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P13667

- PDIA4_HUMAN

UniProt

P13667 - PDIA4_HUMAN

Protein

Protein disulfide-isomerase A4

Gene

PDIA4

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 166 (01 Oct 2014)
      Sequence version 2 (01 May 1991)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    Catalyzes the rearrangement of -S-S- bonds in proteins.

    GO - Molecular functioni

    1. poly(A) RNA binding Source: UniProtKB
    2. protein binding Source: IntAct
    3. protein disulfide isomerase activity Source: UniProt

    GO - Biological processi

    1. cell redox homeostasis Source: InterPro
    2. chaperone-mediated protein folding Source: UniProt
    3. protein folding Source: RefGenome
    4. protein secretion Source: ProtInc
    5. response to endoplasmic reticulum stress Source: RefGenome

    Keywords - Molecular functioni

    Isomerase

    Enzyme and pathway databases

    BRENDAi5.3.4.1. 2681.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein disulfide-isomerase A4 (EC:5.3.4.1)
    Alternative name(s):
    Endoplasmic reticulum resident protein 70
    Short name:
    ER protein 70
    Short name:
    ERp70
    Endoplasmic reticulum resident protein 72
    Short name:
    ER protein 72
    Short name:
    ERp-72
    Short name:
    ERp72
    Gene namesi
    Name:PDIA4
    Synonyms:ERP70, ERP72
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:30167. PDIA4.

    Subcellular locationi

    Endoplasmic reticulum lumen. Melanosome
    Note: Identified by mass spectrometry in melanosome fractions from stage I to stage IV.

    GO - Cellular componenti

    1. cell surface Source: MGI
    2. endoplasmic reticulum Source: RefGenome
    3. endoplasmic reticulum lumen Source: ProtInc
    4. melanosome Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Endoplasmic reticulum

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA142671190.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2020Sequence AnalysisAdd
    BLAST
    Chaini21 – 645625Protein disulfide-isomerase A4PRO_0000034229Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi91 ↔ 94Redox-activePROSITE-ProRule annotation
    Disulfide bondi206 ↔ 209Redox-activePROSITE-ProRule annotation
    Modified residuei366 – 3661N6-acetyllysine1 Publication
    Disulfide bondi555 ↔ 558Redox-activePROSITE-ProRule annotation

    Keywords - PTMi

    Acetylation, Disulfide bond

    Proteomic databases

    MaxQBiP13667.
    PaxDbiP13667.
    PeptideAtlasiP13667.
    PRIDEiP13667.

    2D gel databases

    OGPiP13667.
    REPRODUCTION-2DPAGEIPI00009904.

    PTM databases

    PhosphoSiteiP13667.

    Expressioni

    Gene expression databases

    ArrayExpressiP13667.
    BgeeiP13667.
    CleanExiHS_PDIA4.
    GenevestigatoriP13667.

    Organism-specific databases

    HPAiCAB017368.
    HPA006139.
    HPA006140.

    Interactioni

    Subunit structurei

    Part of a large chaperone multiprotein complex comprising DNAJB11, HSP90B1, HSPA5, HYOU, PDIA2, PDIA4, PDIA6, PPIB, SDF2L1, UGT1A1 and very small amounts of ERP29, but not, or at very low levels, CALR nor CANX.

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Q763533EBI-1054653,EBI-6248077From a different organism.
    PPIBP232843EBI-1054653,EBI-8771982

    Protein-protein interaction databases

    BioGridi114966. 53 interactions.
    IntActiP13667. 17 interactions.
    MINTiMINT-4999858.
    STRINGi9606.ENSP00000286091.

    Structurei

    Secondary structure

    1
    645
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi59 – 613
    Beta strandi64 – 663
    Turni69 – 713
    Helixi72 – 765
    Beta strandi80 – 878
    Helixi92 – 10918
    Beta strandi111 – 1133
    Beta strandi117 – 1215
    Turni122 – 1243
    Helixi126 – 1316
    Beta strandi136 – 1449
    Beta strandi147 – 1504
    Helixi157 – 16812
    Beta strandi178 – 1814
    Turni184 – 1863
    Helixi187 – 1937
    Beta strandi195 – 2028
    Helixi208 – 2114
    Helixi213 – 22412
    Beta strandi226 – 2283
    Beta strandi232 – 2365
    Turni237 – 2393
    Helixi241 – 2466
    Beta strandi251 – 2599
    Beta strandi262 – 2654
    Helixi272 – 28211

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3IDVX-ray1.95A53-284[»]
    ProteinModelPortaliP13667.
    SMRiP13667. Positions 54-645.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP13667.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini21 – 169149Thioredoxin 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini158 – 301144Thioredoxin 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini505 – 636132Thioredoxin 3PROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi642 – 6454Prevents secretion from ER

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi39 – 5517Asp/Glu-rich (acidic)Add
    BLAST

    Sequence similaritiesi

    Belongs to the protein disulfide isomerase family.Curated
    Contains 3 thioredoxin domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Redox-active center, Repeat, Signal

    Phylogenomic databases

    eggNOGiCOG0526.
    HOGENOMiHOG000162459.
    HOVERGENiHBG005920.
    InParanoidiP13667.
    KOiK09582.
    OMAiIIGVFKG.
    OrthoDBiEOG7VHSX1.
    PhylomeDBiP13667.
    TreeFamiTF106382.

