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P98164 (LRP2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 137. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Low-density lipoprotein receptor-related protein 2
Short name=LRP-2
Alternative name(s):
Glycoprotein 330
Short name=gp330
Megalin
Gene names
Name:LRP2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length4655 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Acts together with cubilin to mediate HDL endocytosis By similarity. May participate in regulation of parathyroid-hormone and para-thyroid-hormone-related protein release.

Subunit structure

Binds plasminogen, extracellular matrix components, plasminogen activator-plasminogen activator inhibitor type I complex, apolipoprotein E-enriched beta-VLDL, lipoprotein lipase, lactoferrin, CLU/clusterin and calcium. Forms a multimeric complex together with a receptor-associated protein (RAP). Binds to ankyrin-repeat family A protein 2 (ANKRA2). Interacts with LRP2BP. Interacts (via NPXY motif) with DAB2; the interaction is not affected by tyrosine phosphorylation of the NPXY motif. Ref.5 Ref.6 Ref.7 Ref.8

Subcellular location

Membrane; Single-pass type I membrane protein. Membrane › coated pit.

Tissue specificity

Absorptive epithelia, including renal proximal tubules.

Involvement in disease

Donnai-Barrow syndrome (DBS) [MIM:222448]: Rare autosomal recessive disorder characterized by major malformations including agenesis of the corpus callosum, congenital diaphragmatic hernia, facial dysmorphology, ocular anomalies, sensorineural hearing loss and developmental delay. The FOAR syndrome was first described as comprising facial anomalies, ocular anomalies, sensorineural hearing loss, and proteinuria. DBS and FOAR were first described as distinct disorders but the classic distinguishing features between the 2 disorders were presence of proteinuria and absence of diaphragmatic hernia and corpus callosum anomalies in FOAR. Early reports noted that the 2 disorders shared many phenotypic features and may be identical. Although there is variability in the expression of some features (e.g., agenesis of the corpus callosum and proteinuria), DBS and FOAR are now considered to represent the same entity.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.10

Sequence similarities

Belongs to the LDLR family.

Contains 17 EGF-like domains.

Contains 36 LDL-receptor class A domains.

Contains 37 LDL-receptor class B repeats.

Ontologies

Keywords
   Biological processEndocytosis
   Cellular componentCoated pit
Membrane
   Coding sequence diversityPolymorphism
   DiseaseDisease mutation
   DomainEGF-like domain
Repeat
SH3-binding
Signal
Transmembrane
Transmembrane helix
   LigandCalcium
Metal-binding
   Molecular functionReceptor
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell proliferation

Inferred from electronic annotation. Source: Compara

forebrain development

Inferred from electronic annotation. Source: Compara

phototransduction, visible light

Traceable author statement. Source: Reactome

protein glycosylation

Traceable author statement PubMed 2786251. Source: ProtInc

receptor-mediated endocytosis

Traceable author statement Ref.5. Source: ProtInc

retinoid metabolic process

Traceable author statement. Source: Reactome

vitamin D metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentGolgi apparatus

Inferred from electronic annotation. Source: Compara

apical plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

brush border membrane

Inferred from electronic annotation. Source: Compara

coated pit

Inferred from electronic annotation. Source: UniProtKB-SubCell

endocytic vesicle

Inferred from electronic annotation. Source: Compara

endoplasmic reticulum

Inferred from electronic annotation. Source: Compara

endosome

Inferred from electronic annotation. Source: Compara

integral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

lysosome

Traceable author statement Ref.5. Source: ProtInc

   Molecular_functioncalcium ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2525 Potential
Chain26 – 46554630Low-density lipoprotein receptor-related protein 2
PRO_0000017321

