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P51681

- CCR5_HUMAN

UniProt

P51681 - CCR5_HUMAN

Protein

C-C chemokine receptor type 5

Gene

CCR5

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 150 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      Previous versions | rss
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    Functioni

    Receptor for a number of inflammatory CC-chemokines including MIP-1-alpha, MIP-1-beta and RANTES and subsequently transduces a signal by increasing the intracellular calcium ion level. May play a role in the control of granulocytic lineage proliferation or differentiation. Acts as a coreceptor (CD4 being the primary receptor) for HIV-1 R5 isolates.6 Publications

    GO - Molecular functioni

    1. actin binding Source: UniProtKB
    2. C-C chemokine binding Source: UniProtKB
    3. C-C chemokine receptor activity Source: UniProtKB
    4. chemokine (C-C motif) ligand 5 binding Source: UniProtKB
    5. chemokine receptor activity Source: ProtInc
    6. coreceptor activity Source: ProtInc
    7. phosphatidylinositol phospholipase C activity Source: ProtInc
    8. protein binding Source: UniProtKB

    GO - Biological processi

    1. calcium ion transport Source: UniProtKB
    2. calcium-mediated signaling Source: UniProtKB
    3. cell-cell signaling Source: UniProtKB
    4. cell surface receptor signaling pathway Source: ProtInc
    5. cellular defense response Source: ProtInc
    6. cellular response to lipopolysaccharide Source: UniProtKB
    7. chemokine-mediated signaling pathway Source: GOC
    8. chemotaxis Source: ProtInc
    9. dendritic cell chemotaxis Source: BHF-UCL
    10. entry into host cell Source: Reactome
    11. G-protein coupled receptor signaling pathway Source: UniProtKB
    12. immune response Source: ProtInc
    13. inflammatory response Source: ProtInc
    14. MAPK cascade Source: UniProtKB
    15. positive regulation of cytosolic calcium ion concentration Source: ProtInc
    16. release of sequestered calcium ion into cytosol by sarcoplasmic reticulum Source: UniProtKB
    17. response to cholesterol Source: UniProtKB
    18. signaling Source: UniProtKB
    19. viral process Source: Reactome

    Keywords - Molecular functioni

    G-protein coupled receptor, Receptor, Transducer

    Keywords - Biological processi

    Host-virus interaction

    Enzyme and pathway databases

    ReactomeiREACT_15344. Chemokine receptors bind chemokines.
    REACT_19231. G alpha (i) signalling events.
    REACT_6903. Binding and entry of HIV virion.
    SignaLinkiP51681.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    C-C chemokine receptor type 5
    Short name:
    C-C CKR-5
    Short name:
    CC-CKR-5
    Short name:
    CCR-5
    Short name:
    CCR5
    Alternative name(s):
    CHEMR13
    HIV-1 fusion coreceptor
    CD_antigen: CD195
    Gene namesi
    Name:CCR5
    Synonyms:CMKBR5
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:1606. CCR5.

    Subcellular locationi

    Cell membrane 1 Publication; Multi-pass membrane protein 1 Publication

    GO - Cellular componenti

    1. cell surface Source: UniProtKB
    2. cytoplasm Source: ProtInc
    3. endosome Source: UniProtKB
    4. external side of plasma membrane Source: UniProtKB
    5. integral component of plasma membrane Source: ProtInc
    6. plasma membrane Source: Reactome

