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RHDF2_HUMAN
ID   RHDF2_HUMAN             Reviewed;         856 AA.
AC   Q6PJF5; A6NEM3; A8K801; Q5U607; Q5YGQ8; Q9H6E9;
DT   01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 2.
DT   03-AUG-2022, entry version 144.
DE   RecName: Full=Inactive rhomboid protein 2;
DE            Short=iRhom2;
DE   AltName: Full=Rhomboid 5 homolog 2;
DE   AltName: Full=Rhomboid family member 2;
DE   AltName: Full=Rhomboid veinlet-like protein 5;
DE   AltName: Full=Rhomboid veinlet-like protein 6;
GN   Name=RHBDF2; Synonyms=IRHOM2, RHBDL5, RHBDL6;
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 2), AND VARIANT LEU-208.
RC   TISSUE=Liver;
RA   Kong X., Teng X., Hu L.;
RT   "Molecular cloning of human RHBDL5.";
RL   Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP   LEU-208.
RC   TISSUE=Kidney epithelium, Spleen, and Synovium;
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=16625196; DOI=10.1038/nature04689;
RA   Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA   Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA   Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA   Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA   DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA   Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA   Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA   LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA   Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA   Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA   Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA   Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA   Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT   "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT   human lineage.";
RL   Nature 440:1045-1049(2006).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT LEU-208.
RC   TISSUE=Eye, 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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90; SER-325 AND SER-328, 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   [6]
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   [7]
RP   TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND VARIANTS TOC THR-186 AND
RP   LEU-189.
RX   PubMed=22265016; DOI=10.1016/j.ajhg.2011.12.008;
RA   Blaydon D.C., Etheridge S.L., Risk J.M., Hennies H.C., Gay L.J.,
RA   Carroll R., Plagnol V., McRonald F.E., Stevens H.P., Spurr N.K.,
RA   Bishop D.T., Ellis A., Jankowski J., Field J.K., Leigh I.M., South A.P.,
RA   Kelsell D.P.;
RT   "RHBDF2 mutations are associated with tylosis, a familial esophageal cancer
RT   syndrome.";
RL   Am. J. Hum. Genet. 90:340-346(2012).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90; SER-113; SER-325 AND
RP   SER-328, 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   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [10]
RP   INTERACTION WITH ADAM17 AND FRMD8, AND SUBCELLULAR LOCATION.
RX   PubMed=29897333; DOI=10.7554/elife.35032;
RA   Oikonomidi I., Burbridge E., Cavadas M., Sullivan G., Collis B.,
RA   Naegele H., Clancy D., Brezinova J., Hu T., Bileck A., Gerner C.,
RA   Bolado A., von Kriegsheim A., Martin S.J., Steinberg F., Strisovsky K.,
RA   Adrain C.;
RT   "iTAP, a novel iRhom interactor, controls TNF secretion by policing the
RT   stability of iRhom/TACE.";
RL   Elife 7:0-0(2018).
RN   [11]
RP   INTERACTION WITH ADAM17 AND FRMD8.
RX   PubMed=29897336; DOI=10.7554/elife.35012;
RA   Kuenzel U., Grieve A.G., Meng Y., Sieber B., Cowley S.A., Freeman M.;
RT   "FRMD8 promotes inflammatory and growth factor signalling by stabilising
RT   the iRhom/ADAM17 sheddase complex.";
RL   Elife 7:0-0(2018).
CC   -!- FUNCTION: Regulates ADAM17 protease, a sheddase of the epidermal growth
CC       factor (EGF) receptor ligands and TNF, thereby plays a role in sleep,
CC       cell survival, proliferation, migration and inflammation. Does not
CC       exhibit any protease activity on its own.
CC       {ECO:0000250|UniProtKB:Q80WQ6}.
CC   -!- SUBUNIT: Interacts with EGF (By similarity). Interacts (via cytoplasmic
CC       N-terminus) with FRMD8/iTAP; this interaction leads to mutual protein
CC       stabilization (PubMed:29897333, PubMed:29897336). Interacts with
CC       ADAM17/TACE (PubMed:29897333, PubMed:29897336).
