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Protein

Low-density lipoprotein receptor-related protein 1B

Gene

LRP1B

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Potential cell surface proteins that bind and internalize ligands in the process of receptor-mediated endocytosis.

GO - Molecular functioni

GO - Biological processi

  • protein transport Source: ProtInc
  • receptor-mediated endocytosis Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Biological processi

Endocytosis

Keywords - Ligandi

Calcium

Enzyme and pathway databases

BioCyciZFISH:ENSG00000168702-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Low-density lipoprotein receptor-related protein 1B
Short name:
LRP-1B
Alternative name(s):
Low-density lipoprotein receptor-related protein-deleted in tumor
Short name:
LRP-DIT
Gene namesi
Name:LRP1B
Synonyms:LRPDIT
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:6693. LRP1B.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini25 – 4444ExtracellularSequence analysisAdd BLAST4420
Transmembranei4445 – 4467HelicalSequence analysisAdd BLAST23
Topological domaini4468 – 4599CytoplasmicSequence analysisAdd BLAST132

GO - Cellular componenti

  • integral component of membrane Source: UniProtKB-KW
  • receptor complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Organism-specific databases

DisGeNETi53353.
OpenTargetsiENSG00000168702.
PharmGKBiPA30451.

Polymorphism and mutation databases

BioMutaiLRP1B.
DMDMi57015418.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 20Sequence analysisAdd BLAST20
ChainiPRO_000001731921 – 4599Low-density lipoprotein receptor-related protein 1BAdd BLAST4579

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi32 ↔ 45By similarity
Disulfide bondi39 ↔ 58By similarity
Disulfide bondi52 ↔ 69By similarity
Disulfide bondi77 ↔ 90By similarity
Disulfide bondi84 ↔ 103By similarity
Disulfide bondi97 ↔ 113By similarity
Disulfide bondi120 ↔ 129By similarity
Disulfide bondi125 ↔ 138By similarity
Glycosylationi134N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi140 ↔ 153By similarity
Disulfide bondi159 ↔ 169By similarity
Disulfide bondi165 ↔ 178By similarity
Disulfide bondi180 ↔ 193By similarity
Glycosylationi190N-linked (GlcNAc...)Sequence analysis1
Glycosylationi220N-linked (GlcNAc...)Sequence analysis1
Glycosylationi313N-linked (GlcNAc...)Sequence analysis1
Glycosylationi360N-linked (GlcNAc...)Sequence analysis1
Glycosylationi443N-linked (GlcNAc...)Sequence analysis1
Glycosylationi725N-linked (GlcNAc...)Sequence analysis1
Glycosylationi758N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi798 ↔ 809By similarity
Disulfide bondi805 ↔ 818By similarity
Disulfide bondi820 ↔ 833By similarity
Glycosylationi829N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi845 ↔ 857By similarity
Disulfide bondi852 ↔ 870By similarity
Disulfide bondi864 ↔ 881By similarity
Glycosylationi883N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi886 ↔ 898By similarity
Disulfide bondi893 ↔ 911By similarity
Disulfide bondi905 ↔ 922By similarity
Glycosylationi919N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi927 ↔ 939By similarity
Disulfide bondi934 ↔ 952By similarity
Disulfide bondi946 ↔ 962By similarity
Disulfide bondi967 ↔ 980By similarity
Disulfide bondi975 ↔ 993By similarity
Disulfide bondi987 ↔ 1002By similarity
Disulfide bondi1006 ↔ 1018By similarity
Disulfide bondi1013 ↔ 1031By similarity
Disulfide bondi1025 ↔ 1042By similarity
Glycosylationi1041N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1053 ↔ 1066By similarity
Disulfide bondi1060 ↔ 1079By similarity
Disulfide bondi1073 ↔ 1088By similarity
Glycosylationi1089N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1095 ↔ 1109By similarity
Disulfide bondi1103 ↔ 1122By similarity
Disulfide bondi1116 ↔ 1131By similarity
Disulfide bondi1136 ↔ 1150By similarity
Disulfide bondi1143 ↔ 1163By similarity
Glycosylationi1145N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1157 ↔ 1173By similarity
Glycosylationi1209N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1298N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1502N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1549N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1636N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1754N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1816N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1838 ↔ 1849By similarity
Disulfide bondi1845 ↔ 1859By similarity
Disulfide bondi1861 ↔ 1874By similarity
Glycosylationi1921N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1983N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2105N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi2147 ↔ 2158By similarity
Disulfide bondi2154 ↔ 2168By similarity
Disulfide bondi2170 ↔ 2182By similarity
Glycosylationi2458N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2488N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2507N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi2510 ↔ 2523By similarity
Disulfide bondi2518 ↔ 2536By similarity
Disulfide bondi2530 ↔ 2547By similarity
Glycosylationi2549N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi2552 ↔ 2564By similarity
Disulfide bondi2559 ↔ 2577By similarity
Disulfide bondi2571 ↔ 2586By similarity
Disulfide bondi2591 ↔ 2603By similarity
Disulfide bondi2598 ↔ 2616By similarity
Disulfide bondi2610 ↔ 2625By similarity
Glycosylationi2626N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi2630 ↔ 2652By similarity
Disulfide bondi2646 ↔ 2665By similarity
Glycosylationi2647N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi2659 ↔ 2674By similarity
Disulfide bondi2682 ↔ 2694By similarity
Disulfide bondi2689 ↔ 2707By similarity
Disulfide bondi2701 ↔ 2716By similarity
Disulfide bondi2720 ↔ 2732By similarity
Disulfide bondi2727 ↔ 2745By similarity
Disulfide bondi2739 ↔ 2756By similarity
Disulfide bondi2761 ↔ 2774By similarity
Disulfide bondi2768 ↔ 2787By similarity
Disulfide bondi2781 ↔ 2799By similarity
Glycosylationi2802N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi2805 ↔ 2817By similarity
Disulfide bondi2812 ↔ 2830By similarity
Disulfide bondi2824 ↔ 2840By similarity
Disulfide bondi2845 ↔ 2857By similarity
Disulfide bondi2852 ↔ 2871By similarity
Disulfide bondi2865 ↔ 2884By similarity
Disulfide bondi2891 ↔ 2903By similarity
Glycosylationi2892N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi2898 ↔ 2916By similarity
Disulfide bondi2910 ↔ 2925By similarity
Disulfide bondi2930 ↔ 2942By similarity
Disulfide bondi2938 ↔ 2951By similarity
Disulfide bondi2953 ↔ 2966By similarity
Disulfide bondi2972 ↔ 2982By similarity
Disulfide bondi2978 ↔ 2991By similarity
Disulfide bondi2993 ↔ 3007By similarity
Glycosylationi3034N-linked (GlcNAc...)Sequence analysis1
Glycosylationi3066N-linked (GlcNAc...)Sequence analysis1
Glycosylationi3076N-linked (GlcNAc...)Sequence analysis1
Glycosylationi3164N-linked (GlcNAc...)Sequence analysis1
Glycosylationi3310N-linked (GlcNAc...)Sequence analysis1
Glycosylationi3316N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi3317 ↔ 3329By similarity
Disulfide bondi3324 ↔ 3342By similarity
Disulfide bondi3336 ↔ 3352By similarity
Disulfide bondi3357 ↔ 3369By similarity
Disulfide bondi3364 ↔ 3382By similarity
Disulfide bondi3376 ↔ 3391By similarity
Disulfide bondi3396 ↔ 3409By similarity
Disulfide bondi3403 ↔ 3422By similarity
Disulfide bondi3416 ↔ 3431By similarity
Disulfide bondi3436 ↔ 3449By similarity
Disulfide bondi3443 ↔ 3462By similarity
Disulfide bondi3456 ↔ 3471By similarity
Disulfide bondi3476 ↔ 3488By similarity
Disulfide bondi3483 ↔ 3501By similarity
Disulfide bondi3495 ↔ 3510By similarity
Disulfide bondi3515 ↔ 3527By similarity
Disulfide bondi3522 ↔ 3540By similarity
Disulfide bondi3534 ↔ 3549By similarity
Disulfide bondi3553 ↔ 3565By similarity
Disulfide bondi3560 ↔ 3578By similarity
Disulfide bondi3572 ↔ 3587By similarity
Disulfide bondi3594 ↔ 3606By similarity
Disulfide bondi3601 ↔ 3619By similarity
Disulfide bondi3613 ↔ 3628By similarity
Disulfide bondi3632 ↔ 3645By similarity
Disulfide bondi3639 ↔ 3658By similarity
Disulfide bondi3652 ↔ 3667By similarity
Disulfide bondi3674 ↔ 3686By similarity
Disulfide bondi3681 ↔ 3699By similarity
Glycosylationi3682N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi3693 ↔ 3710By similarity
Disulfide bondi3715 ↔ 3729By similarity
Disulfide bondi3723 ↔ 3742By similarity
Disulfide bondi3736 ↔ 3751By similarity
Disulfide bondi3762 ↔ 3774By similarity
Disulfide bondi3769 ↔ 3787By similarity
Disulfide bondi3781 ↔ 3796By similarity
Disulfide bondi3805 ↔ 3818By similarity
Disulfide bondi3812 ↔ 3827By similarity
Disulfide bondi3829 ↔ 3842By similarity
Disulfide bondi3848 ↔ 3858By similarity
Disulfide bondi3854 ↔ 3867By similarity
Disulfide bondi3869 ↔ 3880By similarity
Glycosylationi3877N-linked (GlcNAc...)Sequence analysis1
Glycosylationi3894N-linked (GlcNAc...)Sequence analysis1
Glycosylationi3906N-linked (GlcNAc...)Sequence analysis1
Glycosylationi4017N-linked (GlcNAc...)Sequence analysis1
Glycosylationi4204N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi4217 ↔ 4227By similarity
Disulfide bondi4221 ↔ 4237By similarity
Disulfide bondi4253 ↔ 4263By similarity
Disulfide bondi4257 ↔ 4273By similarity
Disulfide bondi4275 ↔ 4284By similarity
Disulfide bondi4289 ↔ 4299By similarity
Disulfide bondi4293 ↔ 4309By similarity
Disulfide bondi4311 ↔ 4320By similarity
Disulfide bondi4325 ↔ 4335By similarity
Disulfide bondi4329 ↔ 4345By similarity
Disulfide bondi4347 ↔ 4356By similarity
Glycosylationi4381N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi4394 ↔ 4404By similarity
Disulfide bondi4398 ↔ 4415By similarity
Disulfide bondi4417 ↔ 4426By similarity
Glycosylationi4420N-linked (GlcNAc...)Sequence analysis1
Modified residuei4562PhosphotyrosineBy similarity1
Modified residuei4575PhosphoserineBy similarity1
Modified residuei4578PhosphoserineBy similarity1

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

EPDiQ9NZR2.
MaxQBiQ9NZR2.
PaxDbiQ9NZR2.
PeptideAtlasiQ9NZR2.
PRIDEiQ9NZR2.

PTM databases

iPTMnetiQ9NZR2.
PhosphoSitePlusiQ9NZR2.

Expressioni

Tissue specificityi

Expressed in thyroid gland and in salivary gland, as well as in adult and fetal brain.1 Publication

Gene expression databases

BgeeiENSG00000168702.
CleanExiHS_LRP1B.
ExpressionAtlasiQ9NZR2. baseline and differential.
GenevisibleiQ9NZR2. HS.

Organism-specific databases

HPAiHPA069094.

Interactioni

Subunit structurei

Binds LRPAP1, PLAU, PLAT and SERPINE1; binding is followed by internalization and degradation of the ligands.

Protein-protein interaction databases

BioGridi119750. 22 interactors.
IntActiQ9NZR2. 3 interactors.
STRINGi9606.ENSP00000374135.

Structurei

3D structure databases

ProteinModelPortaliQ9NZR2.
SMRiQ9NZR2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini31 – 70LDL-receptor class A 1PROSITE-ProRule annotationAdd BLAST40
Domaini76 – 114LDL-receptor class A 2PROSITE-ProRule annotationAdd BLAST39
Domaini116 – 154EGF-like 1PROSITE-ProRule annotationAdd BLAST39
Domaini155 – 194EGF-like 2; calcium-bindingPROSITE-ProRule annotationAdd BLAST40
Repeati295 – 337LDL-receptor class B 1Add BLAST43
Repeati338 – 381LDL-receptor class B 2Add BLAST44
Repeati382 – 425LDL-receptor class B 3Add BLAST44
Domaini471 – 517EGF-like 3PROSITE-ProRule annotationAdd BLAST47
Repeati568 – 610LDL-receptor class B 4Add BLAST43
Repeati611 – 656LDL-receptor class B 5Add BLAST46
Repeati657 – 706LDL-receptor class B 6Add BLAST50
Repeati707 – 750LDL-receptor class B 7Add BLAST44
Domaini794 – 834EGF-like 4PROSITE-ProRule annotationAdd BLAST41
Domaini844 – 882LDL-receptor class A 3PROSITE-ProRule annotationAdd BLAST39
Domaini885 – 923LDL-receptor class A 4PROSITE-ProRule annotationAdd BLAST39
Domaini926 – 963LDL-receptor class A 5PROSITE-ProRule annotationAdd BLAST38
Domaini966 – 1003LDL-receptor class A 6PROSITE-ProRule annotationAdd BLAST38
Domaini1005 – 1043LDL-receptor class A 7PROSITE-ProRule annotationAdd BLAST39
Domaini1052 – 1089LDL-receptor class A 8PROSITE-ProRule annotationAdd BLAST38
Domaini1094 – 1132LDL-receptor class A 9PROSITE-ProRule annotationAdd BLAST39
Domaini1135 – 1174LDL-receptor class A 10PROSITE-ProRule annotationAdd BLAST40
Domaini1174 – 1213EGF-like 5PROSITE-ProRule annotationAdd BLAST40
Domaini1214 – 1253EGF-like 6PROSITE-ProRule annotationAdd BLAST40
Repeati1300 – 1346LDL-receptor class B 8Add BLAST47
Repeati1347 – 1389LDL-receptor class B 9Add BLAST43
Repeati1390 – 1436LDL-receptor class B 10Add BLAST47
Repeati1437 – 1480LDL-receptor class B 11Add BLAST44
Repeati1481 – 1522LDL-receptor class B 12Add BLAST42
Domaini1527 – 1570EGF-like 7PROSITE-ProRule annotationAdd BLAST44
Repeati1618 – 1660LDL-receptor class B 13Add BLAST43
Repeati1661 – 1704LDL-receptor class B 14Add BLAST44
Repeati1705 – 1744LDL-receptor class B 15Add BLAST40
Repeati1745 – 1787LDL-receptor class B 16Add BLAST43
Domaini1834 – 1875EGF-like 8PROSITE-ProRule annotationAdd BLAST42
Repeati1922 – 1964LDL-receptor class B 17Add BLAST43
Repeati1965 – 2007LDL-receptor class B 28Add BLAST43
Repeati2008 – 2051LDL-receptor class B 19Add BLAST44
Repeati2052 – 2095LDL-receptor class B 20Add BLAST44
Domaini2143 – 2183EGF-like 9PROSITE-ProRule annotationAdd BLAST41
Repeati2239 – 2280LDL-receptor class B 21Add BLAST42
Repeati2281 – 2329LDL-receptor class B 22Add BLAST49
Repeati2330 – 2374LDL-receptor class B 23Add BLAST45
Repeati2375 – 2416LDL-receptor class B 24Add BLAST42
Repeati2417 – 2459LDL-receptor class B 25Add BLAST43
Domaini2464 – 2504EGF-like 10PROSITE-ProRule annotationAdd BLAST41
Domaini2509 – 2548LDL-receptor class A 11PROSITE-ProRule annotationAdd BLAST40
Domaini2551 – 2587LDL-receptor class A 12PROSITE-ProRule annotationAdd BLAST37
Domaini2590 – 2626LDL-receptor class A 13PROSITE-ProRule annotationAdd BLAST37
Domaini2629 – 2675LDL-receptor class A 14PROSITE-ProRule annotationAdd BLAST47
Domaini2681 – 2717LDL-receptor class A 15PROSITE-ProRule annotationAdd BLAST37
Domaini2719 – 2757LDL-receptor class A 16PROSITE-ProRule annotationAdd BLAST39
Domaini2760 – 2800LDL-receptor class A 17PROSITE-ProRule annotationAdd BLAST41
Domaini2804 – 2841LDL-receptor class A 18PROSITE-ProRule annotationAdd BLAST38
Domaini2844 – 2885LDL-receptor class A 19PROSITE-ProRule annotationAdd BLAST42
Domaini2890 – 2926LDL-receptor class A 20PROSITE-ProRule annotationAdd BLAST37
Domaini2927 – 2967EGF-like 11PROSITE-ProRule annotationAdd BLAST41
Domaini2968 – 3008EGF-like 12; calcium-bindingPROSITE-ProRule annotationAdd BLAST41
Repeati3055 – 3098LDL-receptor class B 26Add BLAST44
Repeati3099 – 3141LDL-receptor class B 27Add BLAST43
Repeati3142 – 3185LDL-receptor class B 28Add BLAST44
Repeati3186 – 3224LDL-receptor class B 29Add BLAST39
Repeati3225 – 3268LDL-receptor class B 30Add BLAST44
Domaini3273 – 3314EGF-like 13PROSITE-ProRule annotationAdd BLAST42
Domaini3316 – 3353LDL-receptor class A 21PROSITE-ProRule annotationAdd BLAST38
Domaini3356 – 3392LDL-receptor class A 22PROSITE-ProRule annotationAdd BLAST37
Domaini3395 – 3432LDL-receptor class A 23PROSITE-ProRule annotationAdd BLAST38
Domaini3435 – 3472LDL-receptor class A 24PROSITE-ProRule annotationAdd BLAST38
Domaini3475 – 3511LDL-receptor class A 25PROSITE-ProRule annotationAdd BLAST37
Domaini3514 – 3550LDL-receptor class A 26PROSITE-ProRule annotationAdd BLAST37
Domaini3552 – 3588LDL-receptor class A 27PROSITE-ProRule annotationAdd BLAST37
Domaini3593 – 3629LDL-receptor class A 28PROSITE-ProRule annotationAdd BLAST37
Domaini3631 – 3668LDL-receptor class A 29PROSITE-ProRule annotationAdd BLAST38
Domaini3673 – 3711LDL-receptor class A 30PROSITE-ProRule annotationAdd BLAST39
Domaini3714 – 3752LDL-receptor class A 31PROSITE-ProRule annotationAdd BLAST39
Domaini3761 – 3797LDL-receptor class A 32PROSITE-ProRule annotationAdd BLAST37
Domaini3801 – 3843EGF-like 14PROSITE-ProRule annotationAdd BLAST43
Domaini3844 – 3881EGF-like 15PROSITE-ProRule annotationAdd BLAST38
Repeati3933 – 3980LDL-receptor class B 31Add BLAST48
Repeati3981 – 4038LDL-receptor class B 32Add BLAST58
Repeati4039 – 4082LDL-receptor class B 33Add BLAST44
Repeati4083 – 4127LDL-receptor class B 34Add BLAST45
Domaini4171 – 4208EGF-like 16PROSITE-ProRule annotationAdd BLAST38
Domaini4213 – 4249EGF-like 17PROSITE-ProRule annotationAdd BLAST37
Domaini4249 – 4285EGF-like 18PROSITE-ProRule annotationAdd BLAST37
Domaini4285 – 4321EGF-like 19PROSITE-ProRule annotationAdd BLAST37
Domaini4321 – 4357EGF-like 20PROSITE-ProRule annotationAdd BLAST37
Domaini4357 – 4392EGF-like 21PROSITE-ProRule annotationAdd BLAST36
Domaini4390 – 4427EGF-like 22PROSITE-ProRule annotationAdd BLAST38

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi4492 – 4495Endocytosis signalSequence analysis4
Motifi4559 – 4562Endocytosis signalSequence analysis4

Sequence similaritiesi

Belongs to the LDLR family.Curated
Contains 22 EGF-like domains.PROSITE-ProRule annotation
Contains 32 LDL-receptor class A domains.PROSITE-ProRule annotation
Contains 34 LDL-receptor class B repeats.PROSITE-ProRule annotation

Keywords - Domaini

EGF-like domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1215. Eukaryota.
ENOG410XP34. LUCA.
GeneTreeiENSGT00760000118968.
HOGENOMiHOG000230574.
HOVERGENiHBG006292.
InParanoidiQ9NZR2.
KOiK20049.
OMAiVHCRELL.
OrthoDBiEOG091G000N.
PhylomeDBiQ9NZR2.
TreeFamiTF315253.

Family and domain databases

Gene3Di2.120.10.30. 8 hits.
4.10.400.10. 31 hits.
InterProiIPR011042. 6-blade_b-propeller_TolB-like.
IPR026823. cEGF.
IPR032485. DUF5050.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR009030. Growth_fac_rcpt_.
IPR023415. LDLR_class-A_CS.
IPR000033. LDLR_classB_rpt.
IPR002172. LDrepeatLR_classA_rpt.
[Graphical view]
PfamiPF12662. cEGF. 1 hit.
PF16472. DUF5050. 1 hit.
PF00008. EGF. 1 hit.
PF07645. EGF_CA. 2 hits.
PF00057. Ldl_recept_a. 30 hits.
PF00058. Ldl_recept_b. 11 hits.
[Graphical view]
PRINTSiPR00261. LDLRECEPTOR.
SMARTiSM00181. EGF. 25 hits.
SM00179. EGF_CA. 6 hits.
SM00192. LDLa. 32 hits.
SM00135. LY. 37 hits.
[Graphical view]
SUPFAMiSSF57184. SSF57184. 6 hits.
SSF57424. SSF57424. 32 hits.
PROSITEiPS00010. ASX_HYDROXYL. 4 hits.
PS00022. EGF_1. 5 hits.
PS01186. EGF_2. 9 hits.
PS50026. EGF_3. 9 hits.
PS01187. EGF_CA. 3 hits.
PS01209. LDLRA_1. 27 hits.
PS50068. LDLRA_2. 32 hits.
PS51120. LDLRB. 37 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9NZR2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSEFLLALLT LSGLLPIARV LTVGADRDQQ LCDPGEFLCH DHVTCVSQSW
60 70 80 90 100
LCDGDPDCPD DSDESLDTCP EEVEIKCPLN HIACLGTNKC VHLSQLCNGV
110 120 130 140 150
LDCPDGYDEG VHCQELLSNC QQLNCQYKCT MVRNSTRCYC EDGFEITEDG
160 170 180 190 200
RSCKDQDECA VYGTCSQTCR NTHGSYTCSC VEGYLMQPDN RSCKAKIEPT
210 220 230 240 250
DRPPILLIAN FETIEVFYLN GSKMATLSSV NGNEIHTLDF IYNEDMICWI
260 270 280 290 300
ESRESSNQLK CIQITKAGGL TDEWTINILQ SFHNVQQMAI DWLTRNLYFV
310 320 330 340 350
DHVGDRIFVC NSNGSVCVTL IDLELHNPKA IAVDPIAGKL FFTDYGNVAK
360 370 380 390 400
VERCDMDGMN RTRIIDSKTE QPAALALDLV NKLVYWVDLY LDYVGVVDYQ
410 420 430 440 450
GKNRHTVIQG RQVRHLYGIT VFEDYLYATN SDNYNIVRIN RFNGTDIHSL
460 470 480 490 500
IKIENAWGIR IYQKRTQPTV RSHACEVDPY GMPGGCSHIC LLSSSYKTRT
510 520 530 540 550
CRCRTGFNLG SDGRSCKRPK NELFLFYGKG RPGIVRGMDL NTKIADEYMI
560 570 580 590 600
PIENLVNPRA LDFHAETNYI YFADTTSFLI GRQKIDGTER ETILKDDLDN
610 620 630 640 650
VEGIAVDWIG NNLYWTNDGH RKTINVARLE KASQSRKTLL EGEMSHPRGI
660 670 680 690 700
VVDPVNGWMY WTDWEEDEID DSVGRIEKAW MDGFNRQIFV TSKMLWPNGL
710 720 730 740 750
TLDFHTNTLY WCDAYYDHIE KVFLNGTHRK IVYSGRELNH PFGLSHHGNY
760 770 780 790 800
VFWTDYMNGS IFQLDLITSE VTLLRHERPP LFGLQIYDPR KQQGDNMCRV
810 820 830 840 850
NNGGCSTLCL AIPGGRVCAC ADNQLLDENG TTCTFNPGEA LPHICKAGEF
860 870 880 890 900
RCKNRHCIQA RWKCDGDDDC LDGSDEDSVN CFNHSCPDDQ FKCQNNRCIP
910 920 930 940 950
KRWLCDGAND CGSNEDESNQ TCTARTCQVD QFSCGNGRCI PRAWLCDRED
960 970 980 990 1000
DCGDQTDEMA SCEFPTCEPL TQFVCKSGRC ISSKWHCDSD DDCGDGSDEV
1010 1020 1030 1040 1050
GCVHSCFDNQ FRCSSGRCIP GHWACDGDND CGDFSDEAQI NCTKEEIHSP
1060 1070 1080 1090 1100
AGCNGNEFQC HPDGNCVPDL WRCDGEKDCE DGSDEKGCNG TIRLCDHKTK
1110 1120 1130 1140 1150
FSCWSTGRCI NKAWVCDGDI DCEDQSDEDD CDSFLCGPPK HPCANDTSVC
1160 1170 1180 1190 1200
LQPEKLCNGK KDCPDGSDEG YLCDECSLNN GGCSNHCSVV PGRGIVCSCP
1210 1220 1230 1240 1250
EGLQLNKDNK TCEIVDYCSN HLKCSQVCEQ HKHTVKCSCY EGWKLDVDGE
1260 1270 1280 1290 1300
SCTSVDPFEA FIIFSIRHEI RRIDLHKRDY SLLVPGLRNT IALDFHFNQS
1310 1320 1330 1340 1350
LLYWTDVVED RIYRGKLSES GGVSAIEVVV EHGLATPEGL TVDWIAGNIY
1360 1370 1380 1390 1400
WIDSNLDQIE VAKLDGSLRT TLIAGAMEHP RAIALDPRYG ILFWTDWDAN
1410 1420 1430 1440 1450
FPRIESASMS GAGRKTIYKD MKTGAWPNGL TVDHFEKRIV WTDARSDAIY
1460 1470 1480 1490 1500
SALYDGTNMI EIIRGHEYLS HPFAVSLYGS EVYWTDWRTN TLSKANKWTG
1510 1520 1530 1540 1550
QNVSVIQKTS AQPFDLQIYH PSRQPQAPNP CAANDGKGPC SHMCLINHNR
1560 1570 1580 1590 1600
SAACACPHLM KLSSDKKTCY EMKKFLLYAR RSEIRGVDID NPYFNFITAF
1610 1620 1630 1640 1650
TVPDIDDVTV IDFDASEERL YWTDIKTQTI KRAFINGTGL ETVISRDIQS
1660 1670 1680 1690 1700
IRGLAVDWVS RNLYWISSEF DETQINVARL DGSLKTSIIH GIDKPQCLAA
1710 1720 1730 1740 1750
HPVRGKLYWT DGNTINMANM DGSNSKILFQ NQKEPVGLSI DYVENKLYWI
1760 1770 1780 1790 1800
SSGNGTINRC NLDGGNLEVI ESMKEELTKA TALTIMDKKL WWADQNLAQL
1810 1820 1830 1840 1850
GTCSKRDGRN PTILRNKTSG VVHMKVYDKE AQQGSNSCQL NNGGCSQLCL
1860 1870 1880 1890 1900
PTSETTRTCM CTVGYYLQKN RMSCQGIESF LMYSVHEGIR GIPLEPSDKM
1910 1920 1930 1940 1950
DALMPISGTS FAVGIDFHAE NDTIYWTDMG FNKISRAKRD QTWKEDIITN
1960 1970 1980 1990 2000
GLGRVEGIAV DWIAGNIYWT DHGFNLIEVA RLNGSFRYVI ISQGLDQPRS
2010 2020 2030 2040 2050
IAVHPEKGLL FWTEWGQMPC IGKARLDGSE KVVLVSMGIA WPNGISIDYE
2060 2070 2080 2090 2100
ENKLYWCDAR TDKIERIDLE TGGNREMVLS GSNVDMFSVA VFGAYIYWSD
2110 2120 2130 2140 2150
RAHANGSVRR GHKNDATETI TMRTGLGVNL KEVKIFNRVR EKGTNVCARD
2160 2170 2180 2190 2200
NGGCKQLCLY RGNSRRTCAC AHGYLAEDGV TCLRHEGYLL YSGRTILKSI
2210 2220 2230 2240 2250
HLSDETNLNS PIRPYENPRY FKNVIALAFD YNQRRKGTNR IFYSDAHFGN
2260 2270 2280 2290 2300
IQLIKDNWED RQVIVENVGS VEGLAYHRAW DTLYWTSSTT SSITRHTVDQ
2310 2320 2330 2340 2350
TRPGAFDREA VITMSEDDHP HVLALDECQN LMFWTNWNEQ HPSIMRSTLT
2360 2370 2380 2390 2400
GKNAQVVVST DILTPNGLTI DYRAEKLYFS DGSLGKIERC EYDGSQRHVI
2410 2420 2430 2440 2450
VKSGPGTFLS LAVYDNYIFW SDWGRRAILR SNKYTGGDTK ILRSDIPHQP
2460 2470 2480 2490 2500
MGIIAVANDT NSCELSPCAL LNGGCHDLCL LTPNGRVNCS CRGDRILLED
2510 2520 2530 2540 2550
NRCVTKNSSC NAYSEFECGN GECIDYQLTC DGIPHCKDKS DEKLLYCENR
2560 2570 2580 2590 2600
SCRRGFKPCY NRRCIPHGKL CDGENDCGDN SDELDCKVST CATVEFRCAD
2610 2620 2630 2640 2650
GTCIPRSARC NQNIDCADAS DEKNCNNTDC THFYKLGVKT TGFIRCNSTS
2660 2670 2680 2690 2700
LCVLPTWICD GSNDCGDYSD ELKCPVQNKH KCEENYFSCP SGRCILNTWI
2710 2720 2730 2740 2750
CDGQKDCEDG RDEFHCDSSC SWNQFACSAQ KCISKHWICD GEDDCGDGLD
2760 2770 2780 2790 2800
ESDSICGAIT CAADMFSCQG SRACVPRHWL CDGERDCPDG SDELSTAGCA
2810 2820 2830 2840 2850
PNNTCDENAF MCHNKVCIPK QFVCDHDDDC GDGSDESPQC GYRQCGTEEF
2860 2870 2880 2890 2900
SCADGRCLLN TQWQCDGDFD CPDHSDEAPL NPKCKSAEQS CNSSFFMCKN
2910 2920 2930 2940 2950
GRCIPSGGLC DNKDDCGDGS DERNCHINEC LSKKVSGCSQ DCQDLPVSYK
2960 2970 2980 2990 3000
CKCWPGFQLK DDGKTCVDID ECSSGFPCSQ QCINTYGTYK CLCTDGYEIQ
3010 3020 3030 3040 3050
PDNPNGCKSL SDEEPFLILA DHHEIRKIST DGSNYTLLKQ GLNNVIAIDF
3060 3070 3080 3090 3100
DYREEFIYWI DSSRPNGSRI NRMCLNGSDI KVVHNTAVPN ALAVDWIGKN
3110 3120 3130 3140 3150
LYWSDTEKRI IEVSKLNGLY PTILVSKRLK FPRDLSLDPQ AGYLYWIDCC
3160 3170 3180 3190 3200
EYPHIGRVGM DGTNQSVVIE TKISRPMALT IDYVNRRLYW ADENHIEFSN
3210 3220 3230 3240 3250
MDGSHRHKVP NQDIPGVIAL TLFEDYIYWT DGKTKSLSRA HKTSGADRLS
3260 3270 3280 3290 3300
LIYSWHAITD IQVYHSYRQP DVSKHLCMIN NGGCSHLCLL APGKTHTCAC
3310 3320 3330 3340 3350
PTNFYLAADN RTCLSNCTAS QFRCKTDKCI PFWWKCDTVD DCGDGSDEPD
3360 3370 3380 3390 3400
DCPEFRCQPG RFQCGTGLCA LPAFICDGEN DCGDNSDELN CDTHVCLSGQ
3410 3420 3430 3440 3450
FKCTKNQKCI PVNLRCNGQD DCGDEEDERD CPENSCSPDY FQCKTTKHCI
3460 3470 3480 3490 3500
SKLWVCDEDP DCADASDEAN CDKKTCGPHE FQCKNNNCIP DHWRCDSQND
3510 3520 3530 3540 3550
CSDNSDEENC KPQTCTLKDF LCANGDCVSS RFWCDGDFDC ADGSDERNCE
3560 3570 3580 3590 3600
TSCSKDQFRC SNGQCIPAKW KCDGHEDCKY GEDEKSCEPA SPTCSSREYI
3610 3620 3630 3640 3650
CASDGCISAS LKCNGEYDCA DGSDEMDCVT ECKEDQFRCK NKAHCIPIRW
3660 3670 3680 3690 3700
LCDGIHDCVD GSDEENCERG GNICRADEFL CNNSLCKLHF WVCDGEDDCG
3710 3720 3730 3740 3750
DNSDEAPDMC VKFLCPSTRP HRCRNNRICL QSEQMCNGID ECGDNSDEDH
3760 3770 3780 3790 3800
CGGKLTYKAR PCKKDEFACS NKKCIPMDLQ CDRLDDCGDG SDEQGCRIAP
3810 3820 3830 3840 3850
TEYTCEDNVN PCGDDAYCNQ IKTSVFCRCK PGFQRNMKNR QCEDLNECLV
3860 3870 3880 3890 3900
FGTCSHQCIN VEGSYKCVCD QNFQERNNTC IAEGSEDQVL YIANDTDILG
3910 3920 3930 3940 3950
FIYPFNYSGD HQQISHIEHN SRITGMDVYY QRDMIIWSTQ FNPGGIFYKR
3960 3970 3980 3990 4000
IHGREKRQAN SGLICPEFKR PRDIAVDWVA GNIYWTDHSR MHWFSYYTTH
4010 4020 4030 4040 4050
WTSLRYSINV GQLNGPNCTR LLTNMAGEPY AIAVNPKRGM MYWTVVGDHS
4060 4070 4080 4090 4100
HIEEAAMDGT LRRILVQKNL QRPTGLAVDY FSERIYWADF ELSIIGSVLY
4110 4120 4130 4140 4150
DGSNSVVSVS SKQGLLHPHR IDIFEDYIYG AGPKNGVFRV QKFGHGSVEY
4160 4170 4180 4190 4200
LALNIDKTKG VLISHRYKQL DLPNPCLDLA CEFLCLLNPS GATCVCPEGK
4210 4220 4230 4240 4250
YLINGTCNDD SLLDDSCKLT CENGGRCILN EKGDLRCHCW PSYSGERCEV
4260 4270 4280 4290 4300
NHCSNYCQNG GTCVPSVLGR PTCSCALGFT GPNCGKTVCE DFCQNGGTCI
4310 4320 4330 4340 4350
VTAGNQPYCH CQPEYTGDRC QYYVCHHYCV NSESCTIGDD GSVECVCPTR
4360 4370 4380 4390 4400
YEGPKCEVDK CVRCHGGHCI INKDSEDIFC NCTNGKIASS CQLCDGYCYN
4410 4420 4430 4440 4450
GGTCQLDPET NVPVCLCSTN WSGTQCERPA PKSSKSDHIS TRSIAIIVPL
4460 4470 4480 4490 4500
VLLVTLITTL VIGLVLCKRK RRTKTIRRQP IINGGINVEI GNPSYNMYEV
4510 4520 4530 4540 4550
DHDHNDGGLL DPGFMIDPTK ARYIGGGPSA FKLPHTAPPI YLNSDLKGPL
4560 4570 4580 4590
TAGPTNYSNP VYAKLYMDGQ NCRNSLGSVD ERKELLPKKI EIGIRETVA
Length:4,599
Mass (Da):515,498
Last modified:January 4, 2005 - v2
Checksum:i98B70555F46CAE66
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti516C → Y in AAL38107 (PubMed:11031110).Curated1
Sequence conflicti1257P → S in AAL38108 (PubMed:11031110).Curated1
Sequence conflicti1571E → G in AAL38108 (PubMed:11031110).Curated1
Sequence conflicti2654 – 2655LP → CQ in AAL38108 (PubMed:11031110).Curated2

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_04975948Q → R.Corresponds to variant rs12990449dbSNPEnsembl.1
Natural variantiVAR_0497603140Q → R.Corresponds to variant rs34488772dbSNPEnsembl.1
Natural variantiVAR_0183283157R → C in NSCLC cells. 1 PublicationCorresponds to variant rs371536401dbSNPEnsembl.1
Natural variantiVAR_0497613458E → K.Corresponds to variant rs1878740dbSNPEnsembl.1
Natural variantiVAR_0497623734Q → K.Corresponds to variant rs35546150dbSNPEnsembl.1
Natural variantiVAR_0497634264V → L.Corresponds to variant rs17386226dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF176832 mRNA. Translation: AAF70379.1.
AF283343 Genomic DNA. No translation available.
AF283342
, AF283327, AF283328, AF283329, AF283330, AF283331, AF283332, AF283333, AF283334, AF283335, AF283336, AF283337, AF283338, AF283339, AF283340, AF283341 Genomic DNA. Translation: AAL38107.1.
AF283374
, AF283344, AF283345, AF283346, AF283347, AF283348, AF283349, AF283350, AF283351, AF283352, AF283353, AF283354, AF283355, AF283356, AF283357, AF283358, AF283359, AF283360, AF283361, AF283362, AF283363, AF283364, AF283366, AF283367, AF283368, AF283369, AF283370, AF283371, AF283372, AF283373 Genomic DNA. Translation: AAL38108.1.
AF283408
, AF283376, AF283377, AF283378, AF283379, AF283380, AF283381, AF283382, AF283383, AF283384, AF283385, AF283386, AF283387, AF283388, AF283389, AF283390, AF283391, AF283392, AF283393, AF283394, AF283395, AF283396, AF283397, AF283398, AF283399, AF283400, AF283401, AF283402, AF283403, AF283404, AF283405, AF283406, AF283407 Genomic DNA. Translation: AAL38109.1.
CCDSiCCDS2182.1.
RefSeqiNP_061027.2. NM_018557.2.
UniGeneiHs.656461.

Genome annotation databases

EnsembliENST00000389484; ENSP00000374135; ENSG00000168702.
GeneIDi53353.
KEGGihsa:53353.
UCSCiuc002tvj.2. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF176832 mRNA. Translation: AAF70379.1.
AF283343 Genomic DNA. No translation available.
AF283342
, AF283327, AF283328, AF283329, AF283330, AF283331, AF283332, AF283333, AF283334, AF283335, AF283336, AF283337, AF283338, AF283339, AF283340, AF283341 Genomic DNA. Translation: AAL38107.1.
AF283374
, AF283344, AF283345, AF283346, AF283347, AF283348, AF283349, AF283350, AF283351, AF283352, AF283353, AF283354, AF283355, AF283356, AF283357, AF283358, AF283359, AF283360, AF283361, AF283362, AF283363, AF283364, AF283366, AF283367, AF283368, AF283369, AF283370, AF283371, AF283372, AF283373 Genomic DNA. Translation: AAL38108.1.
AF283408
, AF283376, AF283377, AF283378, AF283379, AF283380, AF283381, AF283382, AF283383, AF283384, AF283385, AF283386, AF283387, AF283388, AF283389, AF283390, AF283391, AF283392, AF283393, AF283394, AF283395, AF283396, AF283397, AF283398, AF283399, AF283400, AF283401, AF283402, AF283403, AF283404, AF283405, AF283406, AF283407 Genomic DNA. Translation: AAL38109.1.
CCDSiCCDS2182.1.
RefSeqiNP_061027.2. NM_018557.2.
UniGeneiHs.656461.

3D structure databases

ProteinModelPortaliQ9NZR2.
SMRiQ9NZR2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119750. 22 interactors.
IntActiQ9NZR2. 3 interactors.
STRINGi9606.ENSP00000374135.

PTM databases

iPTMnetiQ9NZR2.
PhosphoSitePlusiQ9NZR2.

Polymorphism and mutation databases

BioMutaiLRP1B.
DMDMi57015418.

Proteomic databases

EPDiQ9NZR2.
MaxQBiQ9NZR2.
PaxDbiQ9NZR2.
PeptideAtlasiQ9NZR2.
PRIDEiQ9NZR2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000389484; ENSP00000374135; ENSG00000168702.
GeneIDi53353.
KEGGihsa:53353.
UCSCiuc002tvj.2. human.

Organism-specific databases

CTDi53353.
DisGeNETi53353.
GeneCardsiLRP1B.
H-InvDBHIX0017207.
HGNCiHGNC:6693. LRP1B.
HPAiHPA069094.
MIMi608766. gene.
neXtProtiNX_Q9NZR2.
OpenTargetsiENSG00000168702.
PharmGKBiPA30451.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1215. Eukaryota.
ENOG410XP34. LUCA.
GeneTreeiENSGT00760000118968.
HOGENOMiHOG000230574.
HOVERGENiHBG006292.
InParanoidiQ9NZR2.
KOiK20049.
OMAiVHCRELL.
OrthoDBiEOG091G000N.
PhylomeDBiQ9NZR2.
TreeFamiTF315253.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000168702-MONOMER.

Miscellaneous databases

ChiTaRSiLRP1B. human.
GeneWikiiLRP1B.
GenomeRNAii53353.
PROiQ9NZR2.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000168702.
CleanExiHS_LRP1B.
ExpressionAtlasiQ9NZR2. baseline and differential.
GenevisibleiQ9NZR2. HS.

Family and domain databases

Gene3Di2.120.10.30. 8 hits.
4.10.400.10. 31 hits.
InterProiIPR011042. 6-blade_b-propeller_TolB-like.
IPR026823. cEGF.
IPR032485. DUF5050.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR009030. Growth_fac_rcpt_.
IPR023415. LDLR_class-A_CS.
IPR000033. LDLR_classB_rpt.
IPR002172. LDrepeatLR_classA_rpt.
[Graphical view]
PfamiPF12662. cEGF. 1 hit.
PF16472. DUF5050. 1 hit.
PF00008. EGF. 1 hit.
PF07645. EGF_CA. 2 hits.
PF00057. Ldl_recept_a. 30 hits.
PF00058. Ldl_recept_b. 11 hits.
[Graphical view]
PRINTSiPR00261. LDLRECEPTOR.
SMARTiSM00181. EGF. 25 hits.
SM00179. EGF_CA. 6 hits.
SM00192. LDLa. 32 hits.
SM00135. LY. 37 hits.
[Graphical view]
SUPFAMiSSF57184. SSF57184. 6 hits.
SSF57424. SSF57424. 32 hits.
PROSITEiPS00010. ASX_HYDROXYL. 4 hits.
PS00022. EGF_1. 5 hits.
PS01186. EGF_2. 9 hits.
PS50026. EGF_3. 9 hits.
PS01187. EGF_CA. 3 hits.
PS01209. LDLRA_1. 27 hits.
PS50068. LDLRA_2. 32 hits.
PS51120. LDLRB. 37 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiLRP1B_HUMAN
AccessioniPrimary (citable) accession number: Q9NZR2
Secondary accession number(s): Q8WY29, Q8WY30, Q8WY31
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 26, 2004
Last sequence update: January 4, 2005
Last modified: November 2, 2016
This is version 140 of the entry and version 2 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 gene is preferentially inactivated in one histological type of lung cancer (non-small cell lung cancer (NSCLC)). May thus play an important role in tumorigenesis of NSCLCs.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: 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. 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.