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Reviewed, UniProtKB/Swiss-Prot Q5JVS0 (HABP4_HUMAN)

Last modified November 24, 2009. Version 41. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Intracellular hyaluronan-binding protein 4
      Short name=IHABP4
Alternative name(s):
    Ki-1/57 intracellular antigen
Gene names
Name: HABP4
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length413 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

May be involved in nuclear functions such as the remodeling of chromatin and the regulation of transcription. Ref.6 Ref.7

Subunit structure

Interacts with the C-terminus of CHD3. Interacts via its C-terminal region with GNB2L1. Interacts with TP53/p53. Ref.6 Ref.7 Ref.5 UniProtKB Q9JKS5

Subcellular location

Cytoplasm. Nucleus. Note: Transported into the nuclear compartment in activated leukocytes. Ref.6 Ref.7 Ref.4

Tissue specificity

Highly expressed in brain, heart, and kidney, and moderately expressed in skeletal muscle. Also expressed in a variety of tumor cell lines and in activated but not resting leukocytes. Ref.5 Ref.4

Post-translational modification

Phosphorylated by phorbol 12-myristate 13-acetate (PMA)-activated PKC isoforms at Thr-354 and Thr-375 Probable. Ref.6

Miscellaneous

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

The interaction with GNB2L1 is abolished upon activation of L540 tumor cells with PMA, which results in phosphorylation and exit of HABP4 from the nucleus. Ref.6

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
   DomainCoiled coil
   PTMPhosphoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processregulation of transcription

Inferred from electronic annotation. Source: UniProtKB-KW

transcription

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 Ref.4 Ref.1 (identifier: Q5JVS0-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 Ref.3 (identifier: Q5JVS0-2)

The sequence of this isoform differs from the canonical sequence as follows:
     172-276: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 413413Intracellular hyaluronan-binding protein 4
PRO_0000257972

Regions

Coiled coil40 – 6425 Potential

Amino acid modifications

Modified residue971Phosphoserine Ref.8
Modified residue1081Phosphoserine Ref.8
Modified residue3541Phosphothreonine; by PKC Probable Ref.6
Modified residue3751Phosphothreonine; by PKC Probable Ref.6

Natural variations

Alternative sequence172 – 276105Missing in isoform 2. Ref.3
VSP_052194

Experimental info

Sequence conflict1041Q → H in AAF62546. Ref.1
Sequence conflict1151A → S in AAC31117. Ref.4
Sequence conflict388 – 3892YG → NY in AAF62546. Ref.1
Sequence conflict388 – 3892YG → NY in AAC31117. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified February 15, 2005. Version 1.
Checksum: 98749EEC5CB92155

FASTA41345,785
        10         20         30         40         50         60 
MKGALGSPVA AAGAAMQESF GCVVANRFHQ LLDDESDPFD ILREAERRRQ QQLQRKRRDE 

        70         80         90        100        110        120 
AAAAAGAGPR GGRSPAGASG HRAGAGGRRE SQKERKSLPA PVAQRPDSPG GGLQAPGQKR 

       130        140        150        160        170        180 
TPRRGEQQGW NDSRGPEGML ERAERRSYRE YRPYETERQA DFTAEKFPDE KPGDRFDRDR 

       190        200        210        220        230        240 
PLRGRGGPRG GMRGRGRGGP GNRVFDAFDQ RGKREFERYG GNDKIAVRTE DNMGGCGVRT 

       250        260        270        280        290        300 
WGSGKDTSDV EPTAPMEEPT VVEESQGTPE EESPAKVPEL EVEEETQVQE MTLDEWKNLQ 

       310        320        330        340        350        360 
EQTRPKPEFN IRKPESTVPS KAVVIHKSKY RDDMVKDDYE DDSHVFRKPA NDITSQLEIN 

       370        380        390        400        410 
FGNLPRPGRG ARGGTRGGRG RIRRAENYGP RAEVVMQDVA PNPDDPEDFP ALS 

« Hide

Isoform 2.

