GRM2B_HUMAN
ID GRM2B_HUMAN Reviewed; 432 AA.
AC Q96HH9; B7Z1F2; B7Z3R1; B7Z6D8; B7Z8T2; D3DSZ3; Q9H753;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=GRAM domain-containing protein 2B;
DE AltName: Full=HCV NS3-transactivated protein 2;
GN Name=GRAMD2B; Synonyms=GRAMD3, NS3TP2;
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 [MRNA] (ISOFORM 1).
RA Liu Y., Cheng J., Mu J., Wang G., Zhang L., Chen J., Li L.;
RT "Cloning and identification of human gene 2 transactivated by hepatitis C
RT virus NS3 protein.";
RL Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3; 4 AND 5).
RC TISSUE=Colon, Placenta, Thalamus, and Trachea;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-252, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-252, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
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. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-252, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-252, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
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 [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP 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).
CC -!- INTERACTION:
CC Q96HH9; B0B1U2: ABO; NbExp=3; IntAct=EBI-2832937, EBI-10175342;
CC Q96HH9; Q9UJ71: CD207; NbExp=6; IntAct=EBI-2832937, EBI-2873235;
CC Q96HH9; Q16543: CDC37; NbExp=3; IntAct=EBI-2832937, EBI-295634;
CC Q96HH9; Q9BZ67: FRMD8; NbExp=6; IntAct=EBI-2832937, EBI-5773072;
CC Q96HH9; Q96F15: GIMAP5; NbExp=3; IntAct=EBI-2832937, EBI-6166686;
CC Q96HH9; Q96HH9: GRAMD2B; NbExp=4; IntAct=EBI-2832937, EBI-2832937;
CC Q96HH9; Q15014: MORF4L2; NbExp=3; IntAct=EBI-2832937, EBI-399257;
CC Q96HH9; Q6XQN6: NAPRT; NbExp=3; IntAct=EBI-2832937, EBI-10254872;
CC Q96HH9; P09466: PAEP; NbExp=8; IntAct=EBI-2832937, EBI-465167;
CC Q96HH9; Q96IW7: SEC22A; NbExp=3; IntAct=EBI-2832937, EBI-8652744;
CC Q96HH9; Q9BTV4: TMEM43; NbExp=6; IntAct=EBI-2832937, EBI-721293;
CC Q96HH9; O95183: VAMP5; NbExp=3; IntAct=EBI-2832937, EBI-10191195;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q96HH9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96HH9-2; Sequence=VSP_042883;
CC Name=3;
CC IsoId=Q96HH9-3; Sequence=VSP_042884;
CC Name=4;
CC IsoId=Q96HH9-4; Sequence=VSP_042885;
CC Name=5;
CC IsoId=Q96HH9-5; Sequence=VSP_044298, VSP_044299;
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DR EMBL; AY116970; AAM77213.1; -; mRNA.
DR EMBL; AK024966; BAB15045.1; -; mRNA.
DR EMBL; AK293307; BAH11488.1; -; mRNA.
DR EMBL; AK296267; BAH12297.1; -; mRNA.
DR EMBL; AK300154; BAH13224.1; -; mRNA.
DR EMBL; AK303857; BAH14068.1; -; mRNA.
DR EMBL; AK316288; BAH14659.1; -; mRNA.
DR EMBL; AC008546; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC093535; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471086; EAW48852.1; -; Genomic_DNA.
DR EMBL; CH471086; EAW48854.1; -; Genomic_DNA.
DR EMBL; CH471086; EAW48855.1; -; Genomic_DNA.
DR EMBL; BC008590; AAH08590.1; -; mRNA.
DR CCDS; CCDS4136.1; -. [Q96HH9-1]
DR CCDS; CCDS54891.1; -. [Q96HH9-3]
DR CCDS; CCDS54892.1; -. [Q96HH9-2]
DR CCDS; CCDS54893.1; -. [Q96HH9-4]
DR CCDS; CCDS54894.1; -. [Q96HH9-5]
DR RefSeq; NP_001139791.1; NM_001146319.1. [Q96HH9-3]
DR RefSeq; NP_001139792.1; NM_001146320.1. [Q96HH9-5]
DR RefSeq; NP_001139793.1; NM_001146321.1. [Q96HH9-2]
DR RefSeq; NP_001139794.1; NM_001146322.1. [Q96HH9-4]
DR RefSeq; NP_076416.2; NM_023927.2. [Q96HH9-1]
DR RefSeq; XP_005272120.1; XM_005272063.3. [Q96HH9-4]
DR RefSeq; XP_016865274.1; XM_017009785.1. [Q96HH9-5]
DR AlphaFoldDB; Q96HH9; -.
DR SMR; Q96HH9; -.
DR BioGRID; 122433; 48.
DR IntAct; Q96HH9; 29.
DR MINT; Q96HH9; -.
DR STRING; 9606.ENSP00000426120; -.
DR iPTMnet; Q96HH9; -.
DR PhosphoSitePlus; Q96HH9; -.
DR BioMuta; GRAMD2B; -.
DR DMDM; 74731934; -.
DR EPD; Q96HH9; -.
DR jPOST; Q96HH9; -.
DR MassIVE; Q96HH9; -.
DR MaxQB; Q96HH9; -.
DR PaxDb; Q96HH9; -.
DR PeptideAtlas; Q96HH9; -.
DR PRIDE; Q96HH9; -.
DR ProteomicsDB; 6327; -.
