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P30533

- AMRP_HUMAN

UniProt

P30533 - AMRP_HUMAN

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Protein
Alpha-2-macroglobulin receptor-associated protein
Gene
LRPAP1, A2MRAP
Organism
Homo sapiens (Human)
Status
Reviewed - 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

  1. asialoglycoprotein receptor activity Source: ProtInc
  2. heparin binding Source: ProtInc
  3. low-density lipoprotein particle receptor binding Source: MGI
  4. protein binding Source: IntAct
  5. receptor antagonist activity Source: BHF-UCL
  6. unfolded protein binding Source: ProtInc
  7. very-low-density lipoprotein particle receptor binding Source: BHF-UCL

GO - Biological processi

  1. extracellular negative regulation of signal transduction Source: GOC
  2. negative regulation of beta-amyloid clearance Source: BHF-UCL
  3. negative regulation of protein binding Source: BHF-UCL
  4. negative regulation of very-low-density lipoprotein particle clearance Source: BHF-UCL
  5. protein folding Source: ProtInc
  6. receptor-mediated endocytosis Source: GOC
  7. 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: Chromosome 4

Organism-specific databases

HGNCiHGNC:6701. LRPAP1.

Subcellular locationi

Endoplasmic reticulum. Cytoplasm. Cell surface
Note: Intracellular and associated with cell surface receptors. Found in the endoplasmic reticulum.2 Publications

GO - Cellular componenti

  1. cell surface Source: UniProtKB-SubCell
  2. endoplasmic reticulum Source: HPA
  3. extracellular region Source: GOC
  4. integral component of membrane Source: ProtInc
  5. plasma membrane Source: MGI
  6. rough endoplasmic reticulum lumen Source: Ensembl
  7. vesicle Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum

Pathology & Biotechi

Involvement in diseasei

Myopia 23, autosomal recessive (MYP23) [MIM:615431]: A 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.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication
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.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3434 Reviewed prediction
Add
BLAST
Chaini35 – 357323Alpha-2-macroglobulin receptor-associated protein
PRO_0000020724Add
BLAST

Amino acid modifications

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

Post-translational modificationi

N-glycosylated.1 Publication

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiP30533.
PaxDbiP30533.
PeptideAtlasiP30533.
PRIDEiP30533.

PTM databases

PhosphoSiteiP30533.

Expressioni

Gene expression databases

ArrayExpressiP30533.
BgeeiP30533.
CleanExiHS_LRPAP1.
GenevestigatoriP30533.

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.

Binary interactionsi

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

Protein-protein interaction databases

BioGridi110221. 20 interactions.
DIPiDIP-39355N.
IntActiP30533. 13 interactions.
MINTiMINT-1382467.
STRINGi9606.ENSP00000296325.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.

Miscellaneous databases

EvolutionaryTraceiP30533.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni237 – 353117LDL receptor binding Reviewed prediction
Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili219 – 31092 Reviewed prediction
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi354 – 3574Prevents secretion from ER Reviewed prediction

Sequence similaritiesi

Belongs to the alpha-2-MRAP family.

Keywords - Domaini

Coiled coil, Signal

Phylogenomic databases

eggNOGiNOG323629.
HOGENOMiHOG000033926.
HOVERGENiHBG000197.
InParanoidiP30533.
OMAiFRMAKLN.
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

MAPRRVRSFL RGLPALLLLL LFLGPWPAAS HGGKYSREKN QPKPSPKRES    50
GEEFRMEKLN QLWEKAQRLH LPPVRLAELH ADLKIQERDE LAWKKLKLDG 100
LDEDGEKEAR LIRNLNVILA KYGLDGKKDA RQVTSNSLSG TQEDGLDDPR 150
LEKLWHKAKT SGKFSGEELD KLWREFLHHK EKVHEYNVLL ETLSRTEEIH 200
ENVISPSDLS DIKGSVLHSR HTELKEKLRS INQGLDRLRR VSHQGYSTEA 250
EFEEPRVIDL WDLAQSANLT DKELEAFREE LKHFEAKIEK HNHYQKQLEI 300
AHEKLRHAES VGDGERVSRS REKHALLEGR TKELGYTVKK HLQDLSGRIS 350
RARHNEL 357
Length:357
Mass (Da):41,466
Last modified:April 1, 1993 - v1
Checksum:iD56A7DA754125CFA
GO

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 conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti100 – 1001G → D in BAD96247. 1 Publication
Sequence conflicti183 – 1831V → A in BAD96224. 1 Publication
Sequence conflicti339 – 3391K → M in BAD96247. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.

Polymorphism databases

DMDMi231539.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS3371.1.
PIRi A39875.
RefSeqi NP_002328.1. NM_002337.3.
UniGenei Hs.40966.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1LRE NMR - A 51-131 [» ]
1NRE NMR - A 51-131 [» ]
1OP1 NMR - A 51-132 [» ]
1OV2 NMR - A 35-133 [» ]
2FCW X-ray 1.26 A 249-357 [» ]
2FTU NMR - A 240-357 [» ]
2FYL NMR - A 51-131 [» ]
2P01 NMR - A 35-357 [» ]
2P03 NMR - A 35-357 [» ]
ProteinModelPortali P30533.
SMRi P30533. Positions 35-357.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110221. 20 interactions.
DIPi DIP-39355N.
IntActi P30533. 13 interactions.
MINTi MINT-1382467.
STRINGi 9606.ENSP00000296325.

PTM databases

PhosphoSitei P30533.

Polymorphism databases

DMDMi 231539.

Proteomic databases

MaxQBi P30533.
PaxDbi P30533.
PeptideAtlasi P30533.
PRIDEi P30533.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000500728 ; ENSP00000421922 ; ENSG00000163956 .
GeneIDi 4043.
KEGGi hsa:4043.
UCSCi uc003ghh.4. human.

Organism-specific databases

CTDi 4043.
GeneCardsi GC04M003508.
HGNCi HGNC:6701. LRPAP1.
HPAi CAB025518.
HPA008001.
MIMi 104225. gene.
615431. phenotype.
neXtProti NX_P30533.
Orphaneti 98619. Rare isolated myopia.
PharmGKBi PA30458.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG323629.
HOGENOMi HOG000033926.
HOVERGENi HBG000197.
InParanoidi P30533.
OMAi FRMAKLN.
OrthoDBi EOG7P5T15.
PhylomeDBi P30533.
TreeFami TF320678.

Miscellaneous databases

ChiTaRSi LRPAP1. human.
EvolutionaryTracei P30533.
GeneWikii LDL-receptor-related_protein_associated_protein.
GenomeRNAii 4043.
NextBioi 15830.
PROi P30533.
SOURCEi Search...

Gene expression databases

ArrayExpressi P30533.
Bgeei P30533.
CleanExi HS_LRPAP1.
Genevestigatori P30533.

Family and domain databases

Gene3Di 1.20.81.10. 1 hit.
InterProi IPR010483. Alpha_2_MRAP_C.
IPR009066. MG_RAP_rcpt_1.
[Graphical view ]
Pfami PF06401. Alpha-2-MRAP_C. 1 hit.
PF06400. Alpha-2-MRAP_N. 1 hit.
[Graphical view ]
SUPFAMi SSF47045. SSF47045. 3 hits.
PROSITEi PS00014. ER_TARGET. 1 hit.
[Graphical view ]
ProtoNeti Search...

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. "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.
  15. "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.
  16. "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.
  17. "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.
  18. 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: July 9, 2014
This is version 142 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

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