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P39687

- AN32A_HUMAN

UniProt

P39687 - AN32A_HUMAN

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Protein

Acidic leucine-rich nuclear phosphoprotein 32 family member A

Gene

ANP32A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Implicated in a number of cellular processes, including proliferation, differentiation, caspase-dependent and caspase-independent apoptosis, suppression of transformation (tumor suppressor), inhibition of protein phosphatase 2A, regulation of mRNA trafficking and stability in association with ELAVL1, and inhibition of acetyltransferases as part of the INHAT (inhibitor of histone acetyltransferases) complex. Plays a role in E4F1-mediated transcriptional repression.4 Publications

GO - Molecular functioni

  1. poly(A) RNA binding Source: UniProtKB

GO - Biological processi

  1. gene expression Source: Reactome
  2. intracellular signal transduction Source: ProtInc
  3. mRNA metabolic process Source: Reactome
  4. nucleocytoplasmic transport Source: UniProtKB
  5. regulation of transcription, DNA-templated Source: UniProtKB-KW
  6. RNA metabolic process Source: Reactome
  7. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Enzyme and pathway databases

ReactomeiREACT_25218. HuR stabilizes mRNA.

Names & Taxonomyi

Protein namesi
Recommended name:
Acidic leucine-rich nuclear phosphoprotein 32 family member A
Alternative name(s):
Acidic nuclear phosphoprotein pp32
Short name:
pp32
Leucine-rich acidic nuclear protein
Short name:
LANP
Mapmodulin
Potent heat-stable protein phosphatase 2A inhibitor I1PP2A
Putative HLA-DR-associated protein I
Short name:
PHAPI
Gene namesi
Name:ANP32A
Synonyms:C15orf1, LANP, MAPM, PHAP1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 15

Organism-specific databases

HGNCiHGNC:13233. ANP32A.

Subcellular locationi

Nucleus. Cytoplasm. Endoplasmic reticulum
Note: Translocates to the cytoplasm during the process of neuritogenesis (By similarity). Shuttles between nucleus and cytoplasm.By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. endoplasmic reticulum Source: UniProtKB
  3. nucleoplasm Source: Reactome
  4. nucleus Source: UniProtKB
  5. perinuclear region of cytoplasm Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA24811.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 249249Acidic leucine-rich nuclear phosphoprotein 32 family member APRO_0000137592Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei15 – 151Phosphothreonine1 Publication
Modified residuei17 – 171Phosphoserine1 Publication

Post-translational modificationi

Phosphorylated on serine residues.1 Publication
The N-terminus is blocked.
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).By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP39687.
PaxDbiP39687.
PRIDEiP39687.

2D gel databases

SWISS-2DPAGEP39687.

PTM databases

PhosphoSiteiP39687.

Miscellaneous databases

PMAP-CutDBP39687.

Expressioni

Tissue specificityi

Expressed in all tissues tested. Highly expressed in kidney and skeletal muscle, moderate levels of expression in brain, placenta and pancreas, and weakly expressed in lung. Found in all regions of the brain examined (amygdala, caudate nucleus, corpus callosum, hippocampus and thalamus), with highest levels in amygdala.1 Publication

Gene expression databases

BgeeiP39687.
CleanExiHS_ANP32A.
ExpressionAtlasiP39687. baseline and differential.
GenevestigatoriP39687.

Organism-specific databases

HPAiCAB005231.

Interactioni

Subunit structurei

Component of the SET complex, composed of at least ANP32A, APEX1, HMGB2, NME1, SET and TREX1. Directly interacts with SET. Interacts with ATXN1/SCA1. Interacts with MAP1B. Interacts with ELAVL1. Part of the INHAT (inhibitor of histone acetyltransferases) complex. Interacts with E4F1.6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
AXIN1O151692EBI-359234,EBI-710484
E4F1Q66K893EBI-359234,EBI-1227043
PPP2CAP677752EBI-359234,EBI-712311
Ppp2caP633312EBI-359234,EBI-7050205From a different organism.

Protein-protein interaction databases

BioGridi113791. 41 interactions.
IntActiP39687. 15 interactions.
MINTiMINT-4999627.
STRINGi9606.ENSP00000417864.

Structurei

Secondary structure

1
249
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 119
Helixi16 – 183
Beta strandi20 – 234
Beta strandi46 – 483
Beta strandi68 – 703
Helixi81 – 866
Beta strandi92 – 943
Helixi103 – 1064
Helixi107 – 1115
Beta strandi117 – 1193
Helixi124 – 1274
Helixi131 – 1388

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2JE0X-ray2.40A/B/C/D/E/F1-149[»]
2JE1X-ray2.69A/B/C/D1-149[»]
ProteinModelPortaliP39687.
SMRiP39687. Positions 1-149.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP39687.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati18 – 3821LRR 11 PublicationAdd
BLAST
Repeati43 – 6422LRR 21 PublicationAdd
BLAST
Repeati65 – 8723LRR 31 PublicationAdd
BLAST
Repeati89 – 11022LRR 41 PublicationAdd
BLAST
Domaini123 – 16139LRRCTAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni150 – 17425Necessary for tumor-suppressive functionAdd
BLAST
Regioni165 – 24985Interaction with E4F1By similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi168 – 24982Asp/Glu-rich (highly acidic)Add
BLAST

Sequence similaritiesi

Belongs to the ANP32 family.Curated
Contains 4 LRR (leucine-rich) repeats.Curated
Contains 1 LRRCT domain.Curated

Keywords - Domaini

Leucine-rich repeat, Repeat

Phylogenomic databases

eggNOGiNOG322008.
GeneTreeiENSGT00560000077130.
HOGENOMiHOG000007361.
HOVERGENiHBG053102.
InParanoidiP39687.
OMAiFTFAVEL.
OrthoDBiEOG7TJ3KH.
PhylomeDBiP39687.
TreeFamiTF317206.

Family and domain databases

InterProiIPR001611. Leu-rich_rpt.
IPR003603. U2A'_phosphoprotein32A_C.
[Graphical view]
SMARTiSM00446. LRRcap. 1 hit.
[Graphical view]
PROSITEiPS51450. LRR. 4 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P39687-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MEMGRRIHLE LRNRTPSDVK ELVLDNSRSN EGKLEGLTDE FEELEFLSTI
60 70 80 90 100
NVGLTSIANL PKLNKLKKLE LSDNRVSGGL EVLAEKCPNL THLNLSGNKI
110 120 130 140 150
KDLSTIEPLK KLENLKSLDL FNCEVTNLND YRENVFKLLP QLTYLDGYDR
160 170 180 190 200
DDKEAPDSDA EGYVEGLDDE EEDEDEEEYD EDAQVVEDEE DEDEEEEGEE
210 220 230 240
EDVSGEEEED EEGYNDGEVD DEEDEEELGE EERGQKRKRE PEDEGEDDD
Length:249
Mass (Da):28,585
Last modified:February 1, 1995 - v1
Checksum:iCA2D1A756FBAEA04
GO

Sequence cautioni

The sequence BAD97000.1 differs from that shown. Reason: Erroneous initiation.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti186 – 1861V → A in BAD97000. 1 PublicationCurated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X75090 mRNA. Translation: CAA52981.1.
U60823 mRNA. Translation: AAC50570.1.
U73477 mRNA. Translation: AAB39706.1.
AF025684 mRNA. Translation: AAB91548.1.
AY349171 mRNA. Translation: AAQ79832.1.
BT007436 mRNA. Translation: AAP36104.1.
AK223280 mRNA. Translation: BAD97000.1. Different initiation.
AK312703 mRNA. Translation: BAG35581.1.
CH471082 Genomic DNA. Translation: EAW77824.1.
BC007200 mRNA. Translation: AAH07200.1.
CCDSiCCDS45292.1.
PIRiS36375.
S43309.
RefSeqiNP_006296.1. NM_006305.3.
UniGeneiHs.458747.

Genome annotation databases

EnsembliENST00000465139; ENSP00000417864; ENSG00000140350.
GeneIDi8125.
KEGGihsa:8125.
UCSCiuc002arl.3. human.

Polymorphism databases

DMDMi730318.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X75090 mRNA. Translation: CAA52981.1 .
U60823 mRNA. Translation: AAC50570.1 .
U73477 mRNA. Translation: AAB39706.1 .
AF025684 mRNA. Translation: AAB91548.1 .
AY349171 mRNA. Translation: AAQ79832.1 .
BT007436 mRNA. Translation: AAP36104.1 .
AK223280 mRNA. Translation: BAD97000.1 . Different initiation.
AK312703 mRNA. Translation: BAG35581.1 .
CH471082 Genomic DNA. Translation: EAW77824.1 .
BC007200 mRNA. Translation: AAH07200.1 .
CCDSi CCDS45292.1.
PIRi S36375.
S43309.
RefSeqi NP_006296.1. NM_006305.3.
UniGenei Hs.458747.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2JE0 X-ray 2.40 A/B/C/D/E/F 1-149 [» ]
2JE1 X-ray 2.69 A/B/C/D 1-149 [» ]
ProteinModelPortali P39687.
SMRi P39687. Positions 1-149.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 113791. 41 interactions.
IntActi P39687. 15 interactions.
MINTi MINT-4999627.
STRINGi 9606.ENSP00000417864.

PTM databases

PhosphoSitei P39687.

Polymorphism databases

DMDMi 730318.

2D gel databases

SWISS-2DPAGE P39687.

Proteomic databases

MaxQBi P39687.
PaxDbi P39687.
PRIDEi P39687.

Protocols and materials databases

DNASUi 8125.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000465139 ; ENSP00000417864 ; ENSG00000140350 .
GeneIDi 8125.
KEGGi hsa:8125.
UCSCi uc002arl.3. human.

Organism-specific databases

CTDi 8125.
GeneCardsi GC15M069070.
HGNCi HGNC:13233. ANP32A.
HPAi CAB005231.
MIMi 600832. gene.
neXtProti NX_P39687.
PharmGKBi PA24811.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG322008.
GeneTreei ENSGT00560000077130.
HOGENOMi HOG000007361.
HOVERGENi HBG053102.
InParanoidi P39687.
OMAi FTFAVEL.
OrthoDBi EOG7TJ3KH.
PhylomeDBi P39687.
TreeFami TF317206.

Enzyme and pathway databases

Reactomei REACT_25218. HuR stabilizes mRNA.

Miscellaneous databases

ChiTaRSi ANP32A. human.
EvolutionaryTracei P39687.
GenomeRNAii 8125.
NextBioi 30786.
PMAP-CutDB P39687.
PROi P39687.
SOURCEi Search...

Gene expression databases

Bgeei P39687.
CleanExi HS_ANP32A.
ExpressionAtlasi P39687. baseline and differential.
Genevestigatori P39687.

