ITPI2_MOUSE
ID ITPI2_MOUSE Reviewed; 1252 AA.
AC Q922B9; A2AQD4; A5D8Z6; Q08E80; Q14BJ9; Q544I3; Q68FN1; Q75WU7; Q8CH96;
AC Q8VEF7;
DT 13-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Protein ITPRID2 {ECO:0000305};
DE AltName: Full=ITPR-interacting domain-containing protein 2 {ECO:0000305};
DE AltName: Full=Ki-ras-induced actin-interacting protein {ECO:0000303|PubMed:14673706};
DE AltName: Full=Sperm-specific antigen 2 homolog {ECO:0000250|UniProtKB:P28290};
GN Name=Itprid2;
GN Synonyms=Kiaa1927, Krap {ECO:0000303|PubMed:14673706},
GN Ssfa2 {ECO:0000312|MGI:MGI:1917849};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND SUBCELLULAR LOCATION.
RX PubMed=14673706; DOI=10.1007/s10038-003-0106-3;
RA Inokuchi J., Komiya M., Baba I., Naito S., Sasazuki T., Shirasawa S.;
RT "Deregulated expression of KRAP, a novel gene encoding actin-interacting
RT protein, in human colon cancer cells.";
RL J. Hum. Genet. 49:46-52(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=C57BL/6J; TISSUE=Skin;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 5-1252.
RC TISSUE=Brain;
RX PubMed=12465718; DOI=10.1093/dnares/9.5.179;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Hara Y., Nagase T., Ohara O.,
RA Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: I.
RT The complete nucleotide sequences of 100 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 9:179-188(2002).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-85; SER-90; SER-736 AND
RP SER-738, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90; SER-109; SER-268;
RP SER-465; SER-667; SER-736; SER-738; SER-745; SER-866; SER-1036; SER-1051;
RP SER-1056; SER-1059 AND SER-1154, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14673706}.
CC Note=Located near the plasma membrane. Associated with actin filaments.
CC May also exist as a membrane-bound form with extracellular regions (By
CC similarity). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q922B9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q922B9-2; Sequence=VSP_023869;
CC Name=3;
CC IsoId=Q922B9-3; Sequence=VSP_023868;
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH08560.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH18526.3; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC Sequence=AAI22520.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC29756.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB120565; BAC87833.1; -; mRNA.
DR EMBL; AL844577; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL928770; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC008560; AAH08560.1; ALT_INIT; mRNA.
DR EMBL; BC018526; AAH18526.3; ALT_TERM; mRNA.
DR EMBL; BC079535; AAH79535.1; -; mRNA.
DR EMBL; BC115799; AAI15800.1; -; mRNA.
DR EMBL; BC122519; AAI22520.1; ALT_INIT; mRNA.
DR EMBL; BC141883; AAI41884.1; -; mRNA.
DR EMBL; AK037213; BAC29756.1; ALT_INIT; mRNA.
DR EMBL; AB093303; BAC41485.1; -; mRNA.
DR CCDS; CCDS16170.1; -. [Q922B9-1]
DR RefSeq; NP_542125.3; NM_080558.4. [Q922B9-1]
DR AlphaFoldDB; Q922B9; -.
DR SMR; Q922B9; -.
DR STRING; 10090.ENSMUSP00000107415; -.
DR iPTMnet; Q922B9; -.
DR PhosphoSitePlus; Q922B9; -.
DR EPD; Q922B9; -.
DR jPOST; Q922B9; -.
DR MaxQB; Q922B9; -.
DR PaxDb; Q922B9; -.
DR PeptideAtlas; Q922B9; -.
DR PRIDE; Q922B9; -.
DR ProteomicsDB; 258624; -. [Q922B9-1]
DR ProteomicsDB; 258625; -. [Q922B9-2]
DR ProteomicsDB; 258626; -. [Q922B9-3]
DR Antibodypedia; 33982; 113 antibodies from 20 providers.
DR DNASU; 70599; -.
DR Ensembl; ENSMUST00000111785; ENSMUSP00000107415; ENSMUSG00000027007. [Q922B9-1]
DR GeneID; 70599; -.
DR KEGG; mmu:70599; -.
DR UCSC; uc008kgw.2; mouse. [Q922B9-1]
DR CTD; 6744; -.
DR MGI; MGI:1917849; Itprid2.
DR VEuPathDB; HostDB:ENSMUSG00000027007; -.
DR eggNOG; ENOG502QSG8; Eukaryota.
DR GeneTree; ENSGT00940000158532; -.
DR HOGENOM; CLU_007016_0_0_1; -.
DR InParanoid; Q922B9; -.
DR OMA; QHSNPDF; -.
DR OrthoDB; 94956at2759; -.
DR TreeFam; TF331566; -.
DR BioGRID-ORCS; 70599; 2 hits in 70 CRISPR screens.
DR ChiTaRS; Ssfa2; mouse.
DR PRO; PR:Q922B9; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q922B9; protein.
DR Bgee; ENSMUSG00000027007; Expressed in skin of external ear and 234 other tissues.
DR ExpressionAtlas; Q922B9; baseline and differential.
DR Genevisible; Q922B9; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0051015; F:actin filament binding; ISO:MGI.
DR GO; GO:0005102; F:signaling receptor binding; IEA:InterPro.
