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Protein

Alpha-2-macroglobulin receptor-associated protein

Gene

LRPAP1

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

Functioni

Interacts with LRP1/alpha-2-macroglobulin receptor and glycoprotein 330.

GO - Molecular functioni

  • asialoglycoprotein receptor activity Source: ProtInc
  • heparin binding Source: ProtInc
  • low-density lipoprotein particle receptor binding Source: MGI
  • receptor antagonist activity Source: BHF-UCL
  • unfolded protein binding Source: ProtInc
  • very-low-density lipoprotein particle receptor binding Source: BHF-UCL

GO - Biological processi

  • extracellular negative regulation of signal transduction Source: GOC
  • negative regulation of beta-amyloid clearance Source: BHF-UCL
  • negative regulation of protein binding Source: BHF-UCL
  • negative regulation of very-low-density lipoprotein particle clearance Source: BHF-UCL
  • protein folding Source: ProtInc
  • receptor-mediated endocytosis Source: GOC
  • vesicle-mediated transport Source: ProtInc
Complete GO annotation...

Keywords - Ligandi

Heparin-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-2-macroglobulin receptor-associated protein
Short name:
Alpha-2-MRAP
Alternative name(s):
Low density lipoprotein receptor-related protein-associated protein 1
Short name:
RAP
Gene namesi
Name:LRPAP1
Synonyms:A2MRAP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 4

Organism-specific databases

HGNCiHGNC:6701. LRPAP1.

Subcellular locationi

GO - Cellular componenti

  • cell surface Source: UniProtKB-SubCell
  • endoplasmic reticulum Source: HPA
  • extracellular region Source: GOC
  • integral component of membrane Source: ProtInc
  • plasma membrane Source: MGI
  • rough endoplasmic reticulum lumen Source: Ensembl
  • vesicle Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum

Pathology & Biotechi

Involvement in diseasei

Myopia 23, autosomal recessive (MYP23)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA refractive error of the eye, in which parallel rays from a distant object come to focus in front of the retina, vision being better for near objects than for far.

See also OMIM:615431

In complex with the alpha-2-MR or gp330, it may have some role in the pathogenesis of membrane glomerular nephritis.

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi283 – 2831H → A: Strongly reduced interaction with LRP1; when associated with A-291; A-293; A-302; A-307 and A-341. 1 Publication
Mutagenesisi291 – 2911H → A: Strongly reduced interaction with LRP1; when associated with A-283; A-293; A-302; A-307 and A-341. 1 Publication
Mutagenesisi293 – 2931H → A: Strongly reduced interaction with LRP1; when associated with A-283; A-291; A-302; A-307 and A-341. 1 Publication
Mutagenesisi302 – 3021H → A: Strongly reduced interaction with LRP1; when associated with A-283; A-291; A-293; A-307 and A-341. 1 Publication
Mutagenesisi307 – 3071H → A: Strongly reduced interaction with LRP1; when associated with A-283; A-291; A-293; A-302 and A-341. 1 Publication
Mutagenesisi341 – 3411H → A: Strongly reduced interaction with LRP1; when associated with A-283; A-291; A-293; A-302 and A-307. 1 Publication

Organism-specific databases

MIMi615431. phenotype.
Orphaneti98619. Rare isolated myopia.
PharmGKBiPA30458.

Polymorphism and mutation databases

BioMutaiLRPAP1.
DMDMi231539.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3434Sequence AnalysisAdd
BLAST
Chaini35 – 357323Alpha-2-macroglobulin receptor-associated proteinPRO_0000020724Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei248 – 2481Phosphothreonine1 Publication
Glycosylationi268 – 2681N-linked (GlcNAc...)1 Publication

Post-translational modificationi

N-glycosylated.2 Publications

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiP30533.
PaxDbiP30533.
PeptideAtlasiP30533.
PRIDEiP30533.

PTM databases

PhosphoSiteiP30533.

Expressioni

Gene expression databases

BgeeiP30533.
CleanExiHS_LRPAP1.
ExpressionAtlasiP30533. baseline and differential.
GenevisibleiP30533. HS.

Organism-specific databases

HPAiCAB025518.
HPA008001.

