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O75044

- SRGP2_HUMAN

UniProt

O75044 - SRGP2_HUMAN

Protein

SLIT-ROBO Rho GTPase-activating protein 2

Gene

SRGAP2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 126 (01 Oct 2014)
      Sequence version 2 (07 Jun 2004)
      Previous versions | rss
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    Functioni

    RAC1 GTPase activating protein (GAP) that binds and deforms membranes, and regulates actin dynamics to regulate cell migration and differentiation. Plays an important role in different aspects of neuronal morphogenesis and migration mainly during development of the cerebral cortex. This includes the biogenesis of neurites, where it is required for both axons and dendrites outgrowth, and the maturation of the dendritic spines. Also stimulates the branching of the leading process and negatively regulates neuron radial migration in the cerebral cortex. Its interaction and inhibition by SRGAP2C reduces the rate of spine maturation, alters dendritic spine morphology and density and indirectly increases neuronal migration. It may have implications for cognition, learning and memory. In non-neuronal cells, it may also play a role in cell migration by regulating the formation of lamellipodia and filopodia.3 Publications

    GO - Molecular functioni

    1. protein binding Source: UniProtKB
    2. protein homodimerization activity Source: UniProtKB
    3. Rac GTPase activator activity Source: UniProtKB
    4. Rac GTPase binding Source: UniProtKB

    GO - Biological processi

    1. actin filament severing Source: UniProtKB
    2. axon guidance Source: Reactome
    3. dendritic spine development Source: UniProtKB
    4. extension of a leading process involved in cell motility in cerebral cortex radial glia guided migration Source: UniProtKB
    5. filopodium assembly Source: UniProtKB
    6. lamellipodium assembly involved in ameboidal cell migration Source: UniProtKB
    7. negative regulation of neuron migration Source: UniProtKB
    8. neuron projection morphogenesis Source: UniProtKB
    9. positive regulation of Rac GTPase activity Source: UniProtKB
    10. regulation of small GTPase mediated signal transduction Source: Reactome
    11. small GTPase mediated signal transduction Source: Reactome
    12. substrate adhesion-dependent cell spreading Source: UniProtKB

    Keywords - Molecular functioni

    GTPase activation

    Keywords - Biological processi

    Neurogenesis

    Enzyme and pathway databases

    ReactomeiREACT_11051. Rho GTPase cycle.
    REACT_19342. Inactivation of Cdc42 and Rac.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    SLIT-ROBO Rho GTPase-activating protein 2
    Short name:
    srGAP2
    Alternative name(s):
    Formin-binding protein 2
    Rho GTPase-activating protein 34
    Gene namesi
    Name:SRGAP2
    Synonyms:ARHGAP34, FNBP2, KIAA0456, SRGAP2A
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:19751. SRGAP2.

    Subcellular locationi

    Cell membrane. Cell projectiondendritic spine. Cell junctionsynapsepostsynaptic cell membranepostsynaptic density By similarity. Cell junctionsynapsepostsynaptic cell membrane By similarity. Cell projectionlamellipodium. Cytoplasmic vesiclephagosome By similarity. Nucleus By similarity. Cytoplasm By similarity
    Note: Recruited to actin-rich phagosomes during phagocytosis. Translocates from nucleus to cytoplasm during development.By similarity

    GO - Cellular componenti

    1. cell junction Source: UniProtKB-KW
    2. cytosol Source: UniProtKB
    3. dendritic spine head Source: UniProtKB
    4. lamellipodium Source: UniProtKB
    5. nucleus Source: UniProtKB-SubCell
    6. phagocytic vesicle Source: UniProtKB
    7. plasma membrane Source: UniProtKB
    8. postsynaptic density Source: UniProtKB
    9. postsynaptic membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cell junction, Cell membrane, Cell projection, Cytoplasm, Cytoplasmic vesicle, Membrane, Nucleus, Postsynaptic cell membrane, Synapse

    Pathology & Biotechi

    Involvement in diseasei

    A chromosomal aberration disrupting SRGAP2 has been found in a patient with early infantile epileptic encephalopathy. Balanced translocation t(1;9)(q32;q13).

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi927 – 9271R → A: Loss of the ability to stimulate cell migration, to localize at the plasma membrane protrusions and to dimerize. 1 Publication

    Organism-specific databases

    PharmGKBiPA164742513.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 10711071SLIT-ROBO Rho GTPase-activating protein 2PRO_0000056767Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei927 – 9271Omega-N-methylated arginine; by PRMT51 Publication
    Modified residuei930 – 9301Phosphoserine1 Publication

    Post-translational modificationi

    Methylation at Arg-927 is required for the stimulation of cell migration, dimerization and localization at the plasma membrane protrusions.1 Publication

    Keywords - PTMi

    Methylation, Phosphoprotein

    Proteomic databases

    MaxQBiO75044.
    PaxDbiO75044.
    PRIDEiO75044.

    PTM databases

    PhosphoSiteiO75044.

    Expressioni

    Gene expression databases

    BgeeiO75044.
    CleanExiHS_SRGAP2.
    GenevestigatoriO75044.

    Organism-specific databases

    HPAiHPA028191.
    HPA028196.

    Interactioni

    Subunit structurei

    Homodimer Probable. Forms a heterooligomer with SRGAP1 and SRGAP3 through its F-BAR domain. Interacts (via SH3 domain) with GPHN By similarity. Interacts with SRGAP2C; formation of the heterodimer alters SRGAP2 function. Interacts (via SH3 domain) with FMNL1 (activated by RAC1); regulates the actin filament severing activity of FMNL1 and actin dynamics. Interacts (via SH3 domain) with FMNL3. Interacts with RAC1; specifically stimulates RAC1 GTPase activity. Probably interacts with ROBO1 and ROBO2. Interacts with FASLG. Interacts with PRMT5.By similarity5 PublicationsCurated

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    FASLGP480232EBI-1051034,EBI-495538
    FMNL1O954663EBI-1051034,EBI-720020
    HTTP428583EBI-1051034,EBI-466029
    PRMT5O147444EBI-1051034,EBI-351098

    Protein-protein interaction databases

    BioGridi116956. 17 interactions.
    IntActiO75044. 16 interactions.
    MINTiMINT-1682591.
    STRINGi9606.ENSP00000408089.

    Structurei

    Secondary structure

    1
    1071
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi731 – 7377
    Beta strandi742 – 7465
    Beta strandi754 – 7629
    Beta strandi765 – 7706
    Beta strandi773 – 7775
    Beta strandi779 – 7846

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2DL8NMR-A729-787[»]
    ProteinModelPortaliO75044.
    SMRiO75044. Positions 505-679, 723-787.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO75044.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini22 – 8766FCHPROSITE-ProRule annotationAdd
    BLAST
    Domaini489 – 679191Rho-GAPPROSITE-ProRule annotationAdd
    BLAST
    Domaini728 – 78760SH3PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 501501F-BAR domainAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili362 – 40140Sequence AnalysisAdd
    BLAST
    Coiled coili940 – 96728Sequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi843 – 90967Ser-richAdd
    BLAST

    Domaini

    The F-BAR domain mediates oligomerization, binds membranes, and induces plasma membrane protrusions.1 Publication

    Sequence similaritiesi

    Contains 1 FCH domain.PROSITE-ProRule annotation
    Contains 1 Rho-GAP domain.PROSITE-ProRule annotation
    Contains 1 SH3 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil, SH3 domain

    Phylogenomic databases

    eggNOGiNOG264793.
    HOGENOMiHOG000039980.
    HOVERGENiHBG051637.
    InParanoidiO75044.
    KOiK07526.
    PhylomeDBiO75044.

