RSRC2_HUMAN
ID RSRC2_HUMAN Reviewed; 434 AA.
AC Q7L4I2; Q6N040; Q6NW16; Q9H864;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Arginine/serine-rich coiled-coil protein 2;
GN Name=RSRC2;
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 Kurehara H., Ishiguro H., Kuwabara Y., Kimura M., Haruki N., Sugiura H.,
RA Andoh T., Tomoda K., Sugito N., Takashima N., Fujii Y.;
RT "Identification of esophageal cancer gene.";
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Small intestine;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, and Colon;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 85-434.
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 [6]
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30 AND SER-32, AND
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 ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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-30 AND SER-32, 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 ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-4; THR-6; THR-16; SER-17; SER-32 AND SER-104, CLEAVAGE OF
RP INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4; SER-17; SER-32 AND
RP SER-376, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [13]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-375, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA Impens F., Radoshevich L., Cossart P., Ribet D.;
RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT external stimuli.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN [14]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-375, AND IDENTIFICATION BY MASS
RP 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 Q7L4I2; Q6PJH3: AKAP9; NbExp=3; IntAct=EBI-953753, EBI-11745576;
CC Q7L4I2; Q96DZ9-2: CMTM5; NbExp=3; IntAct=EBI-953753, EBI-11522780;
CC Q7L4I2; P78358: CTAG1B; NbExp=3; IntAct=EBI-953753, EBI-1188472;
CC Q7L4I2; Q8NEY1-3: NAV1; NbExp=3; IntAct=EBI-953753, EBI-11953718;
CC Q7L4I2; Q99471: PFDN5; NbExp=3; IntAct=EBI-953753, EBI-357275;
CC Q7L4I2; Q5PRF9: SAMD4B; NbExp=3; IntAct=EBI-953753, EBI-1047489;
CC Q7L4I2; Q9UHD9: UBQLN2; NbExp=3; IntAct=EBI-953753, EBI-947187;
CC Q7L4I2-2; Q96DZ9: CMTM5; NbExp=3; IntAct=EBI-10256202, EBI-2548702;
CC Q7L4I2-2; Q08379: GOLGA2; NbExp=3; IntAct=EBI-10256202, EBI-618309;
CC Q7L4I2-2; Q8N6L0: KASH5; NbExp=3; IntAct=EBI-10256202, EBI-749265;
CC Q7L4I2-2; Q8ND90: PNMA1; NbExp=3; IntAct=EBI-10256202, EBI-302345;
CC Q7L4I2-2; Q6NUQ1: RINT1; NbExp=3; IntAct=EBI-10256202, EBI-726876;
CC Q7L4I2-2; P36406: TRIM23; NbExp=3; IntAct=EBI-10256202, EBI-740098;
CC Q7L4I2-2; Q9BYV2: TRIM54; NbExp=3; IntAct=EBI-10256202, EBI-2130429;
CC Q7L4I2-2; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-10256202, EBI-741480;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q7L4I2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7L4I2-2; Sequence=VSP_030440;
CC -!- SIMILARITY: Belongs to the RSRC2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB14755.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=EAW98327.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB212664; BAE93762.1; -; mRNA.
DR EMBL; BX640711; CAE45830.1; -; mRNA.
DR EMBL; CH471054; EAW98327.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CH471054; EAW98330.1; -; Genomic_DNA.
DR EMBL; BC008684; AAH08684.2; -; mRNA.
DR EMBL; BC067773; AAH67773.1; -; mRNA.
DR EMBL; AK023985; BAB14755.1; ALT_INIT; mRNA.
DR CCDS; CCDS31920.1; -. [Q7L4I2-1]
DR RefSeq; NP_075388.2; NM_023012.5. [Q7L4I2-1]
DR RefSeq; XP_016875322.1; XM_017019833.1.
DR AlphaFoldDB; Q7L4I2; -.
DR BioGRID; 122398; 60.
DR IntAct; Q7L4I2; 33.
DR MINT; Q7L4I2; -.
DR STRING; 9606.ENSP00000330188; -.
DR iPTMnet; Q7L4I2; -.
DR MetOSite; Q7L4I2; -.
DR PhosphoSitePlus; Q7L4I2; -.
DR BioMuta; RSRC2; -.
DR DMDM; 74739167; -.
DR EPD; Q7L4I2; -.
DR jPOST; Q7L4I2; -.
DR MassIVE; Q7L4I2; -.
DR MaxQB; Q7L4I2; -.
