SCHI1_HUMAN
ID SCHI1_HUMAN Reviewed; 487 AA.
AC P0DPB3; B3KRM0; O75543; Q00P30; Q00P31; Q7Z3Y3; Q8IY83; Q9P0W3; Q9P0W4;
AC Q9P0W5;
DT 22-NOV-2017, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2017, sequence version 1.
DT 03-AUG-2022, entry version 29.
DE RecName: Full=Schwannomin-interacting protein 1 {ECO:0000312|HGNC:HGNC:15678};
DE Short=SCHIP-1 {ECO:0000303|PubMed:10669747};
GN Name=SCHIP1 {ECO:0000312|HGNC:HGNC:15678};
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] {ECO:0000312|EMBL:AAF34241.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS SCHIP1-1; SCHIP1-2 AND SCHIP1-3),
RP INTERACTION WITH NF2, SUBUNIT, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=10669747; DOI=10.1128/mcb.20.5.1699-1712.2000;
RA Goutebroze L., Brault E., Muchardt C., Camonis J., Thomas G.;
RT "Cloning and characterization of SCHIP-1, a novel protein interacting
RT specifically with spliced isoforms and naturally occurring mutant NF2
RT proteins.";
RL Mol. Cell. Biol. 20:1699-1712(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SCHIP1-4).
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] (ISOFORMS SCHIP1-1 AND SCHIP1-4),
RP AND VARIANT VAL-481.
RC TISSUE=Skeletal muscle;
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 107-487 (ISOFORM SCHIP1-1).
RC TISSUE=Brain;
RA Yu W., Gibbs R.A.;
RL Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP ALTERNATIVE SPLICING.
RX PubMed=17045569; DOI=10.1016/j.bbrc.2006.09.136;
RA Kwasnicka-Crawford D.A., Carson A.R., Scherer S.W.;
RT "IQCJ-SCHIP1, a novel fusion transcript encoding a calmodulin-binding IQ
RT motif protein.";
RL Biochem. Biophys. Res. Commun. 350:890-899(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-117, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
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 [8]
RP INTERACTION WITH ANK3.
RX PubMed=25950943; DOI=10.1111/jnc.13158;
RA Papandreou M.J., Vacher H., Fache M.P., Klingler E., Rueda-Boroni F.,
RA Ferracci G., Debarnot C., Piperoglou C., Garcia Del Cano G., Goutebroze L.,
RA Dargent B.;
RT "CK2-regulated schwannomin-interacting protein IQCJ-SCHIP-1 association
RT with AnkG contributes to the maintenance of the axon initial segment.";
RL J. Neurochem. 134:527-537(2015).
CC -!- SUBUNIT: Homooligomer (via coiled coil domain) (PubMed:10669747).
CC Interacts with NF2; the interaction is direct (PubMed:10669747).
CC Interacts with ANK3 (PubMed:25950943). {ECO:0000269|PubMed:10669747,
CC ECO:0000269|PubMed:25950943}.
CC -!- INTERACTION:
CC P0DPB3; P55036: PSMD4; NbExp=2; IntAct=EBI-1397509, EBI-359318;
CC P0DPB3; P0DPB3: SCHIP1; NbExp=2; IntAct=EBI-1397509, EBI-1397509;
CC P0DPB3; Q9UIL1: SCOC; NbExp=4; IntAct=EBI-1397509, EBI-2686537;
CC P0DPB3; Q5T200: ZC3H13; NbExp=2; IntAct=EBI-1397509, EBI-2679720;
CC P0DPB3-4; Q99633: PRPF18; NbExp=3; IntAct=EBI-11962426, EBI-2798416;
CC P0DPB3-4; Q9UIL1-3: SCOC; NbExp=5; IntAct=EBI-11962426, EBI-10692913;
CC P0DPB3-4; Q96GM5: SMARCD1; NbExp=3; IntAct=EBI-11962426, EBI-358489;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10669747}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=SCHIP1-1; Synonyms=SCHIP-1 {ECO:0000303|PubMed:10669747}, SCHIP-1a
CC {ECO:0000303|PubMed:25950943};
CC IsoId=P0DPB3-1, Q9P0W5-1;
CC Sequence=Displayed;
CC Name=SCHIP1-2; Synonyms=SCHIP-1-D241/253 {ECO:0000303|PubMed:10669747};
CC IsoId=P0DPB3-2, Q9P0W5-2;
CC Sequence=VSP_025829;
CC Name=SCHIP1-3; Synonyms=SCHIP-1-D22/253 {ECO:0000303|PubMed:10669747};
CC IsoId=P0DPB3-3, Q9P0W5-3;
CC Sequence=VSP_025828;
CC Name=SCHIP1-4;
CC IsoId=P0DPB3-4, Q9P0W5-4;
CC Sequence=VSP_025827, VSP_025830;
CC Name=IQCJ-SCHIP1-1;
CC IsoId=B3KU38-1; Sequence=External;
CC Name=IQCJ-SCHIP1-2;
CC IsoId=B3KU38-2; Sequence=External;
CC -!- TISSUE SPECIFICITY: Preferentially expressed in brain, skeletal muscles
CC and heart. Also expressed in detected in pancreas, kidney, liver, lung,
CC and placenta. {ECO:0000269|PubMed:10669747}.
CC -!- SIMILARITY: Belongs to the SCHIP1 family. {ECO:0000305}.
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DR EMBL; AF145713; AAF34241.1; -; mRNA.
DR EMBL; AF145714; AAF34242.1; -; mRNA.
DR EMBL; AF145715; AAF34243.1; -; mRNA.
DR EMBL; AK091871; BAG52432.1; -; mRNA.
DR EMBL; CH471052; EAW78662.1; -; Genomic_DNA.
