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Protein

Rab3 GTPase-activating protein catalytic subunit

Gene

RAB3GAP1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Probable catalytic subunit of a GTPase activating protein that has specificity for Rab3 subfamily (RAB3A, RAB3B, RAB3C and RAB3D). Rab3 proteins are involved in regulated exocytosis of neurotransmitters and hormones. Specifically converts active Rab3-GTP to the inactive form Rab3-GDP. Required for normal eye and brain development. May participate in neurodevelopmental processes such as proliferation, migration and differentiation before synapse formation, and non-synaptic vesicular release of neurotransmitters.2 Publications

Kineticsi

  1. KM=75 µM for GTP-loaded RAB3A1 Publication

    GO - Molecular functioni

    • GTPase activator activity Source: UniProtKB
    • Rab GTPase binding Source: UniProtKB

    GO - Biological processi

    • brain development Source: BHF-UCL
    • camera-type eye development Source: BHF-UCL
    • establishment of protein localization to endoplasmic reticulum membrane Source: UniProtKB
    • face morphogenesis Source: BHF-UCL
    • hypothalamus development Source: BHF-UCL
    • lipid particle organization Source: MGI
    • positive regulation of endoplasmic reticulum tubular network organization Source: UniProtKB
    • positive regulation of glutamate neurotransmitter secretion in response to membrane depolarization Source: ParkinsonsUK-UCL
    • positive regulation of GTPase activity Source: UniProtKB
    • regulation of calcium ion-dependent exocytosis of neurotransmitter Source: ParkinsonsUK-UCL
    • regulation of excitatory postsynaptic membrane potential Source: ParkinsonsUK-UCL
    • regulation of GTPase activity Source: UniProtKB
    • regulation of short-term neuronal synaptic plasticity Source: ParkinsonsUK-UCL
    Complete GO annotation...

    Keywords - Molecular functioni

    GTPase activation

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Rab3 GTPase-activating protein catalytic subunit
    Alternative name(s):
    RAB3 GTPase-activating protein 130 kDa subunit
    Rab3-GAP p130
    Short name:
    Rab3-GAP
    Gene namesi
    Name:RAB3GAP1
    Synonyms:KIAA0066, RAB3GAP
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640 Componenti: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:17063. RAB3GAP1.

    Subcellular locationi

    GO - Cellular componenti

    • cytoplasm Source: HPA
    • endoplasmic reticulum tubular network Source: UniProtKB
    • extracellular exosome Source: UniProtKB
    • protein complex Source: UniProtKB
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Involvement in diseasei

    Warburg micro syndrome 1 (WARBM1)1 Publication

    The disease is caused by mutations affecting the gene represented in this entry.

    Disease descriptionA rare syndrome characterized by microcephaly, microphthalmia, microcornia, congenital cataracts, optic atrophy, cortical dysplasia, in particular corpus callosum hypoplasia, severe mental retardation, spastic diplegia, and hypogonadism.

    See also OMIM:600118

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi619 – 6191R → A: No effect. 1 Publication
    Mutagenesisi700 – 7001R → A: No effect. 1 Publication
    Mutagenesisi728 – 7281R → A: Loss of function. 1 Publication
    Mutagenesisi753 – 7531R → A: No effect. 1 Publication

    Organism-specific databases

    MIMi600118. phenotype.
    Orphaneti1387. Cataract - intellectual disability - hypogonadism.
    2510. Micro syndrome.
    PharmGKBiPA134969639.

    Polymorphism and mutation databases

    BioMutaiRAB3GAP1.
    DMDMi62511099.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 981980Rab3 GTPase-activating protein catalytic subunitPRO_0000191655Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei590 – 5901Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ15042.
    PaxDbiQ15042.
    PRIDEiQ15042.

    PTM databases

    PhosphoSiteiQ15042.

    Expressioni

    Tissue specificityi

    Ubiquitous.1 Publication

    Gene expression databases

    BgeeiQ15042.
    CleanExiHS_RAB3GAP1.
    ExpressionAtlasiQ15042. baseline and differential.
    GenevisibleiQ15042. HS.