CC       {ECO:0000250|UniProtKB:Q80WQ6, ECO:0000269|PubMed:29897333,
CC       ECO:0000269|PubMed:29897336}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:Q80WQ6}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:Q80WQ6}. Cell membrane
CC       {ECO:0000269|PubMed:22265016, ECO:0000269|PubMed:29897333}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q6PJF5-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6PJF5-2; Sequence=VSP_034368;
CC   -!- TISSUE SPECIFICITY: Found in the epidermis and esophageal epithelium.
CC       {ECO:0000269|PubMed:22265016}.
CC   -!- DISEASE: Tylosis with esophageal cancer (TOC) [MIM:148500]: An
CC       autosomal dominant syndrome characterized by diffuse palmoplantar
CC       keratoderma, oral leukokeratosis, and a high lifetime risk of
CC       esophageal cancer. {ECO:0000269|PubMed:22265016}. Note=The disease is
CC       caused by variants affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the peptidase S54 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH35829.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAB15310.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AY500247; AAS77567.1; -; mRNA.
DR   EMBL; AK025994; BAB15310.1; ALT_INIT; mRNA.
DR   EMBL; AK292135; BAF84824.1; -; mRNA.
DR   EMBL; AK292166; BAF84855.1; -; mRNA.
DR   EMBL; AC015802; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC035829; AAH35829.1; ALT_INIT; mRNA.
DR   EMBL; BC016034; AAH16034.2; -; mRNA.
DR   CCDS; CCDS32743.1; -. [Q6PJF5-1]
DR   CCDS; CCDS32744.1; -. [Q6PJF5-2]
DR   RefSeq; NP_001005498.2; NM_001005498.3. [Q6PJF5-2]
DR   RefSeq; NP_078875.4; NM_024599.5. [Q6PJF5-1]
DR   RefSeq; XP_005257726.1; XM_005257669.3. [Q6PJF5-1]
DR   RefSeq; XP_005257727.1; XM_005257670.1.
DR   RefSeq; XP_011523551.1; XM_011525249.2. [Q6PJF5-2]
DR   RefSeq; XP_011523552.1; XM_011525250.2. [Q6PJF5-2]
DR   RefSeq; XP_011523553.1; XM_011525251.2. [Q6PJF5-2]
DR   RefSeq; XP_016880568.1; XM_017025079.1.
DR   AlphaFoldDB; Q6PJF5; -.
DR   BioGRID; 122779; 200.
DR   ELM; Q6PJF5; -.
DR   IntAct; Q6PJF5; 11.
DR   STRING; 9606.ENSP00000322775; -.
DR   MEROPS; S54.953; -.
DR   GlyGen; Q6PJF5; 1 site.
DR   iPTMnet; Q6PJF5; -.
DR   PhosphoSitePlus; Q6PJF5; -.
DR   BioMuta; RHBDF2; -.
DR   DMDM; 193806488; -.
DR   EPD; Q6PJF5; -.
DR   jPOST; Q6PJF5; -.
DR   MassIVE; Q6PJF5; -.
DR   MaxQB; Q6PJF5; -.
DR   PaxDb; Q6PJF5; -.
DR   PeptideAtlas; Q6PJF5; -.
DR   PRIDE; Q6PJF5; -.
DR   ProteomicsDB; 67199; -. [Q6PJF5-1]
DR   ProteomicsDB; 67200; -. [Q6PJF5-2]
DR   Antibodypedia; 19692; 81 antibodies from 21 providers.
DR   DNASU; 79651; -.
DR   Ensembl; ENST00000313080.8; ENSP00000322775.3; ENSG00000129667.13. [Q6PJF5-1]
DR   Ensembl; ENST00000591885.5; ENSP00000466867.1; ENSG00000129667.13. [Q6PJF5-2]
DR   Ensembl; ENST00000675367.1; ENSP00000501790.1; ENSG00000129667.13. [Q6PJF5-2]
DR   GeneID; 79651; -.
DR   KEGG; hsa:79651; -.
