Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P12271

- RLBP1_HUMAN

UniProt

P12271 - RLBP1_HUMAN

Protein

Retinaldehyde-binding protein 1

Gene

RLBP1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 142 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Soluble retinoid carrier essential the proper function of both rod and cone photoreceptors. Participates in the regeneration of active 11-cis-retinol and 11-cis-retinaldehyde, from the inactive 11-trans products of the rhodopsin photocycle and in the de novo synthesis of these retinoids from 11-trans metabolic precursors. The cycling of retinoids between photoreceptor and adjacent pigment epithelium cells is known as the 'visual cycle'.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei180 – 180111-cis-retinal1 Publication
    Binding sitei202 – 202111-cis-retinal1 Publication

    GO - Molecular functioni

    1. 11-cis retinal binding Source: Ensembl
    2. retinol binding Source: UniProtKB-KW
    3. transporter activity Source: InterPro

    GO - Biological processi

    1. phototransduction, visible light Source: Reactome
    2. retinoid metabolic process Source: Reactome
    3. visual perception Source: ProtInc
    4. vitamin A metabolic process Source: ProtInc

    Keywords - Biological processi

    Sensory transduction, Transport, Vision

    Keywords - Ligandi

    Retinol-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:ENSG00000140522-MONOMER.
    ReactomeiREACT_160083. The retinoid cycle in cones (daylight vision).
    REACT_160130. Retinoid cycle disease events.
    REACT_160156. The canonical retinoid cycle in rods (twilight vision).

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Retinaldehyde-binding protein 1
    Alternative name(s):
    Cellular retinaldehyde-binding protein
    Gene namesi
    Name:RLBP1
    Synonyms:CRALBP
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 15

    Organism-specific databases

    HGNCiHGNC:10024. RLBP1.

    Subcellular locationi

    GO - Cellular componenti

    1. cell body Source: Ensembl
    2. cytosol Source: Reactome

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Involvement in diseasei

    Retinitis pigmentosa autosomal recessive (ARRP) [MIM:268000]: A retinal dystrophy belonging to the group of pigmentary retinopathies. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti151 – 1511R → Q in ARRP; loss of ability to bind 11-cis-retinaldehyde. 1 Publication
    Corresponds to variant rs28933989 [ dbSNP | Ensembl ].
    VAR_005140
    Bothnia retinal dystrophy (BRD) [MIM:607475]: A type of retinitis punctata albescens. Affected individuals show night blindness from early childhood with features consistent with retinitis punctata albescens and macular degeneration.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti234 – 2341R → W in BRD. 1 Publication
    Corresponds to variant rs28933990 [ dbSNP | Ensembl ].
    VAR_015172
    Rod-cone dystrophy Newfoundland (NFRCD) [MIM:607476]: A rod-cone dystrophy reminiscent of retinitis punctata albescens but with a substantially lower age at onset and more-rapid and distinctive progression. Rod-cone dystrophies results from initial loss of rod photoreceptors, later followed by cone photoreceptors loss.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Retinitis punctata albescens (RPA) [MIM:136880]: Rare form of stationary night blindness characterized by a delay in the regeneration of cone and rod photopigments.
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Keywords - Diseasei

    Disease mutation, Retinitis pigmentosa

    Organism-specific databases

    MIMi136880. phenotype.
    268000. phenotype.
    607475. phenotype.
    607476. phenotype.
    Orphaneti85128. Bothnia retinal dystrophy.
    227796. Fundus albipunctatus.
    791. Retinitis pigmentosa.
    52427. Retinitis punctata albescens.
    PharmGKBiPA34397.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 317316Retinaldehyde-binding protein 1PRO_0000079330Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PaxDbiP12271.
    PRIDEiP12271.

    PTM databases

    PhosphoSiteiP12271.

    Expressioni

    Tissue specificityi

    Retina and pineal gland. Not present in photoreceptor cells but is expressed abundantly in the adjacent retinal pigment epithelium (RPE) and in the Mueller glial cells of the retina.1 Publication

    Gene expression databases

    ArrayExpressiP12271.
    BgeeiP12271.
    CleanExiHS_RLBP1.
    GenevestigatoriP12271.

    Interactioni

    Protein-protein interaction databases

    BioGridi111949. 2 interactions.
    STRINGi9606.ENSP00000268125.

    Structurei

    Secondary structure

    1
    317
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi27 – 293
    Beta strandi33 – 353
    Turni41 – 433
    Helixi44 – 496
    Turni50 – 523
    Turni55 – 573
    Helixi58 – 7417
    Turni75 – 773
    Helixi79 – 879
    Turni88 – 903
    Helixi93 – 10210
    Turni103 – 1053
    Helixi107 – 12317
    Helixi125 – 1273
    Turni128 – 1303
    Helixi133 – 1419
    Beta strandi144 – 1474
    Beta strandi157 – 1626
    Turni168 – 1703
    Helixi173 – 18715
    Helixi191 – 1966
    Beta strandi198 – 2036
    Helixi209 – 2146
    Helixi217 – 22812
    Turni232 – 2343
    Beta strandi235 – 2428
    Helixi247 – 2548
    Helixi255 – 2573
    Helixi260 – 2634
    Beta strandi266 – 2705
    Helixi274 – 2796
    Helixi282 – 2843
    Helixi287 – 2893
    Beta strandi291 – 2933
    Helixi299 – 3057

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1XGGmodel-A67-295[»]
    1XGHmodel-A67-295[»]
    3HX3X-ray1.69A2-317[»]
    3HY5X-ray3.04A2-317[»]
    4CIZX-ray3.40A1-317[»]
    4CJ6X-ray1.90A1-317[»]
    ProteinModelPortaliP12271.
    SMRiP12271. Positions 23-306.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP12271.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini136 – 297162CRAL-TRIOPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 CRAL-TRIO domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG317741.
    HOGENOMiHOG000059544.
    HOVERGENiHBG004720.
    InParanoidiP12271.
    OMAiLFGPRAQ.
    OrthoDBiEOG7H4DTZ.
    PhylomeDBiP12271.

    Family and domain databases

    Gene3Di3.40.525.10. 1 hit.
    InterProiIPR001071. CRAL-bd_toc_tran.
    IPR001251. CRAL-TRIO_dom.
    IPR011074. CRAL/TRIO_N_dom.
    [Graphical view]
    PfamiPF00650. CRAL_TRIO. 1 hit.
    PF03765. CRAL_TRIO_N. 1 hit.
    [Graphical view]
    PRINTSiPR00180. CRETINALDHBP.
    SMARTiSM01100. CRAL_TRIO_N. 1 hit.
    SM00516. SEC14. 1 hit.
    [Graphical view]
    SUPFAMiSSF46938. SSF46938. 1 hit.
    SSF52087. SSF52087. 1 hit.
    PROSITEiPS50191. CRAL_TRIO. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P12271-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSEGVGTFRM VPEEEQELRA QLEQLTTKDH GPVFGPCSQL PRHTLQKAKD    50
    ELNEREETRE EAVRELQEMV QAQAASGEEL AVAVAERVQE KDSGFFLRFI 100
    RARKFNVGRA YELLRGYVNF RLQYPELFDS LSPEAVRCTI EAGYPGVLSS 150
    RDKYGRVVML FNIENWQSQE ITFDEILQAY CFILEKLLEN EETQINGFCI 200
    IENFKGFTMQ QAASLRTSDL RKMVDMLQDS FPARFKAIHF IHQPWYFTTT 250
    YNVVKPFLKS KLLERVFVHG DDLSGFYQEI DENILPSDFG GTLPKYDGKA 300
    VAEQLFGPQA QAENTAF 317
    Length:317
    Mass (Da):36,474
    Last modified:January 23, 2007 - v2
    Checksum:i80A3B0AE65FDA6EB
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti151 – 1511R → Q in ARRP; loss of ability to bind 11-cis-retinaldehyde. 1 Publication
    Corresponds to variant rs28933989 [ dbSNP | Ensembl ].
    VAR_005140
    Natural varianti226 – 2261M → K in FA. 1 Publication
    VAR_037317
    Natural varianti234 – 2341R → W in BRD. 1 Publication
    Corresponds to variant rs28933990 [ dbSNP | Ensembl ].
    VAR_015172

