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P34932

- HSP74_HUMAN

UniProt

P34932 - HSP74_HUMAN

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Protein

Heat shock 70 kDa protein 4

Gene

HSPA4

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

  1. ATP binding Source: UniProtKB

GO - Biological processi

  1. chaperone-mediated protein complex assembly Source: BHF-UCL
  2. protein import into mitochondrial outer membrane Source: BHF-UCL
  3. response to unfolded protein Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Stress response

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Heat shock 70 kDa protein 4
Alternative name(s):
HSP70RY
Heat shock 70-related protein APG-2
Gene namesi
Name:HSPA4
Synonyms:APG2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 5

Organism-specific databases

HGNCiHGNC:5237. HSPA4.

Subcellular locationi

Cytoplasm Curated

GO - Cellular componenti

  1. cytosol Source: UniProt
  2. extracellular vesicular exosome Source: UniProtKB
  3. mitochondrion Source: GOC
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA29503.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 840840Heat shock 70 kDa protein 4PRO_0000078262Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei53 – 531N6-acetyllysineBy similarity
Modified residuei76 – 761Phosphoserine2 Publications
Modified residuei89 – 891Phosphotyrosine1 Publication
Modified residuei336 – 3361Phosphotyrosine2 Publications
Modified residuei430 – 4301N6-acetyllysine1 Publication
Modified residuei538 – 5381Phosphothreonine1 Publication
Modified residuei546 – 5461Phosphoserine1 Publication
Modified residuei660 – 6601PhosphotyrosineBy similarity
Modified residuei679 – 6791N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP34932.
PaxDbiP34932.
PRIDEiP34932.

2D gel databases

DOSAC-COBS-2DPAGEP34932.
REPRODUCTION-2DPAGEIPI00002966.
P34932.

PTM databases

PhosphoSiteiP34932.

Expressioni

Gene expression databases

BgeeiP34932.
CleanExiHS_HSPA4.
ExpressionAtlasiP34932. baseline and differential.
GenevestigatoriP34932.

Organism-specific databases

HPAiCAB025529.
HPA010023.

Interactioni

Subunit structurei

Interacts with TJP1/ZO-1.By similarity

Protein-protein interaction databases

BioGridi109540. 288 interactions.
DIPiDIP-460N.
IntActiP34932. 26 interactions.
MINTiMINT-1159519.
STRINGi9606.ENSP00000302961.

Structurei

3D structure databases

ProteinModelPortaliP34932.
SMRiP34932. Positions 5-697.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the heat shock protein 70 family.Curated

Phylogenomic databases

eggNOGiCOG0443.
GeneTreeiENSGT00390000016919.
HOGENOMiHOG000228138.
HOVERGENiHBG047955.
InParanoidiP34932.
KOiK09489.
OMAiKVKYMEE.
OrthoDBiEOG77M8N0.
PhylomeDBiP34932.
TreeFamiTF105043.