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Involvement in diseasei

    Diabetes mellitus, insulin-dependent, 22 (IDDM22) [MIM:612522]: A multifactorial disorder of glucose homeostasis that is characterized by susceptibility to ketoacidosis in the absence of insulin therapy. Clinical features are polydipsia, polyphagia and polyuria which result from hyperglycemia-induced osmotic diuresis and secondary thirst. These derangements result in long-term complications that affect the eyes, kidneys, nerves, and blood vessels.1 Publication
    Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi3 – 31Y → D: No sulfation and greatly decreased binding CCL4 and CCL5; when associated with D-10; D-14 and D-15. Restored most CCL4 binding; when associated with D-10 and D-15. 2 Publications
    Mutagenesisi3 – 31Y → F: No sulfation and greatly decreases binding of CCL4 and CCL5; when associated with F-10; F-14 and F-15. 2 Publications
    Mutagenesisi6 – 61S → A: No change in glycosylation status and greatly decreased CCL4 binding. Loss of molecular mass of about 2 kDa as compared to wild type. Dramatically reduced binding of CCL4; when associated with A-7; A-16; A-17. Similar molecular mass loss. Dramatically reduced binding of CCL4; when associated with A-7 only. 1 Publication
    Mutagenesisi7 – 71S → A: No change in glycosylation status and binds CCL4 as efficiently as wild type. Loss of molecular mass of about 2 kDa as compared to wild type. Dramatically reduced binding of CCL4; when associated with A-6; A-16; A-17. Similar molecular mass loss. Dramatically reduced binding of CCL4; when associated with A-6 only. 1 Publication
    Mutagenesisi10 – 101Y → F: No sulfation and greatly decreases binding of CCL4 and CCL5; when associated with F-3; F-14 and F-15. Small loss of sulfation; when associated with F-14 and F-15. 2 Publications
    Mutagenesisi14 – 141Y → D: No sulfation and greatly decreased binding CCL4 and CCL5; when associated with D-3; D-10 and D-14. No restoration of CCL4 binding; when associated with D-10 and D-15. 2 Publications
    Mutagenesisi14 – 141Y → F: No sulfation and greatly decreases binding of CCL4 and CCL5; when associated with F-3; F-10; and F-15. Small loss of sulfation; when associated with F-10 and F-15. 2 Publications
    Mutagenesisi15 – 151Y → D: No sulfation and greatly decreased binding CCL4 and CCL5; when associated with D-3; D-10 and D-14. Restored most CCL4 binding; when associated with D-3 and D-10. 2 Publications
    Mutagenesisi15 – 151Y → F: No sulfation and greatly decreases binding of CCL4 and CCL5; when associated with F-3; F-10 and F-14. Small loss of sulfation; when associated with F-10 and F-14. 2 Publications
    Mutagenesisi16 – 161T → A: Similar decrease in molecular mass when treated with O-glycosidase as for wild type; when associated with A-17. 1 Publication
    Mutagenesisi17 – 171S → A: Similar decrease in molecular mass when treated with O-glycosidase as for wild type; when associated with A-16. 1 Publication
    Mutagenesisi321 – 3211C → A: Small reduction in palmitoylation. Cell surface expression reduced by 50%. Greatly reduced palmitoylation. Cell surface expression greatly reduced; when associated with A-323 or A-324. No palmitoylation. Cell surface expression greatly reduced. HIV entry reduced by 50%; when associated with A-323 and A-324. 1 Publication
    Mutagenesisi323 – 3231C → A: Small reduction in palmitoylation. Cell surface expression reduced by 50%. Greatly reduced palmitoylation. Cell surface expression greatly reduced; when associated with A-321 or A-324. No palmitoylation. Cell surface expression greatly reduced. HIV entry reduced by 50%; when associated with A-321 and A-324. 1 Publication
    Mutagenesisi324 – 3241C → A: Small reduction in palmitoylation. Cell surface expression reduced by 50%. Greatly reduced palmitoylation. Cell surface expression greatly reduced; when associated with A-321 or A-323. No palmitoylation. Cell surface expression greatly reduced. HIV entry reduced by 50%; when associated with A-321 and A-323. 1 Publication
    Mutagenesisi336 – 3361S → A: APO-RANTES-stimulated phosphorylation reduced by 15%; APO-RANTES-stimulated phosphorylation reduced by 30-50%; when associated with A-337 or A-342 or A-349; APO-RANTES-stimulated phosphorylation reduced by 80%; when associated with A-337 and A-342 or A-349; No APO-RANTES-stimulated phosphorylation; when associated with A-337; A-342 and A349; abolishes interaction with ARRB2; when associated with S-337; S-342 and S-349. 2 Publications
    Mutagenesisi337 – 3371S → A: APO-RANTES-stimulated phosphorylation reduced by 18%; APO-RANTES-stimulated phosphorylation reduced by 30-50% on APO-RANTES stimulation; when associated with A-336 or A-342 or A-349; APO-RANTES-stimulated phosphorylation reduced by 80%; when associated with A-336 and A-342 or A-349; No APO-RANTES-stimulated phosphorylation; when associated with A-336; A-342 and A349; abolishes interaction with ARRB2; when associated with S-336; S-342 and S-349. 2 Publications
    Mutagenesisi342 – 3421S → A: APO-RANTES-stimulated phosphorylation reduced by 42%. Phosphorylation reduced by 50% on APO-RANTES stimulation; when associated with A-336 or A-337 or A-349; APO-RANTES-stimulated phosphorylation reduced by 80% when associated with A-336 and A-337 or A-349; No APO-RANTES-stimulated phosphorylation; when associated with A-336; A-337 and A349; abolishes interaction with ARRB2; when associated with S-336; S-337 and S-349. 2 Publications
    Mutagenesisi349 – 3491S → A: APO-RANTES-stimulated phosphorylation reduced by 43%; APO-RANTES-stimulated phosphorylation reduced by 30-50%; when associated with A-336 or A-337 or A-342; APO-RANTES-stimulated phosphorylation reduced by 80%; when associated with A-336 and A-337 or A-342; No APO-RANTES-stimulated phosphorylation stimulation; when associated with A-336; A-337 and A347; abolishes interaction with ARRB2; when associated with S-336; S-337 and S-342. 2 Publications