    Family and domain databases

    Gene3Di3.40.30.10. 4 hits.
    InterProiIPR005788. Disulphide_isomerase.
    IPR005792. Prot_disulphide_isomerase.
    IPR017068. Protein_diS-isomerase_A4.
    IPR012336. Thioredoxin-like_fold.
    IPR017937. Thioredoxin_CS.
    IPR013766. Thioredoxin_domain.
    [Graphical view]
    PfamiPF00085. Thioredoxin. 3 hits.
    [Graphical view]
    PIRSFiPIRSF036862. Disulphide_isom_A4. 1 hit.
    SUPFAMiSSF52833. SSF52833. 5 hits.
    TIGRFAMsiTIGR01130. ER_PDI_fam. 1 hit.
    TIGR01126. pdi_dom. 3 hits.
    PROSITEiPS00014. ER_TARGET. 1 hit.
    PS00194. THIOREDOXIN_1. 3 hits.
    PS51352. THIOREDOXIN_2. 3 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P13667-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRPRKAFLLL LLLGLVQLLA VAGAEGPDED SSNRENAIED EEEEEEEDDD    50
    EEEDDLEVKE ENGVLVLNDA NFDNFVADKD TVLLEFYAPW CGHCKQFAPE 100
    YEKIANILKD KDPPIPVAKI DATSASVLAS RFDVSGYPTI KILKKGQAVD 150
    YEGSRTQEEI VAKVREVSQP DWTPPPEVTL VLTKENFDEV VNDADIILVE 200
    FYAPWCGHCK KLAPEYEKAA KELSKRSPPI PLAKVDATAE TDLAKRFDVS 250
    GYPTLKIFRK GRPYDYNGPR EKYGIVDYMI EQSGPPSKEI LTLKQVQEFL 300
    KDGDDVIIIG VFKGESDPAY QQYQDAANNL REDYKFHHTF STEIAKFLKV 350
    SQGQLVVMQP EKFQSKYEPR SHMMDVQGST QDSAIKDFVL KYALPLVGHR 400
    KVSNDAKRYT RRPLVVVYYS VDFSFDYRAA TQFWRSKVLE VAKDFPEYTF 450
    AIADEEDYAG EVKDLGLSES GEDVNAAILD ESGKKFAMEP EEFDSDTLRE 500
    FVTAFKKGKL KPVIKSQPVP KNNKGPVKVV VGKTFDSIVM DPKKDVLIEF 550
    YAPWCGHCKQ LEPVYNSLAK KYKGQKGLVI AKMDATANDV PSDRYKVEGF 600
    PTIYFAPSGD KKNPVKFEGG DRDLEHLSKF IEEHATKLSR TKEEL 645
    Length:645
    Mass (Da):72,932
    Last modified:May 1, 1991 - v2
    Checksum:i1919C2AE12CD2684
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti102 – 1021E → G in BAF83660. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti173 – 1731T → M.
    Corresponds to variant rs2290971 [ dbSNP | Ensembl ].
    VAR_052580

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J05016 mRNA. Translation: AAA58460.1.
    AK290971 mRNA. Translation: BAF83660.1.
    AC093743 Genomic DNA. Translation: AAQ96863.1.
    CH471146 Genomic DNA. Translation: EAW80065.1.
    CH471146 Genomic DNA. Translation: EAW80066.1.
    BC000425 mRNA. Translation: AAH00425.1.
    BC001928 mRNA. Translation: AAH01928.1.
    BC006344 mRNA. Translation: AAH06344.1.
    BC011754 mRNA. Translation: AAH11754.1.
    CCDSiCCDS5893.1.
    PIRiA23723.
    RefSeqiNP_004902.1. NM_004911.4.
    UniGeneiHs.93659.

    Genome annotation databases

    EnsembliENST00000286091; ENSP00000286091; ENSG00000155660.
    GeneIDi9601.
    KEGGihsa:9601.
    UCSCiuc003wff.2. human.