Family and domain databases

Gene3Di1.20.1270.10. 2 hits.
2.60.34.10. 2 hits.
InterProiIPR018181. Heat_shock_70_CS.
IPR029048. HSP70_C.
IPR029047. HSP70_peptide-bd.
IPR013126. Hsp_70_fam.
[Graphical view]
PfamiPF00012. HSP70. 1 hit.
[Graphical view]
PRINTSiPR00301. HEATSHOCK70.
SUPFAMiSSF100920. SSF100920. 2 hits.
SSF100934. SSF100934. 2 hits.
PROSITEiPS00329. HSP70_2. 1 hit.
PS01036. HSP70_3. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P34932-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MSVVGIDLGF QSCYVAVARA GGIETIANEY SDRCTPACIS FGPKNRSIGA
60 70 80 90 100
AAKSQVISNA KNTVQGFKRF HGRAFSDPFV EAEKSNLAYD IVQLPTGLTG
110 120 130 140 150
IKVTYMEEER NFTTEQVTAM LLSKLKETAE SVLKKPVVDC VVSVPCFYTD
160 170 180 190 200
AERRSVMDAT QIAGLNCLRL MNETTAVALA YGIYKQDLPA LEEKPRNVVF
210 220 230 240 250
VDMGHSAYQV SVCAFNRGKL KVLATAFDTT LGGRKFDEVL VNHFCEEFGK
260 270 280 290 300
KYKLDIKSKI RALLRLSQEC EKLKKLMSAN ASDLPLSIEC FMNDVDVSGT
310 320 330 340 350
MNRGKFLEMC NDLLARVEPP LRSVLEQTKL KKEDIYAVEI VGGATRIPAV
360 370 380 390 400
KEKISKFFGK ELSTTLNADE AVTRGCALQC AILSPAFKVR EFSITDVVPY
410 420 430 440 450
PISLRWNSPA EEGSSDCEVF SKNHAAPFSK VLTFYRKEPF TLEAYYSSPQ
460 470 480 490 500
DLPYPDPAIA QFSVQKVTPQ SDGSSSKVKV KVRVNVHGIF SVSSASLVEV
510 520 530 540 550
HKSEENEEPM ETDQNAKEEE KMQVDQEEPH VEEQQQQTPA ENKAESEEME
560 570 580 590 600
TSQAGSKDKK MDQPPQAKKA KVKTSTVDLP IENQLLWQID REMLNLYIEN
610 620 630 640 650
EGKMIMQDKL EKERNDAKNA VEEYVYEMRD KLSGEYEKFV SEDDRNSFTL
660 670 680 690 700
KLEDTENWLY EDGEDQPKQV YVDKLAELKN LGQPIKIRFQ ESEERPKLFE
710 720 730 740 750
ELGKQIQQYM KIISSFKNKE DQYDHLDAAD MTKVEKSTNE AMEWMNNKLN
760 770 780 790 800
LQNKQSLTMD PVVKSKEIEA KIKELTSTCS PIISKPKPKV EPPKEEQKNA
810 820 830 840
EQNGPVDGQG DNPGPQAAEQ GTDTAVPSDS DKKLPEMDID
Length:840
Mass (Da):94,331
Last modified:September 23, 2008 - v4
Checksum:i8B690A52A0729C2A
GO
Isoform 2 (identifier: P34932-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     109-800: Missing.

Show »
Length:148
Mass (Da):15,689
Checksum:iC269BCA9925F562F
GO

Sequence cautioni

The sequence AAA02807.1 differs from that shown. Reason: Frameshift at positions 567, 586, 697, 715 and 722. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti94 – 941L → W in AAA02807. (PubMed:8335910)Curated
Sequence conflicti190 – 1901A → R in AAA02807. (PubMed:8335910)Curated
Sequence conflicti583 – 5864NQLL → ESAI in AAA02807. (PubMed:8335910)Curated
Sequence conflicti622 – 6221E → R in BAA75062. 1 PublicationCurated
Sequence conflicti644 – 6441D → G in BAA75062. 1 PublicationCurated
Sequence conflicti746 – 7494NNKL → EVTP in AAA02807. (PubMed:8335910)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei109 – 800692Missing in isoform 2. 2 PublicationsVSP_056885Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB023420 mRNA. Translation: BAA75062.1.
BT007375 mRNA. Translation: AAP36039.1.
AC113410 Genomic DNA. No translation available.
BC002526 mRNA. Translation: AAH02526.1.
BC110861 mRNA. Translation: AAI10862.1.
BC126122 mRNA. Translation: AAI26123.1.
BC126124 mRNA. Translation: AAI26125.1.
L12723 mRNA. Translation: AAA02807.1. Frameshift.
CCDSiCCDS4166.1.
PIRiI56208.
RefSeqiNP_002145.3. NM_002154.3.
UniGeneiHs.90093.