    Keywords - Diseasei

    Diabetes mellitus

    Organism-specific databases

    MIMi609423. phenotype.
    610379. phenotype.
    612522. phenotype.
    Orphaneti319269. Susceptibility/resistance to HIV infection.
    PharmGKBiPA26170.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 352352C-C chemokine receptor type 5PRO_0000069257Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei3 – 31Sulfotyrosine2 Publications
    Glycosylationi6 – 61O-linked (GalNAc...)2 Publications
    Glycosylationi7 – 71O-linked (GalNAc...)1 Publication
    Modified residuei10 – 101Sulfotyrosine2 Publications
    Modified residuei14 – 141Sulfotyrosine2 Publications
    Modified residuei15 – 151SulfotyrosineSequence Analysis
    Glycosylationi16 – 161O-linked (GalNAc...)Sequence Analysis
    Glycosylationi17 – 171O-linked (GalNAc...)Sequence Analysis
    Disulfide bondi101 ↔ 178PROSITE-ProRule annotation
    Lipidationi321 – 3211S-palmitoyl cysteine1 Publication
    Lipidationi323 – 3231S-palmitoyl cysteine1 Publication
    Lipidationi324 – 3241S-palmitoyl cysteine1 Publication
    Modified residuei336 – 3361Phosphoserine; by BARK11 Publication
    Modified residuei337 – 3371Phosphoserine; by BARK11 Publication
    Modified residuei342 – 3421Phosphoserine; by BARK11 Publication
    Modified residuei349 – 3491Phosphoserine; by BARK11 Publication

    Post-translational modificationi

    Sulfated on at least 2 of the N-terminal tyrosines. Sulfation contributes to the efficiency of HIV-1 entry and is required for efficient binding of the chemokines, CCL3 and CCL4.3 Publications
    O-glycosylated, but not N-glycosylated. Ser-6 appears to be the major site. Also sialylated glycans present which contribute to chemokine binding. Thr-16 and Ser-17 may also be glycosylated and, if so, with small moieties such as a T-antigen.2 Publications
    Palmitoylation in the C-terminal is important for cell surface expression, and to a lesser extent, for HIV entry.1 Publication
    Phosphorylation on serine residues in the C-terminal is stimulated by binding CC chemokines especially by APO-RANTES.1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Lipoprotein, Palmitate, Phosphoprotein, Sulfation

    Proteomic databases

    PaxDbiP51681.
    PRIDEiP51681.

    PTM databases

    PhosphoSiteiP51681.

    Expressioni

    Tissue specificityi

    Highly expressed in spleen, thymus, in the myeloid cell line THP-1, in the promyeloblastic cell line KG-1a and on CD4+ and CD8+ T-cells. Medium levels in peripheral blood leukocytes and in small intestine. Low levels in ovary and lung.2 Publications

    Gene expression databases

    ArrayExpressiP51681.
    BgeeiP51681.
    GenevestigatoriP51681.

    Interactioni

    Subunit structurei

    Interacts with PRAF2. Interacts with HIV-1 surface protein gp120. Efficient ligand binding to CCL3/MIP-1alpha and CCL4/MIP-1beta requires sulfation, O-glycosylation and sialic acid modifications. Glycosylation on Ser-6 is required for efficient binding of CCL4. Interacts with ADRBK1. Interacts with ARRB1 and ARRB2. Interacts with human cytomegalovirus/HHV-5 protein UL78.10 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CCL4P132362EBI-489374,EBI-6625160
    CCL5P135014EBI-489374,EBI-2848366

    Protein-protein interaction databases

    BioGridi107639. 17 interactions.
    DIPiDIP-5866N.
    IntActiP51681. 11 interactions.
    MINTiMINT-103024.

    Structurei

    Secondary structure

    1
    352
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi10 – 134
    Helixi14 – 174
    Turni20 – 223
    Helixi26 – 5732
    Helixi64 – 9128
    Helixi98 – 13134
    Helixi133 – 1397
    Helixi142 – 16524
    Beta strandi167 – 1726
    Beta strandi175 – 1806
    Helixi187 – 20216
    Helixi204 – 22320
    Helixi229 – 2324
    Helixi234 – 25926
    Helixi261 – 2644
    Helixi269 – 28820
    Helixi289 – 2913
    Helixi293 – 3008
    Helixi302 – 31211

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1ND8model-A1-352[»]
    1NE0model-A1-352[»]
    1OPNmodel-A1-352[»]
    1OPTmodel-A1-352[»]
    1OPWmodel-A1-352[»]
    2L87NMR-A1-27[»]
    2RLLNMR-A7-15[»]
    2RRSNMR-A157-174[»]
    4MBSX-ray2.71A/B3-223[»]
    ProteinModelPortaliP51681.
    SMRiP51681. Positions 19-313.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP51681.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 3030ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini59 – 6810CytoplasmicSequence Analysis
    Topological domaini90 – 10213ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini125 – 14117CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini167 – 19832ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini219 – 23517CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini261 – 27717ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini302 – 35251CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei31 – 5828Helical; Name=1Sequence AnalysisAdd
    BLAST
    Transmembranei69 – 8921Helical; Name=2Sequence AnalysisAdd
    BLAST
    Transmembranei103 – 12422Helical; Name=3Sequence AnalysisAdd
    BLAST
    Transmembranei142 – 16625Helical; Name=4Sequence AnalysisAdd
    BLAST
    Transmembranei199 – 21820Helical; Name=5Sequence AnalysisAdd
    BLAST
    Transmembranei236 – 26025Helical; Name=6Sequence AnalysisAdd
    BLAST
    Transmembranei278 – 30124Helical; Name=7Sequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the G-protein coupled receptor 1 family.PROSITE-ProRule annotation

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG148353.
    HOVERGENiHBG106917.
    InParanoidiP51681.
    KOiK04180.
    OMAiIIFTRSQ.
    OrthoDBiEOG738051.
    PhylomeDBiP51681.
    TreeFamiTF330966.