    Organism-specific databases

    HPAiHPA034494.
    HPA034495.

    Interactioni

    Subunit structurei

    The Rab3 GTPase-activating complex is a heterodimer composed of RAB3GAP and RAB3-GAP150. The Rab3 GTPase-activating complex interacts with DMXL2 (By similarity).By similarity

    Protein-protein interaction databases

    BioGridi116590. 24 interactions.
    IntActiQ15042. 2 interactions.
    STRINGi9606.ENSP00000411418.

    Structurei

    3D structure databases

    ProteinModelPortaliQ15042.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the Rab3-GAP catalytic subunit family.Curated

    Phylogenomic databases

    eggNOGiNOG307494.
    GeneTreeiENSGT00390000006705.
    HOGENOMiHOG000253924.
    HOVERGENiHBG079116.
    InParanoidiQ15042.
    KOiK18270.
    OMAiPIQAPHW.
    OrthoDBiEOG783MTK.
    PhylomeDBiQ15042.
    TreeFamiTF314500.

    Family and domain databases

    InterProiIPR026147. Rab3-GAP_cat_su.
    [Graphical view]
    PANTHERiPTHR21422. PTHR21422. 1 hit.
    PfamiPF13890. Rab3-GTPase_cat. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

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

    This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

    Isoform 1 (identifier: Q15042-1) [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

            10         20         30         40         50
    MAADSEPESE VFEITDFTTA SEWERFISKV EEVLNDWKLI GNSLGKPLEK
    60 70 80 90 100
    GIFTSGTWEE KSDEISFADF KFSVTHHYLV QESTDKEGKD ELLEDVVPQS
    110 120 130 140 150
    MQDLLGMNND FPPRAHCLVR WYGLREFVVI APAAHSDAVL SESKCNLLLS
    160 170 180 190 200
    SVSIALGNTG CQVPLFVQIH HKWRRMYVGE CQGPGVRTDF EMVHLRKVPN
    210 220 230 240 250
    QYTHLSGLLD IFKSKIGCPL TPLPPVSIAI RFTYVLQDWQ QYFWPQQPPD
    260 270 280 290 300
    IDALVGGEVG GLEFGKLPFG ACEDPISELH LATTWPHLTE GIIVDNDVYS
    310 320 330 340 350
    DLDPIQAPHW SVRVRKAENP QCLLGDFVTE FFKICRRKES TDEILGRSAF
    360 370 380 390 400
    EEEGKETADI THALSKLTEP ASVPIHKLSV SNMVHTAKKK IRKHRGVEES
    410 420 430 440 450
    PLNNDVLNTI LLFLFPDAVS EKPLDGTTST DNNNPPSESE DYNLYNQFKS
    460 470 480 490 500
    APSDSLTYKL ALCLCMINFY HGGLKGVAHL WQEFVLEMRF RWENNFLIPG
    510 520 530 540 550
    LASGPPDLRC CLLHQKLQML NCCIERKKAR DEGKKTSASD VTNIYPGDAG
    560 570 580 590 600
    KAGDQLVPDN LKETDKEKGE VGKSWDSWSD SEEEFFECLS DTEELKGNGQ
    610 620 630 640 650
    ESGKKGGPKE MANLRPEGRL YQHGKLTLLH NGEPLYIPVT QEPAPMTEDL
    660 670 680 690 700
    LEEQSEVLAK LGTSAEGAHL RARMQSACLL SDMESFKAAN PGCSLEDFVR
    710 720 730 740 750
    WYSPRDYIEE EVIDEKGNVV LKGELSARMK IPSNMWVEAW ETAKPIPARR
    760 770 780 790 800
    QRRLFDDTRE AEKVLHYLAI QKPADLARHL LPCVIHAAVL KVKEEESLEN
    810 820 830 840 850
    ISSVKKIIKQ IISHSSKVLH FPNPEDKKLE EIIHQITNVE ALIARARSLK
    860 870 880 890 900
    AKFGTEKCEQ EEEKEDLERF VSCLLEQPEV LVTGAGRGHA GRIIHKLFVN
    910 920 930 940 950
    AQRAAAMTPP EEELKRMGSP EERRQNSVSD FPPPAGREFI LRTTVPRPAP
    960 970 980
    YSKALPQRMY SVLTKEDFRL AGAFSSDTSF F
    Length:981
    Mass (Da):110,524
    Last modified:January 23, 2007 - v3
    Checksum:i0673611C5C49641C
    GO
    Isoform 2 (identifier: Q15042-3) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         903-903: R → RLTESSDE