DR PaxDb; Q7L4I2; -.
DR PeptideAtlas; Q7L4I2; -.
DR PRIDE; Q7L4I2; -.
DR ProteomicsDB; 68777; -. [Q7L4I2-1]
DR ProteomicsDB; 68778; -. [Q7L4I2-2]
DR Antibodypedia; 31659; 118 antibodies from 20 providers.
DR DNASU; 65117; -.
DR Ensembl; ENST00000331738.12; ENSP00000330188.6; ENSG00000111011.18. [Q7L4I2-1]
DR GeneID; 65117; -.
DR KEGG; hsa:65117; -.
DR MANE-Select; ENST00000331738.12; ENSP00000330188.6; NM_023012.6; NP_075388.2.
DR UCSC; uc001ucr.4; human. [Q7L4I2-1]
DR CTD; 65117; -.
DR DisGeNET; 65117; -.
DR GeneCards; RSRC2; -.
DR HGNC; HGNC:30559; RSRC2.
DR HPA; ENSG00000111011; Tissue enhanced (bone).
DR neXtProt; NX_Q7L4I2; -.
DR OpenTargets; ENSG00000111011; -.
DR PharmGKB; PA162402249; -.
DR VEuPathDB; HostDB:ENSG00000111011; -.
DR eggNOG; ENOG502QQ3C; Eukaryota.
DR GeneTree; ENSGT00730000111142; -.
DR HOGENOM; CLU_051694_0_0_1; -.
DR InParanoid; Q7L4I2; -.
DR OMA; LWANKSK; -.
DR OrthoDB; 1343985at2759; -.
DR PhylomeDB; Q7L4I2; -.
DR TreeFam; TF325523; -.
DR PathwayCommons; Q7L4I2; -.
DR SignaLink; Q7L4I2; -.
DR BioGRID-ORCS; 65117; 303 hits in 1070 CRISPR screens.
DR ChiTaRS; RSRC2; human.
DR GenomeRNAi; 65117; -.
DR Pharos; Q7L4I2; Tdark.
DR PRO; PR:Q7L4I2; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q7L4I2; protein.
DR Bgee; ENSG00000111011; Expressed in sural nerve and 209 other tissues.
DR ExpressionAtlas; Q7L4I2; baseline and differential.
DR Genevisible; Q7L4I2; HS.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR InterPro; IPR028124; SMAP_dom.
DR Pfam; PF15477; SMAP; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Coiled coil; Isopeptide bond;
KW Phosphoprotein; Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:21406692"
FT CHAIN 2..434
FT /note="Arginine/serine-rich coiled-coil protein 2"
FT /id="PRO_0000314937"
FT REGION 1..230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 230..270
FT /evidence="ECO:0000255"
FT COMPBIAS 1..32
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..115
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..212
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 4
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 6
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 16
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 17
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 30
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 32
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 104
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 376
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 375
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 375
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..69
FT /note="MAASDTERDGLAPEKTSPDRDKKKEQSEVSVSPRASKHHYSRSRSRSRERKR
FT KSDNEGRKHRSRSRSKE -> MKEENTGAGAEAKRTNFFLKQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_030440"
FT VARIANT 88
FT /note="H -> R (in dbSNP:rs17886684)"
FT /id="VAR_038133"
FT CONFLICT 224
FT /note="P -> R (in Ref. 4; AAH67773)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 434 AA; 50560 MW; D744ADEFF395E888 CRC64;
MAASDTERDG LAPEKTSPDR DKKKEQSEVS VSPRASKHHY SRSRSRSRER KRKSDNEGRK
HRSRSRSKEG RRHESKDKSS KKHKSEEHND KEHSSDKGRE RLNSSENGED RHKRKERKSS
RGRSHSRSRS RERRHRSRSR ERKKSRSRSR ERKKSRSRSR ERKKSRSRSR ERKRRIRSRS
RSRSRHRHRT RSRSRTRSRS RDRKKRIEKP RRFSRSLSRT PSPPPFRGRN TAMDAQEALA
RRLERAKKLQ EQREKEMVEK QKQQEIAAAA ATGGSVLNVA ALLASGTQVT PQIAMAAQMA
ALQAKALAET GIAVPSYYNP AAVNPMKFAE QEKKRKMLWQ GKKEGDKSQS AEIWEKLNFG
NKDQNVKFRK LMGIKSEDEA GCSSVDEESY KTLKQQEEVF RNLDAQYEMA RSQTHTQRGM
GLGFTSSMRG MDAV