DR EMBL; BC005947; AAH05947.1; -; mRNA.
DR EMBL; BC036535; AAH36535.1; -; mRNA.
DR EMBL; AF070614; AAC25386.1; -; mRNA.
DR CCDS; CCDS3186.1; -.
DR CCDS; CCDS56292.1; -. [P0DPB3-2]
DR CCDS; CCDS56293.1; -. [P0DPB3-3]
DR CCDS; CCDS56294.1; -. [P0DPB3-4]
DR RefSeq; NP_001184036.1; NM_001197107.1. [P0DPB3-2]
DR RefSeq; NP_001184037.1; NM_001197108.1. [P0DPB3-3]
DR RefSeq; NP_001184038.1; NM_001197109.1. [P0DPB3-4]
DR RefSeq; NP_055390.1; NM_014575.3. [P0DPB3-1]
DR AlphaFoldDB; P0DPB3; -.
DR SMR; P0DPB3; -.
DR IntAct; P0DPB3; 50.
DR iPTMnet; P0DPB3; -.
DR PhosphoSitePlus; P0DPB3; -.
DR BioMuta; SCHIP1; -.
DR EPD; P0DPB3; -.
DR jPOST; P0DPB3; -.
DR MassIVE; P0DPB3; -.
DR PeptideAtlas; P0DPB3; -.
DR PRIDE; P0DPB3; -.
DR Antibodypedia; 1013; 113 antibodies from 16 providers.
DR DNASU; 29970; -.
DR Ensembl; ENST00000445224.6; ENSP00000404860.2; ENSG00000151967.18. [P0DPB3-4]
DR GeneID; 29970; -.
DR KEGG; hsa:29970; -.
DR MANE-Select; ENST00000638749.2; ENSP00000491030.1; NM_014575.4; NP_055390.1.
DR CTD; 29970; -.
DR DisGeNET; 29970; -.
DR GeneCards; SCHIP1; -.
DR HGNC; HGNC:15678; SCHIP1.
DR HPA; ENSG00000151967; Tissue enhanced (brain, heart muscle, skeletal muscle, tongue).
DR MIM; 619206; gene.
DR neXtProt; NX_P0DPB3; -.
DR OpenTargets; ENSG00000151967; -.
DR OpenTargets; ENSG00000283154; -.
DR VEuPathDB; HostDB:ENSG00000151967; -.
DR GeneTree; ENSGT00390000011127; -.
DR OrthoDB; 1290403at2759; -.
DR PathwayCommons; P0DPB3; -.
DR SignaLink; P0DPB3; -.
DR Pharos; P0DPB3; Tbio.
DR PRO; PR:P0DPB3; -.
DR Proteomes; UP000005640; Chromosome 3.
DR Bgee; ENSG00000151967; Expressed in ventricular zone and 105 other tissues.
DR ExpressionAtlas; P0DPB3; baseline and differential.
DR Genevisible; Q9P0W5; HS.
DR GO; GO:0030054; C:cell junction; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0035332; P:positive regulation of hippo signaling; IBA:GO_Central.
DR InterPro; IPR039045; SCHIP_1.
DR InterPro; IPR015649; SCHIP_1_C.
DR PANTHER; PTHR13103; PTHR13103; 1.
DR Pfam; PF10148; SCHIP-1; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Cytoplasm; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..487
FT /note="Schwannomin-interacting protein 1"
FT /id="PRO_0000288927"
FT REGION 1..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 88..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 236..260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 308..354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 424..458
FT /evidence="ECO:0000255"
FT COMPBIAS 1..29
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..68
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 94..108
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 109..123
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 239..257
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 323..339
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 117
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..243
FT /note="Missing (in isoform SCHIP1-4)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_025827"
FT VAR_SEQ 22..253
FT /note="Missing (in isoform SCHIP1-3)"
FT /evidence="ECO:0000303|PubMed:10669747"
FT /id="VSP_025828"
FT VAR_SEQ 241..253
FT /note="Missing (in isoform SCHIP1-2)"
FT /evidence="ECO:0000303|PubMed:10669747"
FT /id="VSP_025829"
FT VAR_SEQ 244..253
FT /note="QGQARTNSTS -> MVHQDNCSYQ (in isoform SCHIP1-4)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_025830"
FT VARIANT 101
FT /note="E -> K (in dbSNP:rs3732851)"
FT /id="VAR_051332"
FT VARIANT 481
FT /note="A -> V (in dbSNP:rs17850021)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_032534"
FT CONFLICT 178
FT /note="Missing (in Ref. 4; AAH36535)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 487 AA; 53480 MW; 86F86EDD64A475BF CRC64;
MERSGQRVTT WDCDQGKHSD SDYREDGMDL GSDAGSSSSS SRASSQSNST KVTPCSECKS
SSSPGGSLDL VSALEDYEEP FPVYQKKVID EWAPEEDGEE EEEEDERDQR GYRDDRSPAR
EPGDVSARTR SGGGGGRSAT TAMPPPVPNG NLHQHDPQDL RHNGNVVVAG RPSCSRGPRR
AIQKPQPAGG RRSGRGPAAG GLCLQPPDGG TCVPEEPPVP PMDWEALEKH LAGLQFREQE
VRNQGQARTN STSAQKNERE SIRQKLALGS FFDDGPGIYT SCSKSGKPSL SSRLQSGMNL
QICFVNDSGS DKDSDADDSK TETSLDTPLS PMSKQSSSYS DRDTTEEESE SLDDMDFLTR
QKKLQAEAKM ALAMAKPMAK MQVEVEKQNR KKSPVADLLP HMPHISECLM KRSLKPTDLR
DMTIGQLQVI VNDLHSQIES LNEELVQLLL IRDELHTEQD AMLVDIEDLT RHAESQQKHM
AEKMPAK