DR InterPro; IPR029325; ITPR-bd.
DR InterPro; IPR026648; ITPRID2.
DR InterPro; IPR029326; SSFA2_C.
DR InterPro; IPR043444; TESPA1-like.
DR PANTHER; PTHR17469; PTHR17469; 1.
DR PANTHER; PTHR17469:SF11; PTHR17469:SF11; 1.
DR Pfam; PF14722; KRAP_IP3R_bind; 1.
DR Pfam; PF14723; SSFA2_C; 1.
DR SMART; SM01257; KRAP_IP3R_bind; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Cytoplasm; Isopeptide bond;
KW Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..1252
FT /note="Protein ITPRID2"
FT /id="PRO_0000072212"
FT REGION 28..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 306..483
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 552..575
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 595..636
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1095..1131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1147..1180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 955..1031
FT /evidence="ECO:0000255"
FT COMPBIAS 42..57
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 350..373
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 374..428
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 429..447
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 596..616
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1097..1124
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1149..1165
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 85
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES 90
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 109
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 207
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P28290"
FT MOD_RES 268
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 328
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P28290"
FT MOD_RES 465
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 643
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P28290"
FT MOD_RES 667
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 736
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 738
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 745
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 758
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P28290"
FT MOD_RES 766
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P28290"
FT MOD_RES 866
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 898
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P28290"
FT MOD_RES 1036
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1051
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1056
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1059
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1114
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P28290"
FT MOD_RES 1149
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P28290"
FT MOD_RES 1154
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1161
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P28290"
FT CROSSLNK 807
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P28290"
FT VAR_SEQ 1..1063
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_023869"
FT VAR_SEQ 1..151
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_023868"
FT CONFLICT 319
FT /note="T -> A (in Ref. 1; BAC87833, 3; AAI22520/AAI41884
FT and 5; BAC41485)"
FT /evidence="ECO:0000305"
FT CONFLICT 1071
FT /note="I -> M (in Ref. 1; BAC87833, 3; AAH18526/AAI41884/
FT AAI22520 and 5; BAC41485)"
FT /evidence="ECO:0000305"
FT CONFLICT 1240
FT /note="S -> A (in Ref. 1; BAC87833)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1252 AA; 136947 MW; 2FA8C5874C1A573E CRC64;
MNRPLSAEAE EELEWQVASR RRKAWAKCRS SWQASETEDL STETTTQDED EDDEEDLPGT
KLPAPAGRGN VPNEKIAIWL KDCRTPLGAS LDEQSSGTPK GVLVRNGGSF EDDLSLGAEA
NHLHEPDAQV ENCNNILAKE RRLQFHQKGR SMNSTGSGKS SGTVSSVSEL LELYEEDPEE
ILYNLGFGRD EPDIASKIPS RFFNSSSFAR GIDIKVFLSA QMQRMEVENP NYALTSRFRQ
IEVLTTVANA FSSLYSQVSG TPLQRIGSMS SVTSTKEVAD SPPPLTRSNT ANRLMKTLSK
LNLCVDKTEK GEGGSSPATE KGRTLSISLS EDGGGGKSDP KLQKVVKKKE SSSMLATVTE
EVSGSSSTVT DSVDADRLSE EADSTISHQE ESEESREAHS QEKDPLRKSA VTDPDLGHDG
RVSSHCELES SSELKSAQAS SSEKEPCAPL TIPSIRNIMT QQKDSFEMEE VQSTEGEAPH
VPATCQLSLA KSKRDHLLRT ASQHSDSSGF AEDSTDCVSL NHLLVNESLQ AMGSSADSCD
SETTVTSLGE DHVTPTAQDQ PYFNESEEES LAPLQKGRAK VEIVAEKRKA DNQDFPQCVT
AENAGNNEST KGPCEPGHQI TETGEHPPLA ATGELPREES VESDVEKGSE CEFAQYTTHH
ILRSLASFEA QGSGMSSEKK TGFPSSVDRV NTALQRAQMK VCSMSGQRVG RSLIKSKDLL
KQRYLLAKAG YPLRRSQSLP TTLLSPVRVV SSVNVRLSPG KETRCSPPSF TYKYTPEEEQ
DLEKQGTEHD GQSLVKSTIF IPPPSVKKEE APQSEGTRLE ECHHGRLAPC PQFAPISQST
CSLHSVHSEW QDRPLCEHMR TLSAHSVPNI SGAACSAFSP FGCPYSHRHA AHPYRACSVN
PPSAIEMQLR RVLHDIRSSL QNLSQYPMTR GPDLAAAPYS TQNSSVLPLY ENTFQELQVV
RRSLNLFRTQ MMDLELAMLR QQTVVYPHMT EEDRYEVDQL QGLRNSVRME LQDLEMQLEE
RLLGLDEQLR AVRVPSPFRP SALPGMCGSR SVDNLSCPSP LNVMEPVTEL IREQSYLKSE
LGLGLGDMAY EIPPGESSES VFSQATSESS SVCSSPSHTN RRSRGLPGSK PRARLVARKK
IFRASVALTP TAPSRTGSVQ TPPDLESSEE AGGAEEASPV VGLASHVEEE PEDLSLMPAA
EEMHRNVEQD ELQQVIREIK ESIVGEIRRE IVSGLLAAVS SSKAPGPKQD SH