Regions

Topological domain26 – 44234398Extracellular Potential
Transmembrane4424 – 444623Helical; Potential
Topological domain4447 – 4655209Cytoplasmic Potential
Domain26 – 6439LDL-receptor class A 1
Domain65 – 10541LDL-receptor class A 2
Domain106 – 14439LDL-receptor class A 3
Domain145 – 18137LDL-receptor class A 4
Domain182 – 21938LDL-receptor class A 5
Domain220 – 25839LDL-receptor class A 6
Domain264 – 30845LDL-receptor class A 7
Domain309 – 34739EGF-like 1
Domain348 – 38639EGF-like 2
Repeat436 – 47843LDL-receptor class B 1
Repeat479 – 52143LDL-receptor class B 2
Repeat522 – 56847LDL-receptor class B 3
Repeat569 – 61244LDL-receptor class B 4
Repeat613 – 65341LDL-receptor class B 5
Domain659 – 70547EGF-like 3
Repeat753 – 79543LDL-receptor class B 6
Repeat796 – 83742LDL-receptor class B 7
Repeat838 – 88144LDL-receptor class B 8
Repeat882 – 92544LDL-receptor class B 9
Domain970 – 101445EGF-like 4
Domain1024 – 106239LDL-receptor class A 8
Domain1065 – 110339LDL-receptor class A 9
Domain1107 – 114539LDL-receptor class A 10
Domain1147 – 118539LDL-receptor class A 11
Domain1186 – 122439LDL-receptor class A 12
Domain1228 – 126841LDL-receptor class A 13
Domain1269 – 130739LDL-receptor class A 14
Domain1310 – 135041LDL-receptor class A 15
Domain1349 – 138941EGF-like 5
Domain1390 – 142940EGF-like 6; calcium-binding Potential
Repeat1478 – 152043LDL-receptor class B 10
Repeat1521 – 156343LDL-receptor class B 11
Repeat1566 – 160944LDL-receptor class B 12
Repeat1610 – 165445LDL-receptor class B 13
Repeat1655 – 169541LDL-receptor class B 14
Domain1700 – 174142EGF-like 7
Repeat1790 – 183243LDL-receptor class B 15
Repeat1833 – 188250LDL-receptor class B 16
Repeat1883 – 193048LDL-receptor class B 17
Repeat1931 – 197141LDL-receptor class B 18
Repeat1972 – 201342LDL-receptor class B 19
Domain2018 – 205942EGF-like 8
Repeat2107 – 215650LDL-receptor class B 20
Repeat2157 – 220145LDL-receptor class B 21
Repeat2202 – 224544LDL-receptor class B 22
Repeat2246 – 228944LDL-receptor class B 23
Repeat2290 – 233142LDL-receptor class B 24
Domain2342 – 238342EGF-like 9
Repeat2431 – 247747LDL-receptor class B 25
Repeat2478 – 251841LDL-receptor class B 26
Repeat2519 – 256244LDL-receptor class B 27
Repeat2563 – 260341LDL-receptor class B 28
Repeat2604 – 264643LDL-receptor class B 29
Domain2651 – 269343EGF-like 10
Domain2698 – 273841LDL-receptor class A 16
Domain2739 – 277739LDL-receptor class A 17
Domain2778 – 281942LDL-receptor class A 18
Domain2820 – 286142LDL-receptor class A 19
Domain2862 – 290140LDL-receptor class A 20
Domain2904 – 294542LDL-receptor class A 21
Domain2946 – 299045LDL-receptor class A 22
Domain2991 – 302939LDL-receptor class A 23
Domain3030 – 307041LDL-receptor class A 24
Domain3073 – 311038LDL-receptor class A 25
Domain3111 – 315141EGF-like 11
Domain3152 – 319241EGF-like 12; calcium-binding Potential
Repeat3239 – 328143LDL-receptor class B 30
Repeat3282 – 332443LDL-receptor class B 31
Repeat3333 – 337644LDL-receptor class B 32
Repeat3377 – 341842LDL-receptor class B 33
Repeat3419 – 346042LDL-receptor class B 34
Domain3465 – 350945EGF-like 13
Domain3510 – 355041LDL-receptor class A 26
Domain3551 – 359141LDL-receptor class A 27
Domain3592 – 363241LDL-receptor class A 28
Domain3633 – 367341LDL-receptor class A 29
Domain3676 – 371641LDL-receptor class A 30
Domain3717 – 375640LDL-receptor class A 31
Domain3757 – 379539LDL-receptor class A 32
Domain3796 – 383439LDL-receptor class A 33
Domain3840 – 388041LDL-receptor class A 34
Domain3881 – 392242LDL-receptor class A 35
Domain3926 – 396439LDL-receptor class A 36
Domain3966 – 400641EGF-like 14
Domain4007 – 404842EGF-like 15; calcium-binding Potential
Repeat4154 – 419643LDL-receptor class B 35
Repeat4197 – 424044LDL-receptor class B 36
Repeat4242 – 428342LDL-receptor class B 37
Domain4330 – 436839EGF-like 16
Domain4377 – 441135EGF-like 17
Region4589 – 460214Interaction with DAB2
Motif4453 – 446210SH3-binding Potential
Motif4521 – 45266Endocytosis signal Potential
Motif4593 – 45986NPXY motif
Motif4598 – 46014SH2-binding Potential
Motif4611 – 462212SH3-binding Potential

Sites

Metal binding12081Calcium By similarity
Metal binding12101Calcium; via carbonyl oxygen By similarity
Metal binding12121Calcium By similarity
Metal binding12181Calcium By similarity
Metal binding12191Calcium By similarity

