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Q92688 (AN32B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 130. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Acidic leucine-rich nuclear phosphoprotein 32 family member B
Alternative name(s):
Acidic protein rich in leucines
Putative HLA-DR-associated protein I-2
Short name=PHAPI2
Silver-stainable protein SSP29
Gene names
Name:ANP32B
Synonyms:APRIL, PHAPI2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length251 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Multifunctional protein working as a cell cycle progression factor as well as a cell survival factor. Required for the progression from the G1 to the S phase. Anti-apoptotic protein which functions as a caspase-3 inhibitor. Has no phosphatase 2A (PP2A) inhibitor activity By similarity. Exhibits histone chaperone properties, stimulating core histones to assemble into a nucleosome. Ref.15

Subunit structure

Monomer. Interacts with histones H3 and H4. Ref.15

Subcellular location

Isoform 1: Nucleus. Note: Accumulates in the nuclei at the S phase By similarity.

Isoform 2: Cytoplasm. Note: Lacks a nuclear localization signal.

Tissue specificity

Expressed in heart, lung, pancreas, prostate and in spleen, thymus and placenta. Ref.3

Domain

Histone binding is mediated by the concave surface of the LRR region.

Post-translational modification

Some glutamate residues are glycylated by TTLL8. This modification occurs exclusively on glutamate residues and results in a glycine chain on the gamma-carboxyl group By similarity.

Sequence similarities

Belongs to the ANP32 family.

Contains 4 LRR (leucine-rich) repeats.

Contains 1 LRRCT domain.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q92688-1)

Also known as: Anp32b1; PHAPI2b;

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 (identifier: Q92688-2)

Also known as: Anp32b2; PHAPI2b;

The sequence of this isoform differs from the canonical sequence as follows:
     196-251: Missing.
Note: No canonical donor splice site.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 251251Acidic leucine-rich nuclear phosphoprotein 32 family member B
PRO_0000137595

Regions

Repeat16 – 4025LRR 1
Repeat43 – 6422LRR 2
Repeat65 – 8420LRR 3
Repeat89 – 11022LRR 4
Domain123 – 16139LRRCT
Compositional bias146 – 251106Asp/Glu-rich (highly acidic)

Amino acid modifications

Modified residue861N6-acetyllysine Ref.11
Modified residue2441Phosphothreonine Ref.9 Ref.10 Ref.12 Ref.14

Natural variations

Alternative sequence196 – 25156Missing in isoform 2.
VSP_019304

Experimental info

Sequence conflict1 – 22Missing in CAA69265. Ref.3

Secondary structure

............................. 251
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Anp32b1) (PHAPI2b) [UniParc].

Last modified February 1, 1997. Version 1.
Checksum: 93A1AADF8EDE7D53

FASTA25128,788
        10         20         30         40         50         60 
MDMKRRIHLE LRNRTPAAVR ELVLDNCKSN DGKIEGLTAE FVNLEFLSLI NVGLISVSNL 

        70         80         90        100        110        120 
PKLPKLKKLE LSENRIFGGL DMLAEKLPNL THLNLSGNKL KDISTLEPLK KLECLKSLDL 

       130        140        150        160        170        180 
FNCEVTNLND YRESVFKLLP QLTYLDGYDR EDQEAPDSDA EVDGVDEEEE DEEGEDEEDE 

       190        200        210        220        230        240 
DDEDGEEEEF DEEDDEDEDV EGDEDDDEVS EEEEEFGLDE EDEDEDEDEE EEEGGKGEKR 

       250 
KRETDDEGED D 

« Hide

Isoform 2 (Anp32b2) (PHAPI2b) [UniParc].