    Family and domain databases

    Gene3Di1.20.1070.10. 1 hit.
    InterProiIPR002240. Chemokine_CCR5.
    IPR000355. Chemokine_rcpt.
    IPR000276. GPCR_Rhodpsn.
    IPR017452. GPCR_Rhodpsn_7TM.
    [Graphical view]
    PANTHERiPTHR24227. PTHR24227. 1 hit.
    PfamiPF00001. 7tm_1. 1 hit.
    [Graphical view]
    PRINTSiPR00657. CCCHEMOKINER.
    PR01110. CHEMOKINER5.
    PR00237. GPCRRHODOPSN.
    PROSITEiPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
    PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P51681-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDYQVSSPIY DINYYTSEPC QKINVKQIAA RLLPPLYSLV FIFGFVGNML    50
    VILILINCKR LKSMTDIYLL NLAISDLFFL LTVPFWAHYA AAQWDFGNTM 100
    CQLLTGLYFI GFFSGIFFII LLTIDRYLAV VHAVFALKAR TVTFGVVTSV 150
    ITWVVAVFAS LPGIIFTRSQ KEGLHYTCSS HFPYSQYQFW KNFQTLKIVI 200
    LGLVLPLLVM VICYSGILKT LLRCRNEKKR HRAVRLIFTI MIVYFLFWAP 250
    YNIVLLLNTF QEFFGLNNCS SSNRLDQAMQ VTETLGMTHC CINPIIYAFV 300
    GEKFRNYLLV FFQKHIAKRF CKCCSIFQQE APERASSVYT RSTGEQEISV 350
    GL 352
    Length:352
    Mass (Da):40,524
    Last modified:October 1, 1996 - v1
    Checksum:i88ECE1F38E6D45A7
    GO

    Polymorphismi

    Variations in CCR5 are associated with resistance or susceptibility to immunodeficiency virus type 1 (resistance or susceptibility to HIV-1) [MIMi:609423]. Variations in CCR5 gene also influence the rate of progression to AIDS after infection.
    Ser-60 variant, a naturally occurring mutation in a conserved residue in the first intracellular domain of CCR5, results in reduced amounts of the protein in the membrane and consequently may be associated with reduced susceptibility to infection by microbes that depend on these molecules as their receptors.
    Variations in CCR5 are associated with susceptibility to West Nile virus (WNV) infection [MIMi:610379].

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti10 – 101Y → D in INCCR5-71A) (No sulfation and greatly decreased binding CCL4 and CCL5; when associated with D-3; D-10 and D-15. Restored most CCL4 binding; when associated with D-3 and D-15.
    VAR_003481
    Natural varianti12 – 121I → L.1 Publication
    VAR_024066
    Natural varianti20 – 201C → S.1 Publication
    VAR_024067
    Natural varianti29 – 291A → S.1 Publication
    Corresponds to variant rs1800939 [ dbSNP | Ensembl ].
    VAR_011839
    Natural varianti31 – 311R → H in INCCR5-72A.
    Corresponds to variant rs56340326 [ dbSNP | Ensembl ].
    VAR_003482
    Natural varianti34 – 341P → L in TZCCR5-179.
    VAR_003483
    Natural varianti42 – 421I → F.1 Publication
    VAR_024068
    Natural varianti55 – 551L → Q.2 Publications
    Corresponds to variant rs1799863 [ dbSNP | Ensembl ].
    VAR_011840
    Natural varianti60 – 601R → S Associated with susceptibility to HIV-1; reduced surface expression and function of CCR5 protein. 1 Publication
    Corresponds to variant rs1800940 [ dbSNP | Ensembl ].
    VAR_011841
    Natural varianti62 – 621K → R in UGCCR5-145B.
    VAR_003484
    Natural varianti68 – 681Y → H in ZWCCR5-7.
    VAR_003485
    Natural varianti73 – 731A → V.1 Publication
    Corresponds to variant rs56198941 [ dbSNP | Ensembl ].
    VAR_024069
    Natural varianti95 – 951D → N in MWCCR5-107.
    VAR_003486
    Natural varianti97 – 971G → E in INCCR5-467.
    VAR_003487
    Natural varianti122 – 1221L → P in ZWCCR5-7.
    VAR_003488
    Natural varianti158 – 1581F → S in UGCCR5-145A.
    VAR_003489
    Natural varianti176 – 1761Y → C in KECCR5-116.
    VAR_003490
    Natural varianti177 – 1771T → A in INCCR5-45C.
    VAR_003491
    Natural varianti178 – 1781C → R Found in a HIV-resistant individiual. 1 Publication
    Corresponds to variant rs199824195 [ dbSNP | Ensembl ].
    VAR_012481
    Natural varianti185 – 1851S → N in UGCCR5-145A.
    VAR_003492
    Natural varianti210 – 2101M → V in ZWCCR5-7.
    VAR_003493
    Natural varianti214 – 2141Y → C in KECCR5-3B.
    VAR_003494
    Natural varianti215 – 2151S → L.1 Publication
    VAR_024070
    Natural varianti223 – 2231R → Q.2 Publications
    Corresponds to variant rs1800452 [ dbSNP | Ensembl ].
    VAR_011842
    Natural varianti228 – 2281Missing.1 Publication
    VAR_024071
    Natural varianti239 – 2391T → S in INCCR5-71A.
    VAR_003495
    Natural varianti246 – 2461L → P in UGCCR5-145A.
    VAR_003496
    Natural varianti288 – 2881T → M in INCCR5-72A.
    VAR_003497
    Natural varianti301 – 3011G → V.1 Publication
    Corresponds to variant rs1800943 [ dbSNP | Ensembl ].
    VAR_011843
    Natural varianti302 – 3021E → G in TZCCR5-179.
    VAR_003498
    Natural varianti303 – 3031K → E in THCCR5-5.
    VAR_003499
    Natural varianti306 – 3061N → S in MWCCR5-1567.
    VAR_003500
    Natural varianti322 – 3221K → R in THCCR5-5.
    VAR_003501
    Natural varianti333 – 3331E → G in THCCR5-2.
    VAR_003502
    Natural varianti335 – 3351A → V in MWCCR5-1567, MWCCR5-1568, ZWCCR5-14 and ZWCCR5-112. 2 Publications
    Corresponds to variant rs1800944 [ dbSNP | Ensembl ].
    VAR_003503
    Natural varianti339 – 3391Y → F in TZCCR5-181A and MWCCR5-107. 2 Publications
    Corresponds to variant rs1800945 [ dbSNP | Ensembl ].
    VAR_003504
    Natural varianti345 – 3451E → G in UGCCR5-145C.
    VAR_003505

