HABP4_HUMAN
ID HABP4_HUMAN Reviewed; 413 AA.
AC Q5JVS0; O75804; Q8WV33; Q9NYJ2;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Intracellular hyaluronan-binding protein 4 {ECO:0000303|PubMed:10887182};
DE Short=IHABP-4 {ECO:0000303|PubMed:10887182};
DE Short=IHABP4 {ECO:0000303|PubMed:10887182};
DE AltName: Full=Hyaluronan-binding protein 4 {ECO:0000312|HGNC:HGNC:17062};
DE AltName: Full=Ki-1/57 intracellular antigen {ECO:0000303|PubMed:10887182, ECO:0000303|PubMed:28695742};
GN Name=HABP4 {ECO:0000312|HGNC:HGNC:17062};
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:0000305, ECO:0000312|EMBL:AAF62546.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=10887182; DOI=10.1074/jbc.m002737200;
RA Huang L., Grammatikakis N., Yoneda M., Banerjee S.D., Toole B.P.;
RT "Molecular characterization of a novel intracellular hyaluronan-binding
RT protein.";
RL J. Biol. Chem. 275:29829-29839(2000).
RN [2] {ECO:0000312|EMBL:AL133477}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [3] {ECO:0000305, ECO:0000312|EMBL:AAH18788.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain {ECO:0000312|EMBL:AAH18788.1};
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] {ECO:0000305, ECO:0000312|EMBL:AAC31117.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 115-413 (ISOFORM 1), SUBCELLULAR LOCATION,
RP AND TISSUE SPECIFICITY.
RX PubMed=9523163;
RA Kobarg J., Schnittger S., Fonatsch C., Lemke H., Bowen M.A., Buck F.,
RA Hansen H.P.;
RT "Characterization, mapping and partial cDNA sequence of the 57-kD
RT intracellular Ki-1 antigen.";
RL Exp. Clin. Immunogenet. 14:273-280(1997).
RN [5] {ECO:0000305}
RP INTERACTION WITH CHD3, AND TISSUE SPECIFICITY.
RX PubMed=12505151; DOI=10.1016/s0014-5793(02)03737-7;
RA Lemos T.A., Passos D.O., Nery F.C., Kobarg J.;
RT "Characterization of a new family of proteins that interact with the C-
RT terminal region of the chromatin-remodeling factor CHD-3.";
RL FEBS Lett. 533:14-20(2003).
RN [6] {ECO:0000305}
RP FUNCTION, INTERACTION WITH RACK1, SUBCELLULAR LOCATION, AND PHOSPHORYLATION
RP AT THR-354 AND THR-375.
RX PubMed=14699138; DOI=10.1074/jbc.m306672200;
RA Nery F.C., Passos D.O., Garcia V.S., Kobarg J.;
RT "Ki-1/57 interacts with RACK1 and is a substrate for the phosphorylation by
RT phorbol 12-myristate 13-acetate-activated protein kinase C.";
RL J. Biol. Chem. 279:11444-11455(2004).
RN [7]
RP INTERACTION WITH MEF2C.
RX PubMed=15862299; DOI=10.1016/j.febslet.2005.03.078;
RA Kobarg C.B., Kobarg J., Crosara-Alberto D.P., Theizen T.H., Franchini K.G.;
RT "MEF2C DNA-binding activity is inhibited through its interaction with the
RT regulatory protein Ki-1/57.";
RL FEBS Lett. 579:2615-2622(2005).
RN [8]
RP FUNCTION, INTERACTION WITH TP53, AND SUBCELLULAR LOCATION.
RX PubMed=16455055; DOI=10.1016/j.bbrc.2006.01.036;
RA Nery F.C., Rui E., Kuniyoshi T.M., Kobarg J.;
RT "Evidence for the interaction of the regulatory protein Ki-1/57 with p53
RT and its interacting proteins.";
RL Biochem. Biophys. Res. Commun. 341:847-855(2006).
RN [9]
RP METHYLATION BY PRMT1, INTERACTION WITH PRMT1, SUBCELLULAR LOCATION, AND
RP REGION.
RX PubMed=16879614; DOI=10.1111/j.1742-4658.2006.05399.x;
RA Passos D.O., Bressan G.C., Nery F.C., Kobarg J.;
RT "Ki-1/57 interacts with PRMT1 and is a substrate for arginine
RT methylation.";
RL FEBS J. 273:3946-3961(2006).
