000374695; ENSP00000363827; ENSG00000142798.

GeneID

3339.

KEGG

hsa:3339.

UCSC

uc001bfj.3. human.

Organism-specific databases

CTD

3339.

GeneCards

GC01M022148.

H-InvDB

HIX0023554.
HIX0023598.

HGNC

HGNC:5273. HSPG2.

HPA

CAB009820.
CAB020718.
HPA018892.

MIM

142461. gene.
224410. phenotype.
255800. phenotype.

neXtProt

NX_P98160.

Orphanet

1865. Dyssegmental dysplasia, Silverman-Handmaker type.
800. Schwartz-Jampel syndrome.

PharmGKB

PA29537.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG258321.

HOGENOM

HOG000049276.

HOVERGEN

HBG008174.

InParanoid

P98160.

K06255.

OMA

GVTQQCA.

OrthoDB

EOG44QT00.

Enzyme and pathway databases

Reactome

REACT_111217. Metabolism.
REACT_116125. Disease.

Gene expression databases

ArrayExpress

P98160.

Bgee

P98160.

CleanEx

HS_HSPG2.

Genevestigator

P98160.

GermOnline

ENSG00000142798. Homo sapiens.

Family and domain databases

Gene3D

2.60.120.200. 3 hits.
2.60.40.10. 22 hits.
4.10.400.10. 4 hits.

InterPro

IPR008985. ConA-like_lec_gl_sf.
IPR013320. ConA-like_subgrp.
IPR000742. EG-like_dom.
IPR013032. EGF-like_CS.
IPR002049. EGF_laminin.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003598. Ig_sub2.
IPR018031. Laminin_B_subgr.
IPR000034. Laminin_B_type_IV.
IPR001791. Laminin_G.
IPR023415. LDLR_class-A_CS.
IPR002172. LDrepeatLR_classA_rpt.
IPR000082. SEA_dom.
[Graphical view]

Pfam

PF00008. EGF. 2 hits.
PF12661. hEGF. 1 hit.
PF07679. I-set. 18 hits.
PF00052. Laminin_B. 3 hits.
PF00053. Laminin_EGF. 9 hits.
PF00054. Laminin_G_1. 1 hit.
PF02210. Laminin_G_2. 2 hits.
PF00057. Ldl_recept_a. 4 hits.
[Graphical view]

SMART

SM00181. EGF. 4 hits.
SM00180. EGF_Lam. 8 hits.
SM00408. IGc2. 22 hits.
SM00281. LamB. 3 hits.
SM00282. LamG. 3 hits.
SM00192. LDLa. 4 hits.
SM00200. SEA. 1 hit.
[Graphical view]

SUPFAM

SSF49899. ConA_like_lec_gl. 3 hits.
SSF57424. LDL_rcpt_classA_cys-rich. 4 hits.

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.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

HSPG2. human.

DrugBank

DB00102. Becaplermin.
DB00039. Palifermin.

GenomeRNAi

3339.

NextBio

13216.

SOURCE

Search...

Entry information

Entry name

PGBM_HUMAN

Accession

Primary (citable) accession number: P98160
Secondary accession number(s): Q16287, Q5SZI3, Q9H3V5

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	January 11, 2011
Last modified:	May 29, 2013
This is version 156 of the entry and version 4 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.

Relevant documents

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Cleaved into the following 2 chains:

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Natural variations

Experimental info

Secondary structure

Sequences

References

Web resources

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Polymorphism databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents