Share to:

HSPA2

HSPA2

Available structures

Ortholog search: PDBe RCSB

List of PDB id codes
3I33, 4FSV, 5FPM, 5FPN, 5FPD, 5FPE

Identifiers

HSPA2, HSP70-2, HSP70-3, heat shock protein family A (Hsp70) member 2

External IDs

OMIM: 140560; MGI: 96243; HomoloGene: 68564; GeneCards: HSPA2; OMA:HSPA2 - orthologs

Gene location (Human)

Chr.	Chromosome 14 (human)^[1]

Band	14q23.3	Start	64,535,905 bp^[1]
Band	14q23.3	End	64,546,173 bp^[1]

Gene location (Mouse)

Chr.	Chromosome 12 (mouse)^[2]

Band	12 C3\|12 33.73 cM	Start	76,450,950 bp^[2]
Band	12 C3\|12 33.73 cM	End	76,453,712 bp^[2]

RNA expression pattern

Human

Mouse (ortholog)

Top expressed in

inferior ganglion of vagus nerve

middle frontal gyrus

subthalamic nucleus

external globus pallidus

Medulla Oblongata

pars reticulata

internal globus pallidus

superior vestibular nucleus

Skeletal muscle tissue of rectus abdominis

corpus callosum

Top expressed in

seminiferous tubule

spermatocyte

spermatid

ascending aorta

aortic valve

dentate gyrus of hippocampal formation granule cell

piriform cortex

hippocampus proper

supraoptic nucleus

olfactory epithelium

More reference expression data


More reference expression data

Gene ontology
Molecular function	nucleotide binding unfolded protein binding protein binding enzyme binding ATP binding disordered domain specific binding glycolipid binding ATPase activity heat shock protein binding protein folding chaperone activity tau protein binding chaperone binding misfolded protein binding
Cellular component	cytoplasm cytosol blood microparticle membrane spindle extracellular exosome cytoskeleton nucleus synaptonemal complex male germ cell nucleus mitochondrion cell surface CatSper complex myelin sheath meiotic spindle plasma membrane
Biological process	cell differentiation negative regulation of inclusion body assembly response to heat response to unfolded protein protein refolding spermatogenesis response to cold positive regulation of protein phosphorylation male meiotic nuclear division male meiosis I spermatid development positive regulation of ATP-dependent activity synaptonemal complex disassembly positive regulation of ATPase-coupled calcium transmembrane transporter activity positive regulation of G2/M transition of mitotic cell cycle vesicle-mediated transport cellular response to heat Unfolded Protein Response chaperone cofactor-dependent protein refolding
Sources:Amigo / QuickGO

Species

Human

Mouse


3306


15512


ENSG00000126803


ENSMUSG00000059970


P54652


P17156

RefSeq (mRNA)


NM_021979 NM_001387931


NM_001002012 NM_008301

RefSeq (protein)


NP_068814


NP_001002012 NP_032327

Location (UCSC)

Chr 14: 64.54 – 64.55 Mb

Chr 12: 76.45 – 76.45 Mb

PubMed search

^[3]

^[4]

View/Edit Human

View/Edit Mouse

Heat shock-related 70 kDa protein 2 is a protein that in humans is encoded by the HSPA2 gene.^[5]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000126803 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000059970 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Entrez Gene: HSPA2 heat shock 70kDa protein 2".

