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Q9NSI8

- SAMN1_HUMAN

UniProt

Q9NSI8 - SAMN1_HUMAN

Protein

SAM domain-containing protein SAMSN-1

Gene

SAMSN1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 123 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      Previous versions | rss
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    Functioni

    Negative regulator of B-cell activation. Down-regulates cell proliferation (in vitro). Promotes RAC1-dependent membrane ruffle formation and reorganization of the actin cytoskeleton. Regulates cell spreading and cell polarization. Stimulates HDAC1 activity. Regulates LYN activity by modulating its tyrosine phosphorylation By similarity.By similarity

    GO - Molecular functioni

    1. phosphotyrosine binding Source: MGI
    2. poly(A) RNA binding Source: UniProtKB

    GO - Biological processi

    1. negative regulation of adaptive immune response Source: UniProtKB
    2. negative regulation of B cell activation Source: UniProtKB
    3. negative regulation of peptidyl-tyrosine phosphorylation Source: UniProtKB

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    SAM domain-containing protein SAMSN-1
    Alternative name(s):
    Hematopoietic adaptor containing SH3 and SAM domains 1
    Nash1
    SAM domain, SH3 domain and nuclear localization signals protein 1
    SH3-SAM adaptor protein
    Gene namesi
    Name:SAMSN1
    Synonyms:HACS1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 21

    Organism-specific databases

    HGNCiHGNC:10528. SAMSN1.

    Subcellular locationi

    Nucleus 1 Publication. Cytoplasm By similarity. Cell projectionruffle By similarity
    Note: Shuttles between cytoplasm and nucleus. Colocalizes with the actin cytoskeleton and actin-rich membrane ruffles By similarity.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. nucleus Source: UniProtKB
    3. ruffle Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell projection, Cytoplasm, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA34939.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 373373SAM domain-containing protein SAMSN-1PRO_0000097574Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei90 – 901PhosphoserineBy similarity
    Modified residuei160 – 1601PhosphotyrosineBy similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9NSI8.
    PaxDbiQ9NSI8.
    PRIDEiQ9NSI8.

    PTM databases

    PhosphoSiteiQ9NSI8.

    Expressioni

    Tissue specificityi

    Detected in peripheral blood B-cells (at protein level). Detected in spleen, liver and peripheral blood.2 Publications

    Inductioni

    Up-regulated in peripheral blood B-cells by IL4, IL13 and by CD40 stimulation.1 Publication

    Gene expression databases

    ArrayExpressiQ9NSI8.
    BgeeiQ9NSI8.
    CleanExiHS_SAMSN1.
    GenevestigatoriQ9NSI8.

    Organism-specific databases

    HPAiHPA010645.
    HPA017055.

    Interactioni

    Subunit structurei

    Interacts with FASLG. Interacts with phosphotyrosine containing proteins. Interacts (via SH3 domain) with CTTN. Interacts (phosphorylated at Ser-23) with YWHAB, YWHAE, YWHAG, YWHAH, YWHAZ and SFN. Interacts directly with SAP30 and HDAC1. Identified in a complex with SAP30 and HDAC1 By similarity.By similarity

    Protein-protein interaction databases

    BioGridi122054. 13 interactions.
    IntActiQ9NSI8. 2 interactions.
    STRINGi9606.ENSP00000383411.

    Structurei

    Secondary structure

    1
    373
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi167 – 1704
    Beta strandi181 – 1833
    Beta strandi191 – 1966
    Beta strandi203 – 2075
    Beta strandi210 – 2145
    Helixi216 – 2183
    Beta strandi219 – 2213

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2KEANMR-A162-224[»]
    ProteinModelPortaliQ9NSI8.
    SMRiQ9NSI8. Positions 162-224, 234-303.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9NSI8.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini166 – 22257SH3Add
    BLAST
    Domaini241 – 30565SAMPROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi20 – 256Important for interaction with 14-3-3 proteinsBy similarity

    Sequence similaritiesi

    Contains 1 SAM (sterile alpha motif) domain.PROSITE-ProRule annotation
    Contains 1 SH3 domain.Curated

    Keywords - Domaini

    SH3 domain

    Phylogenomic databases

    eggNOGiNOG293245.
    HOGENOMiHOG000049202.
    HOVERGENiHBG000461.
    OMAiGPYSGPF.
    OrthoDBiEOG7KQ20X.
    PhylomeDBiQ9NSI8.
    TreeFamiTF350709.