DR   MANE-Select; ENST00000675367.1; ENSP00000501790.1; NM_001005498.4; NP_001005498.2. [Q6PJF5-2]
DR   UCSC; uc002jrq.3; human. [Q6PJF5-1]
DR   CTD; 79651; -.
DR   DisGeNET; 79651; -.
DR   GeneCards; RHBDF2; -.
DR   HGNC; HGNC:20788; RHBDF2.
DR   HPA; ENSG00000129667; Low tissue specificity.
DR   MalaCards; RHBDF2; -.
DR   MIM; 148500; phenotype.
DR   MIM; 614404; gene.
DR   neXtProt; NX_Q6PJF5; -.
DR   OpenTargets; ENSG00000129667; -.
DR   Orphanet; 2198; Palmoplantar keratoderma-esophageal carcinoma syndrome.
DR   PharmGKB; PA134980674; -.
DR   VEuPathDB; HostDB:ENSG00000129667; -.
DR   eggNOG; KOG2290; Eukaryota.
DR   GeneTree; ENSGT00940000159027; -.
DR   HOGENOM; CLU_011531_1_1_1; -.
DR   InParanoid; Q6PJF5; -.
DR   OMA; IKRSFAY; -.
DR   OrthoDB; 1253228at2759; -.
DR   PhylomeDB; Q6PJF5; -.
DR   TreeFam; TF312988; -.
DR   PathwayCommons; Q6PJF5; -.
DR   Reactome; R-HSA-9662834; CD163 mediating an anti-inflammatory response.
DR   SignaLink; Q6PJF5; -.
DR   BioGRID-ORCS; 79651; 11 hits in 1069 CRISPR screens.
DR   ChiTaRS; RHBDF2; human.
DR   GeneWiki; RHBDF2; -.
DR   GenomeRNAi; 79651; -.
DR   Pharos; Q6PJF5; Tbio.
DR   PRO; PR:Q6PJF5; -.
DR   Proteomes; UP000005640; Chromosome 17.
DR   RNAct; Q6PJF5; protein.
DR   Bgee; ENSG00000129667; Expressed in granulocyte and 158 other tissues.
DR   ExpressionAtlas; Q6PJF5; baseline and differential.
DR   Genevisible; Q6PJF5; HS.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR   GO; GO:0005796; C:Golgi lumen; TAS:Reactome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0019838; F:growth factor binding; IEA:UniProtKB-KW.
DR   GO; GO:0140318; F:protein transporter activity; TAS:Reactome.
DR   GO; GO:0002862; P:negative regulation of inflammatory response to antigenic stimulus; TAS:Reactome.
DR   GO; GO:0050709; P:negative regulation of protein secretion; ISS:UniProtKB.
DR   GO; GO:0072659; P:protein localization to plasma membrane; IEA:Ensembl.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0042058; P:regulation of epidermal growth factor receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:1904683; P:regulation of metalloendopeptidase activity; IEA:Ensembl.
DR   GO; GO:0050708; P:regulation of protein secretion; IBA:GO_Central.
DR   Gene3D; 1.20.1540.10; -; 1.
DR   InterPro; IPR022764; Peptidase_S54_rhomboid_dom.
DR   InterPro; IPR035952; Rhomboid-like_sf.
DR   InterPro; IPR022241; Rhomboid_SP.
DR   Pfam; PF01694; Rhomboid; 1.
DR   Pfam; PF12595; Rhomboid_SP; 1.
