ID E9PD09_HUMAN Unreviewed; 410 AA. AC E9PD09; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 03-MAY-2023, entry version 76. DE SubName: Full=GRAM domain containing 2B {ECO:0000313|Ensembl:ENSP00000426143.1}; GN Name=GRAMD2B {ECO:0000313|Ensembl:ENSP00000426143.1}; 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 {ECO:0000313|Ensembl:ENSP00000426143.1, ECO:0000313|Proteomes:UP000005640}; RN [1] {ECO:0000313|Ensembl:ENSP00000426143.1, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15372022; DOI=10.1038/nature02919; RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S., RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.; RT "The DNA sequence and comparative analysis of human chromosome 5."; RL Nature 431:268-274(2004). RN [2] {ECO:0007829|PubMed:17081983} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [3] {ECO:0007829|PubMed:18220336} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=18220336; DOI=10.1021/pr0705441; RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.D., Yates J.R.; RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient RT phosphoproteomic analysis."; RL J. Proteome Res. 7:1346-1351(2008). RN [4] {ECO:0007829|PubMed:18669648} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [5] {ECO:0007829|PubMed:20068231} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [6] {ECO:0007829|PubMed:22814378} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [7] {ECO:0000313|Ensembl:ENSP00000426143.1} RP IDENTIFICATION. RG Ensembl; RL Submitted (JAN-2023) to UniProtKB. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AC008546; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC093535; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR AlphaFoldDB; E9PD09; -. DR SMR; E9PD09; -. DR MaxQB; E9PD09; -. DR PeptideAtlas; E9PD09; -. DR ProteomicsDB; 19559; -. DR Antibodypedia; 2140; 216 antibodies from 25 providers. DR Ensembl; ENST00000515200.5; ENSP00000426143.1; ENSG00000155324.10. DR UCSC; uc063gnd.1; human. DR HGNC; HGNC:24911; GRAMD2B. DR VEuPathDB; HostDB:ENSG00000155324; -. DR GeneTree; ENSGT00940000156980; -. DR ChiTaRS; GRAMD2B; human. DR Proteomes; UP000005640; Chromosome 5. DR Bgee; ENSG00000155324; Expressed in calcaneal tendon and 191 other tissues. DR ExpressionAtlas; E9PD09; baseline and differential. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW. DR CDD; cd13220; PH-GRAM_GRAMDC; 1. DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1. DR InterPro; IPR004182; GRAM. DR InterPro; IPR011993; PH-like_dom_sf. DR PANTHER; PTHR46645:SF2; GRAM DOMAIN-CONTAINING PROTEIN 2B; 1. DR PANTHER; PTHR46645; GRAM DOMAIN-CONTAINING PROTEIN 2B-RELATED; 1. DR Pfam; PF02893; GRAM; 1. DR SMART; SM00568; GRAM; 1. PE 1: Evidence at protein level; KW Membrane {ECO:0000256|SAM:Phobius}; KW Proteomics identification {ECO:0007829|EPD:E9PD09, KW ECO:0007829|MaxQB:E9PD09}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 320..342 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 87..154 FT /note="GRAM" FT /evidence="ECO:0000259|SMART:SM00568" FT REGION 1..59 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 197..216 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 239..263 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..43 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 197..214 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 240..263 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 410 AA; 45505 MW; 1BB1F7C3C1B8B58E CRC64; MTELQQDVED TKPAKVLGKR ESKLGSAHSE AENGVEEKKK ACRSPTAQSP TPSVEADSPD QKKIISLCPY LLSKSMLHSG PRYKANMHFH KLFLSVPTEE PLKQSFTCAL QKEILYQGKL FVSENWICFH SKVFGKDTKI SIPAFSVTLI KKTKTALLVP NALIIATVTD RYIFVSLLSR DSTYKLLKSV CGHLENTSVG NSPNPSSAEN SFRADRPSSL PLDFNDEFSD LDGVVQQRRQ DMEGYSSSGS QTPESENSRV DFHATESQTV LNVSKGEAKP TRADAHVNRV PEGKAKSLPV QGLSETVGIL HKVKSQKCPM LHHILIFYAI VVCALIISTF YMRYRINTLE EQLGLLTSIV DTHNTEQAAP SGLRSQVQFN VEVLCQELTA NIVKLEKIQN NLQKLLENGD //