Amino acid modifications

Modified residue44631Phosphoserine By similarity
Modified residue44711Phosphoserine By similarity
Glycosylation1591N-linked (GlcNAc...) Potential
Glycosylation1781N-linked (GlcNAc...) Potential
Glycosylation2991N-linked (GlcNAc...) Potential
Glycosylation3001N-linked (GlcNAc...) Potential
Glycosylation3411N-linked (GlcNAc...) Potential
Glycosylation3881N-linked (GlcNAc...) Potential
Glycosylation4631N-linked (GlcNAc...) Potential
Glycosylation8661N-linked (GlcNAc...) Potential
Glycosylation10641N-linked (GlcNAc...) Potential
Glycosylation11441N-linked (GlcNAc...) Potential
Glycosylation11861N-linked (GlcNAc...) Potential
Glycosylation13271N-linked (GlcNAc...) Potential
Glycosylation13401N-linked (GlcNAc...) Potential
Glycosylation13831N-linked (GlcNAc...) Potential
Glycosylation14641N-linked (GlcNAc...) Potential
Glycosylation14961N-linked (GlcNAc...) Potential
Glycosylation15501N-linked (GlcNAc...) Potential
Glycosylation16751N-linked (GlcNAc...) Potential
Glycosylation18101N-linked (GlcNAc...) Potential
Glycosylation20551N-linked (GlcNAc...) Potential
Glycosylation21771N-linked (GlcNAc...) Potential
Glycosylation22241N-linked (GlcNAc...) Potential
Glycosylation24991N-linked (GlcNAc...) Potential
Glycosylation25471N-linked (GlcNAc...) Potential
Glycosylation27811N-linked (GlcNAc...) Potential
Glycosylation28091N-linked (GlcNAc...) Potential
Glycosylation28101N-linked (GlcNAc...) Potential
Glycosylation29471N-linked (GlcNAc...) Potential
Glycosylation29871N-linked (GlcNAc...) Potential
Glycosylation31251N-linked (GlcNAc...) Potential
Glycosylation32111N-linked (GlcNAc...) Potential
Glycosylation32571N-linked (GlcNAc...) Potential
Glycosylation33151N-linked (GlcNAc...) Potential
Glycosylation33551N-linked (GlcNAc...) Potential
Glycosylation34461N-linked (GlcNAc...) Potential
Glycosylation35641N-linked (GlcNAc...) Potential
Glycosylation36801N-linked (GlcNAc...) Potential
Glycosylation39781N-linked (GlcNAc...) Potential
Glycosylation40681N-linked (GlcNAc...) Potential
Glycosylation43271N-linked (GlcNAc...) Potential
Disulfide bond28 ↔ 40 By similarity
Disulfide bond35 ↔ 53 By similarity
Disulfide bond47 ↔ 62 By similarity
Disulfide bond67 ↔ 80 By similarity
Disulfide bond74 ↔ 93 By similarity
Disulfide bond87 ↔ 103 By similarity
Disulfide bond108 ↔ 120 By similarity
Disulfide bond115 ↔ 133 By similarity
Disulfide bond127 ↔ 142 By similarity
Disulfide bond147 ↔ 157 By similarity
Disulfide bond152 ↔ 170 By similarity
Disulfide bond164 ↔ 179 By similarity
Disulfide bond183 ↔ 195 By similarity
Disulfide bond190 ↔ 208 By similarity
Disulfide bond202 ↔ 217 By similarity
Disulfide bond222 ↔ 234 By similarity
Disulfide bond229 ↔ 247 By similarity
Disulfide bond241 ↔ 256 By similarity
Disulfide bond266 ↔ 279 By similarity
Disulfide bond273 ↔ 292 By similarity
Disulfide bond286 ↔ 307 By similarity
Disulfide bond312 ↔ 321 By similarity
Disulfide bond317 ↔ 330 By similarity
Disulfide bond332 ↔ 346 By similarity
Disulfide bond352 ↔ 362 By similarity
Disulfide bond358 ↔ 371 By similarity
Disulfide bond373 ↔ 385 By similarity
Disulfide bond663 ↔ 674 By similarity
Disulfide bond670 ↔ 689 By similarity
Disulfide bond691 ↔ 704 By similarity
Disulfide bond974 ↔ 988 By similarity
Disulfide bond984 ↔ 998 By similarity
Disulfide bond1000 ↔ 1013 By similarity
Disulfide bond1026 ↔ 1038 By similarity
Disulfide bond1033 ↔ 1051 By similarity
Disulfide bond1045 ↔ 1060 By similarity
Disulfide bond1067 ↔ 1079 By similarity
Disulfide bond1074 ↔ 1092 By similarity
Disulfide bond1086 ↔ 1101 By similarity
Disulfide bond1109 ↔ 1121 By similarity
Disulfide bond1116 ↔ 1134 By similarity
Disulfide bond1128 ↔ 1143 By similarity
Disulfide bond1149 ↔ 1161 By similarity
Disulfide bond1156 ↔ 1174 By similarity
Disulfide bond1168 ↔ 1183 By similarity
Disulfide bond1187 ↔ 1200 By similarity
Disulfide bond1194 ↔ 1213 By similarity
Disulfide bond1207 ↔ 1222 By similarity
Disulfide bond1230 ↔ 1243 By similarity
Disulfide bond1237 ↔ 1256 By similarity
Disulfide bond1250 ↔ 1266 By similarity
Disulfide bond1271 ↔ 1283 By similarity
Disulfide bond1278 ↔ 1296 By similarity
Disulfide bond1290 ↔ 1305 By similarity
Disulfide bond1312 ↔ 1325 By similarity
Disulfide bond1319 ↔ 1338 By similarity
Disulfide bond1332 ↔ 1348 By similarity
Disulfide bond1353 ↔ 1364 By similarity
Disulfide bond1360 ↔ 1373 By similarity
Disulfide bond1375 ↔ 1388 By similarity
Disulfide bond1394 ↔ 1404 By similarity
Disulfide bond1400 ↔ 1413 By similarity
Disulfide bond1415 ↔ 1428 By similarity
Disulfide bond1704 ↔ 1713 By similarity
Disulfide bond1709 ↔ 1725 By similarity
Disulfide bond1727 ↔ 1740 By similarity
Disulfide bond2022 ↔ 2033 By similarity
Disulfide bond2029 ↔ 2043 By similarity
Disulfide bond2045 ↔ 2058 By similarity
Disulfide bond2346 ↔ 2357 By similarity
Disulfide bond2353 ↔ 2368 By similarity
Disulfide bond2370 ↔ 2382 By similarity
Disulfide bond2655 ↔ 2666 By similarity
Disulfide bond2662 ↔ 2675 By similarity
Disulfide bond2677 ↔ 2692 By similarity
Disulfide bond2700 ↔ 2712 By similarity
Disulfide bond2707 ↔ 2725 By similarity
Disulfide bond2719 ↔ 2736 By similarity
Disulfide bond2741 ↔ 2753 By similarity
Disulfide bond2748 ↔ 2766 By similarity
Disulfide bond2760 ↔ 2775 By similarity
Disulfide bond2780 ↔ 2793 By similarity
Disulfide bond2788 ↔ 2806 By similarity
Disulfide bond2800 ↔ 2817 By similarity
Disulfide bond2822 ↔ 2835 By similarity
Disulfide bond2829 ↔ 2848 By similarity
Disulfide bond2842 ↔ 2859 By similarity
Disulfide bond2864 ↔ 2876 By similarity
Disulfide bond2871 ↔ 2889 By similarity
Disulfide bond2883 ↔ 2899 By similarity
Disulfide bond2906 ↔ 2918 By similarity
Disulfide bond2913 ↔ 2931 By similarity
Disulfide bond2925 ↔ 2943 By similarity
Disulfide bond2948 ↔ 2965 By similarity
Disulfide bond2955 ↔ 2978 By similarity
Disulfide bond2972 ↔ 2988 By similarity
Disulfide bond2993 ↔ 3005 By similarity
Disulfide bond3000 ↔ 3018 By similarity
Disulfide bond3012 ↔ 3027 By similarity
Disulfide bond3032 ↔ 3044 By similarity
Disulfide bond3039 ↔ 3057 By similarity
Disulfide bond3051 ↔ 3068 By similarity
Disulfide bond3075 ↔ 3087 By similarity
Disulfide bond3082 ↔ 3100 By similarity
Disulfide bond3094 ↔ 3109 By similarity
Disulfide bond3114 ↔ 3126 By similarity
Disulfide bond3122 ↔ 3135 By similarity
Disulfide bond3137 ↔ 3150 By similarity
Disulfide bond3156 ↔ 3167 By similarity
Disulfide bond3163 ↔ 3176 By similarity
Disulfide bond3178 ↔ 3191 By similarity
Disulfide bond3469 ↔ 3480 By similarity
Disulfide bond3476 ↔ 3491 By similarity
Disulfide bond3493 ↔ 3508 By similarity
Disulfide bond3512 ↔ 3525 By similarity
Disulfide bond3519 ↔ 3538 By similarity
Disulfide bond3532 ↔ 3548 By similarity
Disulfide bond3553 ↔ 3565 By similarity
Disulfide bond3560 ↔ 3578 By similarity
Disulfide bond3572 ↔ 3589 By similarity
Disulfide bond3594 ↔ 3606 By similarity
Disulfide bond3601 ↔ 3619 By similarity
Disulfide bond3613 ↔ 3630 By similarity
Disulfide bond3635 ↔ 3647 By similarity
Disulfide bond3642 ↔ 3660 By similarity
Disulfide bond3654 ↔ 3671 By similarity
Disulfide bond3678 ↔ 3692 By similarity
Disulfide bond3686 ↔ 3705 By similarity
Disulfide bond3699 ↔ 3714 By similarity
Disulfide bond3719 ↔ 3732 By similarity
Disulfide bond3727 ↔ 3745 By similarity
Disulfide bond3739 ↔ 3754 By similarity
Disulfide bond3759 ↔ 3771 By similarity
Disulfide bond3766 ↔ 3784 By similarity
Disulfide bond3778 ↔ 3793 By similarity
Disulfide bond3798 ↔ 3810 By similarity
Disulfide bond3805 ↔ 3823 By similarity
Disulfide bond3817 ↔ 3832 By similarity
Disulfide bond3842 ↔ 3854 By similarity
Disulfide bond3849 ↔ 3867 By similarity
Disulfide bond3861 ↔ 3878 By similarity
Disulfide bond3883 ↔ 3896 By similarity
Disulfide bond3891 ↔ 3909 By similarity
Disulfide bond3903 ↔ 3920 By similarity
Disulfide bond3928 ↔ 3940 By similarity
Disulfide bond3935 ↔ 3953 By similarity
Disulfide bond3947 ↔ 3962 By similarity
Disulfide bond3970 ↔ 3979 By similarity
Disulfide bond3975 ↔ 3989 By similarity
Disulfide bond3991 ↔ 4005 By similarity
Disulfide bond4011 ↔ 4021 By similarity
Disulfide bond4017 ↔ 4030 By similarity
Disulfide bond4032 ↔ 4047 By similarity
Disulfide bond4334 ↔ 4342 By similarity
Disulfide bond4338 ↔ 4351 By similarity
Disulfide bond4353 ↔ 4367 By similarity
Disulfide bond4381 ↔ 4389 By similarity
Disulfide bond4383 ↔ 4399 By similarity
Disulfide bond4401 ↔ 4410 By similarity