    Note: No experimental confirmation available.
    Show »
    Length:988
    Mass (Da):111,285
    Checksum:i53B04747CCD4B2D8
    GO
    Isoform 3 (identifier: Q15042-4) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-50: MAADSEPESEVFEITDFTTASEWERFISKVEEVLNDWKLIGNSLGKPLEK → MFSLIS
         972-981: GAFSSDTSFF → VKIIDGDV

    Note: No experimental confirmation available.
    Show »
    Length:935
    Mass (Da):105,296
    Checksum:i15466F1985DFFB72
    GO

    Sequence cautioni

    The sequence BC071602 differs from that shown. Reason: Frameshift at position 211. Curated
    The sequence CAH56411.1 differs from that shown.Probable cloning artifact.Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti598 – 5981N → S.1 Publication
    Corresponds to variant rs10445686 [ dbSNP | Ensembl ].
    VAR_051716

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 5050MAADS…KPLEK → MFSLIS in isoform 3. 1 PublicationVSP_054475Add
    BLAST
    Alternative sequencei903 – 9031R → RLTESSDE in isoform 2. 1 PublicationVSP_054068
    Alternative sequencei972 – 98110GAFSSDTSFF → VKIIDGDV in isoform 3. 1 PublicationVSP_054476

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    D31886 mRNA. Translation: BAA06684.1.
    AC017031 Genomic DNA. No translation available.
    AC020602 Genomic DNA. No translation available.
    BC022977 mRNA. Translation: AAH22977.1.
    BC071602 mRNA. No translation available.
    BC146809 mRNA. Translation: AAI46810.1.
    AL096752 mRNA. Translation: CAH56411.1. Sequence problems.
    CCDSiCCDS33294.1. [Q15042-1]
    CCDS54402.1. [Q15042-3]
    RefSeqiNP_001165906.1. NM_001172435.1. [Q15042-3]
    NP_036365.1. NM_012233.2. [Q15042-1]
    UniGeneiHs.306327.

    Genome annotation databases

    EnsembliENST00000264158; ENSP00000264158; ENSG00000115839. [Q15042-1]
    ENST00000442034; ENSP00000411418; ENSG00000115839. [Q15042-3]
    ENST00000539493; ENSP00000444306; ENSG00000115839. [Q15042-4]
    GeneIDi22930.
    KEGGihsa:22930.
    UCSCiuc002tuj.3. human. [Q15042-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    D31886 mRNA. Translation: BAA06684.1.
    AC017031 Genomic DNA. No translation available.
    AC020602 Genomic DNA. No translation available.
    BC022977 mRNA. Translation: AAH22977.1.
    BC071602 mRNA. No translation available.
    BC146809 mRNA. Translation: AAI46810.1.
    AL096752 mRNA. Translation: CAH56411.1. Sequence problems.
    CCDSiCCDS33294.1. [Q15042-1]
    CCDS54402.1. [Q15042-3]
    RefSeqiNP_001165906.1. NM_001172435.1. [Q15042-3]
    NP_036365.1. NM_012233.2. [Q15042-1]
    UniGeneiHs.306327.

    3D structure databases

    ProteinModelPortaliQ15042.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi116590. 24 interactions.
    IntActiQ15042. 2 interactions.
    STRINGi9606.ENSP00000411418.

    PTM databases

    PhosphoSiteiQ15042.

    Polymorphism and mutation databases

    BioMutaiRAB3GAP1.
    DMDMi62511099.