DR ProteomicsDB; 76749; -. [Q96HH9-1]
DR ProteomicsDB; 76750; -. [Q96HH9-2]
DR ProteomicsDB; 76751; -. [Q96HH9-3]
DR ProteomicsDB; 76752; -. [Q96HH9-4]
DR Antibodypedia; 2140; 216 antibodies from 25 providers.
DR DNASU; 65983; -.
DR Ensembl; ENST00000285689.8; ENSP00000285689.3; ENSG00000155324.10. [Q96HH9-1]
DR Ensembl; ENST00000511134.1; ENSP00000426088.1; ENSG00000155324.10. [Q96HH9-4]
DR Ensembl; ENST00000513040.5; ENSP00000426120.1; ENSG00000155324.10. [Q96HH9-3]
DR Ensembl; ENST00000542322.5; ENSP00000441876.1; ENSG00000155324.10. [Q96HH9-2]
DR Ensembl; ENST00000544396.5; ENSP00000444049.1; ENSG00000155324.10. [Q96HH9-5]
DR GeneID; 65983; -.
DR KEGG; hsa:65983; -.
DR MANE-Select; ENST00000285689.8; ENSP00000285689.3; NM_023927.4; NP_076416.2.
DR UCSC; uc003ktu.4; human. [Q96HH9-1]
DR CTD; 65983; -.
DR DisGeNET; 65983; -.
DR GeneCards; GRAMD2B; -.
DR HGNC; HGNC:24911; GRAMD2B.
DR HPA; ENSG00000155324; Low tissue specificity.
DR neXtProt; NX_Q96HH9; -.
DR OpenTargets; ENSG00000155324; -.
DR PharmGKB; PA142671711; -.
DR VEuPathDB; HostDB:ENSG00000155324; -.
DR eggNOG; KOG1032; Eukaryota.
DR GeneTree; ENSGT00940000156980; -.
DR InParanoid; Q96HH9; -.
DR OMA; DTKXYIF; -.
DR OrthoDB; 944155at2759; -.
DR PhylomeDB; Q96HH9; -.
DR TreeFam; TF332065; -.
DR PathwayCommons; Q96HH9; -.
DR SignaLink; Q96HH9; -.
DR BioGRID-ORCS; 65983; 21 hits in 1072 CRISPR screens.
DR ChiTaRS; GRAMD2B; human.
DR GenomeRNAi; 65983; -.
DR Pharos; Q96HH9; Tdark.
DR PRO; PR:Q96HH9; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q96HH9; protein.
DR Bgee; ENSG00000155324; Expressed in calcaneal tendon and 191 other tissues.
DR ExpressionAtlas; Q96HH9; baseline and differential.
DR Genevisible; Q96HH9; HS.
DR GO; GO:0005881; C:cytoplasmic microtubule; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR004182; GRAM.
DR InterPro; IPR011993; PH-like_dom_sf.
DR Pfam; PF02893; GRAM; 1.
DR SMART; SM00568; GRAM; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Phosphoprotein; Reference proteome.
FT CHAIN 1..432
FT /note="GRAM domain-containing protein 2B"
FT /id="PRO_0000087577"
FT DOMAIN 110..177
FT /note="GRAM"
FT REGION 1..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 74..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 220..239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 262..285
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 81..101
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..237
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 263..285
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 225
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PEM6"
FT MOD_RES 242
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PEM6"
FT MOD_RES 252
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT VAR_SEQ 1..104
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044298"
FT VAR_SEQ 1..68
FT /note="MTELQQDVEDTKPAKVLGKRESKLGSAHSEAENGVEEKKKACRSPTAQSPTP
FT SVEADSPDQKKIISLW -> MWKTQSLRKCSGRGRANLAQPTQRLRMVWRRKRKPAGRQ
FT QPNPLPHLWRRTPQTRRKSLAYAHIFSPNLCFIQDQE (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_042883"
FT VAR_SEQ 1..28
FT /note="MTELQQDVEDTKPAKVLGKRESKLGSAH -> MTRRQQVLQAKRSIQQTFQA
FT QLMPWKSMFHGREVKPVGPDLEL (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_042884"
FT VAR_SEQ 1..28
FT /note="MTELQQDVEDTKPAKVLGKRESKLGSAH -> MSKVKRFPFFFS (in
FT isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_042885"
FT VAR_SEQ 105
FT /note="Q -> M (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044299"
FT CONFLICT 260
FT /note="Q -> R (in Ref. 1; AAM77213 and 2; BAB15045)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 432 AA; 47869 MW; 65F5CE61C13D19C4 CRC64;
MTELQQDVED TKPAKVLGKR ESKLGSAHSE AENGVEEKKK ACRSPTAQSP TPSVEADSPD
QKKIISLWSK SSFDGASLAS DKNDCKTESK NDPKTERKKS SSSSQYKANM HFHKLFLSVP
TEEPLKQSFT CALQKEILYQ GKLFVSENWI CFHSKVFGKD TKISIPAFSV TLIKKTKTAL
LVPNALIIAT VTDRYIFVSL LSRDSTYKLL KSVCGHLENT SVGNSPNPSS AENSFRADRP
SSLPLDFNDE FSDLDGVVQQ RRQDMEGYSS SGSQTPESEN SRDFHATESQ TVLNVSKGEA
KPTRADAHVN RVPEGKAKSL PVQGLSETVG ILHKVKSQKC PMLHHILIFY AIVVCALIIS
TFYMRYRINT LEEQLGLLTS IVDTHNTEQA APSGLRSQVQ FNVEVLCQEL TANIVKLEKI
QNNLQKLLEN GD