Natural variations

Natural variant831N → S. Ref.1
Corresponds to variant rs2229263 [ dbSNP | Ensembl ].
VAR_037009
Natural variant1031C → R Found in a renal cell carcinoma sample; somatic mutation. Ref.11
VAR_064727
Natural variant2591G → R.
Corresponds to variant rs34693334 [ dbSNP | Ensembl ].
VAR_061294
Natural variant6691G → D.
Corresponds to variant rs34291900 [ dbSNP | Ensembl ].
VAR_037010
Natural variant9091H → R.
Corresponds to variant rs36082715 [ dbSNP | Ensembl ].
VAR_037011
Natural variant10831H → Q.
Corresponds to variant rs2302691 [ dbSNP | Ensembl ].
VAR_037012
Natural variant12791D → A.
Corresponds to variant rs17848149 [ dbSNP | Ensembl ].
VAR_029182
Natural variant12871A → P.
VAR_005421
Natural variant20121R → K.
Corresponds to variant rs4667596 [ dbSNP | Ensembl ].
VAR_029183
Natural variant20651I → T.
Corresponds to variant rs2228168 [ dbSNP | Ensembl ].
VAR_020218
Natural variant25221Y → H in DBS. Ref.10
VAR_037013
Natural variant26321N → D.
Corresponds to variant rs17848169 [ dbSNP | Ensembl ].
VAR_029184
Natural variant28721A → T.
Corresponds to variant rs2228171 [ dbSNP | Ensembl ].
VAR_005422
Natural variant30111R → M.
Corresponds to variant rs11674973 [ dbSNP | Ensembl ].
VAR_037014
Natural variant33051R → H.
Corresponds to variant rs3213760 [ dbSNP | Ensembl ].
VAR_020219
Natural variant40941K → E. Ref.3
Corresponds to variant rs2075252 [ dbSNP | Ensembl ].
VAR_005423
Natural variant42101I → L. Ref.3
Corresponds to variant rs4667591 [ dbSNP | Ensembl ].
VAR_005424
Natural variant42721M → V in a colorectal cancer sample; somatic mutation. Ref.9
VAR_035996

Experimental info

Sequence conflict27241D → G in AAB02882. Ref.3
Sequence conflict27731A → T in AAB02882. Ref.3
Sequence conflict28271T → P in AAB02882. Ref.3
Sequence conflict2880 – 28823HWY → TFGI in AAB02882. Ref.3
Sequence conflict28971A → S in AAB02882. Ref.3
Sequence conflict29081A → S in AAB02882. Ref.3
Sequence conflict29211S → N in AAB02882. Ref.3
Sequence conflict29541L → P in AAB02882. Ref.3
Sequence conflict2971 – 29722VC → PP in AAB02882. Ref.3
Sequence conflict29821Y → H in AAB02882. Ref.3
Sequence conflict29851N → I in AAB02882. Ref.3
Sequence conflict36151T → S in AAB02882. Ref.3
Sequence conflict37381Q → K in AAB02882. Ref.3
Sequence conflict37841C → LW in AAB02882. Ref.3
Sequence conflict38101C → R in AAB02882. Ref.3
Sequence conflict42201R → P in AAB02882. Ref.3

Secondary structure

1 ........... 4655
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P98164 [UniParc].

