SRG2B_HUMAN
ID SRG2B_HUMAN Reviewed; 458 AA.
AC P0DMP2;
DT 01-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2014, sequence version 1.
DT 03-AUG-2022, entry version 52.
DE RecName: Full=SLIT-ROBO Rho GTPase-activating protein 2B;
DE AltName: Full=SLIT-ROBO Rho GTPase activating protein 2 pseudogene 2;
GN Name=SRGAP2B; Synonyms=SRGAP2P2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [2]
RP IDENTIFICATION, AND CHROMOSOMAL LOCATION.
RX PubMed=22559943; DOI=10.1016/j.cell.2012.03.033;
RA Dennis M.Y., Nuttle X., Sudmant P.H., Antonacci F., Graves T.A.,
RA Nefedov M., Rosenfeld J.A., Sajjadian S., Malig M., Kotkiewicz H.,
RA Curry C.J., Shafer S., Shaffer L.G., de Jong P.J., Wilson R.K.,
RA Eichler E.E.;
RT "Evolution of human-specific neural SRGAP2 genes by incomplete segmental
RT duplication.";
RL Cell 149:912-922(2012).
RN [3]
RP IDENTIFICATION, AND FUNCTION.
RX PubMed=22559944; DOI=10.1016/j.cell.2012.03.034;
RA Charrier C., Joshi K., Coutinho-Budd J., Kim J.E., Lambert N.,
RA de Marchena J., Jin W.L., Vanderhaeghen P., Ghosh A., Sassa T., Polleux F.;
RT "Inhibition of SRGAP2 function by its human-specific paralogs induces
RT neoteny during spine maturation.";
RL Cell 149:923-935(2012).
RN [4]
RP FUNCTION.
RX PubMed=31822692; DOI=10.1038/s41598-019-54887-4;
RA Schmidt E.R.E., Kupferman J.V., Stackmann M., Polleux F.;
RT "The human-specific paralogs SRGAP2B and SRGAP2C differentially modulate
RT SRGAP2A-dependent synaptic development.";
RL Sci. Rep. 9:18692-18692(2019).
CC -!- FUNCTION: May regulate cell migration and differentiation through
CC interaction with and inhibition of SRGAP2 (PubMed:31822692,
CC PubMed:31822692). In contrast to SRGAP2C, it is not able to induce
CC long-lasting changes in synaptic density throughout adulthood
CC (PubMed:31822692). {ECO:0000269|PubMed:31822692,
CC ECO:0000305|PubMed:22559944, ECO:0000305|PubMed:31822692}.
CC -!- SUBUNIT: May interact with SRGAP2; formation of the heterodimer alters
CC SRGAP2 function. {ECO:0000250|UniProtKB:P0DJJ0}.
CC -!- MISCELLANEOUS: This is one of the 3 duplications of the ancestral gene
CC SRGAP2/SRGAP2A which has undergone human-specific segmental gene
CC duplications (PubMed:22559944). The appearance of SRGAP2B in the human
CC genome is estimated to 3,4 million years. Two larger duplications later
CC copied SRGAP2B to chromosome 1p12 (SRGAP2C) and to proximal 1q21.1
CC (SRGAP2D) (PubMed:22559944). SRGAP2B was identified in some individuals
CC but it is not clear if it produces a functional protein
CC (PubMed:22559944). {ECO:0000305|PubMed:22559944}.
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DR EMBL; AC242498; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; FP700111; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_016857574.1; XM_017002085.1.
DR AlphaFoldDB; P0DMP2; -.
DR SMR; P0DMP2; -.
DR BioGRID; 571916; 8.
DR STRING; 9606.ENSP00000477776; -.
DR iPTMnet; P0DMP2; -.
DR PhosphoSitePlus; P0DMP2; -.
DR BioMuta; SRGAP2B; -.
DR EPD; P0DMP2; -.
DR jPOST; P0DMP2; -.
DR MassIVE; P0DMP2; -.
DR PeptideAtlas; P0DMP2; -.
DR PRIDE; P0DMP2; -.
DR Antibodypedia; 77434; 29 antibodies from 6 providers.
DR Ensembl; ENST00000612199.4; ENSP00000477776.1; ENSG00000196369.12.
DR UCSC; uc031urt.2; human.
DR GeneCards; SRGAP2B; -.
DR HGNC; HGNC:35237; SRGAP2B.
DR HPA; ENSG00000196369; Tissue enhanced (brain).
DR MIM; 614703; gene.
DR neXtProt; NX_P0DMP2; -.
DR OpenTargets; ENSG00000196369; -.
DR VEuPathDB; HostDB:ENSG00000196369; -.
DR eggNOG; KOG3565; Eukaryota.
DR GeneTree; ENSGT00950000182824; -.
DR HOGENOM; CLU_005715_1_0_1; -.
DR PathwayCommons; P0DMP2; -.
DR SignaLink; P0DMP2; -.
DR BioGRID-ORCS; 647135; 30 hits in 158 CRISPR screens.
DR ChiTaRS; SRGAP2B; human.
DR GenomeRNAi; 647135; -.
DR Pharos; P0DMP2; Tdark.
DR PRO; PR:P0DMP2; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P0DMP2; protein.
DR Bgee; ENSG00000196369; Expressed in cerebellar vermis and 107 other tissues.
DR ExpressionAtlas; P0DMP2; baseline and differential.
DR Genevisible; P0DMP2; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0030336; P:negative regulation of cell migration; IBA:GO_Central.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR Gene3D; 1.20.1270.60; -; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR031160; F_BAR.
DR InterPro; IPR001060; FCH_dom.
DR InterPro; IPR030252; srGAP2.
DR PANTHER; PTHR14166:SF6; PTHR14166:SF6; 1.
DR Pfam; PF00611; FCH; 1.
DR SMART; SM00055; FCH; 1.
DR SUPFAM; SSF103657; SSF103657; 1.
DR PROSITE; PS51741; F_BAR; 1.
PE 3: Inferred from homology;
KW Coiled coil; Neurogenesis; Reference proteome.
FT CHAIN 1..458
FT /note="SLIT-ROBO Rho GTPase-activating protein 2B"
FT /id="PRO_0000430362"
FT DOMAIN 22..324
FT /note="F-BAR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01077"
FT REGION 181..214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 362..400
FT /evidence="ECO:0000255"
FT COMPBIAS 181..204
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 458 AA; 53406 MW; 5371FA5DD6245B57 CRC64;
MTSPAKFKKD KEIIAEYDTQ VKEIRAQLTE QMKCLDQQCE LRVQLLQDLQ DFFRKKAEIE
MDYSRNLEKL AERFLAKTCS TKDQQFKKDQ NVLSPVNCWN LLLNQVKRES RDHTTLSDIY
LNNIIPRFVQ VSEDSGRLFK KSKEVGQQLQ DDLMKVLNEL YSVMKTYHMY NADSISAQSK
LKEAEKQEEK QIGKSVKQED RQTPRSPDST ANVRIEEKHV RRSSVKKIEK MKEKRQAKYT
ENKLKAIKAR NEYLLALEAT NASVFKYYIH DLSDLIDCCD LGYHASLNRA LRTFLSAELN
LEQSKHEGLD AIENAVENLD ATSDKQRLME MYNNVFCPPM KFEFQPHMGD MASQLCAQQP
VQSELLQRCQ QLQSRLSTLK IENEEVKKTM EATLQTIQDI VTVEDFDVSD CFQYSNSMES
VKSTVSETFM SKPSIAKRRA NQQETEQFYF TVRECYGF