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J04213 mRNA. Translation: AAA60251.1.
    L34219 Genomic DNA. Translation: AAA65123.1.
    AK312457 mRNA. Translation: BAG35364.1.
    CH471101 Genomic DNA. Translation: EAX02038.1.
    BC004199 mRNA. Translation: AAH04199.1.
    CCDSiCCDS32324.1.
    PIRiB31955.
    RefSeqiNP_000317.1. NM_000326.4.
    UniGeneiHs.1933.

    Genome annotation databases

    EnsembliENST00000268125; ENSP00000268125; ENSG00000140522.
    GeneIDi6017.
    KEGGihsa:6017.
    UCSCiuc002bnl.3. human.

    Polymorphism databases

    DMDMi117391.

    Cross-referencesi

    Web resourcesi

    Mutations of the RLBP1 gene

    Retina International's Scientific Newsletter

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J04213 mRNA. Translation: AAA60251.1 .
    L34219 Genomic DNA. Translation: AAA65123.1 .
    AK312457 mRNA. Translation: BAG35364.1 .
    CH471101 Genomic DNA. Translation: EAX02038.1 .
    BC004199 mRNA. Translation: AAH04199.1 .
    CCDSi CCDS32324.1.
    PIRi B31955.
    RefSeqi NP_000317.1. NM_000326.4.
    UniGenei Hs.1933.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1XGG model - A 67-295 [» ]
    1XGH model - A 67-295 [» ]
    3HX3 X-ray 1.69 A 2-317 [» ]
    3HY5 X-ray 3.04 A 2-317 [» ]
    4CIZ X-ray 3.40 A 1-317 [» ]
    4CJ6 X-ray 1.90 A 1-317 [» ]
    ProteinModelPortali P12271.
    SMRi P12271. Positions 23-306.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111949. 2 interactions.
    STRINGi 9606.ENSP00000268125.

    Chemistry

    DrugBanki DB00162. Vitamin A.

    PTM databases

    PhosphoSitei P12271.

    Polymorphism databases

    DMDMi 117391.

    Proteomic databases

    PaxDbi P12271.
    PRIDEi P12271.

    Protocols and materials databases

    DNASUi 6017.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000268125 ; ENSP00000268125 ; ENSG00000140522 .
    GeneIDi 6017.
    KEGGi hsa:6017.
    UCSCi uc002bnl.3. human.

    Organism-specific databases

    CTDi 6017.
    GeneCardsi GC15M089753.
    GeneReviewsi RLBP1.
    HGNCi HGNC:10024. RLBP1.
    MIMi 136880. phenotype.
    180090. gene.
    268000. phenotype.
    607475. phenotype.
    607476. phenotype.
    neXtProti NX_P12271.
    Orphaneti 85128. Bothnia retinal dystrophy.
    227796. Fundus albipunctatus.
    791. Retinitis pigmentosa.
    52427. Retinitis punctata albescens.
    PharmGKBi PA34397.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG317741.
    HOGENOMi HOG000059544.
    HOVERGENi HBG004720.
    InParanoidi P12271.
    OMAi LFGPRAQ.
    OrthoDBi EOG7H4DTZ.
    PhylomeDBi P12271.

    Enzyme and pathway databases

    BioCyci MetaCyc:ENSG00000140522-MONOMER.
    Reactomei REACT_160083. The retinoid cycle in cones (daylight vision).
    REACT_160130. Retinoid cycle disease events.
    REACT_160156. The canonical retinoid cycle in rods (twilight vision).