Last modified November 13, 2007. Version 3.
Checksum: C73C4206B8B28CE0

FASTA4,655521,958
        10         20         30         40         50         60 
MDRGPAAVAC TLLLALVACL APASGQECDS AHFRCGSGHC IPADWRCDGT KDCSDDADEI 

        70         80         90        100        110        120 
GCAVVTCQQG YFKCQSEGQC IPNSWVCDQD QDCDDGSDER QDCSQSTCSS HQITCSNGQC 

       130        140        150        160        170        180 
IPSEYRCDHV RDCPDGADEN DCQYPTCEQL TCDNGACYNT SQKCDWKVDC RDSSDEINCT 

       190        200        210        220        230        240 
EICLHNEFSC GNGECIPRAY VCDHDNDCQD GSDEHACNYP TCGGYQFTCP SGRCIYQNWV 

       250        260        270        280        290        300 
CDGEDDCKDN GDEDGCESGP HDVHKCSPRE WSCPESGRCI SIYKVCDGIL DCPGREDENN 

       310        320        330        340        350        360 
TSTGKYCSMT LCSALNCQYQ CHETPYGGAC FCPPGYIINH NDSRTCVEFD DCQIWGICDQ 

       370        380        390        400        410        420 
KCESRPGRHL CHCEEGYILE RGQYCKANDS FGEASIIFSN GRDLLIGDIH GRSFRILVES 

       430        440        450        460        470        480 
QNRGVAVGVA FHYHLQRVFW TDTVQNKVFS VDINGLNIQE VLNVSVETPE NLAVDWVNNK 

       490        500        510        520        530        540 
IYLVETKVNR IDMVNLDGSY RVTLITENLG HPRGIAVDPT VGYLFFSDWE SLSGEPKLER 

       550        560        570        580        590        600 
AFMDGSNRKD LVKTKLGWPA GVTLDMISKR VYWVDSRFDY IETVTYDGIQ RKTVVHGGSL 

       610        620        630        640        650        660 
IPHPFGVSLF EGQVFFTDWT KMAVLKANKF TETNPQVYYQ ASLRPYGVTV YHSLRQPYAT 

       670        680        690        700        710        720 
NPCKDNNGGC EQVCVLSHRT DNDGLGFRCK CTFGFQLDTD ERHCIAVQNF LIFSSQVAIR 

       730        740        750        760        770        780 
GIPFTLSTQE DVMVPVSGNP SFFVGIDFDA QDSTIFFSDM SKHMIFKQKI DGTGREILAA 

       790        800        810        820        830        840 
NRVENVESLA FDWISKNLYW TDSHYKSISV MRLADKTRRT VVQYLNNPRS VVVHPFAGYL 

       850        860        870        880        890        900 
FFTDWFRPAK IMRAWSDGSH LLPVINTTLG WPNGLAIDWA ASRLYWVDAY FDKIEHSTFD 

       910        920        930        940        950        960 
GLDRRRLGHI EQMTHPFGLA IFGEHLFFTD WRLGAIIRVR KADGGEMTVI RSGIAYILHL 

       970        980        990       1000       1010       1020 
KSYDVNIQTG SNACNQPTHP NGDCSHFCFP VPNFQRVCGC PYGMRLASNH LTCEGDPTNE 

      1030       1040       1050       1060       1070       1080 
PPTEQCGLFS FPCKNGRCVP NYYLCDGVDD CHDNSDEQLC GTLNNTCSSS AFTCGHGECI 

      1090       1100       1110       1120       1130       1140 
PAHWRCDKRN DCVDGSDEHN CPTHAPASCL DTQYTCDNHQ CISKNWVCDT DNDCGDGSDE 

      1150       1160       1170       1180       1190       1200 
KNCNSTETCQ PSQFNCPNHR CIDLSFVCDG DKDCVDGSDE VGCVLNCTAS QFKCASGDKC 

      1210       1220       1230       1240       1250       1260 
IGVTNRCDGV FDCSDNSDEA GCPTRPPGMC HSDEFQCQED GICIPNFWEC DGHPDCLYGS 

      1270       1280       1290       1300       1310       1320 
DEHNACVPKT CPSSYFHCDN GNCIHRAWLC DRDNDCGDMS DEKDCPTQPF RCPSWQWQCL 

      1330       1340       1350       1360       1370       1380 
GHNICVNLSV VCDGIFDCPN GTDESPLCNG NSCSDFNGGC THECVQEPFG AKCLCPLGFL 

      1390       1400       1410       1420       1430       1440 
LANDSKTCED IDECDILGSC SQHCYNMRGS FRCSCDTGYM LESDGRTCKV TASESLLLLV 

      1450       1460       1470       1480       1490       1500 
ASQNKIIADS VTSQVHNIYS LVENGSYIVA VDFDSISGRI FWSDATQGKT WSAFQNGTDR 

      1510       1520       1530       1540       1550       1560 
RVVFDSSIIL TETIAIDWVG RNLYWTDYAL ETIEVSKIDG SHRTVLISKN LTNPRGLALD 

      1570       1580       1590       1600       1610       1620 
PRMNEHLLFW SDWGHHPRIE RASMDGSMRT VIVQDKIFWP CGLTIDYPNR LLYFMDSYLD 

      1630       1640       1650       1660       1670       1680 
YMDFCDYNGH HRRQVIASDL IIRHPYALTL FEDSVYWTDR ATRRVMRANK WHGGNQSVVM 

      1690       1700       1710       1720       1730       1740 
YNIQWPLGIV AVHPSKQPNS VNPCAFSRCS HLCLLSSQGP HFYSCVCPSG WSLSPDLLNC 