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X91492 Genomic DNA. Translation: CAA62796.1.
    U54994 mRNA. Translation: AAC50598.1.
    U57840 mRNA. Translation: AAB17071.1.
    U83326 Genomic DNA. Translation: AAC51797.1.
    AF011500 mRNA. Translation: AAB65700.1.
    AF011501 mRNA. Translation: AAB65701.1.
    AF011502 mRNA. Translation: AAB65702.1.
    AF011503 mRNA. Translation: AAB65703.1.
    AF011505 mRNA. Translation: AAB65705.1.
    AF011506 mRNA. Translation: AAB65706.1.
    AF011507 mRNA. Translation: AAB65707.1.
    AF011508 mRNA. Translation: AAB65708.1.
    AF011509 mRNA. Translation: AAB65709.1.
    AF011510 mRNA. Translation: AAB65710.1.
    AF011511 mRNA. Translation: AAB65711.1.
    AF011512 mRNA. Translation: AAB65712.1.
    AF011513 mRNA. Translation: AAB65713.1.
    AF011514 mRNA. Translation: AAB65714.1.
    AF011515 mRNA. Translation: AAB65715.1.
    AF011516 mRNA. Translation: AAB65716.1.
    AF011517 mRNA. Translation: AAB65717.1.
    AF011518 mRNA. Translation: AAB65718.1.
    AF011519 mRNA. Translation: AAB65719.1.
    AF011520 mRNA. Translation: AAB65720.1.
    AF011521 mRNA. Translation: AAB65721.1.
    AF011522 mRNA. Translation: AAB65722.1.
    AF011523 mRNA. Translation: AAB65723.1.
    AF011524 mRNA. Translation: AAB65724.1.
    AF011525 mRNA. Translation: AAB65725.1.
    AF011526 mRNA. Translation: AAB65726.1.
    AF011527 mRNA. Translation: AAB65727.1.
    AF011528 mRNA. Translation: AAB65728.1.
    AF011529 mRNA. Translation: AAB65729.1.
    AF011530 mRNA. Translation: AAB65730.1.
    AF011531 mRNA. Translation: AAB65731.1.
    AF011532 mRNA. Translation: AAB65732.1.
    AF011533 mRNA. Translation: AAB65733.1.
    AF011534 mRNA. Translation: AAB65734.1.
    AF011535 mRNA. Translation: AAB65735.1.
    AF011536 mRNA. Translation: AAB65736.1.
    AF011537 mRNA. Translation: AAB65737.1.
    AF031237 Genomic DNA. Translation: AAB94735.1.
    AF052539 Genomic DNA. Translation: AAD18131.1.
    AY221093 Genomic DNA. Translation: AAO65971.1.
    U95626 Genomic DNA. Translation: AAB57793.1.
    BC038398 mRNA. Translation: AAH38398.1.
    CCDSiCCDS2739.1.
    PIRiA43113.
    RefSeqiNP_000570.1. NM_000579.3.
    NP_001093638.1. NM_001100168.1.
    UniGeneiHs.450802.

    Genome annotation databases

    EnsembliENST00000292303; ENSP00000292303; ENSG00000160791.
    ENST00000445772; ENSP00000404881; ENSG00000160791.
    GeneIDi1234.
    KEGGihsa:1234.
    UCSCiuc003cpo.4. human.