DR   SUPFAM; SSF144091; SSF144091; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell membrane; Disease variant;
KW   Endoplasmic reticulum; Growth factor binding; Membrane;
KW   Palmoplantar keratoderma; Phosphoprotein; Protein transport;
KW   Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..856
FT                   /note="Inactive rhomboid protein 2"
FT                   /id="PRO_0000341938"
FT   TOPO_DOM        1..409
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        410..430
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        431..660
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        661..681
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        682..692
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        693..713
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        714..715
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        716..736
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        737..747
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        748..768
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        769..773
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        774..794
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        795..802
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        803..823
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        824..856
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   REGION          1..115
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          165..184
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          191..271
FT                   /note="Involved in interaction with FRMD8"
FT                   /evidence="ECO:0000269|PubMed:29897333"
FT   REGION          531..553
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..26
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         90
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         113
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         117
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q80WQ6"
FT   MOD_RES         323
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q80WQ6"
FT   MOD_RES         325
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         328
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:23186163"
FT   VAR_SEQ         51..79
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.1"
FT                   /id="VSP_034368"
FT   VARIANT         186
FT                   /note="I -> T (in TOC; dbSNP:rs387907129)"
FT                   /evidence="ECO:0000269|PubMed:22265016"
FT                   /id="VAR_067827"
FT   VARIANT         189
FT                   /note="P -> L (in TOC; dbSNP:rs387907130)"
FT                   /evidence="ECO:0000269|PubMed:22265016"
FT                   /id="VAR_067828"
FT   VARIANT         208
FT                   /note="P -> L (in dbSNP:rs3744045)"
FT                   /evidence="ECO:0000269|PubMed:14702039,
FT                   ECO:0000269|PubMed:15489334, ECO:0000269|Ref.1"
FT                   /id="VAR_044125"
FT   VARIANT         249
FT                   /note="A -> T (in dbSNP:rs34814954)"
FT                   /id="VAR_044126"
FT   VARIANT         528
FT                   /note="D -> Y (in dbSNP:rs11553545)"
FT                   /id="VAR_044127"
FT   CONFLICT        67
FT                   /note="A -> S (in Ref. 2; BAF84824 and 4; AAH16034)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        705
FT                   /note="N -> D (in Ref. 2; BAF84855)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        852
FT                   /note="D -> G (in Ref. 2; BAF84855)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   856 AA;  96686 MW;  69C40A21EBDBDDC0 CRC64;
     MASADKNGGS VSSVSSSRLQ SRKPPNLSIT IPPPEKETQA PGEQDSMLPE GFQNRRLKKS
     QPRTWAAHTT ACPPSFLPKR KNPAYLKSVS LQEPRSRWQE SSEKRPGFRR QASLSQSIRK
     GAAQWFGVSG DWEGQRQQWQ RRSLHHCSMR YGRLKASCQR DLELPSQEAP SFQGTESPKP
     CKMPKIVDPL ARGRAFRHPE EMDRPHAPHP PLTPGVLSLT SFTSVRSGYS HLPRRKRMSV
     AHMSLQAAAA LLKGRSVLDA TGQRCRVVKR SFAFPSFLEE DVVDGADTFD SSFFSKEEMS
     SMPDDVFESP PLSASYFRGI PHSASPVSPD GVQIPLKEYG RAPVPGPRRG KRIASKVKHF
     AFDRKKRHYG LGVVGNWLNR SYRRSISSTV QRQLESFDSH RPYFTYWLTF VHVIITLLVI
     CTYGIAPVGF AQHVTTQLVL RNKGVYESVK YIQQENFWVG PSSIDLIHLG AKFSPCIRKD
     GQIEQLVLRE RDLERDSGCC VQNDHSGCIQ TQRKDCSETL ATFVKWQDDT GPPMDKSDLG
     QKRTSGAVCH QDPRTCEEPA SSGAHIWPDD ITKWPICTEQ ARSNHTGFLH MDCEIKGRPC
     CIGTKGSCEI TTREYCEFMH GYFHEEATLC SQVHCLDKVC GLLPFLNPEV PDQFYRLWLS
     LFLHAGVVHC LVSVVFQMTI LRDLEKLAGW HRIAIIFILS GITGNLASAI FLPYRAEVGP
     AGSQFGLLAC LFVELFQSWP LLERPWKAFL NLSAIVLFLF ICGLLPWIDN IAHIFGFLSG
     LLLAFAFLPY ITFGTSDKYR KRALILVSLL AFAGLFAALV LWLYIYPINW PWIEHLTCFP
     FTSRFCEKYE LDQVLH
 
 
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