    Family and domain databases

    Gene3Di1.10.555.10. 1 hit.
    InterProiIPR001060. FCH_dom.
    IPR008936. Rho_GTPase_activation_prot.
    IPR000198. RhoGAP_dom.
    IPR001452. SH3_domain.
    [Graphical view]
    PfamiPF00611. FCH. 1 hit.
    PF00620. RhoGAP. 1 hit.
    PF00018. SH3_1. 1 hit.
    [Graphical view]
    SMARTiSM00055. FCH. 1 hit.
    SM00324. RhoGAP. 1 hit.
    SM00326. SH3. 1 hit.
    [Graphical view]
    SUPFAMiSSF48350. SSF48350. 1 hit.
    SSF50044. SSF50044. 1 hit.
    PROSITEiPS50133. FCH. 1 hit.
    PS50238. RHOGAP. 1 hit.
    PS50002. SH3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    O75044-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTSPAKFKKD KEIIAEYDTQ VKEIRAQLTE QMKCLDQQCE LRVQLLQDLQ     50
    DFFRKKAEIE MDYSRNLEKL AERFLAKTRS TKDQQFKKDQ NVLSPVNCWN 100
    LLLNQVKRES RDHTTLSDIY LNNIIPRFVQ VSEDSGRLFK KSKEVGQQLQ 150
    DDLMKVLNEL YSVMKTYHMY NADSISAQSK LKEAEKQEEK QIGKSVKQED 200
    RQTPRSPDST ANVRIEEKHV RRSSVKKIEK MKEKRQAKYT ENKLKAIKAR 250
    NEYLLALEAT NASVFKYYIH DLSDLIDQCC DLGYHASLNR ALRTFLSAEL 300
    NLEQSKHEGL DAIENAVENL DATSDKQRLM EMYNNVFCPP MKFEFQPHMG 350
    DMASQLCAQQ PVQSELVQRC QQLQSRLSTL KIENEEVKKT MEATLQTIQD 400
    IVTVEDFDVS DCFQYSNSME SVKSTVSETF MSKPSIAKRR ANQQETEQFY 450
    FTKMKEYLEG RNLITKLQAK HDLLQKTLGE SQRTDCSLAR RSSTVRKQDS 500
    SQAIPLVVES CIRFISRHGL QHEGIFRVSG SQVEVNDIKN AFERGEDPLA 550
    GDQNDHDMDS IAGVLKLYFR GLEHPLFPKD IFHDLMACVT MDNLQERALH 600
    IRKVLLVLPK TTLIIMRYLF AFLNHLSQFS EENMMDPYNL AICFGPSLMS 650
    VPEGHDQVSC QAHVNELIKT IIIQHENIFP SPRELEGPVY SRGGSMEDYC 700
    DSPHGETTPV EDSTQDVTAE HHTSDDECEP IEAIAKFDYV GRTARELSFK 750
    KGASLLLYQR ASDDWWEGRH NGIDGLIPHQ YIVVQDTEDG VVERSSPKSE 800
    IEVISEPPEE KVTARAGASC PSGGHVADIY LANINKQRKR PESGSIRKTF 850
    RSDSHGLSSS LTDSSSPGVG ASCRPSSQPI MSQSLPKEGP DKCSISGHGS 900
    LNSISRHSSL KNRLDSPQIR KTATAGRSKS FNNHRPMDPE VIAQDIEATM 950
    NSALNELREL ERQSSVKHTP DVVLDTLEPL KTSPVVAPTS EPSSPLHTQL 1000
    LKDPEPAFQR SASTAGDIAC AFRPVKSVKM AAPVKPPATR PKPTVFPKTN 1050
    ATSPGVNSST SPQSTDKSCT V 1071
    Length:1,071
    Mass (Da):120,881
    Last modified:June 7, 2004 - v2
    Checksum:iD8BC1939D6776312
    GO

    Sequence cautioni

    The sequence BAA32301.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti874 – 8741R → G.
    Corresponds to variant rs17018890 [ dbSNP | Ensembl ].
    VAR_055834

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB007925 mRNA. Translation: BAA32301.1. Different initiation.
    PIRiC59437.
    RefSeqiNP_001164108.1. NM_001170637.2.
    NP_056141.2. NM_015326.3.
    UniGeneiHs.497575.
    Hs.729527.
    Hs.744555.

    Genome annotation databases

    GeneIDi23380.
    KEGGihsa:23380.

    Keywords - Coding sequence diversityi

    Chromosomal rearrangement, Polymorphism

    Cross-referencesi

    Web resourcesi

    Protein Spotlight

    Branching out - Issue 143 of October 2012

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB007925 mRNA. Translation: BAA32301.1 . Different initiation.
    PIRi C59437.
    RefSeqi NP_001164108.1. NM_001170637.2.
    NP_056141.2. NM_015326.3.
    UniGenei Hs.497575.
    Hs.729527.
    Hs.744555.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2DL8 NMR - A 729-787 [» ]
    ProteinModelPortali O75044.
    SMRi O75044. Positions 505-679, 723-787.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116956. 17 interactions.
    IntActi O75044. 16 interactions.
    MINTi MINT-1682591.
    STRINGi 9606.ENSP00000408089.

    PTM databases

    PhosphoSitei O75044.

    Proteomic databases

    MaxQBi O75044.
    PaxDbi O75044.
    PRIDEi O75044.

    Protocols and materials databases

    DNASUi 23380.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 23380.
    KEGGi hsa:23380.

    Organism-specific databases

    CTDi 23380.
    GeneCardsi GC01P206516.
    H-InvDB HIX0001527.
    HIX0029679.
    HIX0116247.
    HGNCi HGNC:19751. SRGAP2.
    HPAi HPA028191.
    HPA028196.
    MIMi 606524. gene.
    neXtProti NX_O75044.
    PharmGKBi PA164742513.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG264793.
    HOGENOMi HOG000039980.
    HOVERGENi HBG051637.
    InParanoidi O75044.
    KOi K07526.
    PhylomeDBi O75044.

    Enzyme and pathway databases

    Reactomei REACT_11051. Rho GTPase cycle.
    REACT_19342. Inactivation of Cdc42 and Rac.