      1750       1760       1770       1780       1790       1800 
LRDDQPFLIT VRQHIIFGIS LNPEVKSNDA MVPIAGIQNG LDVEFDDAEQ YIYWVENPGE 

      1810       1820       1830       1840       1850       1860 
IHRVKTDGTN RTVFASISMV GPSMNLALDW ISRNLYSTNP RTQSIEVLTL HGDIRYRKTL 

      1870       1880       1890       1900       1910       1920 
IANDGTALGV GFPIGITVDP ARGKLYWSDQ GTDSGVPAKI ASANMDGTSV KTLFTGNLEH 

      1930       1940       1950       1960       1970       1980 
LECVTLDIEE QKLYWAVTGR GVIERGNVDG TDRMILVHQL SHPWGIAVHD SFLYYTDEQY 

      1990       2000       2010       2020       2030       2040 
EVIERVDKAT GANKIVLRDN VPNLRGLQVY HRRNAAESSN GCSNNMNACQ QICLPVPGGL 

      2050       2060       2070       2080       2090       2100 
FSCACATGFK LNPDNRSCSP YNSFIVVSML SAIRGFSLEL SDHSETMVPV AGQGRNALHV 

      2110       2120       2130       2140       2150       2160 
DVDVSSGFIY WCDFSSSVAS DNAIRRIKPD GSSLMNIVTH GIGENGVRGI AVDWVAGNLY 

      2170       2180       2190       2200       2210       2220 
FTNAFVSETL IEVLRINTTY RRVLLKVTVD MPRHIVVDPK NRYLFWADYG QRPKIERSFL 

      2230       2240       2250       2260       2270       2280 
DCTNRTVLVS EGIVTPRGLA VDRSDGYVYW VDDSLDIIAR IRINGENSEV IRYGSRYPTP 

      2290       2300       2310       2320       2330       2340 
YGITVFENSI IWVDRNLKKI FQASKEPENT EPPTVIRDNI NWLRDVTIFD KQVQPRSPAE 

      2350       2360       2370       2380       2390       2400 
VNNNPCLENN GGCSHLCFAL PGLHTPKCDC AFGTLQSDGK NCAISTENFL IFALSNSLRS 

      2410       2420       2430       2440       2450       2460 
LHLDPENHSP PFQTINVERT VMSLDYDSVS DRIYFTQNLA SGVGQISYAT LSSGIHTPTV 

      2470       2480       2490       2500       2510       2520 
IASGIGTADG IAFDWITRRI YYSDYLNQMI NSMAEDGSNR TVIARVPKPR AIVLDPCQGY 

      2530       2540       2550       2560       2570       2580 
LYWADWDTHA KIERATLGGN FRVPIVNSSL VMPSGLTLDY EEDLLYWVDA SLQRIERSTL 

      2590       2600       2610       2620       2630       2640 
TGVDREVIVN AAVHAFGLTL YGQYIYWTDL YTQRIYRANK YDGSGQIAMT TNLLSQPRGI 

      2650       2660       2670       2680       2690       2700 
NTVVKNQKQQ CNNPCEQFNG GCSHICAPGP NGAECQCPHE GNWYLANNRK HCIVDNGERC 

      2710       2720       2730       2740       2750       2760 
GASSFTCSNG RCISEEWKCD NDNDCGDGSD EMESVCALHT CSPTAFTCAN GRCVQYSYRC 

      2770       2780       2790       2800       2810       2820 
DYYNDCGDGS DEAGCLFRDC NATTEFMCNN RRCIPREFIC NGVDNCHDNN TSDEKNCPDR 

      2830       2840       2850       2860       2870       2880 
TCQSGYTKCH NSNICIPRVY LCDGDNDCGD NSDENPTYCT THTCSSSEFQ CASGRCIPQH 

      2890       2900       2910       2920       2930       2940 
WYCDQETDCF DASDEPASCG HSERTCLADE FKCDGGRCIP SEWICDGDND CGDMSDEDKR 

      2950       2960       2970       2980       2990       3000 
HQCQNQNCSD SEFLCVNDRP PDRRCIPQSW VCDGDVDCTD GYDENQNCTR RTCSENEFTC 

      3010       3020       3030       3040       3050       3060 
GYGLCIPKIF RCDRHNDCGD YSDERGCLYQ TCQQNQFTCQ NGRCISKTFV CDEDNDCGDG 

      3070       3080       3090       3100       3110       3120 
SDELMHLCHT PEPTCPPHEF KCDNGRCIEM MKLCNHLDDC LDNSDEKGCG INECHDPSIS 

      3130       3140       3150       3160       3170       3180 
GCDHNCTDTL TSFYCSCRPG YKLMSDKRTC VDIDECTEMP FVCSQKCENV IGSYICKCAP 

      3190       3200       3210       3220       3230       3240 
GYLREPDGKT CRQNSNIEPY LIFSNRYYLR NLTIDGYFYS LILEGLDNVV ALDFDRVEKR 

      3250       3260       3270       3280       3290       3300 
LYWIDTQRQV IERMFLNKTN KETIINHRLP AAESLAVDWV SRKLYWLDAR LDGLFVSDLN 

      3310       3320       3330       3340       3350       3360 
GGHRRMLAQH CVDANNTFCF DNPRGLALHP QYGYLYWADW GHRAYIGRVG MDGTNKSVII 

      3370       3380       3390       3400       3410       3420 
STKLEWPNGI TIDYTNDLLY WADAHLGYIE YSDLEGHHRH TVYDGALPHP FAITIFEDTI 

      3430       3440       3450       3460       3470       3480 
YWTDWNTRTV EKGNKYDGSN RQTLVNTTHR PFDIHVYHPY RQPIVSNPCG TNNGGCSHLC 

      3490       3500       3510       3520       3530       3540 
LIKPGGKGFT CECPDDFRTL QLSGSTYCMP MCSSTQFLCA NNEKCIPIWW KCDGQKDCSD 

