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Protein

Basement membrane-specific heparan sulfate proteoglycan core protein

Gene

HSPG2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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.

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
  • protein C-terminus binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Angiogenesis

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000142798-MONOMER.
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-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:
Gene namesi
Name:HSPG2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:5273. HSPG2.

Subcellular locationi

GO - Cellular componenti

  • basement membrane Source: UniProtKB-SubCell
  • extracellular exosome Source: UniProtKB
  • extracellular matrix Source: UniProtKB
  • extracellular region Source: Reactome
  • extracellular space Source: UniProtKB
  • focal adhesion Source: UniProtKB
  • Golgi lumen Source: Reactome
  • lysosomal lumen Source: Reactome
  • plasma membrane Source: Reactome
Complete GO annotation...

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 rs137853248dbSNPEnsembl.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...)1 Publication1
Glycosylationi65O-linked (Xyl...) (heparan sulfate)Sequence analysis1
Glycosylationi71O-linked (Xyl...) (heparan sulfate)Sequence analysis1
Glycosylationi76O-linked (Xyl...) (heparan sulfate)Sequence analysis1
Glycosylationi89N-linked (GlcNAc...)Sequence 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...)1 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...)2 Publications1
Glycosylationi2121N-linked (GlcNAc...)1 Publication1
Glycosylationi2995O-linked (Xyl...) (chondroitin sulfate)Sequence analysis1
Glycosylationi3072N-linked (GlcNAc...)1 Publication1
Glycosylationi3105N-linked (GlcNAc...)Sequence analysis1
Glycosylationi3279N-linked (GlcNAc...)Sequence analysis1
Glycosylationi3780N-linked (GlcNAc...)1 Publication1
Disulfide bondi3819 ↔ 3845By similarity
Glycosylationi3836N-linked (GlcNAc...)1 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)Sequence analysis1
Glycosylationi4068N-linked (GlcNAc...)1 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)Sequence 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.

2D gel databases

DOSAC-COBS-2DPAGEP98160.

PTM databases

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

WithEntry#Exp.IntActNotes
FLT1P17948-22EBI-6896607,EBI-6530464
KDRP359685EBI-947664,EBI-1005487

GO - Molecular functioni

  • protein C-terminus binding Source: UniProtKB

Protein-protein interaction databases

BioGridi109571. 32 interactors.
IntActiP98160. 30 interactors.
MINTiMINT-123304.
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

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3SH4X-ray1.50A4197-4391[»]
3SH5X-ray2.80A4197-4391[»]
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

Sequence similaritiesi

Contains 4 EGF-like domains.PROSITE-ProRule annotation
Contains 11 laminin EGF-like domains.PROSITE-ProRule annotation
Contains 3 laminin G-like domains.PROSITE-ProRule annotation
Contains 3 laminin IV type A domains.PROSITE-ProRule annotation
Contains 4 LDL-receptor class A domains.PROSITE-ProRule annotation
Contains 1 SEA domain.PROSITE-ProRule annotation

Keywords - Domaini

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

Phylogenomic databases

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

Family and domain databases

Gene3Di2.60.120.200. 3 hits.
2.60.40.10. 22 hits.
4.10.400.10. 4 hits.
InterProiIPR013320. ConA-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR007110. Ig-like_dom.
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.
IPR023415. LDLR_class-A_CS.
IPR002172. LDrepeatLR_classA_rpt.
IPR000082. SEA_dom.
[Graphical view]
PfamiPF00008. 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.
[Graphical view]
PRINTSiPR00261. LDLRECEPTOR.
SMARTiSM00181. 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.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 22 hits.
SSF49899. SSF49899. 3 hits.
SSF57424. SSF57424. 4 hits.
PROSITEiPS00022. 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]