Genome annotation databases

EnsembliENST00000304858; ENSP00000302961; ENSG00000170606. [P34932-1]
ENST00000617819; ENSP00000480688; ENSG00000170606. [P34932-2]
GeneIDi3308.
KEGGihsa:3308.
UCSCiuc003kyj.3. human. [P34932-1]

Polymorphism databases

DMDMi206729934.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB023420 mRNA. Translation: BAA75062.1 .
BT007375 mRNA. Translation: AAP36039.1 .
AC113410 Genomic DNA. No translation available.
BC002526 mRNA. Translation: AAH02526.1 .
BC110861 mRNA. Translation: AAI10862.1 .
BC126122 mRNA. Translation: AAI26123.1 .
BC126124 mRNA. Translation: AAI26125.1 .
L12723 mRNA. Translation: AAA02807.1 . Frameshift.
CCDSi CCDS4166.1.
PIRi I56208.
RefSeqi NP_002145.3. NM_002154.3.
UniGenei Hs.90093.

3D structure databases

ProteinModelPortali P34932.
SMRi P34932. Positions 5-697.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109540. 288 interactions.
DIPi DIP-460N.
IntActi P34932. 26 interactions.
MINTi MINT-1159519.
STRINGi 9606.ENSP00000302961.

PTM databases

PhosphoSitei P34932.

Polymorphism databases

DMDMi 206729934.

2D gel databases

DOSAC-COBS-2DPAGE P34932.
REPRODUCTION-2DPAGE IPI00002966.
P34932.

Proteomic databases

MaxQBi P34932.
PaxDbi P34932.
PRIDEi P34932.

Protocols and materials databases

DNASUi 3308.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000304858 ; ENSP00000302961 ; ENSG00000170606 . [P34932-1 ]
ENST00000617819 ; ENSP00000480688 ; ENSG00000170606 . [P34932-2 ]
GeneIDi 3308.
KEGGi hsa:3308.
UCSCi uc003kyj.3. human. [P34932-1 ]

Organism-specific databases

CTDi 3308.
GeneCardsi GC05P132415.
HGNCi HGNC:5237. HSPA4.
HPAi CAB025529.
HPA010023.
MIMi 601113. gene.
neXtProti NX_P34932.
PharmGKBi PA29503.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0443.
GeneTreei ENSGT00390000016919.
HOGENOMi HOG000228138.
HOVERGENi HBG047955.
InParanoidi P34932.
KOi K09489.
OMAi KVKYMEE.
OrthoDBi EOG77M8N0.
PhylomeDBi P34932.
TreeFami TF105043.

Miscellaneous databases

ChiTaRSi HSPA4. human.
GeneWikii HSPA4.
GenomeRNAii 3308.
NextBioi 13119.
PROi P34932.
SOURCEi Search...

Gene expression databases

Bgeei P34932.
CleanExi HS_HSPA4.
ExpressionAtlasi P34932. baseline and differential.
Genevestigatori P34932.

Family and domain databases

Gene3Di 1.20.1270.10. 2 hits.
2.60.34.10. 2 hits.
InterProi IPR018181. Heat_shock_70_CS.
IPR029048. HSP70_C.
IPR029047. HSP70_peptide-bd.
IPR013126. Hsp_70_fam.
[Graphical view ]
Pfami PF00012. HSP70. 1 hit.
[Graphical view ]
PRINTSi PR00301. HEATSHOCK70.
SUPFAMi SSF100920. SSF100920. 2 hits.
SSF100934. SSF100934. 2 hits.
PROSITEi PS00329. HSP70_2. 1 hit.
PS01036. HSP70_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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] (ISOFORM 1).
  2. "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] (ISOFORM 2).
  3. "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].
  4. "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] (ISOFORMS 1 AND 2).
    Tissue: Brain, Placenta and Skin.
  5. "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 (ISOFORM 1).
    Tissue: Lymphocyte.
  6. 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, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
  7. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-538, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  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-430 AND LYS-679, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiHSP74_HUMAN
AccessioniPrimary (citable) accession number: P34932
Secondary accession number(s): O95756, Q2TAL4, Q9BUK9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: September 23, 2008
Last modified: November 26, 2014
This is version 145 of the entry and version 4 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3