HABP4_MOUSE
ID HABP4_MOUSE Reviewed; 411 AA.
AC Q9JKS5; Q3UNH8; Q9D450;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 116.
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=Hyaluronic acid-binding protein 4 {ECO:0000312|MGI:MGI:1891713};
GN Name=Habp4 {ECO:0000312|MGI:MGI:1891713};
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] {ECO:0000305, ECO:0000312|EMBL:AAF36966.1}
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
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:0000305, ECO:0000312|EMBL:BAE25769.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAB30437.1};
RC TISSUE=Testis {ECO:0000312|EMBL:BAB30437.1};
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [4]
RP INTERACTION WITH SRSF9.
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7 AND SER-36, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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).
RN [6]
RP INTERACTION WITH SPIN1.
RX PubMed=23894536; DOI=10.1371/journal.pone.0069764;
RA Chew T.G., Peaston A., Lim A.K., Lorthongpanich C., Knowles B.B.,
RA Solter D.;
RT "A tudor domain protein SPINDLIN1 interacts with the mRNA-binding protein
RT SERBP1 and is involved in mouse oocyte meiotic resumption.";
RL PLoS ONE 8:E69764-E69764(2013).
CC -!- FUNCTION: RNA-binding protein that plays a role in the regulation of
CC transcription, pre-mRNA splicing and mRNA translation. Negatively
CC regulates DNA-binding activity of the transcription factor MEF2C in
CC myocardial cells in response to mechanical stress. Plays a role in pre-
CC mRNA splicing regulation. Binds (via C-terminus) to poly(U) RNA.
CC Involved in mRNA translation regulation, probably at the initiation
CC step. Seems to play a role in PML-nuclear bodies formation (By
CC similarity). {ECO:0000250|UniProtKB:A1L1K8,
CC ECO:0000250|UniProtKB:Q5JVS0}.
CC -!- SUBUNIT: Associates with polysomes. Interacts with FMR1. Interacts with
CC FXR1 and FXR2. Interacts with CHD3 (via C-terminus). Interacts (via C-
CC terminus) with RACK1. Interacts with p53/TP53 (By similarity).
CC Interacts (via N-terminus) with SRSF9; this interaction is direct
CC (PubMed:19523114). Interacts with SYNCRIP; this interaction is direct.
CC Interacts with MEF2C (via N-terminus); this interaction decreases DNA-
CC binding activity of MEF2C in myocardial cells in response to mechanical
CC stress. Interacts with PRMT1 (via N-terminus) (By similarity).
CC Interacts with SPIN1 (PubMed:23894536). {ECO:0000250|UniProtKB:Q5JVS0,
CC ECO:0000269|PubMed:19523114, ECO:0000269|PubMed:23894536}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q5JVS0}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q5JVS0}. Cytoplasm, Stress granule
CC {ECO:0000250|UniProtKB:Q5JVS0}. Cytoplasm, sarcoplasm
CC {ECO:0000250|UniProtKB:A1L1K8}. Nucleus, nuclear body
CC {ECO:0000250|UniProtKB:Q5JVS0}. Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:Q5JVS0}. Nucleus speckle
CC {ECO:0000250|UniProtKB:Q5JVS0}. Nucleus, Cajal body
CC {ECO:0000250|UniProtKB:Q5JVS0}. Nucleus, gem
CC {ECO:0000250|UniProtKB:Q5JVS0}. Note=Transported into the nuclear
CC compartment in activated leukocytes. Inhibition of methylation alters
CC its distribution between the nuclear and cytoplasmic compartments.
CC Methylation may be required for its localization in subnuclear
CC structures, such as nucleoli, nuclear speckles, Cajal bodies and Gemini
CC of coiled bodies (gems). Colocalizes with FMR1, FXR1 and FXR2 in
CC cytoplasmic stress granules. In myocardial cells, localization at the
CC sarcoplasm is reduced in response to mechanical stress.
CC {ECO:0000250|UniProtKB:A1L1K8, ECO:0000250|UniProtKB:Q5JVS0}.
CC -!- TISSUE SPECIFICITY: Expressed in adult heart, brain, liver, kidney,
CC testis, and in various embryonic tissues, but not in adult spleen, lung
CC or skeletal muscle. {ECO:0000269|PubMed:10887182}.
CC -!- DOMAIN: The C-terminal region is necessary for nucleus and cytoplasmic
CC localization. The N-terminal region is necessary for nucleus and
CC nuclear bodies localization. Regions containing Arg-Gly-Gly repeats
CC (RGG/RXR-box) may be preferentially methylated by PRMT1.
CC {ECO:0000250|UniProtKB:Q5JVS0}.
CC -!- PTM: Phosphorylated by phorbol 12-myristate 13-acetate (PMA)-activated
CC PKC isoforms at Thr-352 and Thr-373. {ECO:0000250|UniProtKB:Q5JVS0}.
CC -!- PTM: Methylated. Methylation is decreased by phorbol 12-myristate 13-
CC acetate (PMA)-activated PKC, in vitro. {ECO:0000250|UniProtKB:Q5JVS0}.
CC -!- MISCELLANEOUS: Able to bind hyaluronan. However, its intracellular
CC localization suggests that this interaction may not be relevant in
CC vivo.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB30437.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR EMBL; AF227684; AAF36966.1; -; mRNA.
