P34932 (HSP74_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Heat shock 70 kDa protein 4

Alternative name(s):
HSP70RY
Heat shock 70-related protein APG-2

Gene names

Name:	HSPA4
Synonyms:	APG2

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	840 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Subunit structure	Interacts with TJP1/ZO-1 By similarity.
Subcellular location	Cytoplasm Probable.
Sequence similarities	Belongs to the heat shock protein 70 family.
Sequence caution	The sequence AAA02807.1 differs from that shown. Reason: Frameshift at positions 567, 586, 697, 715 and 722.

Ontologies

Keywords
Biological process	Stress response
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	chaperone-mediated protein complex assembly Inferred from direct assay PubMed 15644312. Source: BHF-UCL protein import into mitochondrial outer membrane Inferred from direct assay PubMed 15644312. Source: BHF-UCL response to unfolded protein Non-traceable author statement Ref.4. Source: UniProtKB
Cellular_component	cytoplasm Non-traceable author statement. Source: UniProtKB nucleus Inferred from direct assay. Source: HPA
Molecular_function	ATP binding Non-traceable author statement Ref.4. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 840	840	Heat shock 70 kDa protein 4		PRO_0000078262
Amino acid modifications
	Modified residue	76	1	Phosphoserine Ref.9 Ref.12
	Modified residue	89	1	Phosphotyrosine Ref.6
	Modified residue	336	1	Phosphotyrosine Ref.6 Ref.9
	Modified residue	430	1	N6-acetyllysine Ref.10
	Modified residue	538	1	Phosphothreonine Ref.8
	Modified residue	546	1	Phosphoserine Ref.12
	Modified residue	660	1	Phosphotyrosine By similarity
	Modified residue	679	1	N6-acetyllysine Ref.10
Experimental info
	Sequence conflict	94	1	L → W in AAA02807. Ref.4
	Sequence conflict	190	1	A → R in AAA02807. Ref.4
	Sequence conflict	583 – 586	4	NQLL → ESAI in AAA02807. Ref.4
	Sequence conflict	622	1	E → R in BAA75062. Ref.1
	Sequence conflict	644	1	D → G in BAA75062. Ref.1
	Sequence conflict	746 – 749	4	NNKL → EVTP in AAA02807. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	P34932 [UniParc]. Last modified September 23, 2008. Version 4. Checksum: 8B690A52A0729C2A	FASTA	840	94,331
	10 20 30 40 50 60 MSVVGIDLGF QSCYVAVARA GGIETIANEY SDRCTPACIS FGPKNRSIGA AAKSQVISNA 70 80 90 100 110 120 KNTVQGFKRF HGRAFSDPFV EAEKSNLAYD IVQLPTGLTG IKVTYMEEER NFTTEQVTAM 130 140 150 160 170 180 LLSKLKETAE SVLKKPVVDC VVSVPCFYTD AERRSVMDAT QIAGLNCLRL MNETTAVALA 190 200 210 220 230 240 YGIYKQDLPA LEEKPRNVVF VDMGHSAYQV SVCAFNRGKL KVLATAFDTT LGGRKFDEVL 250 260 270 280 290 300 VNHFCEEFGK KYKLDIKSKI RALLRLSQEC EKLKKLMSAN ASDLPLSIEC FMNDVDVSGT 310 320 330 340 350 360 MNRGKFLEMC NDLLARVEPP LRSVLEQTKL KKEDIYAVEI VGGATRIPAV KEKISKFFGK 370 380 390 400 410 420 ELSTTLNADE AVTRGCALQC AILSPAFKVR EFSITDVVPY PISLRWNSPA EEGSSDCEVF 430 440 450 460 470 480 SKNHAAPFSK VLTFYRKEPF TLEAYYSSPQ DLPYPDPAIA QFSVQKVTPQ SDGSSSKVKV 490 500 510 520 530 540 KVRVNVHGIF SVSSASLVEV HKSEENEEPM ETDQNAKEEE KMQVDQEEPH VEEQQQQTPA 550 560 570 580 590 600 ENKAESEEME TSQAGSKDKK MDQPPQAKKA KVKTSTVDLP IENQLLWQID REMLNLYIEN 610 620 630 640 650 660 EGKMIMQDKL EKERNDAKNA VEEYVYEMRD KLSGEYEKFV SEDDRNSFTL KLEDTENWLY 670 680 690 700 710 720 EDGEDQPKQV YVDKLAELKN LGQPIKIRFQ ESEERPKLFE ELGKQIQQYM KIISSFKNKE 730 740 750 760 770 780 DQYDHLDAAD MTKVEKSTNE AMEWMNNKLN LQNKQSLTMD PVVKSKEIEA KIKELTSTCS 790 800 810 820 830 840 PIISKPKPKV EPPKEEQKNA EQNGPVDGQG DNPGPQAAEQ GTDTAVPSDS DKKLPEMDID