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 rs1869780dbSNPEnsembl.1
Natural variantiVAR_057051303L → H.Corresponds to variant rs17460381dbSNPEnsembl.1
Natural variantiVAR_047980638M → V.3 PublicationsCorresponds to variant rs1874792dbSNPEnsembl.1
Natural variantiVAR_047981765N → S.3 PublicationsCorresponds to variant rs989994dbSNPEnsembl.1
Natural variantiVAR_0479821186R → Q.Corresponds to variant rs2229481dbSNPEnsembl.1
Natural variantiVAR_0570521323L → V.Corresponds to variant rs10917058dbSNPEnsembl.1
Natural variantiVAR_0479831503A → V.3 PublicationsCorresponds to variant rs897471dbSNPEnsembl.1
Natural variantiVAR_0141221532C → Y in SJS1. 1 PublicationCorresponds to variant rs137853248dbSNPEnsembl.1
Natural variantiVAR_0479841758R → Q.Corresponds to variant rs2229483dbSNPEnsembl.1
Natural variantiVAR_0479851919R → C.Corresponds to variant rs2229474dbSNPEnsembl.1
Natural variantiVAR_0479861967V → I.Corresponds to variant rs2229475dbSNPEnsembl.1
Natural variantiVAR_0479872980L → H.1 PublicationCorresponds to variant rs2229489dbSNPEnsembl.1
Natural variantiVAR_0479882981V → I.Corresponds to variant rs2229490dbSNPEnsembl.1
Natural variantiVAR_0479892995S → G.1 PublicationCorresponds to variant rs2229491dbSNPEnsembl.1
Natural variantiVAR_0479903168A → T.1 PublicationCorresponds to variant rs2228349dbSNPEnsembl.1
Natural variantiVAR_0479913256H → Y.Corresponds to variant rs2291827dbSNPEnsembl.1
Natural variantiVAR_0479923530R → W.Corresponds to variant rs2270699dbSNPEnsembl.1
Natural variantiVAR_0479933632R → Q.1 PublicationCorresponds to variant rs2229493dbSNPEnsembl.1
Natural variantiVAR_0479943640V → I.Corresponds to variant rs17459097dbSNPEnsembl.1
Natural variantiVAR_0479954331S → N.Corresponds to variant rs3736360dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
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

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology
Wikipedia

Perlecan entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS30625.1.
PIRiA38096.
RefSeqiNP_001278789.1. NM_001291860.1.
NP_005520.4. NM_005529.6.
UniGeneiHs.562227.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3SH4X-ray1.50A4197-4391[»]
3SH5X-ray2.80A4197-4391[»]
ProteinModelPortaliP98160.
SMRiP98160.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109571. 32 interactors.
IntActiP98160. 30 interactors.
MINTiMINT-123304.
STRINGi9606.ENSP00000363827.

Chemistry databases

DrugBankiDB00039. Palifermin.

PTM databases

iPTMnetiP98160.
PhosphoSitePlusiP98160.
UniCarbKBiP98160.

Polymorphism and mutation databases

BioMutaiHSPG2.
DMDMi317373536.

2D gel databases

DOSAC-COBS-2DPAGEP98160.

Proteomic databases

EPDiP98160.
MaxQBiP98160.
PaxDbiP98160.
PeptideAtlasiP98160.
PRIDEiP98160.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi3339.
DisGeNETi3339.
GeneCardsiHSPG2.
H-InvDBHIX0023554.
HIX0023598.
HGNCiHGNC:5273. HSPG2.
HPAiCAB009820.
CAB020718.
HPA018892.
MalaCardsiHSPG2.
MIMi142461. gene.
224410. phenotype.
255800. phenotype.
neXtProtiNX_P98160.
OpenTargetsiENSG00000142798.
Orphaneti1865. Dyssegmental dysplasia, Silverman-Handmaker type.
800. Schwartz-Jampel syndrome.
PharmGKBiPA29537.
GenAtlasiSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCyciZFISH:ENSG00000142798-MONOMER.
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-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.

Miscellaneous databases

ChiTaRSiHSPG2. human.
GeneWikiiPerlecan.
GenomeRNAii3339.
PROiP98160.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000142798.
CleanExiHS_HSPG2.
ExpressionAtlasiP98160. baseline and differential.
GenevisibleiP98160. HS.

Family and domain databases

Gene3Di2.60.120.200. 3 hits.
2.60.40.10. 22 hits.
4.10.400.10. 4 hits.
InterProiIPR013320. ConA-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR007110. Ig-like_dom.
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.
IPR023415. LDLR_class-A_CS.
IPR002172. LDrepeatLR_classA_rpt.
IPR000082. SEA_dom.
[Graphical view]
PfamiPF00008. 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.
[Graphical view]
PRINTSiPR00261. LDLRECEPTOR.
SMARTiSM00181. 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.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 22 hits.
SSF49899. SSF49899. 3 hits.
SSF57424. SSF57424. 4 hits.
PROSITEiPS00022. 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]
ProtoNetiSearch...

Entry informationi

Entry nameiPGBM_HUMAN
AccessioniPrimary (citable) accession number: P98160
Secondary accession number(s): Q16287, Q5SZI3, Q9H3V5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 11, 2011
Last modified: November 2, 2016
This is version 194 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

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.

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
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.