O95757 (HS74L_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Heat shock 70 kDa protein 4L

Alternative name(s):
Heat shock 70-related protein APG-1
Osmotic stress protein 94

Gene names

Name:	HSPA4L
Synonyms:	APG1, OSP94

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	839 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Possesses chaperone activity in vitro where it inhibits aggregation of citrate synthase By similarity.
Subunit structure	Homodimer By similarity.
Subcellular location	Cytoplasm By similarity. Nucleus By similarity. Note: May translocate to the nucleus after heat shock By similarity.
Induction	By heat shock.
Post-translational modification	Phosphorylated upon DNA damage, probably by ATM or ATR. Ref.4 Ref.5
Sequence similarities	Belongs to the heat shock protein 70 family.

Ontologies

Keywords
Biological process	Stress response
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Polymorphism
Ligand	ATP-binding Nucleotide-binding
Molecular function	Chaperone
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	protein folding Inferred from sequence or structural similarity. Source: UniProtKB response to unfolded protein Inferred from sequence or structural similarity. Source: UniProtKB
Cellular component	cytoplasm Inferred from sequence or structural similarity. Source: UniProtKB nucleus Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	ATP binding Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 839	839	Heat shock 70 kDa protein 4L		PRO_0000078280
Amino acid modifications
	Modified residue	74	1	Phosphoserine By similarity
	Modified residue	272	1	N6-acetyllysine Ref.6
	Modified residue	571	1	Phosphothreonine Ref.5
	Modified residue	761	1	Phosphothreonine Ref.4
Natural variations
	Natural variant	211	1	L → S. Ref.1 Corresponds to variant rs1380154 [ dbSNP | Ensembl ].		VAR_025405
	Natural variant	216	1	N → T. Corresponds to variant rs12507229 [ dbSNP | Ensembl ].		VAR_031214
	Natural variant	601	1	I → T. Corresponds to variant rs35518193 [ dbSNP | Ensembl ].		VAR_055966
Experimental info
	Sequence conflict	806	1	H → R in BAA75063. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	O95757 [UniParc]. Last modified November 2, 2010. Version 3. Checksum: 549933AECFF4369A	FASTA	839	94,512
	10 20 30 40 50 60 MSVVGIDLGF LNCYIAVARS GGIETIANEY SDRCTPACIS LGSRTRAIGN AAKSQIVTNV 70 80 90 100 110 120 RNTIHGFKKL HGRSFDDPIV QTERIRLPYE LQKMPNGSAG VKVRYLEEER PFAIEQVTGM 130 140 150 160 170 180 LLAKLKETSE NALKKPVADC VISIPSFFTD AERRSVMAAA QVAGLNCLRL MNETTAVALA 190 200 210 220 230 240 YGIYKQDLPP LDEKPRNVVF IDMGHSAYQV LVCAFNKGKL KVLATTFDPY LGGRNFDEAL 250 260 270 280 290 300 VDYFCDEFKT KYKINVKENS RALLRLYQEC EKLKKLMSAN ASDLPLNIEC FMNDLDVSSK 310 320 330 340 350 360 MNRAQFEQLC ASLLARVEPP LKAVMEQANL QREDISSIEI VGGATRIPAV KEQITKFFLK 370 380 390 400 410 420 DISTTLNADE AVARGCALQC AILSPAFKVR EFSITDLVPY SITLRWKTSF EDGSGECEVF 430 440 450 460 470 480 CKNHPAPFSK VITFHKKEPF ELEAFYTNLH EVPYPDARIG SFTIQNVFPQ SDGDSSKVKV 490 500 510 520 530 540 KVRVNIHGIF SVASASVIEK QNLEGDHSDA PMETETSFKN ENKDNMDKMQ VDQEEGHQKC 550 560 570 580 590 600 HAEHTPEEEI DHTGAKTKSA VSDKQDRLNQ TLKKGKVKSI DLPIQSSLCR QLGQDLLNSY 610 620 630 640 650 660 IENEGKMIMQ DKLEKERNDA KNAVEEYVYD FRDRLGTVYE KFITPEDLSK LSAVLEDTEN 670 680 690 700 710 720 WLYEDGEDQP KQVYVDKLQE LKKYGQPIQM KYMEHEERPK ALNDLGKKIQ LVMKVIEAYR 730 740 750 760 770 780 NKDERYDHLD PTEMEKVEKC ISDAMSWLNS KMNAQNKLSL TQDPVVKVSE IVAKSKELDN 790 800 810 820 830 FCNPIIYKPK PKAEVPEDKP KANSEHNGPM DGQSGTETKS DSTKDSSQHT KSSGEMEVD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning of human cDNAs for Apg-1 and Apg-2, members of the Hsp110 family, and chromosomal assignment of their genes." Nonoguchi K., Itoh K., Xue J.H., Tokuchi H., Nishiyama H., Kaneko Y., Tatsumi K., Okuno H., Tomiwa K., Fujita J. Gene 237:21-28(1999) [PubMed: 10524232] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT SER-211. Tissue: Testis.
[2]	"Generation and annotation of the DNA sequences of human chromosomes 2 and 4." Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K. Nature 434:724-731(2005) [PubMed: 15815621] [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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]	"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: 17525332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-761, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[5]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-571, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[6]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-272, MASS SPECTROMETRY.
[7]	"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: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB023421 mRNA. Translation: BAA75063.1. AC093591 Genomic DNA. Translation: AAY40975.1. BC040560 mRNA. Translation: AAH40560.1.
IPI	IPI00295485.
RefSeq	NP_055093.2. NM_014278.2.
UniGene	Hs.135554.
3D structure databases
ProteinModelPortal	O95757.
SMR	O95757. Positions 302-388.
ModBase	Search...
Protein-protein interaction databases
IntAct	O95757. 3 interactions.
MINT	MINT-1135179.
STRING	O95757.
PTM databases
PhosphoSite	O95757.
2D gel databases
REPRODUCTION-2DPAGE	IPI00295485.
Proteomic databases
PRIDE	O95757.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000296464; ENSP00000296464; ENSG00000164070. ENST00000438626; ENSP00000390499; ENSG00000164070.
GeneID	22824.
KEGG	hsa:22824.
Organism-specific databases
CTD	22824.
GeneCards	GC04P128703.
HGNC	HGNC:17041. HSPA4L.
HPA	CAB034450.
neXtProt	NX_O95757.
GenAtlas	Search...
Phylogenomic databases
HOVERGEN	HBG047955.
InParanoid	O95757.
PhylomeDB	O95757.
Gene expression databases
ArrayExpress	O95757.
Bgee	O95757.
CleanEx	HS_HSPA4L.
Genevestigator	O95757.
Family and domain databases
InterPro	IPR018181. Heat_shock_70_CS. IPR001023. Hsp70. IPR013126. Hsp_70. [Graphical view]
KO	K09485.
PANTHER	PTHR19375. Hsp70. 1 hit.
Pfam	PF00012. HSP70. 2 hits. [Graphical view]
PRINTS	PR00301. HEATSHOCK70.
PROSITE	PS00297. HSP70_1. False negative. PS00329. HSP70_2. False negative. PS01036. HSP70_3. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	43228.

Entry information

Entry name

HS74L_HUMAN

Accession

Primary (citable) accession number: O95757
Secondary accession number(s): Q4W5M5, Q8IWA2

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	November 2, 2010
Last modified:	January 25, 2012
This is version 100 of the entry and version 3 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.