DR EMBL; AK016800; BAB30437.1; ALT_SEQ; mRNA.
DR EMBL; AK144206; BAE25769.1; -; mRNA.
DR RefSeq; NP_064370.2; NM_019986.3.
DR AlphaFoldDB; Q9JKS5; -.
DR BioGRID; 208047; 13.
DR IntAct; Q9JKS5; 2.
DR MINT; Q9JKS5; -.
DR STRING; 10090.ENSMUSP00000021929; -.
DR iPTMnet; Q9JKS5; -.
DR PhosphoSitePlus; Q9JKS5; -.
DR MaxQB; Q9JKS5; -.
DR PaxDb; Q9JKS5; -.
DR PRIDE; Q9JKS5; -.
DR ProteomicsDB; 269808; -.
DR GeneID; 56541; -.
DR KEGG; mmu:56541; -.
DR CTD; 22927; -.
DR MGI; MGI:1891713; Habp4.
DR eggNOG; KOG2945; Eukaryota.
DR InParanoid; Q9JKS5; -.
DR OrthoDB; 1183388at2759; -.
DR PhylomeDB; Q9JKS5; -.
DR Reactome; R-MMU-114608; Platelet degranulation.
DR BioGRID-ORCS; 56541; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Habp4; mouse.
DR PRO; PR:Q9JKS5; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q9JKS5; protein.
DR GO; GO:0015030; C:Cajal body; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0010494; C:cytoplasmic stress granule; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0097504; C:Gemini of coiled bodies; ISS:UniProtKB.
DR GO; GO:0031965; C:nuclear membrane; ISO:MGI.
DR GO; GO:0016607; C:nuclear speck; ISS:UniProtKB.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0030017; C:sarcomere; ISS:UniProtKB.
DR GO; GO:0016528; C:sarcoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005540; F:hyaluronic acid binding; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0032183; F:SUMO binding; ISS:UniProtKB.
DR GO; GO:0071260; P:cellular response to mechanical stimulus; ISS:UniProtKB.
DR GO; GO:0030212; P:hyaluronan metabolic process; ISO:MGI.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0043392; P:negative regulation of DNA binding; ISS:UniProtKB.
DR GO; GO:0030578; P:PML body organization; ISS:UniProtKB.
DR GO; GO:0033120; P:positive regulation of RNA splicing; ISS:UniProtKB.
DR GO; GO:0045948; P:positive regulation of translational initiation; ISS: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 Coiled coil; Cytoplasm; Isopeptide bond; Methylation; mRNA processing;
KW mRNA splicing; Nucleus; Phosphoprotein; Reference proteome; RNA-binding;
KW Transcription; Transcription regulation; Translation regulation;
KW Ubl conjugation.
FT CHAIN 1..411
FT /note="Intracellular hyaluronan-binding protein 4"
FT /id="PRO_0000257973"
FT REGION 42..271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 296..318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 358..411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 42..62
FT /evidence="ECO:0000255"
FT COILED 279..301
FT /evidence="ECO:0000255"
FT COMPBIAS 42..64
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..185
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..224
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 7
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 36
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 70
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q5JVS0"
FT MOD_RES 74
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5JVS0"
FT MOD_RES 108
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5JVS0"
FT MOD_RES 352
FT /note="Phosphothreonine; by PKC"
FT /evidence="ECO:0000250|UniProtKB:Q5JVS0"
FT MOD_RES 373
FT /note="Phosphothreonine; by PKC"
FT /evidence="ECO:0000250|UniProtKB:Q5JVS0"
FT CROSSLNK 212
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q5JVS0"
FT CROSSLNK 212
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q5JVS0"
FT CROSSLNK 274
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q5JVS0"
FT CROSSLNK 274
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q5JVS0"
FT CROSSLNK 334
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q5JVS0"
FT CROSSLNK 334
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q5JVS0"
FT CONFLICT 64
FT /note="A -> AA (in Ref. 2; BAB30437)"
FT /evidence="ECO:0000305"
FT CONFLICT 187
FT /note="P -> L (in Ref. 2; BAE25769)"
FT /evidence="ECO:0000305"
FT CONFLICT 194
FT /note="R -> K (in Ref. 1; AAF36966)"
FT /evidence="ECO:0000305"
FT CONFLICT 266
FT /note="T -> A (in Ref. 2; BAB30437)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 411 AA; 45924 MW; 234C0E38C98990F4 CRC64;
MKGALGSPVA AAGAAMQETF GCVVANRFHQ LLDDESDPFD ILREAEHRRQ QQLQRKRRDE
AAAASGAGHR GGRSPAVASG HRPGAGGRRE SQKERKSLAA SGAQQPDSPG GPQPPGQKRT
PRRGEQQGWN DNRGTDVVLE RAERRSYREY RPYETERQAD LPVEKFTDEK PVDRFDRDRP
LRGRGGPRGG LRSRGRGGPG NRAFDSFDQR GKRDFERYSS NDKTNRMEDS MGGCGIRPWG
SGKDTSDTEP PAPMEETSMM EECQGTLDEE SAAKVPELEV EEENQVQEMT LDEWKNLQEQ
TRPKPEFNIR KPESTVPSKA VVIHKSRYRD DMVKEDYEDE SHVFRKAAND ITSQLEINFG
NLPRPGRGAR GSTRGGRGRM RRTENYGPRA EVVTQDVAPN PDDPEDFPAL A