      3550       3560       3570       3580       3590       3600 
GSDELALCPQ RFCRLGQFQC SDGNCTSPQT LCNAHQNCPD GSDEDRLLCE NHHCDSNEWQ 

      3610       3620       3630       3640       3650       3660 
CANKRCIPES WQCDTFNDCE DNSDEDSSHC ASRTCRPGQF RCANGRCIPQ AWKCDVDNDC 

      3670       3680       3690       3700       3710       3720 
GDHSDEPIEE CMSSAHLCDN FTEFSCKTNY RCIPKWAVCN GVDDCRDNSD EQGCEERTCH 

      3730       3740       3750       3760       3770       3780 
PVGDFRCKNH HCIPLRWQCD GQNDCGDNSD EENCAPRECT ESEFRCVNQQ CIPSRWICDH 

      3790       3800       3810       3820       3830       3840 
YNDCGDNSDE RDCEMRTCHP EYFQCTSGHC VHSELKCDGS ADCLDASDEA DCPTRFPDGA 

      3850       3860       3870       3880       3890       3900 
YCQATMFECK NHVCIPPYWK CDGDDDCGDG SDEELHLCLD VPCNSPNRFR CDNNRCIYSH 

      3910       3920       3930       3940       3950       3960 
EVCNGVDDCG DGTDETEEHC RKPTPKPCTE YEYKCGNGHC IPHDNVCDDA DDCGDWSDEL 

      3970       3980       3990       4000       4010       4020 
GCNKGKERTC AENICEQNCT QLNEGGFICS CTAGFETNVF DRTSCLDINE CEQFGTCPQH 

      4030       4040       4050       4060       4070       4080 
CRNTKGSYEC VCADGFTSMS DRPGKRCAAE GSSPLLLLPD NVRIRKYNLS SERFSEYLQD 

      4090       4100       4110       4120       4130       4140 
EEYIQAVDYD WDPKDIGLSV VYYTVRGEGS RFGAIKRAYI PNFESGRNNL VQEVDLKLKY 

      4150       4160       4170       4180       4190       4200 
VMQPDGIAVD WVGRHIYWSD VKNKRIEVAK LDGRYRKWLI STDLDQPAAI AVNPKLGLMF 

      4210       4220       4230       4240       4250       4260 
WTDWGKEPKI ESAWMNGEDR NILVFEDLGW PTGLSIDYLN NDRIYWSDFK EDVIETIKYD 

      4270       4280       4290       4300       4310       4320 
GTDRRVIAKE AMNPYSLDIF EDQLYWISKE KGEVWKQNKF GQGKKEKTLV VNPWLTQVRI 

      4330       4340       4350       4360       4370       4380 
FHQLRYNKSV PNLCKQICSH LCLLRPGGYS CACPQGSSFI EGSTTECDAA IELPINLPPP 

      4390       4400       4410       4420       4430       4440 
CRCMHGGNCY FDETDLPKCK CPSGYTGKYC EMAFSKGISP GTTAVAVLLT ILLIVVIGAL 

      4450       4460       4470       4480       4490       4500 
AIAGFFHYRR TGSLLPALPK LPSLSSLVKP SENGNGVTFR SGADLNMDIG VSGFGPETAI 

      4510       4520       4530       4540       4550       4560 
DRSMAMSEDF VMEMGKQPII FENPMYSARD SAVKVVQPIQ VTVSENVDNK NYGSPINPSE 

      4570       4580       4590       4600       4610       4620 
IVPETNPTSP AADGTQVTKW NLFKRKSKQT TNFENPIYAQ MENEQKESVA ATPPPSPSLP 

      4630       4640       4650 
AKPKPPSRRD PTPTYSATED TFKDTANLVK EDSEV

« Hide

References

« Hide 'large scale' references
[1]"Cloning and sequencing of human gp330, a Ca(2+)-binding receptor with potential intracellular signaling properties."
Hjaelm G., Murray E., Crumley G., Harazim W., Lundgren S., Onyango I., Ek B., Larsson M., Juhlin C., Hellman P., Davis H., Aekerstroem G., Rask L., Morse B.
Eur. J. Biochem. 239:132-137(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT SER-83.
Tissue: Kidney.
[2]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"Chromosomal localization of human genes for the LDL receptor family member glycoprotein 330 (LRP2) and its associated protein RAP (LRPAP1)."
Korenberg J.R., Argraves K.M., Chen X.N., Tran H., Strickland D.K., Argraves W.S.
Genomics 22:88-93(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2705-4453, VARIANTS GLU-4094 AND LEU-4210.
Tissue: Kidney.
[4]"A protein involved in calcium sensing of the human parathyroid and placental cytotrophoblast cells belongs to the LDL-receptor protein superfamily."
Lundgren S., Hjaelm G., Hellman P., Ek B., Juhlin C., Rastad J., Klareskog L., Aakerstroem G., Rask L.
Exp. Cell Res. 212:344-350(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 4139-4406.
[5]"Identification of glycoprotein 330 as an endocytic receptor for apolipoprotein J/clusterin."
Kounnas M.Z., Loukinova E.B., Stefansson S., Harmony J.A.K., Brewer B.H., Strickland D.K., Argraves W.S.
J. Biol. Chem. 270:13070-13075(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CLU.
[6]"Cytosolic adaptor protein Dab2 is an intracellular ligand of endocytic receptor gp600/megalin."
Oleinikov A.V., Zhao J., Makker S.P.
Biochem. J. 347:613-621(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DAB2.
[7]"Functional interaction of megalin with the megalin-binding protein (MegBP), a novel tetratrico peptide repeat-containing adaptor molecule."
Petersen H.H., Hilpert J., Militz D., Zandler V., Jacobsen C., Roebroek A.J.M., Willnow T.E.
J. Cell Sci. 116:453-461(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH LRP2BP.
[8]"The adaptor disabled-2 binds to the third psi xNPxY sequence on the cytoplasmic tail of megalin."
Gallagher H., Oleinikov A.V., Fenske C., Newman D.J.
Biochimie 86:179-182(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DAB2.
[9]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] VAL-4272.
[10]"Mutations in LRP2, which encodes the multiligand receptor megalin, cause Donnai-Barrow and facio-oculo-acoustico-renal syndromes."
Kantarci S., Al-Gazali L., Hill R.S., Donnai D., Black G.C.M., Bieth E., Chassaing N., Lacombe D., Devriendt K., Teebi A., Loscertales M., Robson C., Liu T., MacLaughlin D.T., Noonan K.M., Russell M.K., Walsh C.A., Donahoe P.K., Pober B.R.
Nat. Genet. 39:957-959(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT DBS HIS-2522.
[11]"Exome sequencing identifies frequent mutation of the SWI/SNF complex gene PBRM1 in renal carcinoma."
Varela I., Tarpey P., Raine K., Huang D., Ong C.K., Stephens P., Davies H., Jones D., Lin M.L., Teague J., Bignell G., Butler A., Cho J., Dalgliesh G.L., Galappaththige D., Greenman C., Hardy C., Jia M. expand/collapse author list , Latimer C., Lau K.W., Marshall J., McLaren S., Menzies A., Mudie L., Stebbings L., Largaespada D.A., Wessels L.F.A., Richard S., Kahnoski R.J., Anema J., Tuveson D.A., Perez-Mancera P.A., Mustonen V., Fischer A., Adams D.J., Rust A., Chan-On W., Subimerb C., Dykema K., Furge K., Campbell P.J., Teh B.T., Stratton M.R., Futreal P.A.
Nature 469:539-542(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ARG-103.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U33837 mRNA. Translation: AAB41649.1.
AC007556 Genomic DNA. No translation available.
AC008178 Genomic DNA. No translation available.
U04441 mRNA. Translation: AAB02882.1.
S73145 mRNA. Translation: AAB30825.1.
IPIIPI00024292.
PIRI38467.
I53413.
RefSeqNP_004516.2. NM_004525.2.
UniGeneHs.657729.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2M0PNMR-A1103-1148[»]
ProteinModelPortalP98164.
ModBaseSearch...

