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Protein

Intracellular hyaluronan-binding protein 4

Gene

Habp4

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

May be involved in nuclear functions such as the remodeling of chromatin and the regulation of transcription.By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Names & Taxonomyi

Protein namesi
Recommended name:
Intracellular hyaluronan-binding protein 4
Short name:
IHABP-4
Short name:
IHABP4
Gene namesi
Name:Habp4Imported
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:1891713. Habp4.

Subcellular locationi

  • Cytoplasm By similarity
  • Nucleus By similarity

  • Note: Transported into the nuclear compartment in activated leukocytes (By similarity). Interacts with SPIN1.By similarity

GO - Cellular componenti

  • cytoplasm Source: MGI
  • nucleoplasm Source: MGI
  • nucleus Source: UniProtKB
  • sarcomere Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 411411Intracellular hyaluronan-binding protein 4PRO_0000257973Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei7 – 71PhosphoserineCombined sources
Modified residuei36 – 361PhosphoserineCombined sources
Modified residuei74 – 741PhosphoserineBy similarity
Modified residuei108 – 1081PhosphoserineBy similarity
Modified residuei352 – 3521Phosphothreonine; by PKCBy similarity
Modified residuei373 – 3731Phosphothreonine; by PKCBy similarity

Post-translational modificationi

Phosphorylated by phorbol 12-myristate 13-acetate (PMA)-activated PKC isoforms at Thr-352 and Thr-373.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9JKS5.
MaxQBiQ9JKS5.
PaxDbiQ9JKS5.
PRIDEiQ9JKS5.

PTM databases

iPTMnetiQ9JKS5.
PhosphoSiteiQ9JKS5.

Expressioni

Tissue specificityi

Expressed in adult heart, brain, liver, kidney, testis, and in various embryonic tissues, but not in adult spleen, lung or skeletal muscle.1 Publication

Gene expression databases

CleanExiMM_HABP4.

Interactioni

Subunit structurei

Interacts with the C-terminus of CHD3. Interacts via its C-terminal region with RACK1. Interacts with p53/TP53 (By similarity).By similarity

Protein-protein interaction databases

IntActiQ9JKS5. 1 interaction.
MINTiMINT-4130138.
STRINGi10090.ENSMUSP00000021929.

Structurei

3D structure databases

ProteinModelPortaliQ9JKS5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili42 – 6221Sequence analysisAdd
BLAST
Coiled coili279 – 30123Sequence analysisAdd
BLAST

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG2945. Eukaryota.
ENOG410YBHR. LUCA.
HOGENOMiHOG000220826.
HOVERGENiHBG056357.
InParanoidiQ9JKS5.
KOiK19019.
PhylomeDBiQ9JKS5.

Family and domain databases

InterProiIPR006861. HABP4_PAIRBP1-bd.
IPR032381. IHABP4_N.
[Graphical view]
PfamiPF04774. HABP4_PAI-RBP1. 1 hit.
PF16174. IHABP4_N. 1 hit.
[Graphical view]
SMARTiSM01233. HABP4_PAI-RBP1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9JKS5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKGALGSPVA AAGAAMQETF GCVVANRFHQ LLDDESDPFD ILREAEHRRQ
60 70 80 90 100
QQLQRKRRDE AAAASGAGHR GGRSPAVASG HRPGAGGRRE SQKERKSLAA
110 120 130 140 150
SGAQQPDSPG GPQPPGQKRT PRRGEQQGWN DNRGTDVVLE RAERRSYREY
160 170 180 190 200
RPYETERQAD LPVEKFTDEK PVDRFDRDRP LRGRGGPRGG LRSRGRGGPG
210 220 230 240 250
NRAFDSFDQR GKRDFERYSS NDKTNRMEDS MGGCGIRPWG SGKDTSDTEP
260 270 280 290 300
PAPMEETSMM EECQGTLDEE SAAKVPELEV EEENQVQEMT LDEWKNLQEQ
310 320 330 340 350
TRPKPEFNIR KPESTVPSKA VVIHKSRYRD DMVKEDYEDE SHVFRKAAND
360 370 380 390 400
ITSQLEINFG NLPRPGRGAR GSTRGGRGRM RRTENYGPRA EVVTQDVAPN
410
PDDPEDFPAL A
Length:411
Mass (Da):45,924
Last modified:October 31, 2006 - v2
Checksum:i234C0E38C98990F4
GO

Sequence cautioni

The sequence BAB30437.1 differs from that shown.Intron retention.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti64 – 641A → AA in BAB30437 (PubMed:16141072).Curated
Sequence conflicti187 – 1871P → L in BAE25769 (PubMed:16141072).Curated
Sequence conflicti194 – 1941R → K in AAF36966 (PubMed:10887182).Curated
Sequence conflicti266 – 2661T → A in BAB30437 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF227684 mRNA. Translation: AAF36966.1.
AK016800 mRNA. Translation: BAB30437.1. Sequence problems.
AK144206 mRNA. Translation: BAE25769.1.
RefSeqiNP_064370.2. NM_019986.3.
UniGeneiMm.40989.

Genome annotation databases

GeneIDi56541.
KEGGimmu:56541.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF227684 mRNA. Translation: AAF36966.1.
AK016800 mRNA. Translation: BAB30437.1. Sequence problems.
AK144206 mRNA. Translation: BAE25769.1.
RefSeqiNP_064370.2. NM_019986.3.
UniGeneiMm.40989.

3D structure databases

ProteinModelPortaliQ9JKS5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9JKS5. 1 interaction.
MINTiMINT-4130138.
STRINGi10090.ENSMUSP00000021929.

PTM databases

iPTMnetiQ9JKS5.
PhosphoSiteiQ9JKS5.

Proteomic databases

EPDiQ9JKS5.
MaxQBiQ9JKS5.
PaxDbiQ9JKS5.
PRIDEiQ9JKS5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi56541.
KEGGimmu:56541.

Organism-specific databases

CTDi22927.
MGIiMGI:1891713. Habp4.

Phylogenomic databases

eggNOGiKOG2945. Eukaryota.
ENOG410YBHR. LUCA.
HOGENOMiHOG000220826.
HOVERGENiHBG056357.
InParanoidiQ9JKS5.
KOiK19019.
PhylomeDBiQ9JKS5.

Miscellaneous databases

ChiTaRSiHabp4. mouse.
PROiQ9JKS5.
SOURCEiSearch...

Gene expression databases

CleanExiMM_HABP4.

Family and domain databases

InterProiIPR006861. HABP4_PAIRBP1-bd.
IPR032381. IHABP4_N.
[Graphical view]
PfamiPF04774. HABP4_PAI-RBP1. 1 hit.
PF16174. IHABP4_N. 1 hit.
[Graphical view]
SMARTiSM01233. HABP4_PAI-RBP1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular characterization of a novel intracellular hyaluronan-binding protein."
    Huang L., Grammatikakis N., Yoneda M., Banerjee S.D., Toole B.P.
    J. Biol. Chem. 275:29829-29839(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6JImported.
    Tissue: TestisImported.
  3. "Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
    Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
    Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7 AND SER-36, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  5. "A tudor domain protein SPINDLIN1 interacts with the mRNA-binding protein SERBP1 and is involved in mouse oocyte meiotic resumption."
    Chew T.G., Peaston A., Lim A.K., Lorthongpanich C., Knowles B.B., Solter D.
    PLoS ONE 8:E69764-E69764(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SPIN1.

Entry informationi

Entry nameiHABP4_MOUSE
AccessioniPrimary (citable) accession number: Q9JKS5
Secondary accession number(s): Q3UNH8, Q9D450
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: October 31, 2006
Last modified: June 8, 2016
This is version 89 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Able to bind hyaluronan. However, its intracellular localization suggests that this interaction may not be relevant in vivo.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.