Checksum: CFA9C86A34BF5514
Show »

FASTA30834,365

References

« Hide 'large scale' references
[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: 10887182] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"DNA sequence and analysis of human chromosome 9."
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. expand/collapse author list , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
Nature 429:369-374(2004) [PubMed: 15164053] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Brain.
[4]"Characterization, mapping and partial cDNA sequence of the 57-kD intracellular Ki-1 antigen."
Kobarg J., Schnittger S., Fonatsch C., Lemke H., Bowen M.A., Buck F., Hansen H.P.
Exp. Clin. Immunogenet. 14:273-280(1997) [PubMed: 9523163] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 115-413 (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[5]"Characterization of a new family of proteins that interact with the C-terminal region of the chromatin-remodeling factor CHD-3."
Lemos T.A., Passos D.O., Nery F.C., Kobarg J.
FEBS Lett. 533:14-20(2003) [PubMed: 12505151] [Abstract]
Cited for: INTERACTION WITH CHD3, TISSUE SPECIFICITY.
[6]"Ki-1/57 interacts with RACK1 and is a substrate for the phosphorylation by phorbol 12-myristate 13-acetate-activated protein kinase C."
Nery F.C., Passos D.O., Garcia V.S., Kobarg J.
J. Biol. Chem. 279:11444-11455(2004) [PubMed: 14699138] [Abstract]
Cited for: FUNCTION, INTERACTION WITH GNB2L1, SUBCELLULAR LOCATION, PHOSPHORYLATION.
[7]"Evidence for the interaction of the regulatory protein Ki-1/57 with p53 and its interacting proteins."
Nery F.C., Rui E., Kuniyoshi T.M., Kobarg J.
Biochem. Biophys. Res. Commun. 341:847-855(2006) [PubMed: 16455055] [Abstract]
Cited for: FUNCTION, INTERACTION WITH TP53, SUBCELLULAR LOCATION.
[8]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-97 AND SER-108, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

AF241831 mRNA. Translation: AAF62546.1.
AL133477 Genomic DNA. Translation: CAI39620.1.
AL133477 Genomic DNA. Translation: CAI39621.1.
BC018788 mRNA. Translation: AAH18788.1.
U77327 mRNA. Translation: AAC31117.1.
IPIIPI00018583.
IPI00103004.
RefSeqNP_055097.2.
UniGeneHs.494567

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ5JVS0.

PTM databases

PhosphoSiteQ5JVS0.

Proteomic databases

PRIDEQ5JVS0.

Genome annotation databases

EnsemblENST00000375249; ENSP00000364398; ENSG00000130956; Homo sapiens. [Genome view]
GeneID22927.
KEGGhsa:22927.
NMPDRfig|9606.3.peg.31600.
UCSCuc010msg.1. human.
uc010msh.1. human.

Organism-specific databases

CTD22927.
GeneCardsGC09P098252.
HGNCHGNC:17062. HABP4.
PharmGKBPA38434.
GenAtlasSearch...

Phylogenomic databases

HOVERGENQ5JVS0.
OMARTEDNMG
OrthoDBEOG9X0QC6

Gene expression databases

ArrayExpressQ5JVS0.
BgeeQ5JVS0.
CleanExHS_HABP4.
GenevestigatorQ5JVS0.
GermOnlineENSG00000130956. Homo sapiens.

Family and domain databases

InterProIPR006861. HABP4_PAIRBP1_bd.
[Graphical view]
PfamPF04774. HABP4_PAI-RBP1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio43643.

Entry information

Entry nameHABP4_HUMAN
AccessionPrimary (citable) accession number: Q5JVS0
Secondary accession number(s): O75804, Q8WV33, Q9NYJ2
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: February 15, 2005
Last modified: November 24, 2009
This is version 41 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents