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)

Q96KR1

- ZFR_HUMAN

UniProt

Q96KR1 - ZFR_HUMAN

Protein

Zinc finger RNA-binding protein

Gene

ZFR

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 102 (01 Oct 2014)
      Sequence version 2 (04 Dec 2007)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Involved in postimplantation and gastrulation stages of development. Involved in the nucleocytoplasmic shuttling of STAU2. Binds to DNA and RNA By similarity.By similarity

    GO - Molecular functioni

    1. DNA binding Source: UniProtKB-KW
    2. poly(A) RNA binding Source: UniProtKB
    3. protein binding Source: IntAct
    4. zinc ion binding Source: InterPro

    GO - Biological processi

    1. multicellular organismal development Source: UniProtKB-KW

    Keywords - Molecular functioni

    Developmental protein

    Keywords - Ligandi

    DNA-binding, RNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Zinc finger RNA-binding protein
    Short name:
    hZFR
    Alternative name(s):
    M-phase phosphoprotein homolog
    Gene namesi
    Name:ZFR
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:17277. ZFR.

    Subcellular locationi

    Nucleus By similarity. Cytoplasm By similarity. Cytoplasmic granule By similarity. Chromosome By similarity
    Note: Associated with chromosome foci in meiotic cells. Localizes in somatodendritic compartment of primary hippocampal neurons. Colocalizes with STAU2 in several cytosolic RNA granules By similarity.By similarity

    GO - Cellular componenti

    1. chromosome Source: UniProtKB-SubCell
    2. cytoplasm Source: UniProtKB-SubCell
    3. nucleus Source: HPA

    Keywords - Cellular componenti

    Chromosome, Cytoplasm, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA38219.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 10741074Zinc finger RNA-binding proteinPRO_0000312719Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei509 – 5091N6-acetyllysine1 Publication
    Modified residuei516 – 5161N6-acetyllysineBy similarity
    Modified residuei1054 – 10541Phosphoserine2 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ96KR1.
    PaxDbiQ96KR1.
    PRIDEiQ96KR1.

    PTM databases

    PhosphoSiteiQ96KR1.

    Expressioni

    Tissue specificityi

    Expressed in lung, liver, lymphocytes, heart, pancreas, placenta, brain and kidney.1 Publication

    Gene expression databases

    ArrayExpressiQ96KR1.
    BgeeiQ96KR1.
    CleanExiHS_ZFR.
    GenevestigatoriQ96KR1.

    Organism-specific databases

    HPAiHPA016666.

    Interactioni

    Subunit structurei

    Found in a cytoplasmic RNP complex with STAU2. Interacts with STAU2. Does not interact with STAU1 By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    SMAD2Q157962EBI-2513582,EBI-1040141

    Protein-protein interaction databases

    BioGridi119667. 41 interactions.
    DIPiDIP-47293N.
    IntActiQ96KR1. 15 interactions.
    MINTiMINT-4655113.

    Structurei

    3D structure databases

    ProteinModelPortaliQ96KR1.
    SMRiQ96KR1. Positions 722-1039.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini703 – 1073371DZFAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi36 – 302267Ala-richAdd
    BLAST

    Sequence similaritiesi

    Contains 1 DZF domain.Curated

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG292385.
    HOVERGENiHBG108765.
    InParanoidiQ96KR1.
    KOiK13203.
    OMAiNNCTVNT.
    OrthoDBiEOG72ZCDC.
    PhylomeDBiQ96KR1.
    TreeFamiTF320194.

    Family and domain databases

    InterProiIPR006561. DZF.
    IPR007087. Znf_C2H2.
    IPR015880. Znf_C2H2-like.
    IPR003604. Znf_U1.
    [Graphical view]
    PfamiPF07528. DZF. 1 hit.
    [Graphical view]
    SMARTiSM00572. DZF. 1 hit.
    SM00355. ZnF_C2H2. 3 hits.
    SM00451. ZnF_U1. 3 hits.
    [Graphical view]
    PROSITEiPS00028. ZINC_FINGER_C2H2_1. 3 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q96KR1-1 [UniParc]FASTAAdd to Basket

