MAK16_HUMAN
ID MAK16_HUMAN Reviewed; 300 AA.
AC Q9BXY0; B2RB44; Q5U5T1; Q86UC4; Q96SY6;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Protein MAK16 homolog;
DE AltName: Full=NNP78;
DE AltName: Full=Protein RBM13;
GN Name=MAK16; Synonyms=RBM13;
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], AND VARIANT ARG-277.
RA Mao Y., Xie Y., Zhou Z., Zhao W., Zhao S., Wang W., Huang Y., Wang S.,
RA Tang R., Chen X., Wu C.;
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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].
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ARG-277.
RC TISSUE=Brain, Testis, and Uterus;
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=11790298; DOI=10.1016/s0960-9822(01)00650-9;
RA Andersen J.S., Lyon C.E., Fox A.H., Leung A.K.L., Lam Y.W., Steen H.,
RA Mann M., Lamond A.I.;
RT "Directed proteomic analysis of the human nucleolus.";
RL Curr. Biol. 12:1-11(2002).
RN [6]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=12429849; DOI=10.1091/mbc.e02-05-0271;
RA Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C.,
RA Greco A., Hochstrasser D.F., Diaz J.-J.;
RT "Functional proteomic analysis of human nucleolus.";
RL Mol. Biol. Cell 13:4100-4109(2002).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-229 AND SER-232, AND
RP IDENTIFICATION BY 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 [8]
RP IDENTIFICATION BY 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 ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-229 AND SER-232, AND
RP IDENTIFICATION BY 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-197; SER-200; SER-229 AND
RP SER-232, AND 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 [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [13]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-55 AND LYS-151, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
CC -!- INTERACTION:
CC Q9BXY0; Q96NE9-2: FRMD6; NbExp=5; IntAct=EBI-5280229, EBI-13213391;
CC Q9BXY0; Q9HAP6: LIN7B; NbExp=3; IntAct=EBI-5280229, EBI-821335;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:11790298,
CC ECO:0000269|PubMed:12429849}.
CC -!- SIMILARITY: Belongs to the MAK16 family. {ECO:0000305}.
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DR EMBL; AF251062; AAK34952.1; -; mRNA.
DR EMBL; AK027469; BAB55134.1; -; mRNA.
DR EMBL; AK314491; BAG37091.1; -; mRNA.
DR EMBL; CH471080; EAW63400.1; -; Genomic_DNA.
DR EMBL; BC028230; AAH28230.1; -; mRNA.
DR EMBL; BC039740; AAH39740.1; -; mRNA.
DR EMBL; BC050528; AAH50528.1; -; mRNA.
DR CCDS; CCDS6089.1; -.
DR RefSeq; NP_115898.2; NM_032509.3.
DR AlphaFoldDB; Q9BXY0; -.
DR SMR; Q9BXY0; -.
DR BioGRID; 124134; 163.
DR IntAct; Q9BXY0; 70.
DR MINT; Q9BXY0; -.
DR STRING; 9606.ENSP00000353246; -.
DR iPTMnet; Q9BXY0; -.
DR PhosphoSitePlus; Q9BXY0; -.
DR SwissPalm; Q9BXY0; -.
DR BioMuta; MAK16; -.
DR DMDM; 71152029; -.
DR SWISS-2DPAGE; Q9BXY0; -.
DR EPD; Q9BXY0; -.
DR jPOST; Q9BXY0; -.
DR MassIVE; Q9BXY0; -.
DR MaxQB; Q9BXY0; -.
DR PaxDb; Q9BXY0; -.
DR PeptideAtlas; Q9BXY0; -.
DR PRIDE; Q9BXY0; -.
DR ProteomicsDB; 79539; -.
DR Antibodypedia; 23360; 57 antibodies from 17 providers.
DR DNASU; 84549; -.
DR Ensembl; ENST00000360128.11; ENSP00000353246.5; ENSG00000198042.11.
