HAVR1_HUMAN
ID HAVR1_HUMAN Reviewed; 364 AA.
AC Q96D42; O43656;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 10-APR-2019, sequence version 3.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Hepatitis A virus cellular receptor 1;
DE Short=HAVcr-1;
DE AltName: Full=Kidney injury molecule 1;
DE Short=KIM-1;
DE AltName: Full=T-cell immunoglobulin and mucin domain-containing protein 1;
DE Short=TIMD-1;
DE AltName: Full=T-cell immunoglobulin mucin receptor 1;
DE Short=TIM;
DE Short=TIM-1;
DE AltName: Full=T-cell membrane protein 1;
DE AltName: CD_antigen=CD365;
DE Flags: Precursor;
GN Name=HAVCR1; Synonyms=KIM1, TIM1, TIMD1;
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], TISSUE SPECIFICITY, FUNCTION (MICROBIAL
RP INFECTION), INTERACTION WITH HEPATITIS A VIRUS CAPSID PROTEINS (MICROBIAL
RP INFECTION), AND VARIANT 157-PRO--VAL-161 DEL.
RC TISSUE=Liver;
RX PubMed=9658108; DOI=10.1128/jvi.72.8.6621-6628.1998;
RA Feigelstock D., Thompson P., Mattoo P., Zhang Y., Kaplan G.G.;
RT "The human homolog of HAVcr-1 codes for a hepatitis A virus cellular
RT receptor.";
RL J. Virol. 72:6621-6628(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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 INTERACTION WITH IMMUNOGLUBULIN A.
RX PubMed=17229699; DOI=10.1128/jvi.01585-06;
RA Tami C., Silberstein E., Manangeeswaran M., Freeman G.J., Umetsu S.E.,
RA DeKruyff R.H., Umetsu D.T., Kaplan G.G.;
RT "Immunoglobulin A (IgA) is a natural ligand of hepatitis A virus cellular
RT receptor 1 (HAVCR1), and the association of IgA with HAVCR1 enhances virus-
RT receptor interactions.";
RL J. Virol. 81:3437-3446(2007).
RN [6]
RP FUNCTION, AND INDUCTION.
RX PubMed=17471468; DOI=10.1002/path.2175;
RA van Timmeren M.M., van den Heuvel M.C., Bailly V., Bakker S.J.,
RA van Goor H., Stegeman C.A.;
RT "Tubular kidney injury molecule-1 (KIM-1) in human renal disease.";
RL J. Pathol. 212:209-217(2007).
RN [7]
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 [8]
RP FUNCTION (MICROBIAL INFECTION).
RX PubMed=21536871; DOI=10.1073/pnas.1019030108;
RA Kondratowicz A.S., Lennemann N.J., Sinn P.L., Davey R.A., Hunt C.L.,
RA Moller-Tank S., Meyerholz D.K., Rennert P., Mullins R.F., Brindley M.,
RA Sandersfeld L.M., Quinn K., Weller M., McCray P.B. Jr., Chiorini J.,
RA Maury W.;
RT "T-cell immunoglobulin and mucin domain 1 (TIM-1) is a receptor for Zaire
RT Ebolavirus and Lake Victoria Marburgvirus.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:8426-8431(2011).
RN [9]
RP FUNCTION (MICROBIAL INFECTION).
RX PubMed=23084921; DOI=10.1016/j.chom.2012.08.009;
RA Meertens L., Carnec X., Lecoin M.P., Ramdasi R., Guivel-Benhassine F.,
RA Lew E., Lemke G., Schwartz O., Amara A.;
RT "The TIM and TAM families of phosphatidylserine receptors mediate dengue
RT virus entry.";
RL Cell Host Microbe 12:544-557(2012).
RN [10]
RP FUNCTION, AND INTERACTION WITH SELPLG.
RX PubMed=24703780; DOI=10.1016/j.immuni.2014.03.004;
RA Angiari S., Donnarumma T., Rossi B., Dusi S., Pietronigro E., Zenaro E.,
RA Della Bianca V., Toffali L., Piacentino G., Budui S., Rennert P., Xiao S.,
RA Laudanna C., Casasnovas J.M., Kuchroo V.K., Constantin G.;
RT "TIM-1 glycoprotein binds the adhesion receptor P-selectin and mediates T
RT cell trafficking during inflammation and autoimmunity.";
RL Immunity 40:542-553(2014).
RN [11]
RP FUNCTION (MICROBIAL INFECTION).