RN [10]
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 [11]
RP FUNCTION IN MRNA SPLICING, INTERACTION WITH SRSF9 AND SYNCRIP, AND
RP SUBCELLULAR LOCATION.
RX PubMed=19523114; DOI=10.1111/j.1742-4658.2009.07092.x;
RA Bressan G.C., Quaresma A.J., Moraes E.C., Manfiolli A.O., Passos D.O.,
RA Gomes M.D., Kobarg J.;
RT "Functional association of human Ki-1/57 with pre-mRNA splicing events.";
RL FEBS J. 276:3770-3783(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-74, AND IDENTIFICATION BY
RP 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 [13]
RP FUNCTION IN MRNA TRANSLATION, INTERACTION WITH FMR1; FXR1; FXR2 AND
RP POLYSOMES, AND SUBCELLULAR LOCATION.
RX PubMed=21771594; DOI=10.1016/j.febslet.2011.07.010;
RA Goncalves K.A., Bressan G.C., Saito A., Morello L.G., Zanchin N.I.,
RA Kobarg J.;
RT "Evidence for the association of the human regulatory protein Ki-1/57 with
RT the translational machinery.";
RL FEBS Lett. 585:2556-2560(2011).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108, AND IDENTIFICATION BY
RP 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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108, 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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108, AND IDENTIFICATION BY
RP 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 [17]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-70, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [18]
RP SUMOYLATION AT LYS-213; LYS-276 AND LYS-336, AND MUTAGENESIS OF LYS-213;
RP LYS-276 AND LYS-336.
RX PubMed=28695742; DOI=10.1021/acs.jproteome.7b00001;
RA Saito A., Souza E.E., Costa F.C., Meirelles G.V., Goncalves K.A.,
RA Santos M.T., Bressan G.C., McComb M.E., Costello C.E., Whelan S.A.,
RA Kobarg J.;
RT "Human Regulatory Protein Ki-1/57 Is a Target of SUMOylation and Affects
RT PML Nuclear Body Formation.";
RL J. Proteome Res. 16:3147-3157(2017).
CC -!- FUNCTION: RNA-binding protein that plays a role in the regulation of
CC transcription, pre-mRNA splicing and mRNA translation (PubMed:14699138,
CC PubMed:16455055, PubMed:19523114, PubMed:21771594). Negatively
CC regulates DNA-binding activity of the transcription factor MEF2C in
CC myocardial cells in response to mechanical stress (By similarity).
CC Plays a role in pre-mRNA splicing regulation (PubMed:19523114). Binds
CC (via C-terminus) to poly(U) RNA (PubMed:19523114). Involved in mRNA
CC translation regulation, probably at the initiation step
CC (PubMed:21771594). Seems to play a role in PML-nuclear bodies formation
CC (PubMed:28695742). {ECO:0000250|UniProtKB:A1L1K8,
CC ECO:0000269|PubMed:14699138, ECO:0000269|PubMed:16455055,
CC ECO:0000269|PubMed:19523114, ECO:0000269|PubMed:21771594,
CC ECO:0000269|PubMed:28695742}.
CC -!- SUBUNIT: Associates with polysomes (PubMed:21771594). Interacts with
CC FMR1 (PubMed:21771594). Interacts with FXR1 and FXR2 (PubMed:21771594).
CC Interacts with CHD3 (via C-terminus) (PubMed:12505151). Interacts (via
CC C-terminus) with RACK1 (PubMed:14699138). Interacts with p53/TP53
CC (PubMed:16455055). Interacts (via N-terminus) with SRSF9; this
CC interaction is direct (PubMed:19523114). Interacts with SYNCRIP; this
CC interaction is direct (PubMed:19523114). Interacts with MEF2C (via N-
CC terminus); this interaction decreases DNA-binding activity of MEF2C in
CC myocardial cells in response to mechanical stress (PubMed:15862299).
CC Interacts with PRMT1 (via N-terminus) (PubMed:16879614). Interacts with
CC SPIN1 (By similarity). {ECO:0000250|UniProtKB:Q9JKS5,
CC ECO:0000269|PubMed:12505151, ECO:0000269|PubMed:14699138,
CC ECO:0000269|PubMed:15862299, ECO:0000269|PubMed:16455055,
CC ECO:0000269|PubMed:16879614, ECO:0000269|PubMed:19523114,
CC ECO:0000269|PubMed:21771594, ECO:0000305|PubMed:21771594}.
CC -!- INTERACTION:
CC Q5JVS0; Q99873: PRMT1; NbExp=2; IntAct=EBI-523625, EBI-78738;
CC Q5JVS0; Q13242: SRSF9; NbExp=2; IntAct=EBI-523625, EBI-2949710;
CC Q5JVS0; O60506: SYNCRIP; NbExp=2; IntAct=EBI-523625, EBI-1024357;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14699138,
CC ECO:0000269|PubMed:16455055, ECO:0000269|PubMed:16879614,
CC ECO:0000269|PubMed:19523114, ECO:0000269|PubMed:9523163}. Cytoplasm
CC {ECO:0000269|PubMed:14699138, ECO:0000269|PubMed:16455055,
CC ECO:0000269|PubMed:16879614, ECO:0000269|PubMed:19523114,
CC ECO:0000269|PubMed:9523163}. Cytoplasm, Stress granule
CC {ECO:0000269|PubMed:21771594}. Cytoplasm, sarcoplasm
CC {ECO:0000250|UniProtKB:A1L1K8}. Nucleus, nuclear body
CC {ECO:0000269|PubMed:19523114}. Nucleus, nucleolus
CC {ECO:0000269|PubMed:19523114}. Nucleus speckle
CC {ECO:0000269|PubMed:19523114}. Nucleus, Cajal body
CC {ECO:0000269|PubMed:19523114}. Nucleus, gem
CC {ECO:0000269|PubMed:19523114}. Note=Transported into the nuclear
CC compartment in activated leukocytes (PubMed:9523163). Inhibition of
CC methylation alters its distribution between the nuclear and cytoplasmic
CC compartments (PubMed:16879614, PubMed:19523114). Methylation may be
CC required for its localization in subnuclear structures, such as
CC nucleoli, nuclear speckles, Cajal bodies and Gemini of coiled bodies
CC (gems) (PubMed:19523114). Colocalizes with FMR1, FXR1 and FXR2 in
CC cytoplasmic stress granules (PubMed:21771594). In myocardial cells,
CC localization at the sarcoplasm is reduced in response to mechanical
CC stress (By similarity). {ECO:0000250|UniProtKB:A1L1K8,
CC ECO:0000269|PubMed:16879614, ECO:0000269|PubMed:19523114,
CC ECO:0000269|PubMed:21771594, ECO:0000269|PubMed:9523163}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000269|PubMed:10887182, ECO:0000269|PubMed:9523163};
CC IsoId=Q5JVS0-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:15489334};
CC IsoId=Q5JVS0-2; Sequence=VSP_052194;
CC -!- TISSUE SPECIFICITY: Highly expressed in brain, heart, and kidney, and
CC moderately expressed in skeletal muscle. Also expressed in a variety of
CC tumor cell lines and in activated but not resting leukocytes.
CC {ECO:0000269|PubMed:12505151, ECO:0000269|PubMed:9523163}.
CC -!- DOMAIN: The C-terminal region is necessary for nucleus and cytoplasmic
CC localization (PubMed:19523114). The N-terminal region is necessary for
CC nucleus and nuclear bodies localization (PubMed:19523114). Regions
CC containing Arg-Gly-Gly repeats (RGG/RXR-box) may be preferentially
CC methylated by PRMT1 (PubMed:16879614). {ECO:0000269|PubMed:16879614,
CC ECO:0000269|PubMed:19523114}.
CC -!- PTM: Methylated (PubMed:16879614). Methylation is decreased by phorbol
CC 12-myristate 13-acetate (PMA)-activated PKC, in vitro
CC (PubMed:16879614). {ECO:0000269|PubMed:16879614}.
CC -!- PTM: Phosphorylated by phorbol 12-myristate 13-acetate (PMA)-activated
CC PKC isoforms at Thr-354 and Thr-375. {ECO:0000269|PubMed:14699138}.
CC -!- MISCELLANEOUS: Able to bind hyaluronan. However, its intracellular
CC localization suggests that this interaction may not be relevant in
CC vivo. {ECO:0000305}.
CC -!- MISCELLANEOUS: The interaction with RACK1 is abolished upon activation
CC of L540 tumor cells with PMA, which results in phosphorylation and exit
CC of HABP4 from the nucleus. {ECO:0000269|PubMed:14699138}.
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DR EMBL; AF241831; AAF62546.1; -; mRNA.
DR EMBL; AL133477; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC018788; AAH18788.1; -; mRNA.
DR EMBL; U77327; AAC31117.1; -; mRNA.
DR CCDS; CCDS6719.1; -. [Q5JVS0-1]
DR RefSeq; NP_055097.2; NM_014282.3. [Q5JVS0-1]
DR AlphaFoldDB; Q5JVS0; -.
DR BioGRID; 116587; 151.
DR IntAct; Q5JVS0; 28.
DR MINT; Q5JVS0; -.
DR STRING; 9606.ENSP00000364398; -.
DR DrugBank; DB08818; Hyaluronic acid.
DR iPTMnet; Q5JVS0; -.
DR PhosphoSitePlus; Q5JVS0; -.
DR BioMuta; HABP4; -.
DR DMDM; 74742472; -.
DR EPD; Q5JVS0; -.
DR jPOST; Q5JVS0; -.
DR MassIVE; Q5JVS0; -.
DR MaxQB; Q5JVS0; -.
DR PaxDb; Q5JVS0; -.
DR PeptideAtlas; Q5JVS0; -.
DR PRIDE; Q5JVS0; -.
DR ProteomicsDB; 63346; -. [Q5JVS0-1]
DR ProteomicsDB; 63347; -. [Q5JVS0-2]
DR Antibodypedia; 55498; 57 antibodies from 13 providers.
DR DNASU; 22927; -.
DR Ensembl; ENST00000375249.5; ENSP00000364398.4; ENSG00000130956.14. [Q5JVS0-1]
DR Ensembl; ENST00000375251.7; ENSP00000364400.3; ENSG00000130956.14. [Q5JVS0-2]
DR GeneID; 22927; -.
DR KEGG; hsa:22927; -.
DR MANE-Select; ENST00000375249.5; ENSP00000364398.4; NM_014282.4; NP_055097.2.
DR UCSC; uc010msg.5; human. [Q5JVS0-1]
DR CTD; 22927; -.
DR DisGeNET; 22927; -.
DR GeneCards; HABP4; -.
DR HGNC; HGNC:17062; HABP4.
DR HPA; ENSG00000130956; Tissue enhanced (brain).
DR MIM; 617369; gene.
DR neXtProt; NX_Q5JVS0; -.
DR OpenTargets; ENSG00000130956; -.
DR PharmGKB; PA38434; -.
DR VEuPathDB; HostDB:ENSG00000130956; -.
DR eggNOG; KOG2945; Eukaryota.
DR GeneTree; ENSGT00520000055591; -.
DR HOGENOM; CLU_037366_0_0_1; -.
DR InParanoid; Q5JVS0; -.
DR OMA; FNIRQAG; -.
DR OrthoDB; 1183388at2759; -.
DR PhylomeDB; Q5JVS0; -.
DR TreeFam; TF318374; -.
DR PathwayCommons; Q5JVS0; -.
DR Reactome; R-HSA-114608; Platelet degranulation.
DR SignaLink; Q5JVS0; -.
DR SIGNOR; Q5JVS0; -.
DR BioGRID-ORCS; 22927; 9 hits in 1078 CRISPR screens.
DR ChiTaRS; HABP4; human.
DR GeneWiki; HABP4; -.
DR GenomeRNAi; 22927; -.
DR Pharos; Q5JVS0; Tbio.
DR PRO; PR:Q5JVS0; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q5JVS0; protein.
DR Bgee; ENSG00000130956; Expressed in endothelial cell and 194 other tissues.
DR Genevisible; Q5JVS0; HS.
DR GO; GO:0015030; C:Cajal body; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0010494; C:cytoplasmic stress granule; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0097504; C:Gemini of coiled bodies; IDA:UniProtKB.
DR GO; GO:0031965; C:nuclear membrane; IDA:HPA.
DR GO; GO:0016607; C:nuclear speck; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0030017; C:sarcomere; ISS:UniProtKB.
DR GO; GO:0016528; C:sarcoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0032183; F:SUMO binding; IDA:UniProtKB.
DR GO; GO:0071260; P:cellular response to mechanical stimulus; ISS:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0043392; P:negative regulation of DNA binding; IDA:UniProtKB.
DR GO; GO:0030578; P:PML body organization; IDA:UniProtKB.
DR GO; GO:0033120; P:positive regulation of RNA splicing; IMP:UniProtKB.
DR GO; GO:0045948; P:positive regulation of translational initiation; IMP:UniProtKB.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR InterPro; IPR039764; HABP4/SERBP1.
DR InterPro; IPR006861; HABP4_PAIRBP1-bd.
DR InterPro; IPR032381; IHABP4_N.
DR PANTHER; PTHR12299; PTHR12299; 1.
DR Pfam; PF04774; HABP4_PAI-RBP1; 1.
DR Pfam; PF16174; IHABP4_N; 1.
DR SMART; SM01233; HABP4_PAI-RBP1; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Cytoplasm; Isopeptide bond; Methylation;
KW mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW Reference proteome; RNA-binding; Transcription; Transcription regulation;
KW Translation regulation; Ubl conjugation.
FT CHAIN 1..413
FT /note="Intracellular hyaluronan-binding protein 4"
FT /id="PRO_0000257972"
FT REGION 42..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 227..320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 360..413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 40..64
FT /evidence="ECO:0000255"
FT COMPBIAS 42..63
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 137..186
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..311
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 7
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JKS5"
FT MOD_RES 36
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JKS5"
FT MOD_RES 70
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 74
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 108
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 354
FT /note="Phosphothreonine; by PKC"
FT /evidence="ECO:0000305|PubMed:14699138"
FT MOD_RES 375
FT /note="Phosphothreonine; by PKC"
FT /evidence="ECO:0000305|PubMed:14699138"
FT CROSSLNK 213
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000269|PubMed:28695742"
FT CROSSLNK 213
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000269|PubMed:28695742"
FT CROSSLNK 276
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000269|PubMed:28695742"
FT CROSSLNK 276
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000269|PubMed:28695742"
FT CROSSLNK 336
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000269|PubMed:28695742"
FT CROSSLNK 336
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000269|PubMed:28695742"
FT VAR_SEQ 172..276
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_052194"
FT MUTAGEN 213
FT /note="K->R: Decreases sumoylation; when associated with R-
FT 336. Abolishes sumoylation; when associated with R-276 and
FT R-336."
FT /evidence="ECO:0000269|PubMed:28695742"
FT MUTAGEN 276
FT /note="K->R: Decreases sumoylation; when associated with R-
FT 336. Abolishes sumoylation; when associated with R-213 and
FT R-336."
FT /evidence="ECO:0000269|PubMed:28695742"
FT MUTAGEN 336
FT /note="K->R: Decreases sumoylation; when associated with R-
FT 213 or R-276. Abolishes sumoylation; when associated with
FT R-213 and R-276."
FT /evidence="ECO:0000269|PubMed:28695742"
FT CONFLICT 104
FT /note="Q -> H (in Ref. 1; AAF62546)"
FT /evidence="ECO:0000305"
FT CONFLICT 115
FT /note="A -> S (in Ref. 4; AAC31117)"
FT /evidence="ECO:0000305"
FT CONFLICT 388..389
FT /note="YG -> NY (in Ref. 1; AAF62546 and 4; AAC31117)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 413 AA; 45785 MW; 98749EEC5CB92155 CRC64;
MKGALGSPVA AAGAAMQESF GCVVANRFHQ LLDDESDPFD ILREAERRRQ QQLQRKRRDE
AAAAAGAGPR GGRSPAGASG HRAGAGGRRE SQKERKSLPA PVAQRPDSPG GGLQAPGQKR
TPRRGEQQGW NDSRGPEGML ERAERRSYRE YRPYETERQA DFTAEKFPDE KPGDRFDRDR
PLRGRGGPRG GMRGRGRGGP GNRVFDAFDQ RGKREFERYG GNDKIAVRTE DNMGGCGVRT
WGSGKDTSDV EPTAPMEEPT VVEESQGTPE EESPAKVPEL EVEEETQVQE MTLDEWKNLQ
EQTRPKPEFN IRKPESTVPS KAVVIHKSKY RDDMVKDDYE DDSHVFRKPA NDITSQLEIN
FGNLPRPGRG ARGGTRGGRG RIRRAENYGP RAEVVMQDVA PNPDDPEDFP ALS