DR GeneID; 84549; -.
DR KEGG; hsa:84549; -.
DR MANE-Select; ENST00000360128.11; ENSP00000353246.5; NM_032509.4; NP_115898.2.
DR UCSC; uc003xjj.4; human.
DR CTD; 84549; -.
DR DisGeNET; 84549; -.
DR GeneCards; MAK16; -.
DR HGNC; HGNC:13703; MAK16.
DR HPA; ENSG00000198042; Low tissue specificity.
DR MalaCards; MAK16; -.
DR neXtProt; NX_Q9BXY0; -.
DR OpenTargets; ENSG00000198042; -.
DR PharmGKB; PA162394925; -.
DR VEuPathDB; HostDB:ENSG00000198042; -.
DR eggNOG; KOG3064; Eukaryota.
DR GeneTree; ENSGT00390000012859; -.
DR HOGENOM; CLU_050888_2_0_1; -.
DR InParanoid; Q9BXY0; -.
DR OMA; GTYRDIY; -.
DR OrthoDB; 1394336at2759; -.
DR PhylomeDB; Q9BXY0; -.
DR TreeFam; TF105759; -.
DR PathwayCommons; Q9BXY0; -.
DR SignaLink; Q9BXY0; -.
DR BioGRID-ORCS; 84549; 802 hits in 1056 CRISPR screens.
DR ChiTaRS; MAK16; human.
DR GeneWiki; RBM13; -.
DR GenomeRNAi; 84549; -.
DR Pharos; Q9BXY0; Tdark.
DR PRO; PR:Q9BXY0; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q9BXY0; protein.
DR Bgee; ENSG00000198042; Expressed in calcaneal tendon and 197 other tissues.
DR ExpressionAtlas; Q9BXY0; baseline and differential.
DR Genevisible; Q9BXY0; HS.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0030687; C:preribosome, large subunit precursor; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0000460; P:maturation of 5.8S rRNA; IBA:GO_Central.
DR GO; GO:0000470; P:maturation of LSU-rRNA; IBA:GO_Central.
DR InterPro; IPR029004; L28e/Mak16.
DR InterPro; IPR006958; Mak16.
DR Pfam; PF04874; Mak16; 1.
DR Pfam; PF01778; Ribosomal_L28e; 1.
DR PIRSF; PIRSF003352; MAK16; 1.
PE 1: Evidence at protein level;
KW Acetylation; Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1..300
FT /note="Protein MAK16 homolog"
FT /id="PRO_0000203794"
FT REGION 191..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..218
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..243
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 244..266
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895"
FT MOD_RES 197
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 200
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 229
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT MOD_RES 232
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT CROSSLNK 55
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 151
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 277
FT /note="Q -> R (in dbSNP:rs6468171)"
FT /evidence="ECO:0000269|PubMed:15489334, ECO:0000269|Ref.1"
FT /id="VAR_023076"
FT CONFLICT 200
FT /note="S -> L (in Ref. 2; BAB55134)"
FT /evidence="ECO:0000305"
FT CONFLICT 281
FT /note="A -> V (in Ref. 4; AAH39740)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 300 AA; 35369 MW; 2A757589C4749760 CRC64;
MQSDDVIWDT LGNKQFCSFK IRTKTQSFCR NEYSLTGLCN RSSCPLANSQ YATIKEEKGQ
CYLYMKVIER AAFPRRLWER VRLSKNYEKA LEQIDENLIY WPRFIRHKCK QRFTKITQYL
IRIRKLTLKR QRKLVPLSKK VERREKRREE KALIAAQLDN AIEKELLERL KQDTYGDIYN
FPIHAFDKAL EQQEAESDSS DTEEKDDDDD DEEDVGKREF VEDGEVDESD ISDFEDMDKL
DASSDEDQDG KSSSEEEEEK ALSAKHKGKM PLRGPLQRKR AYVEIEYEQE TEPVAKAKTT