    Family and domain databases

    Gene3Di1.10.150.50. 1 hit.
    InterProiIPR021090. rSAM/SH3_domain-containing.
    IPR001660. SAM.
    IPR013761. SAM/pointed.
    IPR011510. SAM_2.
    IPR011511. SH3_2.
    IPR001452. SH3_domain.
    [Graphical view]
    PfamiPF07647. SAM_2. 1 hit.
    PF07653. SH3_2. 1 hit.
    PF12485. SLY. 1 hit.
    [Graphical view]
    SMARTiSM00454. SAM. 1 hit.
    SM00326. SH3. 1 hit.
    [Graphical view]
    SUPFAMiSSF47769. SSF47769. 1 hit.
    SSF50044. SSF50044. 1 hit.
    PROSITEiPS50105. SAM_DOMAIN. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9NSI8-1) [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

    MLKRKPSNVS EKEKHQKPKR SSSFGNFDRF RNNSLSKPDD STEAHEGDPT    50
    NGSGEQSKTS NNGGGLGKKM RAISWTMKKK VGKKYIKALS EEKDEEDGEN 100
    AHPYRNSDPV IGTHTEKVSL KASDSMDSLY SGQSSSSGIT SCSDGTSNRD 150
    SFRLDDDGPY SGPFCGRARV HTDFTPSPYD TDSLKIKKGD IIDIICKTPM 200
    GMWTGMLNNK VGNFKFIYVD VISEEEAAPK KIKANRRSNS KKSKTLQEFL 250
    ERIHLQEYTS TLLLNGYETL EDLKDIKESH LIELNIENPD DRRRLLSAAE 300
    NFLEEEIIQE QENEPEPLSL SSDISLNKSQ LDDCPRDSGC YISSGNSDNG 350
    KEDLESENLS DMVHKIIITE PSD 373
    Length:373
    Mass (Da):41,708
    Last modified:October 1, 2000 - v1
    Checksum:i964B852ADBA2D777
    GO
    Isoform 2 (identifier: Q9NSI8-2) [UniParc]FASTAAdd to Basket

    Also known as: b

    The sequence of this isoform differs from the canonical sequence as follows:
         19-186: Missing.

    Show »
    Length:205
    Mass (Da):23,466
    Checksum:i362B2FB490B972BE
    GO
    Isoform 3 (identifier: Q9NSI8-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-19: MLKRKPSNVSEKEKHQKPK → MEIRLDTLSA...CSDMDLLHSW

    Show »
    Length:441
    Mass (Da):49,627
    Checksum:iC2757916D880F563
    GO

    Sequence cautioni

    The sequence AAK07746.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti105 – 1051R → G in BAG54155. (PubMed:14702039)Curated
    Isoform 3 (identifier: Q9NSI8-3)
    Sequence conflicti20 – 201N → D in AAK07746. (PubMed:11536050)Curated
    Sequence conflicti64 – 641H → Y in AAK07746. (PubMed:11536050)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti63 – 631G → A.
    Corresponds to variant rs34607574 [ dbSNP | Ensembl ].
    VAR_051331

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 1919MLKRK…HQKPK → MEIRLDTLSASLGRSSTLNN CNLEDKLAWYEGEAYMWHHW KPFPENPLWTCLDFQIAQVG PWDHCSSCIRHTRLKSSCSD MDLLHSW in isoform 3. 1 PublicationVSP_008120Add
    BLAST
    Alternative sequencei19 – 186168Missing in isoform 2. 1 PublicationVSP_008119Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF222927 mRNA. Translation: AAG23355.1.
    AF218085 mRNA. Translation: AAK07746.1. Different initiation.
    AF519621 mRNA. Translation: AAM75349.1.
    AK125144 mRNA. Translation: BAG54155.1.
    AL163206 Genomic DNA. Translation: CAB90391.1.
    AF165138 Genomic DNA. No translation available.
    BC029112 mRNA. Translation: AAH29112.1.
    CCDSiCCDS42906.1. [Q9NSI8-1]
    CCDS58786.1. [Q9NSI8-3]
    RefSeqiNP_001243299.1. NM_001256370.1. [Q9NSI8-3]
    NP_001273452.1. NM_001286523.1.
    NP_071419.3. NM_022136.4. [Q9NSI8-1]
    UniGeneiHs.473341.
    Hs.719474.

    Genome annotation databases

    EnsembliENST00000285670; ENSP00000285670; ENSG00000155307. [Q9NSI8-3]
    ENST00000400564; ENSP00000383409; ENSG00000155307. [Q9NSI8-2]
    ENST00000400566; ENSP00000383411; ENSG00000155307. [Q9NSI8-1]
    GeneIDi64092.
    KEGGihsa:64092.
    UCSCiuc002yju.2. human. [Q9NSI8-1]
    uc010gky.2. human. [Q9NSI8-2]

    Polymorphism databases

    DMDMi12230638.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF222927 mRNA. Translation: AAG23355.1 .
    AF218085 mRNA. Translation: AAK07746.1 . Different initiation.
    AF519621 mRNA. Translation: AAM75349.1 .
    AK125144 mRNA. Translation: BAG54155.1 .
    AL163206 Genomic DNA. Translation: CAB90391.1 .
    AF165138 Genomic DNA. No translation available.
    BC029112 mRNA. Translation: AAH29112.1 .
    CCDSi CCDS42906.1. [Q9NSI8-1 ]
    CCDS58786.1. [Q9NSI8-3 ]
    RefSeqi NP_001243299.1. NM_001256370.1. [Q9NSI8-3 ]
    NP_001273452.1. NM_001286523.1.
    NP_071419.3. NM_022136.4. [Q9NSI8-1 ]
    UniGenei Hs.473341.
    Hs.719474.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2KEA NMR - A 162-224 [» ]
    ProteinModelPortali Q9NSI8.
    SMRi Q9NSI8. Positions 162-224, 234-303.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 122054. 13 interactions.
    IntActi Q9NSI8. 2 interactions.
    STRINGi 9606.ENSP00000383411.