Further reading

Schwab CG, Bozak CK, Whitehouse NL, Olson VM (1993). "Amino acid limitation and flow to the duodenum at four stages of lactation. 2. Extent of lysine limitation". J. Dairy Sci. 75 (12): 3503–18. doi:10.3168/jds.S0022-0302(92)78126-0. PMID 1474216.
Dworniczak B, Mirault ME (1987). "Structure and expression of a human gene coding for a 71 kd heat shock 'cognate' protein". Nucleic Acids Res. 15 (13): 5181–97. doi:10.1093/nar/15.13.5181. PMC 305955. PMID 3037489.
Bonnycastle LL, Yu CE, Hunt CR, et al. (1995). "Cloning, sequencing, and mapping of the human chromosome 14 heat shock protein gene (HSPA2)". Genomics. 23 (1): 85–93. doi:10.1006/geno.1994.1462. PMID 7829106.
Roux AF, Nguyen VT, Squire JA, Cox DW (1995). "A heat shock gene at 14q22: mapping and expression". Hum. Mol. Genet. 3 (10): 1819–22. doi:10.1093/hmg/3.10.1819. PMID 7849706.
Furlini G, Vignoli M, Re MC, et al. (1994). "Human immunodeficiency virus type 1 interaction with the membrane of CD4+ cells induces the synthesis and nuclear translocation of 70K heat shock protein". J. Gen. Virol. 75 (1): 193–9. doi:10.1099/0022-1317-75-1-193. PMID 7906708.
Allen JW, Dix DJ, Collins BW, et al. (1996). "HSP70-2 is part of the synaptonemal complex in mouse and hamster spermatocytes". Chromosoma. 104 (6): 414–21. doi:10.1007/BF00352265. PMID 8601336. S2CID 7244472.
Dix DJ, Allen JW, Collins BW, et al. (1996). "Targeted gene disruption of Hsp70-2 results in failed meiosis, germ cell apoptosis, and male infertility". Proc. Natl. Acad. Sci. U.S.A. 93 (8): 3264–8. Bibcode:1996PNAS...93.3264D. doi:10.1073/pnas.93.8.3264. PMC 39594. PMID 8622925.
Zhu D, Dix DJ, Eddy EM (1997). "HSP70-2 is required for CDC2 kinase activity in meiosis I of mouse spermatocytes". Development. 124 (15): 3007–14. doi:10.1242/dev.124.15.3007. PMID 9247342.
O'Keeffe B, Fong Y, Chen D, et al. (2000). "Requirement for a kinase-specific chaperone pathway in the production of a Cdk9/cyclin T1 heterodimer responsible for P-TEFb-mediated tat stimulation of HIV-1 transcription". J. Biol. Chem. 275 (1): 279–87. doi:10.1074/jbc.275.1.279. PMID 10617616.
Agostini I, Popov S, Li J, et al. (2000). "Heat-shock protein 70 can replace viral protein R of HIV-1 during nuclear import of the viral preintegration complex". Exp. Cell Res. 259 (2): 398–403. doi:10.1006/excr.2000.4992. PMID 10964507.
Andersen JS, Lyon CE, Fox AH, et al. (2002). "Directed proteomic analysis of the human nucleolus". Curr. Biol. 12 (1): 1–11. Bibcode:2002CBio...12....1A. doi:10.1016/S0960-9822(01)00650-9. PMID 11790298.
Gurer C, Cimarelli A, Luban J (2002). "Specific incorporation of heat shock protein 70 family members into primate lentiviral virions". J. Virol. 76 (9): 4666–70. doi:10.1128/JVI.76.9.4666-4670.2002. PMC 155079. PMID 11932435.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
Shin BK, Wang H, Yim AM, et al. (2003). "Global profiling of the cell surface proteome of cancer cells uncovers an abundance of proteins with chaperone function". J. Biol. Chem. 278 (9): 7607–16. doi:10.1074/jbc.M210455200. PMID 12493773.
Lim MC, Brooke SM, Sapolsky RM (2003). "gp120 neurotoxicity fails to induce heat shock defenses, while the over expression of hsp70 protects against gp120". Brain Res. Bull. 61 (2): 183–8. doi:10.1016/S0361-9230(03)00113-8. PMID 12832005. S2CID 35451084.
Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
Bouwmeester T, Bauch A, Ruffner H, et al. (2004). "A physical and functional map of the human TNF-alpha/NF-kappa B signal transduction pathway". Nat. Cell Biol. 6 (2): 97–105. doi:10.1038/ncb1086. PMID 14743216. S2CID 11683986.
Brandenberger R, Wei H, Zhang S, et al. (2005). "Transcriptome characterization elucidates signaling networks that control human ES cell growth and differentiation". Nat. Biotechnol. 22 (6): 707–16. doi:10.1038/nbt971. PMID 15146197. S2CID 27764390.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.

PDB gallery

1hpm: HOW POTASSIUM AFFECTS THE ACTIVITY OF THE MOLECULAR CHAPERONE HSC70. II. POTASSIUM BINDS SPECIFICALLY IN THE ATPASE ACTIVE SITE
1hx1: CRYSTAL STRUCTURE OF A BAG DOMAIN IN COMPLEX WITH THE HSC70 ATPASE DOMAIN
1kax: 70KD HEAT SHOCK COGNATE PROTEIN ATPASE DOMAIN, K71M MUTANT
1kay: 70KD HEAT SHOCK COGNATE PROTEIN ATPASE DOMAIN, K71A MUTANT
1kaz: 70KD HEAT SHOCK COGNATE PROTEIN ATPASE DOMAIN, K71E MUTANT
1ngi: STRUCTURAL BASIS OF THE 70-KILODALTON HEAT SHOCK COGNATE PROTEIN ATP HYDROLYTIC ACTIVITY, II. STRUCTURE OF THE ACTIVE SITE WITH ADP OR ATP BOUND TO WILD TYPE AND MUTANT ATPASE FRAGMENT
1ngj: STRUCTURAL BASIS OF THE 70-KILODALTON HEAT SHOCK COGNATE PROTEIN ATP HYDROLYTIC ACTIVITY, II. STRUCTURE OF THE ACTIVE SITE WITH ADP OR ATP BOUND TO WILD TYPE AND MUTANT ATPASE FRAGMENT
1qqo: E175S MUTANT OF BOVINE 70 KILODALTON HEAT SHOCK PROTEIN
2bup: T13G MUTANT OF THE ATPASE FRAGMENT OF BOVINE HSC70
3hsc: THREE-DIMENSIONAL STRUCTURE OF THE ATPASE FRAGMENT OF A 70K HEAT-SHOCK COGNATE PROTEIN

External links

HSPA2+protein,+human at the U.S. National Library of Medicine Medical Subject Headings (MeSH)

Posttranslational modification

Chaperones/
protein folding

Heat shock proteins/ Chaperonins	Hsp10/GroES Hsp27 Hsp47 HSP60/GroEL Hsp40/DnaJ A1 A2 A3 B1 B2 B11 B4 B6 B9 C1 C3 C5 C6 C7 C10 C11 C13 C14 C19 Hsp70 1A 1B 1L 2 4 4L 5 6 7 8 9 12A 14 Hsp90 α₁ α₂ β ER TRAP1
Other	Alpha crystallin Clusterin Survival of motor neuron SMN1 SMN2

Protein targeting

Ubiquitin
(ubiquitylation)

E1 Ubiquitin-activating enzyme
- UBA1
- UBA2
- UBA3
- UBA5
- UBA6
- UBA7
- ATG7
- NAE1
- SAE1

E2 Ubiquitin-conjugating enzyme
- A
- B
- C
- D1
- D2
- D3
- E1
- E2
- E3
- G1
- G2
- H
- I
- J1
- J2
- K
- L1
- L2
- L3
- L4
- L6
- M
- N
- O
- Q1
- Q2
- R1 (CDC34)
- R2
- S
- V1
- V2
- Z

E3 Ubiquitin ligase
- VHL
- Cullin
- CBL
- MDM2
- FANCL
- UBR1

Ubiquitin-like proteins
(UBL)

SUMO protein (SUMOylation)	E1 SUMO-activating enzyme SAE1 SAE2 E2 SUMO-conjugating enzyme UBC9 E3 SUMO ligase PIAS1 PIAS2 PIAS3 PIAS4
Other	ISG15 URM1 UFM1 NEDD8 (neddylation) FAT10 ATG8 ATG12 FUB1 MUB UBL5 Prokaryotic ubiquitin-like protein

This article on a gene on human chromosome 14 is a stub. You can help Wikipedia by expanding it.

Information related to HSPA2

Index: pl ar de en es fr it arz nl ja pt ceb sv uk vi war zh ru af ast az bg zh-min-nan bn be ca cs cy da et el eo eu fa gl ko hi hr id he ka la lv lt hu mk ms min no nn ce uz kk ro simple sk sl sr sh fi ta tt th tg azb tr ur zh-yue hy my ace als am an hyw ban bjn map-bms ba be-tarask bcl bpy bar bs br cv nv eml hif fo fy ga gd gu hak ha hsb io ig ilo ia ie os is jv kn ht ku ckb ky mrj lb lij li lmo mai mg ml zh-classical mr xmf mzn cdo mn nap new ne frr oc mhr or as pa pnb ps pms nds crh qu sa sah sco sq scn si sd szl su sw tl shn te bug vec vo wa wuu yi yo diq bat-smg zu lad kbd ang smn ab roa-rup frp arc gn av ay bh bi bo bxr cbk-zam co za dag ary se pdc dv dsb myv ext fur gv gag inh ki glk gan guw xal haw rw kbp pam csb kw km kv koi kg gom ks gcr lo lbe ltg lez nia ln jbo lg mt mi tw mwl mdf mnw nqo fj nah na nds-nl nrm nov om pi pag pap pfl pcd krc kaa ksh rm rue sm sat sc trv stq nso sn cu so srn kab roa-tara tet tpi to chr tum tk tyv udm ug vep fiu-vro vls wo xh zea ty ak bm ch ny ee ff got iu ik kl mad cr pih ami pwn pnt dz rmy rn sg st tn ss ti din chy ts kcg ve

Prefix: a b c d e f g h i j k l m n o p q r s t u v w x y z 0 1 2 3 4 5 6 7 8 9

Portal di Ensiklopedia Dunia

Kembali kehalaman sebelumnya