    Polymorphism databases

    DMDMi1705896.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    Wikipedia

    CC chemokine receptors entry

    Wikipedia

    CCR5 receptor entry

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X91492 Genomic DNA. Translation: CAA62796.1 .
    U54994 mRNA. Translation: AAC50598.1 .
    U57840 mRNA. Translation: AAB17071.1 .
    U83326 Genomic DNA. Translation: AAC51797.1 .
    AF011500 mRNA. Translation: AAB65700.1 .
    AF011501 mRNA. Translation: AAB65701.1 .
    AF011502 mRNA. Translation: AAB65702.1 .
    AF011503 mRNA. Translation: AAB65703.1 .
    AF011505 mRNA. Translation: AAB65705.1 .
    AF011506 mRNA. Translation: AAB65706.1 .
    AF011507 mRNA. Translation: AAB65707.1 .
    AF011508 mRNA. Translation: AAB65708.1 .
    AF011509 mRNA. Translation: AAB65709.1 .
    AF011510 mRNA. Translation: AAB65710.1 .
    AF011511 mRNA. Translation: AAB65711.1 .
    AF011512 mRNA. Translation: AAB65712.1 .
    AF011513 mRNA. Translation: AAB65713.1 .
    AF011514 mRNA. Translation: AAB65714.1 .
    AF011515 mRNA. Translation: AAB65715.1 .
    AF011516 mRNA. Translation: AAB65716.1 .
    AF011517 mRNA. Translation: AAB65717.1 .
    AF011518 mRNA. Translation: AAB65718.1 .
    AF011519 mRNA. Translation: AAB65719.1 .
    AF011520 mRNA. Translation: AAB65720.1 .
    AF011521 mRNA. Translation: AAB65721.1 .
    AF011522 mRNA. Translation: AAB65722.1 .
    AF011523 mRNA. Translation: AAB65723.1 .
    AF011524 mRNA. Translation: AAB65724.1 .
    AF011525 mRNA. Translation: AAB65725.1 .
    AF011526 mRNA. Translation: AAB65726.1 .
    AF011527 mRNA. Translation: AAB65727.1 .
    AF011528 mRNA. Translation: AAB65728.1 .
    AF011529 mRNA. Translation: AAB65729.1 .
    AF011530 mRNA. Translation: AAB65730.1 .
    AF011531 mRNA. Translation: AAB65731.1 .
    AF011532 mRNA. Translation: AAB65732.1 .
    AF011533 mRNA. Translation: AAB65733.1 .
    AF011534 mRNA. Translation: AAB65734.1 .
    AF011535 mRNA. Translation: AAB65735.1 .
    AF011536 mRNA. Translation: AAB65736.1 .
    AF011537 mRNA. Translation: AAB65737.1 .
    AF031237 Genomic DNA. Translation: AAB94735.1 .
    AF052539 Genomic DNA. Translation: AAD18131.1 .
    AY221093 Genomic DNA. Translation: AAO65971.1 .
    U95626 Genomic DNA. Translation: AAB57793.1 .
    BC038398 mRNA. Translation: AAH38398.1 .
    CCDSi CCDS2739.1.
    PIRi A43113.
    RefSeqi NP_000570.1. NM_000579.3.
    NP_001093638.1. NM_001100168.1.
    UniGenei Hs.450802.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1ND8 model - A 1-352 [» ]
    1NE0 model - A 1-352 [» ]
    1OPN model - A 1-352 [» ]
    1OPT model - A 1-352 [» ]
    1OPW model - A 1-352 [» ]
    2L87 NMR - A 1-27 [» ]
    2RLL NMR - A 7-15 [» ]
    2RRS NMR - A 157-174 [» ]
    4MBS X-ray 2.71 A/B 3-223 [» ]
    ProteinModelPortali P51681.
    SMRi P51681. Positions 19-313.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107639. 17 interactions.
    DIPi DIP-5866N.
    IntActi P51681. 11 interactions.
    MINTi MINT-103024.

    Chemistry

    BindingDBi P51681.
    ChEMBLi CHEMBL274.
    DrugBanki DB04835. Maraviroc.
    GuidetoPHARMACOLOGYi 62.

    Protein family/group databases

    GPCRDBi Search...

    PTM databases

    PhosphoSitei P51681.

    Polymorphism databases

    DMDMi 1705896.

    Proteomic databases

    PaxDbi P51681.
    PRIDEi P51681.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000292303 ; ENSP00000292303 ; ENSG00000160791 .
    ENST00000445772 ; ENSP00000404881 ; ENSG00000160791 .
    GeneIDi 1234.
    KEGGi hsa:1234.
    UCSCi uc003cpo.4. human.

    Organism-specific databases

    CTDi 1234.
    GeneCardsi GC03P046386.
    HGNCi HGNC:1606. CCR5.
    MIMi 601373. gene.
    609423. phenotype.
    610379. phenotype.
    612522. phenotype.
    neXtProti NX_P51681.
    Orphaneti 319269. Susceptibility/resistance to HIV infection.
    PharmGKBi PA26170.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG148353.
    HOVERGENi HBG106917.
    InParanoidi P51681.
    KOi K04180.
    OMAi IIFTRSQ.
    OrthoDBi EOG738051.
    PhylomeDBi P51681.
    TreeFami TF330966.