    « Hide

    MIPICPVVSF TYVPSRLGED AKMATGNYFG FTHSGAAAAA AAAQYSQQPA     50
    SGVAYSHPTT VASYTVHQAP VAAHTVTAAY APAAATVAVA RPAPVAVAAA 100
    ATAAAYGGYP TAHTATDYGY TQRQQEAPPP PPPATTQNYQ DSYSYVRSTA 150
    PAVAYDSKQY YQQPTATAAA VAAAAQPQPS VAETYYQTAP KAGYSQGATQ 200
    YTQAQQTRQV TAIKPATPSP ATTTFSIYPV SSTVQPVAAA ATVVPSYTQS 250
    ATYSTTAVTY SGTSYSGYEA AVYSAASSYY QQQQQQQKQA AAAAAAAAAT 300
    AAWTGTTFTK KAPFQNKQLK PKQPPKPPQI HYCDVCKISC AGPQTYKEHL 350
    EGQKHKKKEA ALKASQNTSS SNSSTRGTQN QLRCELCDVS CTGADAYAAH 400
    IRGAKHQKVV KLHTKLGKPI PSTEPNVVSQ ATSSTAVSAS KPTASPSSIA 450
    ANNCTVNTSS VATSSMKGLT TTGNSSLNST SNTKVSAVPT NMAAKKTSTP 500
    KINFVGGNKL QSTGNKAEDI KGTECVKSTP VTSAVQIPEV KQDTVSEPVT 550
    PASLAALQSD VQPVGHDYVE EVRNDEGKVI RFHCKLCECS FNDPNAKEMH 600
    LKGRRHRLQY KKKVNPDLQV EVKPSIRARK IQEEKMRKQM QKEEYWRRRE 650
    EEERWRMEMR RYEEDMYWRR MEEEQHHWDD RRRMPDGGYP HGPPGPLGLL 700
    GVRPGMPPQP QGPAPLRRPD SSDDRYVMTK HATIYPTEEE LQAVQKIVSI 750
    TERALKLVSD SLSEHEKNKN KEGDDKKEGG KDRALKGVLR VGVLAKGLLL 800
    RGDRNVNLVL LCSEKPSKTL LSRIAENLPK QLAVISPEKY DIKCAVSEAA 850
    IILNSCVEPK MQVTITLTSP IIREENMREG DVTSGMVKDP PDVLDRQKCL 900
    DALAALRHAK WFQARANGLQ SCVIIIRILR DLCQRVPTWS DFPSWAMELL 950
    VEKAISSASS PQSPGDALRR VFECISSGII LKGSPGLLDP CEKDPFDTLA 1000
    TMTDQQREDI TSSAQFALRL LAFRQIHKVL GMDPLPQMSQ RFNIHNNRKR 1050
    RRDSDGVDGF EAEGKKDKKD YDNF 1074
    Length:1,074
    Mass (Da):117,012
    Last modified:December 4, 2007 - v2
    Checksum:i3E43654E7134E9FC
    GO

    Sequence cautioni

    The sequence AAH30540.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.
    The sequence AAI07418.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.
    The sequence CAC40818.1 differs from that shown. Reason: Frameshift at position 1057.
    The sequence AAD40385.1 differs from that shown. Reason: Erroneous initiation.
    The sequence BAB15147.1 differs from that shown. Reason: Erroneous initiation.
    The sequence CAC40818.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti7 – 71V → I in AAI07418. (PubMed:15489334)Curated
    Sequence conflicti643 – 6431E → L in AAD40385. (PubMed:10931946)Curated
    Sequence conflicti659 – 6591M → I in CAC40818. (PubMed:11574164)Curated
    Sequence conflicti794 – 7941L → F in AAD40385. (PubMed:10931946)Curated
    Sequence conflicti834 – 8341V → F in AAD40385. (PubMed:10931946)Curated
    Sequence conflicti913 – 9131Q → QE in CAC40818. (PubMed:11574164)Curated
    Sequence conflicti1016 – 10161F → K in CAC40818. (PubMed:11574164)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti461 – 4611V → I.1 Publication
    Corresponds to variant rs4867440 [ dbSNP | Ensembl ].
    VAR_037554
    Natural varianti520 – 5201I → T.1 Publication
    Corresponds to variant rs1051489 [ dbSNP | Ensembl ].
    VAR_037555

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ314790 mRNA. Translation: CAC40818.1. Sequence problems.
    AC008949 Genomic DNA. No translation available.
    BC030540 mRNA. Translation: AAH30540.1. Sequence problems.
    BC051893 mRNA. Translation: AAH51893.1.
    BC062986 mRNA. Translation: AAH62986.1.
    BC107417 mRNA. Translation: AAI07418.1. Sequence problems.
    BC137084 mRNA. Translation: AAI37085.1.
    AF100742 mRNA. Translation: AAD40385.1. Different initiation.
    AK025481 mRNA. Translation: BAB15147.1. Different initiation.
    AL137258 mRNA. Translation: CAB70659.1.
    CCDSiCCDS34139.1.
    PIRiT46329.
    RefSeqiNP_057191.2. NM_016107.3.
    UniGeneiHs.435231.