    Miscellaneous databases

    EvolutionaryTracei P12271.
    GeneWikii Retinaldehyde-binding_protein_1.
    GenomeRNAii 6017.
    NextBioi 23475.
    PROi P12271.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P12271.
    Bgeei P12271.
    CleanExi HS_RLBP1.
    Genevestigatori P12271.

    Family and domain databases

    Gene3Di 3.40.525.10. 1 hit.
    InterProi IPR001071. CRAL-bd_toc_tran.
    IPR001251. CRAL-TRIO_dom.
    IPR011074. CRAL/TRIO_N_dom.
    [Graphical view ]
    Pfami PF00650. CRAL_TRIO. 1 hit.
    PF03765. CRAL_TRIO_N. 1 hit.
    [Graphical view ]
    PRINTSi PR00180. CRETINALDHBP.
    SMARTi SM01100. CRAL_TRIO_N. 1 hit.
    SM00516. SEC14. 1 hit.
    [Graphical view ]
    SUPFAMi SSF46938. SSF46938. 1 hit.
    SSF52087. SSF52087. 1 hit.
    PROSITEi PS50191. CRAL_TRIO. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning of the cDNAs encoding the cellular retinaldehyde-binding protein from bovine and human retina and comparison of the protein structures."
      Crabb J.W., Goldflam S., Harris S.E., Saari J.C.
      J. Biol. Chem. 263:18688-18692(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Molecular cloning and structural analysis of the human gene encoding cellular retinaldehyde-binding protein."
      Intres R., Goldflam S., Cook J.R., Crabb J.W.
      J. Biol. Chem. 269:25411-25418(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Caudate nucleus.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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: Uterus.
    6. "Structural and functional characterization of recombinant human cellular retinaldehyde-binding protein."
      Crabb J.W., Carlson A., Hen Y., Goldflam S., Intres R., West K.A., Hulmes J.D., Kapron J.T., Luck L.A., Horwitz J., Bok D.
      Protein Sci. 7:746-757(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    7. "Newfoundland rod-cone dystrophy, an early-onset retinal dystrophy, is caused by splice-junction mutations in RLBP1."
      Eichers E.R., Green J.S., Stockton D.W., Jackman C.S., Whelan J., McNamara J.A., Johnson G.J., Lupski J.R., Katsanis N.
      Am. J. Hum. Genet. 70:955-964(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN NFRCD.
    8. "Bothnia dystrophy is caused by domino-like rearrangements in cellular retinaldehyde-binding protein mutant R234W."
      He X., Lobsiger J., Stocker A.
      Proc. Natl. Acad. Sci. U.S.A. 106:18545-18550(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.69 ANGSTROMS) OF 2-317 OF WILD-TYPE AND MUTANT TRP-234 IN COMPLEX WITH 11-CIS-RETINAL, FUNCTION, TISSUE SPECIFICITY, RETINAL-BINDING SITES.
    9. "Mutation of the gene encoding cellular retinaldehyde-binding protein in autosomal recessive retinitis pigmentosa."
      Maw M.A., Kennedy B., Knight A., Bridges R., Roth K.E., Mani E.J., Mukkadan J.K., Nancarrow D., Crabb J.W., Denton M.J.
      Nat. Genet. 17:198-200(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT ARRP GLN-151.
    10. "Bothnia dystrophy caused by mutations in the cellular retinaldehyde-binding protein gene (RLBP1) on chromosome 15q26."
      Burstedt M.S., Sandgren O., Holmgren G., Forsman-Semb K.
      Invest. Ophthalmol. Vis. Sci. 40:995-1000(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT BRD TRP-234.
    11. "Recessive mutations in the RLBP1 gene encoding cellular retinaldehyde-binding protein in a form of retinitis punctata albescens."
      Morimura H., Berson E.L., Dryja T.P.
      Invest. Ophthalmol. Vis. Sci. 40:1000-1004(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT FA LYS-226.

    Entry informationi

    Entry nameiRLBP1_HUMAN
    AccessioniPrimary (citable) accession number: P12271
    Secondary accession number(s): B2R667
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1989
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 142 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

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 15
      Human chromosome 15: 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