Family and domain databases

InterProi IPR001611. Leu-rich_rpt.
IPR003603. U2A'_phosphoprotein32A_C.
[Graphical view ]
SMARTi SM00446. LRRcap. 1 hit.
[Graphical view ]
PROSITEi PS51450. LRR. 4 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Purification and characterization of two putative HLA class II associated proteins: PHAPI and PHAPII."
    Vaesen M., Barnikol-Watanabe S., Goetz H., Adil Awni L., Cole T., Zimmermann B., Kratzin H.D., Hilschmann N.
    Biol. Chem. Hoppe-Seyler 375:113-126(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 1-26; 29-47; 71-97 AND 100-161.
    Tissue: B-cell lymphoma.
  2. "Molecular identification of I1PP2A, a novel potent heat-stable inhibitor protein of protein phosphatase 2A."
    Li M., Makkinje A., Damuni Z.
    Biochemistry 35:6998-7002(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 7-12 AND 29-44.
    Tissue: Kidney.
  3. "Structure of pp32, an acidic nuclear protein which inhibits oncogene-induced formation of transformed foci."
    Chen T.-H., Brody J.R., Romantsev F.E., Yu J.-G., Kayler A.E., Voneiff E., Kuhajda F.P., Pasternack G.R.
    Mol. Biol. Cell 7:2045-2056(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  4. "The cerebellar leucine-rich acidic nuclear protein interacts with ataxin-1."
    Matilla A., Koshy B.T., Cummings C.J., Isobe T., Orr H.T., Zoghbi H.Y.
    Nature 389:974-978(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  5. "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].
  6. "Inhibitors of protein phosphatase-2A from human brain structures, immunocytological localization and activities towards dephosphorylation of the Alzheimer type hyperphosphorylated tau."
    Tsujio I., Zaidi T., Xu J., Kotula L., Grundke-Iqbal I., Iqbal K.
    FEBS Lett. 579:363-372(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Tissue: Brain.
  7. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  8. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
    Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Synovium.
  9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  10. "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].
    Tissue: Lymph.
  11. "Identification of sequences required for inhibition of oncogene-mediated transformation by pp32."
    Brody J.R., Kadkol S.S., Mahmoud M.A., Rebel J.M., Pasternack G.R.
    J. Biol. Chem. 274:20053-20055(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  12. "Regulation of histone acetylation and transcription by INHAT, a human cellular complex containing the Set oncoprotein."
    Seo S.-B., McNamara P., Heo S., Turner A., Lane W.S., Chakravarti D.
    Cell 104:119-130(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH THE INHAT COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
  13. "Granzyme A activates an endoplasmic reticulum-associated caspase-independent nuclease to induce single-stranded DNA nicks."
    Beresford P.J., Zhang D., Oh D.Y., Fan Z., Greer E.L., Russo M.L., Jaju M., Lieberman J.
    J. Biol. Chem. 276:43285-43293(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SET.
  14. "Tumor suppression and potentiation by manipulation of pp32 expression."
    Bai J., Brody J.R., Kadkol S.S., Pasternack G.R.
    Oncogene 20:2153-2160(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  15. "Delineation of mRNA export pathways by the use of cell-permeable peptides."
    Gallouzi I.-E., Steitz J.A.
    Science 294:1895-1901(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ELAVL1, SUBCELLULAR LOCATION.
  16. "Tumor suppressor NM23-H1 is a granzyme A-activated DNase during CTL-mediated apoptosis, and the nucleosome assembly protein SET is its inhibitor."
    Fan Z., Beresford P.J., Oh D.Y., Zhang D., Lieberman J.
    Cell 112:659-672(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE SET COMPLEX.
  17. "Cleaving the oxidative repair protein Ape1 enhances cell death mediated by granzyme A."
    Fan Z., Beresford P.J., Zhang D., Xu Z., Novina C.D., Yoshida A., Pommier Y., Lieberman J.
    Nat. Immunol. 4:145-153(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  18. "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.
  19. "The exonuclease TREX1 is in the SET complex and acts in concert with NM23-H1 to degrade DNA during granzyme A-mediated cell death."
    Chowdhury D., Beresford P.J., Zhu P., Zhang D., Sung J.S., Demple B., Perrino F.W., Lieberman J.
    Mol. Cell 23:133-142(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE SET COMPLEX.
  20. "The role of LANP and ataxin 1 in E4F-mediated transcriptional repression."
    Cvetanovic M., Rooney R.J., Garcia J.J., Toporovskaya N., Zoghbi H.Y., Opal P.
    EMBO Rep. 8:671-677(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH E4F1.
  21. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-15 AND SER-17, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  22. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  23. "The crystal structure of the tumor suppressor protein pp32 (Anp32a): structural insights into Anp32 family of proteins."
    Huyton T., Wolberger C.
    Protein Sci. 16:1308-1315(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-149, LEUCINE-RICH REPEATS.

Entry informationi

Entry nameiAN32A_HUMAN
AccessioniPrimary (citable) accession number: P39687
Secondary accession number(s): B2R6T4
, Q53FK4, Q5J8L8, Q7M4N6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: October 29, 2014
This is version 153 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 15
    Human chromosome 15: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3