    Genome annotation databases

    EnsembliENST00000265069; ENSP00000265069; ENSG00000056097.
    GeneIDi51663.
    KEGGihsa:51663.
    UCSCiuc003jhr.1. human.

    Polymorphism databases

    DMDMi162416228.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ314790 mRNA. Translation: CAC40818.1 . Sequence problems.
    AC008949 Genomic DNA. No translation available.
    BC030540 mRNA. Translation: AAH30540.1 . Sequence problems.
    BC051893 mRNA. Translation: AAH51893.1 .
    BC062986 mRNA. Translation: AAH62986.1 .
    BC107417 mRNA. Translation: AAI07418.1 . Sequence problems.
    BC137084 mRNA. Translation: AAI37085.1 .
    AF100742 mRNA. Translation: AAD40385.1 . Different initiation.
    AK025481 mRNA. Translation: BAB15147.1 . Different initiation.
    AL137258 mRNA. Translation: CAB70659.1 .
    CCDSi CCDS34139.1.
    PIRi T46329.
    RefSeqi NP_057191.2. NM_016107.3.
    UniGenei Hs.435231.

    3D structure databases

    ProteinModelPortali Q96KR1.
    SMRi Q96KR1. Positions 722-1039.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 119667. 41 interactions.
    DIPi DIP-47293N.
    IntActi Q96KR1. 15 interactions.
    MINTi MINT-4655113.

    PTM databases

    PhosphoSitei Q96KR1.

    Polymorphism databases

    DMDMi 162416228.

    Proteomic databases

    MaxQBi Q96KR1.
    PaxDbi Q96KR1.
    PRIDEi Q96KR1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000265069 ; ENSP00000265069 ; ENSG00000056097 .
    GeneIDi 51663.
    KEGGi hsa:51663.
    UCSCi uc003jhr.1. human.

    Organism-specific databases

    CTDi 51663.
    GeneCardsi GC05M032354.
    H-InvDB HIX0004787.
    HGNCi HGNC:17277. ZFR.
    HPAi HPA016666.
    MIMi 615635. gene.
    neXtProti NX_Q96KR1.
    PharmGKBi PA38219.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG292385.
    HOVERGENi HBG108765.
    InParanoidi Q96KR1.
    KOi K13203.
    OMAi NNCTVNT.
    OrthoDBi EOG72ZCDC.
    PhylomeDBi Q96KR1.
    TreeFami TF320194.

    Miscellaneous databases

    ChiTaRSi ZFR. human.
    GenomeRNAii 51663.
    NextBioi 55646.
    PROi Q96KR1.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q96KR1.
    Bgeei Q96KR1.
    CleanExi HS_ZFR.
    Genevestigatori Q96KR1.

    Family and domain databases

    InterProi IPR006561. DZF.
    IPR007087. Znf_C2H2.
    IPR015880. Znf_C2H2-like.
    IPR003604. Znf_U1.
    [Graphical view ]
    Pfami PF07528. DZF. 1 hit.
    [Graphical view ]
    SMARTi SM00572. DZF. 1 hit.
    SM00355. ZnF_C2H2. 3 hits.
    SM00451. ZnF_U1. 3 hits.
    [Graphical view ]
    PROSITEi PS00028. ZINC_FINGER_C2H2_1. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and expression of the human single copy homologue of the mouse zinc finger protein zfr."
      Kleines M., Gaertner A., Ritter K., Schaade L.
      Gene 275:157-162(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    2. "The DNA sequence and comparative analysis of human chromosome 5."
      Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
      , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
      Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "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], VARIANTS ILE-461 AND THR-520.
      Tissue: Bone marrow, Duodenum, Eye, Lung and Uterus.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 643-1074.
      Tissue: Pituitary.
    5. "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] OF 744-1074.
      Tissue: Hepatoma.
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 970-1074.
      Tissue: Testis.
    7. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1054, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1054, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    11. "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-509, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiZFR_HUMAN
    AccessioniPrimary (citable) accession number: Q96KR1
    Secondary accession number(s): B2RNR5
    , Q05C08, Q3B7X5, Q6P5A3, Q86UA0, Q9H6V4, Q9NTI1, Q9Y687
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 4, 2007
    Last sequence update: December 4, 2007
    Last modified: October 1, 2014
    This is version 102 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 5
      Human chromosome 5: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3