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and characterization of human apg-1 and apg-2, members of the hsp110 family, cDNAs and chromosomal assignment of the genes." Nonoguchi K., Fujita J. Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"The DNA sequence and comparative analysis of human chromosome 5." Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S. , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M. Nature 431:268-274(2004) [PubMed] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain and Skin.
[4]	"Molecular cloning of a novel human hsp70 from a B cell line and its assignment to chromosome 5." Fathallah D.M., Cherif D., Dellagi K., Arnaout M.A. J. Immunol. 151:810-813(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-749. Tissue: Lymphocyte.
[5]	Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y. Submitted (DEC-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 20-33; 111-124; 170-185; 222-234; 333-346; 361-374 AND 391-422, MASS SPECTROMETRY. Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
[6]	"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells." Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J. Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-89 AND TYR-336, MASS SPECTROMETRY.
[7]	"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Embryonic kidney.
[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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-538, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-76 AND TYR-336, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[10]	"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-430 AND LYS-679, MASS SPECTROMETRY.
[11]	"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].
[12]	"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 SER-76 AND SER-546, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB023420 mRNA. Translation: BAA75062.1. AC113410 Genomic DNA. No translation available. BC110861 mRNA. Translation: AAI10862.1. BC126122 mRNA. Translation: AAI26123.1. BC126124 mRNA. Translation: AAI26125.1. L12723 mRNA. Translation: AAA02807.1. Frameshift.
IPI	IPI00002966.
PIR	I56208.
RefSeq	NP_002145.3. NM_002154.3.
UniGene	Hs.90093.
3D structure databases
ProteinModelPortal	P34932.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-460N.
IntAct	P34932. 16 interactions.
MINT	MINT-1159519.
STRING	9606.ENSP00000302961.
PTM databases
PhosphoSite	P34932.
Polymorphism databases
DMDM	206729934.
2D gel databases
DOSAC-COBS-2DPAGE	P34932.
REPRODUCTION-2DPAGE	IPI00002966. P34932.
Proteomic databases
PaxDb	P34932.
PRIDE	P34932.
Protocols and materials databases
DNASU	3308.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000304858; ENSP00000302961; ENSG00000170606.
GeneID	3308.
KEGG	hsa:3308.
UCSC	uc003kyj.3. human.
Organism-specific databases
CTD	3308.
GeneCards	GC05P132415.
HGNC	HGNC:5237. HSPA4.
HPA	CAB025529. HPA010023.
MIM	601113. gene.
neXtProt	NX_P34932.
PharmGKB	PA29503.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0443.
HOGENOM	HOG000228138.
HOVERGEN	HBG047955.
InParanoid	P34932.
KO	K09489.
OMA	LYIENEG.
OrthoDB	EOG415GCS.
PhylomeDB	P34932.
Gene expression databases
ArrayExpress	P34932.
Bgee	P34932.
CleanEx	HS_HSPA4.
Genevestigator	P34932.
GermOnline	ENSG00000170606. Homo sapiens.
Family and domain databases
InterPro	IPR018181. Heat_shock_70_CS. IPR013126. Hsp_70_fam. [Graphical view]
Pfam	PF00012. HSP70. 1 hit. [Graphical view]
PRINTS	PR00301. HEATSHOCK70.
PROSITE	PS00297. HSP70_1. False negative. PS00329. HSP70_2. 1 hit. PS01036. HSP70_3. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	HSPA4. human.
GenomeRNAi	3308.
NextBio	13119.
SOURCE	Search...

Entry information

Entry name

HSP74_HUMAN

Accession

Primary (citable) accession number: P34932
Secondary accession number(s): O95756, Q2TAL4

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1994
Last sequence update:	September 23, 2008
Last modified:	May 1, 2013
This is version 130 of the entry and version 4 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.