RX PubMed=29437974; DOI=10.1128/jvi.02065-17;
RA Costafreda M.I., Kaplan G.;
RT "HAVCR1 (CD365) and its mouse ortholog are functional hepatitis A virus
RT (HAV) cellular receptors that mediate HAV infection.";
RL J. Virol. 92:0-0(2018).
RN [12]
RP FUNCTION (MICROBIAL INFECTION), UBIQUITINATION AT LYS-338 AND LYS-346,
RP INTERACTION WITH STAM, MUTAGENESIS OF LYS-338 AND LYS-346, AND SUBCELLULAR
RP LOCATION.
RX PubMed=29742433; DOI=10.1016/j.celrep.2018.04.013;
RA Dejarnac O., Hafirassou M.L., Chazal M., Versapuech M., Gaillard J.,
RA Perera-Lecoin M., Umana-Diaz C., Bonnet-Madin L., Carnec X., Tinevez J.Y.,
RA Delaugerre C., Schwartz O., Roingeard P., Jouvenet N., Berlioz-Torrent C.,
RA Meertens L., Amara A.;
RT "TIM-1 Ubiquitination Mediates Dengue Virus Entry.";
RL Cell Rep. 23:1779-1793(2018).
RN [13]
RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH ZIKA VIRUS ENVELOPE
RP PROTEIN E (MICROBIAL INFECTION).
RX PubMed=32641828; DOI=10.1038/s41586-020-2457-8;
RA Giraldo M.I., Xia H., Aguilera-Aguirre L., Hage A., van Tol S., Shan C.,
RA Xie X., Sturdevant G.L., Robertson S.J., McNally K.L., Meade-White K.,
RA Azar S.R., Rossi S.L., Maury W., Woodson M., Ramage H., Johnson J.R.,
RA Krogan N.J., Morais M.C., Best S.M., Shi P.Y., Rajsbaum R.;
RT "Envelope protein ubiquitination drives entry and pathogenesis of Zika
RT virus.";
RL Nature 585:414-419(2020).
RN [14]
RP FUNCTION (MICROBIAL INFECTION), AND MUTAGENESIS OF ASN-114 AND ASP-115.
RX PubMed=34359995; DOI=10.3390/cells10071828;
RA Kirui J., Abidine Y., Lenman A., Islam K., Gwon Y.D., Lasswitz L.,
RA Evander M., Bally M., Gerold G.;
RT "The Phosphatidylserine Receptor TIM-1 Enhances Authentic Chikungunya Virus
RT Cell Entry.";
RL Cells 10:0-0(2021).
RN [15]
RP POLYMORPHISM, AND VARIANTS 157-PRO--VAL-161 DEL AND THR-200 DEL.
RX PubMed=14534576; DOI=10.1038/425576a;
RA McIntire J.J., Umetsu S.E., Macaubas C., Hoyte E.G., Cinnioglu C.,
RA Cavalli-Sforza L.L., Barsh G.S., Hallmayer J.F., Underhill P.A.,
RA Risch N.J., Freeman G.J., DeKruyff R.H., Umetsu D.T.;
RT "Hepatitis A virus link to atopic disease.";
RL Nature 425:576-576(2003).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (1.30 ANGSTROMS) OF 22-127, FUNCTION (MICROBIAL
RP INFECTION), INTERACTION WITH EBOLAVIRUS GP PROTEIN (MICROBIAL INFECTION),
RP AND DISULFIDE BOND.
RX PubMed=26487564; DOI=10.1007/s13238-015-0220-y;
RA Yuan S., Cao L., Ling H., Dang M., Sun Y., Zhang X., Chen Y., Zhang L.,
RA Su D., Wang X., Rao Z.;
RT "TIM-1 acts a dual-attachment receptor for Ebolavirus by interacting
RT directly with viral GP and the PS on the viral envelope.";
RL Protein Cell 6:814-824(2015).
CC -!- FUNCTION: Phosphatidylserine receptor that plays an important
CC functional role in regulatory B-cells homeostasis including generation,
CC expansion and suppressor functions (By similarity). As P-
CC selectin/SELPLG ligand, plays a specialized role in activated but not
CC naive T-cell trafficking during inflammatory responses
CC (PubMed:24703780). Controls thereby T-cell accumulation in the inflamed
CC central nervous system (CNS) and the induction of autoimmune disease
CC (PubMed:24703780). Regulates also expression of various anti-
CC inflammatory cytokines and co-inhibitory ligands including IL10 (By
CC similarity). Acts as regulator of T-cell proliferation (By similarity).
CC May play a role in kidney injury and repair (PubMed:17471468).
CC {ECO:0000250|UniProtKB:Q5QNS5, ECO:0000269|PubMed:17471468,
CC ECO:0000269|PubMed:24703780}.
CC -!- FUNCTION: (Microbial infection) Acts as a receptor for Hepatitis A
CC virus. {ECO:0000269|PubMed:29437974, ECO:0000269|PubMed:9658108}.
CC -!- FUNCTION: (Microbial infection) Acts as a receptor for Ebolavirus and
CC Marburg virus by binding exposed phosphatidyl-serine at the surface of
CC virion membrane (PubMed:21536871). Serves as a dual receptor for
CC Ebolavirus by also interacting with envelope glycoprotein GP
CC (PubMed:26487564). {ECO:0000269|PubMed:21536871,
CC ECO:0000269|PubMed:26487564}.
CC -!- FUNCTION: (Microbial infection) Acts as a receptor for Dengue virus by
CC binding exposed phosphatidyl-serine at the surface of virion membrane
CC (PubMed:23084921). TIM1 and Dengue virus are co-internalized during
CC virus entry (PubMed:29742433). {ECO:0000269|PubMed:23084921,
CC ECO:0000269|PubMed:29742433}.
CC -!- FUNCTION: (Microbial infection) Acts as a receptor for Zika virus by
CC binding to envelope protein E. {ECO:0000269|PubMed:32641828}.
CC -!- FUNCTION: (Microbial infection) Plays a positive role in Chikungunya
CC virus cell entry. {ECO:0000269|PubMed:34359995}.
CC -!- SUBUNIT: Interacts with STAM (PubMed:29742433). Interacts with SELPLG
CC (PubMed:24703780). {ECO:0000269|PubMed:24703780,
CC ECO:0000269|PubMed:29742433}.
CC -!- SUBUNIT: (Microbial infection) Interacts with hepatitis A virus capsid
CC proteins. {ECO:0000269|PubMed:29437974, ECO:0000269|PubMed:9658108}.
CC -!- SUBUNIT: (Microbial infection) Interacts with Ebolavirus envelope
CC glycoprotein GP. {ECO:0000269|PubMed:26487564}.
CC -!- SUBUNIT: (Microbial infection) Interacts with Zika virus envelope
CC protein E. {ECO:0000269|PubMed:26487564}.
CC -!- INTERACTION:
CC Q96D42; P0DTC2: S; Xeno; NbExp=7; IntAct=EBI-953786, EBI-25474821;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:29742433};
CC Single-pass type I membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Widely expressed, with highest levels in kidney and
CC testis. Expressed by activated CD4+ T-cells during the development of
CC helper T-cells responses. {ECO:0000269|PubMed:9658108}.
CC -!- INDUCTION: Up-regulated in the kidney in renal diseases (at protein
CC level). {ECO:0000269|PubMed:17471468}.
CC -!- PTM: Ubiquitinated at two lysine residues Lys-338 and Lys-346 on its
CC cytoplasmic domain. Ubiquitination promotes receptor endocytosis and
CC target receptors for lysosomal degradation and termination of receptor
CC signaling. {ECO:0000269|PubMed:29742433}.
CC -!- PTM: (Microbial infection) Ubiquitination is required for Dengue virus
CC endocytosis. {ECO:0000269|PubMed:29742433}.
CC -!- POLYMORPHISM: The region containing tandem repeats is polymorphic and
CC the sequence shown here corresponds to the most common allele
CC (PubMed:14534576). An association between hepatitis A virus (HAV)
CC infection and atopic diseases has been observed in individuals with
CC that allele (PubMed:14534576). Allelic variation does not affect HAV-
CC infection rates in Caucasians, Asians and African Americans
CC (PubMed:14534576). {ECO:0000269|PubMed:14534576}.
CC -!- MISCELLANEOUS: The extracellular part of the protein can be cleaved and
CC detected in urine and is in correlation with the expression in the
CC kidney.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. TIM family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF043724; AAC39862.1; -; mRNA.
DR EMBL; CR457114; CAG33395.1; -; mRNA.
DR EMBL; AC026777; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC013325; AAH13325.1; -; mRNA.
DR CCDS; CCDS43392.1; -.
DR RefSeq; NP_001166864.1; NM_001173393.2.
DR RefSeq; NP_001295085.1; NM_001308156.1.
DR RefSeq; NP_036338.2; NM_012206.3.
DR PDB; 5DZO; X-ray; 1.30 A; A=22-127.
DR PDB; 5F70; X-ray; 1.80 A; A=21-123.
DR PDBsum; 5DZO; -.
DR PDBsum; 5F70; -.
DR AlphaFoldDB; Q96D42; -.
DR SMR; Q96D42; -.
DR BioGRID; 117812; 29.
DR IntAct; Q96D42; 5.
DR STRING; 9606.ENSP00000344844; -.
DR GlyGen; Q96D42; 5 sites, 1 O-linked glycan (1 site).
DR iPTMnet; Q96D42; -.
DR PhosphoSitePlus; Q96D42; -.
DR BioMuta; HAVCR1; -.
DR DMDM; 73919877; -.
DR jPOST; Q96D42; -.
DR MassIVE; Q96D42; -.
DR MaxQB; Q96D42; -.
DR PaxDb; Q96D42; -.
DR PeptideAtlas; Q96D42; -.
DR PRIDE; Q96D42; -.
DR ProteomicsDB; 76250; -.
DR Antibodypedia; 2353; 1014 antibodies from 37 providers.
DR DNASU; 26762; -.
DR Ensembl; ENST00000339252.7; ENSP00000344844.3; ENSG00000113249.13.
DR Ensembl; ENST00000523175.6; ENSP00000427898.1; ENSG00000113249.13.
DR GeneID; 26762; -.
DR KEGG; hsa:26762; -.
DR MANE-Select; ENST00000523175.6; ENSP00000427898.1; NM_001173393.3; NP_001166864.1.
DR UCSC; uc003lwi.3; human.
DR CTD; 26762; -.
DR DisGeNET; 26762; -.
DR GeneCards; HAVCR1; -.
DR HGNC; HGNC:17866; HAVCR1.
DR HPA; ENSG00000113249; Group enriched (intestine, kidney).
DR MIM; 606518; gene.
DR neXtProt; NX_Q96D42; -.
DR OpenTargets; ENSG00000113249; -.
DR PharmGKB; PA134924567; -.
DR VEuPathDB; HostDB:ENSG00000113249; -.
DR eggNOG; ENOG502S454; Eukaryota.
DR GeneTree; ENSGT00940000159345; -.
DR HOGENOM; CLU_047504_2_1_1; -.
DR InParanoid; Q96D42; -.
DR OMA; CRYNGAI; -.
DR PhylomeDB; Q96D42; -.
DR TreeFam; TF336163; -.
DR PathwayCommons; Q96D42; -.
DR SignaLink; Q96D42; -.
DR BioGRID-ORCS; 26762; 12 hits in 1064 CRISPR screens.
DR ChiTaRS; HAVCR1; human.
DR GeneWiki; HAVCR1; -.
DR GenomeRNAi; 26762; -.
DR Pharos; Q96D42; Tbio.
DR PRO; PR:Q96D42; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q96D42; protein.
DR Bgee; ENSG00000113249; Expressed in adult mammalian kidney and 87 other tissues.
DR ExpressionAtlas; Q96D42; baseline and differential.
DR Genevisible; Q96D42; HS.
DR GO; GO:0009986; C:cell surface; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031514; C:motile cilium; IDA:CACAO.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0001786; F:phosphatidylserine binding; IBA:GO_Central.
DR GO; GO:0001618; F:virus receptor activity; IDA:CACAO.
DR GO; GO:0006911; P:phagocytosis, engulfment; IBA:GO_Central.
DR GO; GO:0033005; P:positive regulation of mast cell activation; IBA:GO_Central.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003006; Ig/MHC_CS.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR013106; Ig_V-set.
DR Pfam; PF07686; V-set; 1.
DR SMART; SM00409; IG; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS00290; IG_MHC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Disulfide bond; Glycoprotein;
KW Host cell receptor for virus entry; Host-virus interaction;
KW Immunoglobulin domain; Isopeptide bond; Membrane; Receptor;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix;
KW Ubl conjugation.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..364
FT /note="Hepatitis A virus cellular receptor 1"
FT /id="PRO_0000014981"
FT TOPO_DOM 21..295
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 296..316
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 317..364
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 21..121
FT /note="Ig-like V-type"
FT REPEAT 138..143
FT /note="1"
FT REPEAT 144..149
FT /note="2"
FT REPEAT 150..155
FT /note="3"
FT REPEAT 156..160
FT /note="4"
FT REPEAT 161..165
FT /note="5"
FT REPEAT 166..171
FT /note="6"
FT REPEAT 172..177
FT /note="7"
FT REPEAT 178..183
FT /note="8"
FT REPEAT 184..189
FT /note="9"
FT REPEAT 190..195
FT /note="10"
FT REPEAT 196..201
FT /note="11"
FT REPEAT 202..207
FT /note="12"
FT REGION 138..207
FT /note="12 X 6 AA approximate tandem repeats of V-P-T-T-T-
FT T]"
FT REGION 216..257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 223..257
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 65
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 263
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 277
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 291
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 36..105
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:26487564, ECO:0007744|PDB:5DZO"
FT DISULFID 46..57
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:26487564, ECO:0007744|PDB:5DZO"
FT DISULFID 52..104
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:26487564, ECO:0007744|PDB:5DZO"
FT CROSSLNK 338
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:29742433"
FT CROSSLNK 346
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:29742433"
FT VARIANT 51
FT /note="S -> L (in dbSNP:rs2270922)"
FT /id="VAR_056080"
FT VARIANT 157..161
FT /note="Missing"
FT /evidence="ECO:0000269|PubMed:14534576,
FT ECO:0000269|PubMed:9658108"
FT /id="VAR_081334"
FT VARIANT 200
FT /note="Missing"
FT /evidence="ECO:0000269|PubMed:14534576"
FT /id="VAR_023323"
FT MUTAGEN 114
FT /note="N->A: About 60% loss of Chikungunya virus entry."
FT /evidence="ECO:0000269|PubMed:34359995"
FT MUTAGEN 115
FT /note="D->A: About 25% loss of Chikungunya virus entry."
FT /evidence="ECO:0000269|PubMed:34359995"
FT MUTAGEN 338
FT /note="K->R: About 50% loss of ubiquitination."
FT /evidence="ECO:0000269|PubMed:29742433"
FT MUTAGEN 338
FT /note="K->R: Complete loss of ubiquitination; when
FT associated with R-346."
FT /evidence="ECO:0000269|PubMed:29742433"
FT MUTAGEN 346
FT /note="K->R: About 50% loss of ubiquitination."
FT /evidence="ECO:0000269|PubMed:29742433"
FT MUTAGEN 346
FT /note="K->R: Complete loss of ubiquitination; when
FT associated with R-338."
FT /evidence="ECO:0000269|PubMed:29742433"
FT CONFLICT 179
FT /note="L -> P (in Ref. 1; AAC39862)"
FT /evidence="ECO:0000305"
FT STRAND 22..30
FT /evidence="ECO:0007829|PDB:5DZO"
FT STRAND 32..34
FT /evidence="ECO:0007829|PDB:5DZO"
FT STRAND 45..50
FT /evidence="ECO:0007829|PDB:5DZO"
FT TURN 56..59
FT /evidence="ECO:0007829|PDB:5DZO"
FT STRAND 60..64
FT /evidence="ECO:0007829|PDB:5DZO"
FT STRAND 66..74
FT /evidence="ECO:0007829|PDB:5DZO"
FT HELIX 83..85
FT /evidence="ECO:0007829|PDB:5DZO"
FT STRAND 90..94
FT /evidence="ECO:0007829|PDB:5DZO"
FT HELIX 97..99
FT /evidence="ECO:0007829|PDB:5DZO"
FT STRAND 101..107
FT /evidence="ECO:0007829|PDB:5DZO"
FT STRAND 110..113
FT /evidence="ECO:0007829|PDB:5DZO"
FT STRAND 116..125
FT /evidence="ECO:0007829|PDB:5DZO"
SQ SEQUENCE 364 AA; 39250 MW; AA67C7DC7FAC81F1 CRC64;
MHPQVVILSL ILHLADSVAG SVKVGGEAGP SVTLPCHYSG AVTSMCWNRG SCSLFTCQNG
IVWTNGTHVT YRKDTRYKLL GDLSRRDVSL TIENTAVSDS GVYCCRVEHR GWFNDMKITV
SLEIVPPKVT TTPIVTTVPT VTTVRTSTTV PTTTTVPMTT VPTTTVPTTM SIPTTTTVLT
TMTVSTTTSV PTTTSIPTTT SVPVTTTVST FVPPMPLPRQ NHEPVATSPS SPQPAETHPT
TLQGAIRREP TSSPLYSYTT DGNDTVTESS DGLWNNNQTQ LFLEHSLLTA NTTKGIYAGV
CISVLVLLAL LGVIIAKKYF FKKEVQQLSV SFSSLQIKAL QNAVEKEVQA EDNIYIENSL
YATD