    Enzyme and pathway databases

    Reactomei REACT_15344. Chemokine receptors bind chemokines.
    REACT_19231. G alpha (i) signalling events.
    REACT_6903. Binding and entry of HIV virion.
    SignaLinki P51681.

    Miscellaneous databases

    EvolutionaryTracei P51681.
    GeneWikii CCR5.
    GenomeRNAii 1234.
    NextBioi 5035.
    PROi P51681.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P51681.
    Bgeei P51681.
    Genevestigatori P51681.

    Family and domain databases

    Gene3Di 1.20.1070.10. 1 hit.
    InterProi IPR002240. Chemokine_CCR5.
    IPR000355. Chemokine_rcpt.
    IPR000276. GPCR_Rhodpsn.
    IPR017452. GPCR_Rhodpsn_7TM.
    [Graphical view ]
    PANTHERi PTHR24227. PTHR24227. 1 hit.
    Pfami PF00001. 7tm_1. 1 hit.
    [Graphical view ]
    PRINTSi PR00657. CCCHEMOKINER.
    PR01110. CHEMOKINER5.
    PR00237. GPCRRHODOPSN.
    PROSITEi PS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
    PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning and functional expression of a new human CC-chemokine receptor gene."
      Samson M., Labbe O., Mollereau C., Vassart G., Parmentier M.
      Biochemistry 35:3362-3367(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, TISSUE SPECIFICITY.
    2. "Molecular cloning and functional characterization of a novel human CC chemokine receptor (CCR5) for RANTES, MIP-1beta, and MIP-1alpha."
      Raport C.J., Gosling J., Schweichart V.L., Gray P.W., Charo I.F.
      J. Biol. Chem. 271:17161-17166(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH CCL4 AND CCL5, TISSUE SPECIFICITY.
      Tissue: Macrophage.
    3. "Cloning and functional expression of CC CKR5, a human monocyte CC chemokine receptor selective for MIP-1(alpha), MIP-1(beta), and RANTES."
      Combadiere C., Ahuja S.K., Tiffany H.L., Murphy P.M.
      J. Leukoc. Biol. 60:147-152(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH CCL3; CCL4 AND CCL5.
    4. "Polymorphisms in the CCR5 genes of African green monkeys and mice implicate specific amino acids in infections by simian and human immunodeficiency viruses."
      Kuhmann S.E., Platt E.J., Kozak S.L., Kabat D.
      J. Virol. 71:8642-8656(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [MRNA], POLYMORPHISM.
    6. "The human CC chemokine receptor 5 (CCR5) gene. Multiple transcripts with 5'-end heterogeneity, dual promoter usage, and evidence for polymorphisms within the regulatory regions and noncoding exons."
      Mummidi S., Ahuja S.S., McDaniel B.L., Ahuja S.K.
      J. Biol. Chem. 272:30662-30671(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    7. Magierowska M., Barre-Sinoussi F., Issafras H., Theodorou I., Debre P.
      Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ARG-178.
    8. "cDNA clones of human proteins involved in signal transduction sequenced by the Guthrie cDNA resource center (www.cdna.org)."
      Kopatz S.A., Aronstam R.S., Sharma S.V.
      Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    9. "The DNA sequence, annotation and analysis of human chromosome 3."
      Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
      , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
      Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    10. "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].
    11. Cited for: FUNCTION AS A HIV-1 CORECEPTOR.
    12. Cited for: FUNCTION AS A HIV-1 CORECEPTOR.
    13. "A conserved HIV gp120 glycoprotein structure involved in chemokine receptor binding."
      Rizzuto C.D., Wyatt R., Hernandez-Ramos N., Sun Y., Kwong P.D., Hendrickson W.A., Sodroski J.
      Science 280:1949-1953(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HIV-1 SURFACE PROTEIN GP120.
    14. "Tyrosine sulfation of the amino terminus of CCR5 facilitates HIV-1 entry."
      Farzan M., Mirzabekov T., Kolchinsky P., Wyatt R., Cayabyab M., Gerard N.P., Gerard C., Sodroski J., Choe H.
      Cell 96:667-676(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: SULFATION AT TYR-3, GLYCOSYLATION, MUTAGENESIS OF TYR-3; TYR-10; TYR-14 AND TYR-15.
    15. "Differential effects of CC chemokines on CC chemokine receptor 5 (CCR5) phosphorylation and identification of phosphorylation sites on the CCR5 carboxyl terminus."
      Oppermann M., Mack M., Proudfoot A.E., Olbrich H.
      J. Biol. Chem. 274:8875-8885(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-336; SER-337; SER-342 AND SER-349, MUTAGENESIS OF SER-336; SER-337; SER-342 AND SER-349, INTERACTION WITH ADRBK1.
    16. "Palmitoylation of CCR5 is critical for receptor trafficking and efficient activation of intracellular signaling pathways."
      Blanpain C., Wittamer V., Vanderwinden J.-M., Boom A., Renneboog B., Lee B., Le Poul E., El Asmar L., Govaerts C., Vassart G., Doms R.W., Parmentier M.
