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Protein

SLIT-ROBO Rho GTPase-activating protein 2

Gene

SRGAP2

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

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. GTPase activator activity Source: UniProtKB
  2. protein homodimerization activity Source: UniProtKB
  3. 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 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
Complete GO annotation...

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 Componenti: Unplaced

Organism-specific databases

HGNCiHGNC:19751. SRGAP2.

Subcellular locationi

  1. Cell membrane
  2. Cell projectiondendritic spine
  3. Cell junctionsynapsepostsynaptic cell membranepostsynaptic density By similarity
  4. Cell junctionsynapsepostsynaptic cell membrane By similarity
  5. Cell projectionlamellipodium
  6. Cytoplasmic vesiclephagosome By similarity
  7. Nucleus By similarity
  8. Cytoplasm By similarity

  9. 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. cytoplasm Source: GO_Central
  3. cytosol Source: UniProtKB
  4. dendritic spine head Source: UniProtKB
  5. lamellipodium Source: UniProtKB
  6. nucleus Source: UniProtKB-SubCell
  7. phagocytic vesicle Source: UniProtKB
  8. plasma membrane Source: UniProtKB
  9. postsynaptic density Source: UniProtKB
  10. postsynaptic membrane Source: UniProtKB
Complete GO annotation...

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.
HPA061384.

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 similarityCurated5 Publications

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. 21 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:
PDBei
RCSB PDBi
PDBji
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 – 325304F-BARPROSITE-ProRule annotationAdd
BLAST
Domaini489 – 679191Rho-GAPPROSITE-ProRule annotationAdd
BLAST
Domaini728 – 78760SH3PROSITE-ProRule annotationAdd
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 F-BAR 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.
IPR030252. srGAP2.
[Graphical view]
PANTHERiPTHR14166:SF6. PTHR14166:SF6. 1 hit.
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.
PROSITEiPS51741. F_BAR. 1 hit.
PS50238. RHOGAP. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O75044-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTSPAKFKKD KEIIAEYDTQ VKEIRAQLTE QMKCLDQQCE LRVQLLQDLQ
60 70 80 90 100
DFFRKKAEIE MDYSRNLEKL AERFLAKTRS TKDQQFKKDQ NVLSPVNCWN
110 120 130 140 150
LLLNQVKRES RDHTTLSDIY LNNIIPRFVQ VSEDSGRLFK KSKEVGQQLQ
160 170 180 190 200
DDLMKVLNEL YSVMKTYHMY NADSISAQSK LKEAEKQEEK QIGKSVKQED
210 220 230 240 250
RQTPRSPDST ANVRIEEKHV RRSSVKKIEK MKEKRQAKYT ENKLKAIKAR
260 270 280 290 300
NEYLLALEAT NASVFKYYIH DLSDLIDQCC DLGYHASLNR ALRTFLSAEL
310 320 330 340 350
NLEQSKHEGL DAIENAVENL DATSDKQRLM EMYNNVFCPP MKFEFQPHMG
360 370 380 390 400
DMASQLCAQQ PVQSELVQRC QQLQSRLSTL KIENEEVKKT MEATLQTIQD
410 420 430 440 450
IVTVEDFDVS DCFQYSNSME SVKSTVSETF MSKPSIAKRR ANQQETEQFY
460 470 480 490 500
FTKMKEYLEG RNLITKLQAK HDLLQKTLGE SQRTDCSLAR RSSTVRKQDS
510 520 530 540 550
SQAIPLVVES CIRFISRHGL QHEGIFRVSG SQVEVNDIKN AFERGEDPLA
560 570 580 590 600
GDQNDHDMDS IAGVLKLYFR GLEHPLFPKD IFHDLMACVT MDNLQERALH
610 620 630 640 650
IRKVLLVLPK TTLIIMRYLF AFLNHLSQFS EENMMDPYNL AICFGPSLMS
660 670 680 690 700
VPEGHDQVSC QAHVNELIKT IIIQHENIFP SPRELEGPVY SRGGSMEDYC
710 720 730 740 750
DSPHGETTPV EDSTQDVTAE HHTSDDECEP IEAIAKFDYV GRTARELSFK
760 770 780 790 800
KGASLLLYQR ASDDWWEGRH NGIDGLIPHQ YIVVQDTEDG VVERSSPKSE
810 820 830 840 850
IEVISEPPEE KVTARAGASC PSGGHVADIY LANINKQRKR PESGSIRKTF
860 870 880 890 900
RSDSHGLSSS LTDSSSPGVG ASCRPSSQPI MSQSLPKEGP DKCSISGHGS
910 920 930 940 950
LNSISRHSSL KNRLDSPQIR KTATAGRSKS FNNHRPMDPE VIAQDIEATM
960 970 980 990 1000
NSALNELREL ERQSSVKHTP DVVLDTLEPL KTSPVVAPTS EPSSPLHTQL
1010 1020 1030 1040 1050
LKDPEPAFQR SASTAGDIAC AFRPVKSVKM AAPVKPPATR PKPTVFPKTN
1060 1070
ATSPGVNSST SPQSTDKSCT V
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.Curated

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:
EMBLi
GenBanki
DDBJi
Links Updated
AB007925 mRNA. Translation: BAA32301.1. Different initiation.
CCDSiCCDS73017.1.
PIRiC59437.
RefSeqiNP_001164108.1. NM_001170637.3.
NP_056141.2. NM_015326.4.
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:
EMBLi
GenBanki
DDBJi
Links Updated
AB007925 mRNA. Translation: BAA32301.1. Different initiation.
CCDSiCCDS73017.1.
PIRiC59437.
RefSeqiNP_001164108.1. NM_001170637.3.
NP_056141.2. NM_015326.4.
UniGeneiHs.497575.
Hs.729527.
Hs.744555.

3D structure databases

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

Protein-protein interaction databases

BioGridi116956. 21 interactions.
IntActiO75044. 16 interactions.
MINTiMINT-1682591.
STRINGi9606.ENSP00000408089.

PTM databases

PhosphoSiteiO75044.

Proteomic databases

MaxQBiO75044.
PaxDbiO75044.
PRIDEiO75044.

Protocols and materials databases

DNASUi23380.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi23380.
KEGGihsa:23380.

Organism-specific databases

CTDi23380.
GeneCardsiGC01P206516.
H-InvDBHIX0001527.
HIX0029679.
HIX0116247.
HGNCiHGNC:19751. SRGAP2.
HPAiHPA028191.
HPA028196.
HPA061384.
MIMi606524. gene.
neXtProtiNX_O75044.
PharmGKBiPA164742513.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

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

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSiSRGAP2. human.
EvolutionaryTraceiO75044.
GeneWikiiSRGAP2.
GenomeRNAii23380.
NextBioi45477.
PROiO75044.
SOURCEiSearch...

Gene expression databases

BgeeiO75044.
CleanExiHS_SRGAP2.
GenevestigatoriO75044.

Family and domain databases

Gene3Di1.10.555.10. 1 hit.
InterProiIPR001060. FCH_dom.
IPR008936. Rho_GTPase_activation_prot.
IPR000198. RhoGAP_dom.
IPR001452. SH3_domain.
IPR030252. srGAP2.
[Graphical view]
PANTHERiPTHR14166:SF6. PTHR14166:SF6. 1 hit.
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.
PROSITEiPS51741. F_BAR. 1 hit.
PS50238. RHOGAP. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: April 29, 2015
This is version 131 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

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.