    Proteomic databases

    MaxQBiQ15042.
    PaxDbiQ15042.
    PRIDEiQ15042.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000264158; ENSP00000264158; ENSG00000115839. [Q15042-1]
    ENST00000442034; ENSP00000411418; ENSG00000115839. [Q15042-3]
    ENST00000539493; ENSP00000444306; ENSG00000115839. [Q15042-4]
    GeneIDi22930.
    KEGGihsa:22930.
    UCSCiuc002tuj.3. human. [Q15042-1]

    Organism-specific databases

    CTDi22930.
    GeneCardsiGC02P135809.
    HGNCiHGNC:17063. RAB3GAP1.
    HPAiHPA034494.
    HPA034495.
    MIMi600118. phenotype.
    602536. gene.
    neXtProtiNX_Q15042.
    Orphaneti1387. Cataract - intellectual disability - hypogonadism.
    2510. Micro syndrome.
    PharmGKBiPA134969639.
    HUGEiSearch...
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiNOG307494.
    GeneTreeiENSGT00390000006705.
    HOGENOMiHOG000253924.
    HOVERGENiHBG079116.
    InParanoidiQ15042.
    KOiK18270.
    OMAiPIQAPHW.
    OrthoDBiEOG783MTK.
    PhylomeDBiQ15042.
    TreeFamiTF314500.

    Miscellaneous databases

    ChiTaRSiRAB3GAP1. human.
    GeneWikiiRAB3GAP1.
    GenomeRNAii22930.
    NextBioi35462401.
    PROiQ15042.
    SOURCEiSearch...

    Gene expression databases

    BgeeiQ15042.
    CleanExiHS_RAB3GAP1.
    ExpressionAtlasiQ15042. baseline and differential.
    GenevisibleiQ15042. HS.

    Family and domain databases

    InterProiIPR026147. Rab3-GAP_cat_su.
    [Graphical view]
    PANTHERiPTHR21422. PTHR21422. 1 hit.
    PfamiPF13890. Rab3-GTPase_cat. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Prediction of the coding sequences of unidentified human genes. II. The coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by analysis of cDNA clones from human cell line KG-1."
      Nomura N., Nagase T., Miyajima N., Sazuka T., Tanaka A., Sato S., Seki N., Kawarabayasi Y., Ishikawa K., Tabata S.
      DNA Res. 1:223-229(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Bone marrow.
    2. "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].
    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] (ISOFORMS 2 AND 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 439-981 (ISOFORM 1), VARIANT SER-598.
      Tissue: Placenta.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 764-981.
      Tissue: Testis.
    5. "Isolation and characterization of a GTPase activating protein specific for the Rab3 subfamily of small G proteins."
      Fukui K., Sasaki T., Imazumi K., Matsuura Y., Nakanishi H., Takai Y.
      J. Biol. Chem. 272:4655-4658(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY.
    6. "Localization of the Rab3 small G protein regulators in nerve terminals and their involvement in Ca2+-dependent exocytosis."
      Oishi H., Sasaki T., Nagano F., Ikeda W., Ohya T., Wada M., Ide N., Nakanishi H., Takai Y.
      J. Biol. Chem. 273:34580-34585(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    7. "Biochemical characterization of Rab3-GTPase-activating protein reveals a mechanism similar to that of Ras-GAP."
      Clabecq A., Henry J.-P., Darchen F.
      J. Biol. Chem. 275:31786-31791(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ARG-619; ARG-700; ARG-728 AND ARG-753.
    8. Cited for: INVOLVEMENT IN WARBM1.
    9. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    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].
    14. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
      Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
      J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-590, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.

    Entry informationi

    Entry nameiRB3GP_HUMAN
    AccessioniPrimary (citable) accession number: Q15042
    Secondary accession number(s): A6H8Z3
    , C9J837, Q659F5, Q8TBB4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 12, 2005
    Last sequence update: January 23, 2007
    Last modified: June 24, 2015
    This is version 109 of the entry and version 3 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 2
      Human chromosome 2: 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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.