      J. Biol. Chem. 276:23795-23804(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: PALMITOYLATION AT CYS-321; CYS-323 AND CYS-324, SUBCELLULAR LOCATION, FUNCTION, MUTAGENESIS OF CYS-321; CYS-323 AND CYS-324.
    17. "Characterization of sequence determinants within the carboxyl-terminal domain of chemokine receptor CCR5 that regulate signaling and receptor internalization."
      Kraft K., Olbrich H., Majoul I., Mack M., Proudfoot A., Oppermann M.
      J. Biol. Chem. 276:34408-34418(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ARRB2, MUTAGENESIS OF SER-336; SER-337; SER-342 AND SER-349.
    18. "Sialylated O-glycans and sulfated tyrosines in the NH2-terminal domain of CC chemokine receptor 5 contribute to high affinity binding of chemokines."
      Bannert N., Craig S., Farzan M., Sogah D., Santo N.V., Choe H., Sodroski J.
      J. Exp. Med. 194:1661-1673(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: SULFATION, GLYCOSYLATION AT SER-6, INTERACTION WITH CCL3; CCL4 AND CCL5, MUTAGENESIS OF TYR-3; SER-6; SER-7; TYR-10; TYR-14; TYR-15; THR-16 AND SER-17, CHARACTERIZATION OF VARIANT ASP-10.
    19. "JM4 is a four-transmembrane protein binding to the CCR5 receptor."
      Schweneker M., Bachmann A.S., Moelling K.
      FEBS Lett. 579:1751-1758(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PRAF2.
    20. "G protein-coupled receptor kinases promote phosphorylation and beta-arrestin-mediated internalization of CCR5 homo- and hetero-oligomers."
      Huettenrauch F., Pollok-Kopp B., Oppermann M.
      J. Biol. Chem. 280:37503-37515(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ARRB1 AND ARRB2.
    21. "CCR5 deficiency increases risk of symptomatic West Nile virus infection."
      Glass W.G., McDermott D.H., Lim J.K., Lekhong S., Yu S.F., Frank W.A., Pape J., Cheshier R.C., Murphy P.M.
      J. Exp. Med. 203:35-40(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN WEST NILE VIRUS INFECTION SUSCEPTIBILITY.
    22. "Human cytomegalovirus-encoded UL33 and UL78 heteromerize with host CCR5 and CXCR4 impairing their HIV coreceptor activity."
      Tadagaki K., Tudor D., Gbahou F., Tschische P., Waldhoer M., Bomsel M., Jockers R., Kamal M.
      Blood 119:4908-4918(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HHV-5 PROTEIN UL78.
    23. "Structure modeling of the chemokine receptor CCR5: implications for ligand binding and selectivity."
      Paterlini M.G.
      Biophys. J. 83:3012-3031(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: 3D-STRUCTURE MODELING.
    24. "Structural and functional characterization of the human CCR5 receptor in complex with HIV gp120 envelope glycoprotein and CD4 receptor by molecular modeling studies."
      Liu S., Fan S., Sun Z.
      J. Mol. Model. 9:329-336(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: 3D-STRUCTURE MODELING.
    25. "The conformation and orientation of a 27-residue CCR5 peptide in a ternary complex with HIV-1 gp120 and a CD4-mimic peptide."
      Schnur E., Noah E., Ayzenshtat I., Sargsyan H., Inui T., Ding F.X., Arshava B., Sagi Y., Kessler N., Levy R., Scherf T., Naider F., Anglister J.
      J. Mol. Biol. 410:778-797(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 1-27 IN COMPLEX WITH HIV-1 GP120 AND CD4 MIMIC PEPTIDE, SULFATION AT TYR-10 AND TYR-14.
    26. Cited for: VARIANTS GLN-55; LEU-215; GLN-223; VAL-335 AND PHE-339.
    27. Cited for: VARIANTS LEU-12; SER-20; SER-29; PHE-42; GLN-55; SER-60; VAL-73; GLN-223; LYS-228 DEL; VAL-301; VAL-335 AND PHE-339, ASSOCIATION WITH SUSCEPTIBILITY TO HIV-1.
    28. "A homologous naturally occurring mutation in Duffy and CCR5 leading to reduced receptor expression."
      Tamasauskas D., Powell V., Saksela K., Yazdanbakhsh K.
      Blood 97:3651-3654(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION OF VARIANT SER-60.
    29. Cited for: INVOLVEMENT IN IDDM22.

    Entry informationi

    Entry nameiCCR5_HUMAN
    AccessioniPrimary (citable) accession number: P51681
    Secondary accession number(s): O14692
    , O14693, O14695, O14696, O14697, O14698, O14699, O14700, O14701, O14702, O14703, O14704, O14705, O14706, O14707, O14708, O15538, Q9UPA4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 150 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, Reference proteome

    Documents

    1. 7-transmembrane G-linked receptors
      List of 7-transmembrane G-linked receptor entries
    2. Human cell differentiation molecules
      CD nomenclature of surface proteins of human leucocytes and list of entries
    3. Human chromosome 3
      Human chromosome 3: entries, gene names and cross-references to MIM
    4. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    5. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    6. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    7. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    8. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3