    Miscellaneous databases

    ChiTaRSi SRGAP2. human.
    EvolutionaryTracei O75044.
    GeneWikii SRGAP2.
    GenomeRNAii 23380.
    NextBioi 45477.
    PROi O75044.
    SOURCEi Search...

    Gene expression databases

    Bgeei O75044.
    CleanExi HS_SRGAP2.
    Genevestigatori O75044.

    Family and domain databases

    Gene3Di 1.10.555.10. 1 hit.
    InterProi IPR001060. FCH_dom.
    IPR008936. Rho_GTPase_activation_prot.
    IPR000198. RhoGAP_dom.
    IPR001452. SH3_domain.
    [Graphical view ]
    Pfami PF00611. FCH. 1 hit.
    PF00620. RhoGAP. 1 hit.
    PF00018. SH3_1. 1 hit.
    [Graphical view ]
    SMARTi SM00055. FCH. 1 hit.
    SM00324. RhoGAP. 1 hit.
    SM00326. SH3. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48350. SSF48350. 1 hit.
    SSF50044. SSF50044. 1 hit.
    PROSITEi PS50133. FCH. 1 hit.
    PS50238. RHOGAP. 1 hit.
    PS50002. SH3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Characterization of cDNA clones in size-fractionated cDNA libraries from human brain."
      Seki N., Ohira M., Nagase T., Ishikawa K., Miyajima N., Nakajima D., Nomura N., Ohara O.
      DNA Res. 4:345-349(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain.
    2. "Signal transduction in neuronal migration: roles of GTPase activating proteins and the small GTPase Cdc42 in the Slit-Robo pathway."
      Wong K., Ren X.R., Huang Y.Z., Xie Y., Liu G., Saito H., Tang H., Wen L., Brady-Kalnay S.M., Mei L., Wu J.Y., Xiong W.C., Rao Y.
      Cell 107:209-221(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ROBO1.
    3. "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.
    4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    5. "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].
    6. "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.
    7. "srGAP2 arginine methylation regulates cell migration and cell spreading through promoting dimerization."
      Guo S., Bao S.
      J. Biol. Chem. 285:35133-35141(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN CELL MIGRATION, SUBCELLULAR LOCATION, INTERACTION WITH PRMT5, METHYLATION AT ARG-927 BY PRMT5, MUTAGENESIS OF ARG-927.
    8. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-930, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "Early infantile epileptic encephalopathy associated with the disrupted gene encoding Slit-Robo Rho GTPase activating protein 2 (SRGAP2)."
      Saitsu H., Osaka H., Sugiyama S., Kurosawa K., Mizuguchi T., Nishiyama K., Nishimura A., Tsurusaki Y., Doi H., Miyake N., Harada N., Kato M., Matsumoto N.
      Am. J. Med. Genet. A 158A:199-205(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHROMOSOMAL REARRANGEMENT.
    12. Cited for: FUNCTION IN ACTIN FILAMENT SEVERING, RAC1 GAP ACTIVITY, INTERACTION WITH FMNL1; FMNL3 AND ROBO2, SUBCELLULAR LOCATION.
    13. "Inhibition of SRGAP2 function by its human-specific paralogs induces neoteny during spine maturation."
      Charrier C., Joshi K., Coutinho-Budd J., Kim J.E., Lambert N., de Marchena J., Jin W.L., Vanderhaeghen P., Ghosh A., Sassa T., Polleux F.
      Cell 149:923-935(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SRGAP2C.
    14. "The F-BAR domains from srGAP1, srGAP2, and srGAP3 differentially regulate membrane deformation."
      Coutinho-Budd J., Ghukasyan V., Zylka M.J., Polleux F.
      J. Cell Sci. 125:3390-3401(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: HETEROOLIGOMERIZATION, DOMAIN F-BAR.
    15. "Solution structure of the SH3 domain of human SLIT-ROBO Rho GTPase-activating protein 2."
      RIKEN structural genomics initiative (RSGI)
      Submitted (OCT-2006) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 729-787.

    Entry informationi

    Entry nameiSRGP2_HUMAN
    AccessioniPrimary (citable) accession number: O75044
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 7, 2004
    Last sequence update: June 7, 2004
    Last modified: October 1, 2014
    This is version 126 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

    Miscellaneous

    There are 3 duplications of SRGAP2 in the human genome as a result of segmental gene duplications. SRGAP2C is the only one to be fixed at a diploid state in the human genome. Moreover, SRGAP2C is functional, interacts with and inhibits SRGAP2 and is human-specific. The appearance of SRGAP2C in the human genome is estimated to 2,4 million years ago, which corresponds to the beginning of neocortex expansion in human evolution and it may have played an important role in this process through its interaction with SRGAP2 function.

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: 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. Protein Spotlight
      Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3