Protein-protein interaction databases

IntActP98164. 5 interactions.
MINTMINT-2860496.
STRING9606.ENSP00000263816.

PTM databases

PhosphoSiteP98164.

Polymorphism databases

DMDM160332309.

Proteomic databases

PaxDbP98164.
PRIDEP98164.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000263816; ENSP00000263816; ENSG00000081479.
GeneID4036.
KEGGhsa:4036.
UCSCuc002ues.3. human.

Organism-specific databases

CTD4036.
GeneCardsGC02M169947.
H-InvDBHIX0029894.
HGNCHGNC:6694. LRP2.
HPAHPA005980.
MIM222448. phenotype.
600073. gene.
neXtProtNX_P98164.
Orphanet2143. Donnai-Barrow syndrome.
PharmGKBPA30452.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG235850.
HOGENOMHOG000230574.
HOVERGENHBG097941.
InParanoidP98164.
KOK06233.
OMATRPPGMC.
OrthoDBEOG4WQ11K.
PhylomeDBP98164.

Enzyme and pathway databases

Pathway_Interaction_DBhedgehog_2pathway. Signaling events mediated by the Hedgehog family.
ReactomeREACT_111217. Metabolism.
REACT_15493. Steroid hormones.
SignaLinkP98164.

Gene expression databases

ArrayExpressP98164.
BgeeP98164.
CleanExHS_LRP2.
GenevestigatorP98164.
GermOnlineENSG00000081479. Homo sapiens.

Family and domain databases

Gene3D2.120.10.30. 8 hits.
4.10.400.10. 35 hits.
InterProIPR011042. 6-blade_b-propeller_TolB-like.
IPR026823. cEGF.
IPR000742. EG-like_dom.
IPR001881. EGF-like_Ca-bd.
IPR013032. EGF-like_CS.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR009030. Growth_fac_rcpt_N_dom.
IPR023415. LDLR_class-A_CS.
IPR000033. LDLR_classB_rpt.
IPR002172. LDrepeatLR_classA_rpt.
IPR019825. Lectin_legB_Mn/Ca_BS.
IPR002919. TIL_dom.
[Graphical view]
PfamPF12662. cEGF. 1 hit.
PF07645. EGF_CA. 2 hits.
PF00057. Ldl_recept_a. 34 hits.
PF00058. Ldl_recept_b. 14 hits.
[Graphical view]
SMARTSM00181. EGF. 15 hits.
SM00179. EGF_CA. 3 hits.
SM00192. LDLa. 36 hits.
SM00135. LY. 38 hits.
[Graphical view]
SUPFAMSSF57567. Cysrich_TIL. 1 hit.
SSF57184. Grow_fac_recept. 3 hits.
SSF57424. LDL_rcpt_classA_cys-rich. 35 hits.
PROSITEPS00010. ASX_HYDROXYL. 4 hits.
PS00022. EGF_1. 1 hit.
PS01186. EGF_2. 9 hits.
PS50026. EGF_3. 6 hits.
PS01187. EGF_CA. 3 hits.
PS01209. LDLRA_1. 31 hits.
PS50068. LDLRA_2. 36 hits.
PS51120. LDLRB. 35 hits.
[Graphical view]
ProtoNetSearch...

Other

ChEMBLCHEMBL1255140.
ChiTaRSLRP2. human.
DrugBankDB00798. Gentamicin.
DB00047. Insulin Glargine recombinant.
DB00046. Insulin Lyspro recombinant.
DB00030. Insulin recombinant.
DB00071. Insulin, porcine.
DB00013. Urokinase.
GenomeRNAi4036.
NextBio15810.
SOURCESearch...

Entry information

Entry nameLRP2_HUMAN
AccessionPrimary (citable) accession number: P98164
Secondary accession number(s): O00711, Q16215
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: November 13, 2007
Last modified: May 29, 2013
This is version 137 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

Human chromosome 2

Human chromosome 2: 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

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