    Polymorphism databases

    DMDMi119530.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J05016 mRNA. Translation: AAA58460.1 .
    AK290971 mRNA. Translation: BAF83660.1 .
    AC093743 Genomic DNA. Translation: AAQ96863.1 .
    CH471146 Genomic DNA. Translation: EAW80065.1 .
    CH471146 Genomic DNA. Translation: EAW80066.1 .
    BC000425 mRNA. Translation: AAH00425.1 .
    BC001928 mRNA. Translation: AAH01928.1 .
    BC006344 mRNA. Translation: AAH06344.1 .
    BC011754 mRNA. Translation: AAH11754.1 .
    CCDSi CCDS5893.1.
    PIRi A23723.
    RefSeqi NP_004902.1. NM_004911.4.
    UniGenei Hs.93659.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3IDV X-ray 1.95 A 53-284 [» ]
    ProteinModelPortali P13667.
    SMRi P13667. Positions 54-645.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114966. 53 interactions.
    IntActi P13667. 17 interactions.
    MINTi MINT-4999858.
    STRINGi 9606.ENSP00000286091.

    PTM databases

    PhosphoSitei P13667.

    Polymorphism databases

    DMDMi 119530.

    2D gel databases

    OGPi P13667.
    REPRODUCTION-2DPAGE IPI00009904.

    Proteomic databases

    MaxQBi P13667.
    PaxDbi P13667.
    PeptideAtlasi P13667.
    PRIDEi P13667.

    Protocols and materials databases

    DNASUi 9601.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000286091 ; ENSP00000286091 ; ENSG00000155660 .
    GeneIDi 9601.
    KEGGi hsa:9601.
    UCSCi uc003wff.2. human.

    Organism-specific databases

    CTDi 9601.
    GeneCardsi GC07M148700.
    HGNCi HGNC:30167. PDIA4.
    HPAi CAB017368.
    HPA006139.
    HPA006140.
    neXtProti NX_P13667.
    PharmGKBi PA142671190.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0526.
    HOGENOMi HOG000162459.
    HOVERGENi HBG005920.
    InParanoidi P13667.
    KOi K09582.
    OMAi IIGVFKG.
    OrthoDBi EOG7VHSX1.
    PhylomeDBi P13667.
    TreeFami TF106382.

    Enzyme and pathway databases

    BRENDAi 5.3.4.1. 2681.

    Miscellaneous databases

    ChiTaRSi PDIA4. human.
    EvolutionaryTracei P13667.
    GenomeRNAii 9601.
    NextBioi 36019.
    PROi P13667.

    Gene expression databases

    ArrayExpressi P13667.
    Bgeei P13667.
    CleanExi HS_PDIA4.
    Genevestigatori P13667.

    Family and domain databases

    Gene3Di 3.40.30.10. 4 hits.
    InterProi IPR005788. Disulphide_isomerase.
    IPR005792. Prot_disulphide_isomerase.
    IPR017068. Protein_diS-isomerase_A4.
    IPR012336. Thioredoxin-like_fold.
    IPR017937. Thioredoxin_CS.
    IPR013766. Thioredoxin_domain.
    [Graphical view ]
    Pfami PF00085. Thioredoxin. 3 hits.
    [Graphical view ]
    PIRSFi PIRSF036862. Disulphide_isom_A4. 1 hit.
    SUPFAMi SSF52833. SSF52833. 5 hits.
    TIGRFAMsi TIGR01130. ER_PDI_fam. 1 hit.
    TIGR01126. pdi_dom. 3 hits.
    PROSITEi PS00014. ER_TARGET. 1 hit.
    PS00194. THIOREDOXIN_1. 3 hits.
    PS51352. THIOREDOXIN_2. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Human deoxycytidine kinase. Sequence of cDNA clones and analysis of expression in cell lines with and without enzyme activity."
      Huang S.-H., Tomich J.M., Wu H., Jong A., Holcenberg J.S.
      J. Biol. Chem. 264:14762-14768(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
    2. Erratum
      Huang S.-H., Tomich J.M., Wu H., Jong A., Holcenberg J.S.
      J. Biol. Chem. 266:5353-5353(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: SEQUENCE REVISION.
    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].
    4. "The DNA sequence of human chromosome 7."
      Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
      , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
      Nature 424:157-164(2003) [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: Lung and Muscle.
    7. "A subset of chaperones and folding enzymes form multiprotein complexes in endoplasmic reticulum to bind nascent proteins."
      Meunier L., Usherwood Y.-K., Chung K.T., Hendershot L.M.
      Mol. Biol. Cell 13:4456-4469(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: COMPONENT OF A CHAPERONE COMPLEX.
    8. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
      Tissue: Melanoma.
    9. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
      Tissue: Melanoma.
    10. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-366, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiPDIA4_HUMAN
    AccessioniPrimary (citable) accession number: P13667
    Secondary accession number(s): A8K4K6, Q549T6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1990
    Last sequence update: May 1, 1991
    Last modified: October 1, 2014
    This is version 166 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

    Caution

    Was originally thought to be a deoxycytidine kinase.1 Publication

    Keywords - Technical termi

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

    Documents

    1. Human chromosome 7
      Human chromosome 7: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3