Checksum: C504A0E604F16F73
Show »

FASTA19522,277

References

« Hide 'large scale' references
[1]Vaesen M., Barnikol-Watanabe S., Kratzin H.D., Hilschmann N.
Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"Molecular cloning and partial characterization of a new silver-stainable protein."
Zhu L., Henning D., Valdez B.C.
Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]"Expression analysis and chromosomal mapping of a novel human gene, APRIL, encoding an acidic protein rich in leucines."
Mencinger M., Panagopoulos I., Contreras J.A., Mitelman F., Aman P.
Biochim. Biophys. Acta 1395:176-180(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY.
Tissue: Pancreas.
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[5]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Muscle and Testis.
[8]"The Anp32 family of proteins containing leucine-rich repeats."
Matilla A., Radrizzani M.
Cerebellum 4:7-18(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: GENE FAMILY, NOMENCLATURE.
[9]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-244, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-244, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[11]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-86, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-244, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-244, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"Solution structure of histone chaperone ANP32B: interaction with core histones H3-H4 through its acidic concave domain."
Tochio N., Umehara T., Munemasa Y., Suzuki T., Sato S., Tsuda K., Koshiba S., Kigawa T., Nagai R., Yokoyama S.
J. Mol. Biol. 401:97-114(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 1-161, FUNCTION, SUBUNIT, INTERACTION WITH HISTONES H3 AND H4, LEUCINE-RICH REPEATS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y07569 mRNA. Translation: CAA68855.1.
U70439 mRNA. Translation: AAB37579.1.
Y07969 mRNA. Translation: CAA69265.1.
Y07570 mRNA. Translation: CAA68856.1.
AK313733 mRNA. Translation: BAG36474.1.
AL354726 Genomic DNA. Translation: CAI15260.1.
CH471105 Genomic DNA. Translation: EAW58865.1.
BC013003 mRNA. Translation: AAH13003.1.
BC019658 mRNA. Translation: AAH19658.1.
CCDSCCDS6732.1. [Q92688-1]
RefSeqNP_006392.1. NM_006401.2. [Q92688-1]
UniGeneHs.730654.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2ELLNMR-A1-161[»]
2RR6NMR-A1-161[»]
ProteinModelPortalQ92688.
SMRQ92688. Positions 1-161.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115795. 34 interactions.
IntActQ92688. 13 interactions.
STRING9606.ENSP00000345848.

PTM databases

PhosphoSiteQ92688.

Polymorphism databases

DMDM26390818.

Proteomic databases

MaxQBQ92688.
PaxDbQ92688.
PRIDEQ92688.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000339399; ENSP00000345848; ENSG00000136938. [Q92688-1]
GeneID10541.
KEGGhsa:10541.
UCSCuc004aya.3. human. [Q92688-1]

Organism-specific databases

CTD10541.
GeneCardsGC09P100745.
HGNCHGNC:16677. ANP32B.
neXtProtNX_Q92688.
PharmGKBPA24812.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG322008.
HOGENOMHOG000007361.
HOVERGENHBG053102.
InParanoidQ92688.
OMADEVSGEX.
OrthoDBEOG7TJ3KH.
PhylomeDBQ92688.
TreeFamTF317206.

Gene expression databases

ArrayExpressQ92688.
BgeeQ92688.
CleanExHS_ANP32B.
GenevestigatorQ92688.

Family and domain databases

InterProIPR001611. Leu-rich_rpt.
IPR003603. U2A'_phosphoprotein32A_C.
[Graphical view]
SMARTSM00446. LRRcap. 1 hit.
[Graphical view]
PROSITEPS51450. LRR. 4 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSANP32B. human.
EvolutionaryTraceQ92688.
GeneWikiANP32B.
GenomeRNAi10541.
NextBio39993.
PMAP-CutDBQ92688.
PROQ92688.

Entry information

Entry nameAN32B_HUMAN
AccessionPrimary (citable) accession number: Q92688
Secondary accession number(s): B2R9C7 expand/collapse secondary AC list , O00655, P78458, P78459
Entry history
Integrated into UniProtKB/Swiss-Prot: December 6, 2002
Last sequence update: February 1, 1997
Last modified: July 9, 2014
This is version 130 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
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

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Human chromosome 9

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