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Q14194

- DPYL1_HUMAN

UniProt

Q14194 - DPYL1_HUMAN

Protein

Dihydropyrimidinase-related protein 1

Gene

CRMP1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 145 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    Necessary for signaling by class 3 semaphorins and subsequent remodeling of the cytoskeleton. Plays a role in axon guidance, invasive growth and cell migration. May participate in cytokinesis.2 Publications

    GO - Molecular functioni

    1. hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides Source: InterPro
    2. protein binding Source: IntAct

    GO - Biological processi

    1. axon guidance Source: Reactome
    2. nervous system development Source: ProtInc
    3. nucleobase-containing compound metabolic process Source: ProtInc
    4. pyrimidine nucleobase catabolic process Source: InterPro

    Enzyme and pathway databases

    ReactomeiREACT_19199. CRMPs in Sema3A signaling.

    Protein family/group databases

    MEROPSiM38.974.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dihydropyrimidinase-related protein 1
    Short name:
    DRP-1
    Alternative name(s):
    Collapsin response mediator protein 1
    Short name:
    CRMP-1
    Unc-33-like phosphoprotein 3
    Short name:
    ULIP-3
    Gene namesi
    Name:CRMP1
    Synonyms:DPYSL1, ULIP3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 4

    Organism-specific databases

    HGNCiHGNC:2365. CRMP1.

    Subcellular locationi

    Cytoplasm 1 Publication. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome 1 Publication. Cytoplasmcytoskeletonspindle 1 Publication
    Note: Associated with centrosomes and the mitotic spindle during metaphase.

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. cytosol Source: Reactome
    3. dendrite Source: Ensembl
    4. microtubule organizing center Source: UniProtKB-SubCell
    5. neuronal cell body Source: Ensembl
    6. spindle Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi101 – 1022TT → AA: 2.5-fold increase in cells with a defect of cytokinesis. 1 Publication

    Organism-specific databases

    PharmGKBiPA26885.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 572572Dihydropyrimidinase-related protein 1PRO_0000165909Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei101 – 1011Phosphothreonine; by AURKA1 Publication
    Modified residuei102 – 1021Phosphothreonine; by AURKA1 Publication
    Modified residuei316 – 3161Nitrated tyrosineBy similarity
    Modified residuei504 – 5041PhosphotyrosineBy similarity
    Modified residuei509 – 5091PhosphothreonineBy similarity

    Keywords - PTMi

    Nitration, Phosphoprotein

    Proteomic databases

    MaxQBiQ14194.
    PaxDbiQ14194.
    PRIDEiQ14194.

    PTM databases

    PhosphoSiteiQ14194.

    Expressioni

    Tissue specificityi

    Brain.

    Gene expression databases

    ArrayExpressiQ14194.
    BgeeiQ14194.
    CleanExiHS_CRMP1.
    GenevestigatoriQ14194.

    Organism-specific databases

    HPAiHPA035640.

    Interactioni

    Subunit structurei

    Homotetramer, and heterotetramer with DPYSL2, DPYSL3, DPYSL4 or DPYSL5. Interacts with PLXNA1 By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    AXIN1O151692EBI-473101,EBI-710484
    HTTP428582EBI-473101,EBI-466029
    VIMP086703EBI-473101,EBI-353844

    Protein-protein interaction databases

    BioGridi107790. 83 interactions.
    IntActiQ14194. 71 interactions.
    MINTiMINT-1423114.
    STRINGi9606.ENSP00000321606.

    Structurei

    Secondary structure

    1
    572
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi16 – 2510
    Beta strandi30 – 389
    Beta strandi41 – 488
    Beta strandi53 – 597
    Beta strandi64 – 674
    Beta strandi69 – 746
    Helixi89 – 9911
    Beta strandi101 – 1088
    Helixi116 – 13015
    Beta strandi132 – 1409
    Helixi148 – 15710
    Beta strandi163 – 1708
    Turni171 – 1744
    Helixi178 – 19013
    Beta strandi194 – 1985
    Helixi202 – 21312
    Turni214 – 2163
    Helixi221 – 2255
    Helixi229 – 24618
    Beta strandi250 – 2556
    Helixi258 – 27013
    Beta strandi274 – 2796
    Helixi280 – 2845
    Helixi288 – 2914
    Helixi295 – 3006
    Helixi313 – 32210
    Helixi338 – 3414
    Helixi342 – 3443
    Helixi348 – 3503
    Turni358 – 3603
    Helixi361 – 3699
    Turni370 – 3734
    Helixi377 – 3848
    Helixi386 – 3916
    Turni395 – 3973
    Beta strandi409 – 41911
    Beta strandi426 – 4305
    Turni433 – 4364
    Beta strandi438 – 44811
    Beta strandi451 – 4555
    Helixi476 – 48914

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4B3ZX-ray3.05A/B/C/D1-572[»]
    ProteinModelPortaliQ14194.
    SMRiQ14194. Positions 15-490.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0044.
    HOGENOMiHOG000219145.
    HOVERGENiHBG000806.
    OMAiEDIHTGT.
    OrthoDBiEOG7SJD48.
    PhylomeDBiQ14194.
    TreeFamiTF314706.

    Family and domain databases

    Gene3Di2.30.40.10. 2 hits.
    InterProiIPR006680. Amidohydro_1.
    IPR011778. Hydantoinase/dihydroPyrase.
    IPR011059. Metal-dep_hydrolase_composite.
    [Graphical view]
    PfamiPF01979. Amidohydro_1. 1 hit.
    [Graphical view]
    SUPFAMiSSF51338. SSF51338. 2 hits.
    TIGRFAMsiTIGR02033. D-hydantoinase. 1 hit.

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q14194-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MSYQGKKSIP HITSDRLLIK GGRIINDDQS LYADVYLEDG LIKQIGENLI    50
    VPGGVKTIEA NGRMVIPGGI DVNTYLQKPS QGMTAADDFF QGTRAALVGG 100
    TTMIIDHVVP EPGSSLLTSF EKWHEAADTK SCCDYSLHVD ITSWYDGVRE 150
    ELEVLVQDKG VNSFQVYMAY KDVYQMSDSQ LYEAFTFLKG LGAVILVHAE 200
    NGDLIAQEQK RILEMGITGP EGHALSRPEE LEAEAVFRAI TIAGRINCPV 250
    YITKVMSKSA ADIIALARKK GPLVFGEPIA ASLGTDGTHY WSKNWAKAAA 300
    FVTSPPLSPD PTTPDYLTSL LACGDLQVTG SGHCPYSTAQ KAVGKDNFTL 350
    IPEGVNGIEE RMTVVWDKAV ATGKMDENQF VAVTSTNAAK IFNLYPRKGR 400
    IAVGSDADVV IWDPDKLKTI TAKSHKSAVE YNIFEGMECH GSPLVVISQG 450
    KIVFEDGNIN VNKGMGRFIP RKAFPEHLYQ RVKIRNKVFG LQGVSRGMYD 500
    GPVYEVPATP KYATPAPSAK SSPSKHQPPP IRNLHQSNFS LSGAQIDDNN 550
    PRRTGHRIVA PPGGRSNITS LG 572
    Length:572
    Mass (Da):62,184
    Last modified:November 1, 1996 - v1
    Checksum:iA5385FCC79328A30
    GO
    Isoform LCRMP-1 (identifier: Q14194-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-13: MSYQGKKSIPHIT → MADRRRAWNT...DLPLGRDNGQ

    Show »
    Length:686
    Mass (Da):74,262
    Checksum:i2C897F656E5F34FA
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti351 – 37020Missing in AAK55500. (PubMed:10048489)CuratedAdd
    BLAST
    Sequence conflicti504 – 5041Y → H in AAA93201. (PubMed:7637782)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti461 – 4611V → I.
    Corresponds to variant rs34611001 [ dbSNP | Ensembl ].
    VAR_037745

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 1313MSYQG…IPHIT → MADRRRAWNTEDDLPVYLAR PGSAAQTPRQKYGGMFAAVE GAYENKTIDFDAYSVGRRGS ARTPRSAGRPDAVGLPGPGG SEDTASDVSEPSGSAVSSPG ERDERPPTLRIRRPAPRDLP LGRDNGQ in isoform LCRMP-1. 1 PublicationVSP_042545Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D78012 mRNA. Translation: BAA11190.1.
    DQ206871 mRNA. Translation: ABB22046.1.
    BT006806 mRNA. Translation: AAP35452.1.
    AC105915 Genomic DNA. Translation: AAY40959.1.
    CH471131 Genomic DNA. Translation: EAW82405.1.
    CH471131 Genomic DNA. Translation: EAW82407.1.
    BC000252 mRNA. Translation: AAH00252.1.
    BC007613 mRNA. Translation: AAH07613.1.
    AH010780 Genomic DNA. Translation: AAK55500.1.
    U17278 mRNA. Translation: AAA93201.1.
    CCDSiCCDS33950.1. [Q14194-2]
    CCDS43207.1. [Q14194-1]
    PIRiJC5316.
    RefSeqiNP_001014809.1. NM_001014809.2. [Q14194-2]
    NP_001275590.1. NM_001288661.1.
    NP_001275591.1. NM_001288662.1.
    NP_001304.1. NM_001313.4. [Q14194-1]
    UniGeneiHs.135270.

    Genome annotation databases

    EnsembliENST00000324989; ENSP00000321606; ENSG00000072832. [Q14194-2]
    ENST00000397890; ENSP00000380987; ENSG00000072832. [Q14194-1]
    GeneIDi1400.
    KEGGihsa:1400.
    UCSCiuc003giq.3. human. [Q14194-1]
    uc003gis.3. human. [Q14194-2]

    Polymorphism databases

    DMDMi3122031.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D78012 mRNA. Translation: BAA11190.1 .
    DQ206871 mRNA. Translation: ABB22046.1 .
    BT006806 mRNA. Translation: AAP35452.1 .
    AC105915 Genomic DNA. Translation: AAY40959.1 .
    CH471131 Genomic DNA. Translation: EAW82405.1 .
    CH471131 Genomic DNA. Translation: EAW82407.1 .
    BC000252 mRNA. Translation: AAH00252.1 .
    BC007613 mRNA. Translation: AAH07613.1 .
    AH010780 Genomic DNA. Translation: AAK55500.1 .
    U17278 mRNA. Translation: AAA93201.1 .
    CCDSi CCDS33950.1. [Q14194-2 ]
    CCDS43207.1. [Q14194-1 ]
    PIRi JC5316.
    RefSeqi NP_001014809.1. NM_001014809.2. [Q14194-2 ]
    NP_001275590.1. NM_001288661.1.
    NP_001275591.1. NM_001288662.1.
    NP_001304.1. NM_001313.4. [Q14194-1 ]
    UniGenei Hs.135270.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4B3Z X-ray 3.05 A/B/C/D 1-572 [» ]
    ProteinModelPortali Q14194.
    SMRi Q14194. Positions 15-490.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107790. 83 interactions.
    IntActi Q14194. 71 interactions.
    MINTi MINT-1423114.
    STRINGi 9606.ENSP00000321606.

    Protein family/group databases

    MEROPSi M38.974.

    PTM databases

    PhosphoSitei Q14194.

    Polymorphism databases

    DMDMi 3122031.

    Proteomic databases

    MaxQBi Q14194.
    PaxDbi Q14194.
    PRIDEi Q14194.

    Protocols and materials databases

    DNASUi 1400.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000324989 ; ENSP00000321606 ; ENSG00000072832 . [Q14194-2 ]
    ENST00000397890 ; ENSP00000380987 ; ENSG00000072832 . [Q14194-1 ]
    GeneIDi 1400.
    KEGGi hsa:1400.
    UCSCi uc003giq.3. human. [Q14194-1 ]
    uc003gis.3. human. [Q14194-2 ]

    Organism-specific databases

    CTDi 1400.
    GeneCardsi GC04M005815.
    HGNCi HGNC:2365. CRMP1.
    HPAi HPA035640.
    MIMi 602462. gene.
    neXtProti NX_Q14194.
    PharmGKBi PA26885.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0044.
    HOGENOMi HOG000219145.
    HOVERGENi HBG000806.
    OMAi EDIHTGT.
    OrthoDBi EOG7SJD48.
    PhylomeDBi Q14194.
    TreeFami TF314706.

    Enzyme and pathway databases

    Reactomei REACT_19199. CRMPs in Sema3A signaling.

    Miscellaneous databases

    ChiTaRSi CRMP1. human.
    GeneWikii CRMP1.
    GenomeRNAii 1400.
    NextBioi 5731.
    PROi Q14194.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q14194.
    Bgeei Q14194.
    CleanExi HS_CRMP1.
    Genevestigatori Q14194.

    Family and domain databases

    Gene3Di 2.30.40.10. 2 hits.
    InterProi IPR006680. Amidohydro_1.
    IPR011778. Hydantoinase/dihydroPyrase.
    IPR011059. Metal-dep_hydrolase_composite.
    [Graphical view ]
    Pfami PF01979. Amidohydro_1. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51338. SSF51338. 2 hits.
    TIGRFAMsi TIGR02033. D-hydantoinase. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "A novel gene family defined by human dihydropyrimidinase and three related proteins with differential tissue distribution."
      Hamajima N., Matsuda K., Sakata S., Tamaki N., Sasaki M., Nonaka M.
      Gene 180:157-163(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Brain.
    2. "Long form collapsin response mediator protein-1 (LCRMP-1) expression is associated with clinical outcome and lymph node metastasis in non-small cell lung cancer patients."
      Pan S.-H., Chao Y.-C., Chen H.Y., Hung P.F., Lin P.Y., Lin C.W., Chang Y.L., Wu C.T., Lee Y.C., Yang S.-C., Hong T.-M., Yang P.-C.
      Lung Cancer 67:93-100(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LCRMP-1), ALTERNATIVE SPLICING.
      Tissue: Lung adenocarcinoma.
    3. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    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] (ISOFORM 1).
      Tissue: Eye.
    7. "Genomic organization and localization of the human CRMP-1 gene."
      Torres R., Polymeropoulos M.H.
      DNA Res. 5:393-395(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 14-572 (ISOFORM 1).
    8. "Collapsin-induced growth cone collapse mediated by an intracellular protein related to UNC-33."
      Goshima Y., Nakamura F., Strittmatter P., Strittmatter S.M.
      Nature 376:509-514(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 64-572 (ISOFORM 1).
      Tissue: Brain.
    9. Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.
      Submitted (DEC-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 44-56; 190-210; 246-254; 259-268; 346-361; 391-397; 452-463; 472-481; 488-511 AND 533-552, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
    10. "Brain CRMP forms heterotetramers similar to liver dihydropyrimidinase."
      Wang L.H., Strittmatter S.M.
      J. Neurochem. 69:2261-2269(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT, INTERACTION WITH DPYSL2 AND DPYSL4.
    11. "Collapsin response mediator protein-1 and the invasion and metastasis of cancer cells."
      Shih J.-Y., Yang S.-C., Hong T.-M., Yuan A., Chen J.J.W., Yu C.-J., Chang Y.-L., Lee Y.-C., Peck K., Wu C.-W., Yang P.-C.
      J. Natl. Cancer Inst. 93:1392-1400(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    12. "From midbody protein-protein interaction network construction to novel regulators in cytokinesis."
      Chen T.C., Lee S.A., Hong T.M., Shih J.Y., Lai J.M., Chiou H.Y., Yang S.C., Chan C.H., Kao C.Y., Yang P.C., Huang C.Y.
      J. Proteome Res. 8:4943-4953(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PHOSPHORYLATION AT THR-101 AND THR-102, MUTAGENESIS OF 101-THR-THR-102.

    Entry informationi

    Entry nameiDPYL1_HUMAN
    AccessioniPrimary (citable) accession number: Q14194
    Secondary accession number(s): A0EJG6
    , Q13024, Q4W5F1, Q96TC8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 145 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

    Caution

    Lacks most of the conserved residues that are essential for binding the metal cofactor and hence for dihydropyrimidinase activity. Its enzyme activity is therefore unsure.Curated

    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