Q92688 (AN32B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	251 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing
Domain	Leucine-rich repeat Repeat
Molecular function	Chaperone
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Cellular_component	cytoplasm 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 (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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 251

251

Acidic leucine-rich nuclear phosphoprotein 32 family member B

PRO_0000137595

Regions

Repeat

16 – 40

25

LRR 1

Repeat

43 – 64

22

LRR 2

Repeat

65 – 84

20

LRR 3

Repeat

89 – 110

22

LRR 4

Domain

123 – 161

39

LRRCT

Compositional bias

146 – 251

106

Asp/Glu-rich (highly acidic)

Amino acid modifications

Modified residue

86

1

N6-acetyllysine Ref.11

Modified residue

244

1

Phosphothreonine Ref.9 Ref.10 Ref.12 Ref.14

Natural variations

Alternative sequence

196 – 251

56

Missing in isoform 2.

VSP_019304

Experimental info

Sequence conflict

1 – 2

2

Missing in CAA69265. Ref.3

Secondary structure

1

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251

Helix Strand Turn

Details...

Helix

3 – 11

9

Helix

16 – 18

3

Beta strand

20 – 23

4

Helix

39 – 43

5

Beta strand

46 – 52

7

Beta strand

68 – 73

6

Helix

82 – 86

5

Beta strand

92 – 94

3

Beta strand

96 – 99

4

Helix

104 – 109

6

Beta strand

117 – 119

3

Helix

124 – 126

3

Helix

131 – 136

6

Beta strand

157 – 159

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (Anp32b1) (PHAPI2b) [UniParc]. Last modified February 1, 1997. Version 1. Checksum: 93A1AADF8EDE7D53	FASTA	251	28,788
	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
	Isoform 2 (Anp32b2) (PHAPI2b) [UniParc]. Checksum: C504A0E604F16F73	FASTA	195	22,277
	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 DDEDGEEEEF DEEDD

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY.
[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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY.
[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.

IPI

IPI00007423.
IPI00759824.

RefSeq

NP_006392.1. NM_006401.2.

UniGene

Hs.730654.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2ELL	NMR	-	A	1-161	[»]
2RR6	NMR	-	A	1-161	[»]

ProteinModelPortal

Q92688.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q92688. 12 interactions.

STRING

9606.ENSP00000345848.

PTM databases

PhosphoSite

Q92688.

Polymorphism databases

DMDM

26390818.

Proteomic databases

PaxDb

Q92688.

PRIDE

Q92688.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000339399; ENSP00000345848; ENSG00000136938.

GeneID

10541.

KEGG

hsa:10541.

UCSC

uc004aya.3. human.

Organism-specific databases

CTD

10541.

GeneCards

GC09P100745.

HGNC

HGNC:16677. ANP32B.

neXtProt

NX_Q92688.

PharmGKB

PA24812.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG322008.

HOGENOM

HOG000007361.

HOVERGEN

HBG053102.

InParanoid

Q92688.

OMA

DEVSGEX.

Gene expression databases

ArrayExpress

Q92688.

Bgee

Q92688.

CleanEx

HS_ANP32B.

Genevestigator

Q92688.

GermOnline

ENSG00000136938. Homo sapiens.

Family and domain databases

InterPro

IPR001611. Leu-rich_rpt.
IPR003603. U2A'_phosphoprotein32A_C.
[Graphical view]

SMART

SM00446. LRRcap. 1 hit.
[Graphical view]

PROSITE

PS51450. LRR. 4 hits.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

ANP32B. human.

EvolutionaryTrace

Q92688.

GenomeRNAi

10541.

NextBio

39993.

PMAP-CutDB

Q92688.

Entry information

Entry name

AN32B_HUMAN

Accession

Primary (citable) accession number: Q92688
Secondary accession number(s): B2R9C7 , O00655, P78458, P78459

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 6, 2002
Last sequence update:	February 1, 1997
Last modified:	May 1, 2013
This is version 121 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.