Interactioni

Subunit structurei

Present on cell surface forming a complex with the alpha-2-macroglobulin receptor heavy and light chains. Binds LRP1B; binding is followed by internalization and degradation.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
VLDLRP981554EBI-715927,EBI-9004309

Protein-protein interaction databases

BioGridi110221. 19 interactions.
DIPiDIP-39355N.
IntActiP30533. 13 interactions.
MINTiMINT-1382467.
STRINGi9606.ENSP00000421922.

Structurei

Secondary structure

1
357
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi53 – 564Combined sources
Helixi57 – 6812Combined sources
Helixi73 – 9927Combined sources
Helixi107 – 12216Combined sources
Beta strandi124 – 1263Combined sources
Beta strandi127 – 1304Combined sources
Helixi149 – 16113Combined sources
Helixi166 – 19530Combined sources
Beta strandi208 – 2103Combined sources
Beta strandi213 – 2164Combined sources
Helixi217 – 24327Combined sources
Beta strandi246 – 2494Combined sources
Helixi255 – 26511Combined sources
Helixi271 – 31141Combined sources
Turni314 – 3163Combined sources
Helixi317 – 35337Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LRENMR-A51-131[»]
1NRENMR-A51-131[»]
1OP1NMR-A51-132[»]
1OV2NMR-A35-133[»]
2FCWX-ray1.26A249-357[»]
2FTUNMR-A240-357[»]
2FYLNMR-A51-131[»]
2P01NMR-A35-357[»]
2P03NMR-A35-357[»]
ProteinModelPortaliP30533.
SMRiP30533. Positions 35-357.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP30533.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni237 – 353117LDL receptor bindingSequence AnalysisAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili219 – 31092Sequence AnalysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi354 – 3574Prevents secretion from ERPROSITE-ProRule annotation

Sequence similaritiesi

Belongs to the alpha-2-MRAP family.Curated

Keywords - Domaini

Coiled coil, Signal

Phylogenomic databases

eggNOGiNOG323629.
GeneTreeiENSGT00390000004855.
HOGENOMiHOG000033926.
HOVERGENiHBG000197.
InParanoidiP30533.
OMAiNQVWEKA.
OrthoDBiEOG7P5T15.
PhylomeDBiP30533.
TreeFamiTF320678.

Family and domain databases

Gene3Di1.20.81.10. 1 hit.
InterProiIPR010483. Alpha_2_MRAP_C.
IPR009066. MG_RAP_rcpt_1.
[Graphical view]
PfamiPF06401. Alpha-2-MRAP_C. 1 hit.
PF06400. Alpha-2-MRAP_N. 1 hit.
[Graphical view]
SUPFAMiSSF47045. SSF47045. 3 hits.
PROSITEiPS00014. ER_TARGET. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P30533-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAPRRVRSFL RGLPALLLLL LFLGPWPAAS HGGKYSREKN QPKPSPKRES
60 70 80 90 100
GEEFRMEKLN QLWEKAQRLH LPPVRLAELH ADLKIQERDE LAWKKLKLDG
110 120 130 140 150
LDEDGEKEAR LIRNLNVILA KYGLDGKKDA RQVTSNSLSG TQEDGLDDPR
160 170 180 190 200
LEKLWHKAKT SGKFSGEELD KLWREFLHHK EKVHEYNVLL ETLSRTEEIH
210 220 230 240 250
ENVISPSDLS DIKGSVLHSR HTELKEKLRS INQGLDRLRR VSHQGYSTEA
260 270 280 290 300
EFEEPRVIDL WDLAQSANLT DKELEAFREE LKHFEAKIEK HNHYQKQLEI
310 320 330 340 350
AHEKLRHAES VGDGERVSRS REKHALLEGR TKELGYTVKK HLQDLSGRIS

RARHNEL
Length:357
Mass (Da):41,466
Last modified:April 1, 1993 - v1
Checksum:iD56A7DA754125CFA
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti100 – 1001G → D in BAD96247 (Ref. 3) Curated
Sequence conflicti183 – 1831V → A in BAD96224 (Ref. 3) Curated
Sequence conflicti339 – 3391K → M in BAD96247 (Ref. 3) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti114 – 1141N → S.
Corresponds to variant rs2228158 [ dbSNP | Ensembl ].
VAR_050660
Natural varianti311 – 3111V → M.1 Publication
Corresponds to variant rs1800493 [ dbSNP | Ensembl ].
VAR_011821

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M63959 mRNA. Translation: AAA51553.1.
AF035767
, AF035760, AF035761, AF035762, AF035763, AF035764, AF035765, AF035766 Genomic DNA. Translation: AAC67373.1.
AK222504 mRNA. Translation: BAD96224.1.
AK222527 mRNA. Translation: BAD96247.1.
AL590235 Genomic DNA. Translation: CAM21451.1.
CH471131 Genomic DNA. Translation: EAW82460.1.
CH471131 Genomic DNA. Translation: EAW82461.1.
BC105074 mRNA. Translation: AAI05075.1.
BC112067 mRNA. Translation: AAI12068.1.
U06976 Genomic DNA. Translation: AAA87889.1.
CCDSiCCDS3371.1.
PIRiA39875.
RefSeqiNP_002328.1. NM_002337.3.
UniGeneiHs.40966.

Genome annotation databases

EnsembliENST00000500728; ENSP00000421922; ENSG00000163956.
GeneIDi4043.
KEGGihsa:4043.
UCSCiuc003ghh.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M63959 mRNA. Translation: AAA51553.1.
AF035767
, AF035760, AF035761, AF035762, AF035763, AF035764, AF035765, AF035766 Genomic DNA. Translation: AAC67373.1.
AK222504 mRNA. Translation: BAD96224.1.
AK222527 mRNA. Translation: BAD96247.1.
AL590235 Genomic DNA. Translation: CAM21451.1.
CH471131 Genomic DNA. Translation: EAW82460.1.
CH471131 Genomic DNA. Translation: EAW82461.1.
BC105074 mRNA. Translation: AAI05075.1.
BC112067 mRNA. Translation: AAI12068.1.
U06976 Genomic DNA. Translation: AAA87889.1.
CCDSiCCDS3371.1.
PIRiA39875.
RefSeqiNP_002328.1. NM_002337.3.
UniGeneiHs.40966.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LRENMR-A51-131[»]
1NRENMR-A51-131[»]
1OP1NMR-A51-132[»]
1OV2NMR-A35-133[»]
2FCWX-ray1.26A249-357[»]
2FTUNMR-A240-357[»]
2FYLNMR-A51-131[»]
2P01NMR-A35-357[»]
2P03NMR-A35-357[»]
ProteinModelPortaliP30533.
SMRiP30533. Positions 35-357.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110221. 19 interactions.
DIPiDIP-39355N.
IntActiP30533. 13 interactions.
MINTiMINT-1382467.
STRINGi9606.ENSP00000421922.

PTM databases

PhosphoSiteiP30533.

Polymorphism and mutation databases

BioMutaiLRPAP1.
DMDMi231539.

Proteomic databases

MaxQBiP30533.
PaxDbiP30533.
PeptideAtlasiP30533.
PRIDEiP30533.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000500728; ENSP00000421922; ENSG00000163956.
GeneIDi4043.
KEGGihsa:4043.
UCSCiuc003ghh.4. human.

Organism-specific databases

CTDi4043.
GeneCardsiGC04M003508.
HGNCiHGNC:6701. LRPAP1.
HPAiCAB025518.
HPA008001.
MIMi104225. gene.
615431. phenotype.
neXtProtiNX_P30533.
Orphaneti98619. Rare isolated myopia.
PharmGKBiPA30458.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG323629.
GeneTreeiENSGT00390000004855.
HOGENOMiHOG000033926.
HOVERGENiHBG000197.
InParanoidiP30533.
OMAiNQVWEKA.
OrthoDBiEOG7P5T15.
PhylomeDBiP30533.
TreeFamiTF320678.

Miscellaneous databases

ChiTaRSiLRPAP1. human.
EvolutionaryTraceiP30533.
GeneWikiiLDL-receptor-related_protein_associated_protein.
GenomeRNAii4043.
NextBioi15830.
PROiP30533.
SOURCEiSearch...

Gene expression databases

BgeeiP30533.
CleanExiHS_LRPAP1.
ExpressionAtlasiP30533. baseline and differential.
GenevisibleiP30533. HS.

Family and domain databases

Gene3Di1.20.81.10. 1 hit.
InterProiIPR010483. Alpha_2_MRAP_C.
IPR009066. MG_RAP_rcpt_1.
[Graphical view]
PfamiPF06401. Alpha-2-MRAP_C. 1 hit.
PF06400. Alpha-2-MRAP_N. 1 hit.
[Graphical view]
SUPFAMiSSF47045. SSF47045. 3 hits.
PROSITEiPS00014. ER_TARGET. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Primary structure of alpha 2-macroglobulin receptor-associated protein. Human homologue of a Heymann nephritis antigen."
    Strickland D.K., Ashcom J.D., Williams S., Battey F., Behre E., McTigue K., Battey J.F., Argraves W.S.
    J. Biol. Chem. 266:13364-13369(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 183-195 AND 257-272.
    Tissue: Placenta.
  2. "Analysis of the human LRPAP1 gene coding for the lipoprotein receptor-associated protein: identification of 22 polymorphisms and one mutation."
    Van Leuven F., Thiry E., Stas L., Nelissen B.
    Genomics 52:145-151(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT MET-311.
  3. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
    Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Adipose tissue.
  4. "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.
    , 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].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  7. "Cloning, characterization, and chromosomal localization to 4p16 of the human gene (LRPAP1) coding for the alpha 2-macroglobulin receptor-associated protein and structural comparison with the murine gene coding for the 44-kDa heparin-binding protein."
    Van Leuven F., Hilliker C., Serneels L., Umans L., Overbergh L., Strooper B., Fryns J.-P., Van den Berghe H.
    Genomics 25:492-500(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 204-250.
  8. "The 39-kDa receptor-associated protein interacts with two members of the low density lipoprotein receptor family, alpha 2-macroglobulin receptor and glycoprotein 330."
    Kounnas M.Z., Argraves W.S., Strickland D.K.
    J. Biol. Chem. 267:21162-21166(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  9. "39 kDa receptor-associated protein is an ER resident protein and molecular chaperone for LDL receptor-related protein."
    Bu G., Geuze H.J., Strous G.J., Schwartz A.L.
    EMBO J. 14:2269-2280(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH LRP1.
  10. "The putative tumor suppressor LRP1B, a novel member of the low density lipoprotein (LDL) receptor family, exhibits both overlapping and distinct properties with the LDL receptor-related protein."
    Liu C.-X., Li Y., Obermoeller-McCormick L.M., Schwartz A.L., Bu G.
    J. Biol. Chem. 276:28889-28896(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH LRP1B.
  11. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
    Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
    J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-268.
    Tissue: Liver.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. Cited for: INVOLVEMENT IN MYP23.
  14. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-248, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  15. "The solution structure of the N-terminal domain of alpha2-macroglobulin receptor-associated protein."
    Nielsen P.R., Ellgaard L., Etzerodt M., Thoegersen H.C., Poulsen F.M.
    Proc. Natl. Acad. Sci. U.S.A. 94:7521-7525(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 51-131.
  16. "1H, 13C and 15N resonance assignments of domain 1 of receptor associated protein."
    Wu Y., Migliorini M., Yu P., Strickland D.K., Wang Y.-X.
    J. Biomol. NMR 26:187-188(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 51-132.
  17. "Binding site structure of one LRP-RAP complex: implications for a common ligand-receptor binding motif."
    Jensen G.A., Andersen O.M.J.J., Bonvin A.M., Bjerrum-Bohr I., Etzerodt M., Thoegersen H.C., O'Shea C., Poulsen F.M., Kragelund B.B.
    J. Mol. Biol. 362:700-716(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 51-131 IN COMPLEX WITH LRP1.
  18. "Structure of an LDLR-RAP complex reveals a general mode for ligand recognition by lipoprotein receptors."
    Fisher C., Beglova N., Blacklow S.C.
    Mol. Cell 22:277-283(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.26 ANGSTROMS) OF 250-357 IN COMPLEX WITH LDLR.
  19. Cited for: STRUCTURE BY NMR OF 240-357, INTERACTION WITH LRP1, SUBCELLULAR LOCATION, GLYCOSYLATION, MUTAGENESIS OF HIS-283; HIS-291; HIS-293; HIS-302; HIS-307 AND HIS-341.

Entry informationi

Entry nameiAMRP_HUMAN
AccessioniPrimary (citable) accession number: P30533
Secondary accession number(s): D3DVR9
, Q2M310, Q53HQ3, Q53HS6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: June 24, 2015
This is version 149 of the entry and version 1 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

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: 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

External Data

Dasty 3

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 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.