    PTM databases

    PhosphoSitei Q9NSI8.

    Polymorphism databases

    DMDMi 12230638.

    Proteomic databases

    MaxQBi Q9NSI8.
    PaxDbi Q9NSI8.
    PRIDEi Q9NSI8.

    Protocols and materials databases

    DNASUi 64092.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000285670 ; ENSP00000285670 ; ENSG00000155307 . [Q9NSI8-3 ]
    ENST00000400564 ; ENSP00000383409 ; ENSG00000155307 . [Q9NSI8-2 ]
    ENST00000400566 ; ENSP00000383411 ; ENSG00000155307 . [Q9NSI8-1 ]
    GeneIDi 64092.
    KEGGi hsa:64092.
    UCSCi uc002yju.2. human. [Q9NSI8-1 ]
    uc010gky.2. human. [Q9NSI8-2 ]

    Organism-specific databases

    CTDi 64092.
    GeneCardsi GC21M015857.
    H-InvDB HIX0016027.
    HGNCi HGNC:10528. SAMSN1.
    HPAi HPA010645.
    HPA017055.
    MIMi 607978. gene.
    neXtProti NX_Q9NSI8.
    PharmGKBi PA34939.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG293245.
    HOGENOMi HOG000049202.
    HOVERGENi HBG000461.
    OMAi GPYSGPF.
    OrthoDBi EOG7KQ20X.
    PhylomeDBi Q9NSI8.
    TreeFami TF350709.

    Miscellaneous databases

    EvolutionaryTracei Q9NSI8.
    GenomeRNAii 64092.
    NextBioi 65904.
    PROi Q9NSI8.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9NSI8.
    Bgeei Q9NSI8.
    CleanExi HS_SAMSN1.
    Genevestigatori Q9NSI8.

    Family and domain databases

    Gene3Di 1.10.150.50. 1 hit.
    InterProi IPR021090. rSAM/SH3_domain-containing.
    IPR001660. SAM.
    IPR013761. SAM/pointed.
    IPR011510. SAM_2.
    IPR011511. SH3_2.
    IPR001452. SH3_domain.
    [Graphical view ]
    Pfami PF07647. SAM_2. 1 hit.
    PF07653. SH3_2. 1 hit.
    PF12485. SLY. 1 hit.
    [Graphical view ]
    SMARTi SM00454. SAM. 1 hit.
    SM00326. SH3. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47769. SSF47769. 1 hit.
    SSF50044. SSF50044. 1 hit.
    PROSITEi PS50105. SAM_DOMAIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A novel gene, located on human chromosome 21q11."
      Groet J., Blechschmidt K., Yaspo M., Rosenthal A., Nizetic D.
      Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "HACS1 encodes a novel SH3-SAM adaptor protein differentially expressed in normal and malignant hematopoietic cells."
      Claudio J.O., Zhu Y.X., Benn S.J., Shukla A.H., McGlade C.J., Falcioni N., Stewart A.K.
      Oncogene 20:5373-5377(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
    3. "Transcriptional map of the juxtacentromeric region of human chromosome 21."
      Brun M.-E., Ruault M., Roizes G., De Sario A.
      Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
      Tissue: Thymus.
    4. "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].
    5. "The DNA sequence of human chromosome 21."
      Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S., Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M., Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A.
      , Menzel U., Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A., Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J., Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K., Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G., Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J., Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S., Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K., Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.
      Nature 405:311-319(2000) [PubMed] [Europe PMC] [Abstract]
      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: Lymph.
    7. "Identification of Nash1, a novel protein containing a nuclear localization signal, a sterile alpha motif, and an SH3 domain preferentially expressed in mast cells."
      Uchida T., Nakao A., Nakano N., Kuramasu A., Saito H., Okumura K., Ra C., Ogawa H.
      Biochem. Biophys. Res. Commun. 288:137-141(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    8. "The SH3-SAM adaptor HACS1 is up-regulated in B cell activation signaling cascades."
      Zhu Y.X., Benn S., Li Z.H., Wei E., Masih-Khan E., Trieu Y., Bali M., McGlade C.J., Claudio J.O., Stewart A.K.
      J. Exp. Med. 200:737-747(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INDUCTION, TISSUE SPECIFICITY.
    9. "Identification of SH3 domain interaction partners of human FasL (CD178) by phage display screening."
      Voss M., Lettau M., Janssen O.
      BMC Immunol. 10:53-53(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FASLG.
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "NMR solution structure of the HACS1 SH3 domain."
      Donaldson L.
      Submitted (FEB-2010) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 162-224.

    Entry informationi

    Entry nameiSAMN1_HUMAN
    AccessioniPrimary (citable) accession number: Q9NSI8
    Secondary accession number(s): B3KWJ3
    , F8WAA1, Q8NFF7, Q9C041
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 11, 2001
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 123 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. Human chromosome 21
      Human chromosome 21: 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