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P38647

- GRP75_MOUSE

UniProt

P38647 - GRP75_MOUSE

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Protein

Stress-70 protein, mitochondrial

Gene

Hspa9

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Implicated in the control of cell proliferation and cellular aging. May also act as a chaperone.

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. enzyme binding Source: UniProtKB
  3. poly(A) RNA binding Source: Ensembl

GO - Biological processi

  1. protein export from nucleus Source: MGI
  2. protein folding Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_199101. Mitochondrial protein import.

Names & Taxonomyi

Protein namesi
Recommended name:
Stress-70 protein, mitochondrial
Alternative name(s):
75 kDa glucose-regulated protein
Short name:
GRP-75
Heat shock 70 kDa protein 9
Mortalin
Peptide-binding protein 74
Short name:
PBP74
p66 MOT
Gene namesi
Name:Hspa9
Synonyms:Grp75, Hsp74, Hspa9a
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 18

Organism-specific databases

MGIiMGI:96245. Hspa9.

Subcellular locationi

Mitochondrion 1 Publication. Nucleusnucleolus By similarity

GO - Cellular componenti

  1. cytoplasm Source: MGI
  2. extracellular vesicular exosome Source: Ensembl
  3. mitochondrial nucleoid Source: Ensembl
  4. mitochondrion Source: MGI
  5. nucleus Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4646Mitochondrion1 PublicationAdd
BLAST
Chaini47 – 679633Stress-70 protein, mitochondrialPRO_0000013564Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei76 – 761N6-acetyllysine1 Publication
Modified residuei135 – 1351N6-acetyllysine; alternate2 Publications
Modified residuei135 – 1351N6-succinyllysine; alternate1 Publication
Modified residuei138 – 1381N6-acetyllysine; alternate1 Publication
Modified residuei138 – 1381N6-succinyllysine; alternate1 Publication
Modified residuei143 – 1431N6-acetyllysineBy similarity
Modified residuei206 – 2061N6-acetyllysine; alternate1 Publication
Modified residuei206 – 2061N6-malonyllysine; alternateBy similarity
Modified residuei206 – 2061N6-succinyllysine; alternate1 Publication
Modified residuei234 – 2341N6-acetyllysine1 Publication
Modified residuei288 – 2881N6-acetyllysine1 Publication
Modified residuei300 – 3001N6-acetyllysine; alternate2 Publications
Modified residuei300 – 3001N6-succinyllysine; alternate1 Publication
Modified residuei360 – 3601N6-acetyllysine; alternate2 Publications
Modified residuei360 – 3601N6-succinyllysine; alternate1 Publication
Modified residuei368 – 3681N6-succinyllysine1 Publication
Modified residuei394 – 3941N6-succinyllysine1 Publication
Modified residuei567 – 5671N6-acetyllysine; alternate2 Publications
Modified residuei567 – 5671N6-succinyllysine; alternate1 Publication
Modified residuei600 – 6001N6-acetyllysine; alternate1 Publication
Modified residuei600 – 6001N6-succinyllysine; alternate1 Publication
Modified residuei610 – 6101N6-succinyllysine1 Publication
Modified residuei612 – 6121N6-acetyllysine1 Publication
Modified residuei646 – 6461N6-acetyllysine; alternate1 Publication
Modified residuei646 – 6461N6-succinyllysine; alternate1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP38647.
PRIDEiP38647.

2D gel databases

COMPLUYEAST-2DPAGEP38647.
REPRODUCTION-2DPAGEIPI00133903.
P38647.
SWISS-2DPAGEP38647.

PTM databases

PhosphoSiteiP38647.

Expressioni

Tissue specificityi

Found in all the cell types examined.

Inductioni

Not induced by heat shock, instead protein level is decreased.

Gene expression databases

CleanExiMM_HSPA9.
GenevestigatoriP38647.

Interactioni

Subunit structurei

Interacts with FXN. Interacts with HSCB (By similarity). Component of the MINOS/MitOS complex, that includes IMMT, HSPA9 and CHCHD3 and associates with mitochondrial outer membrane proteins SAMM50, MTX1 and MTX2. Interacts with DNLZ, the interaction is required to prevent self-aggregation (By similarity). Interacts with TESPA1 (By similarity).By similarity

Protein-protein interaction databases

BioGridi200457. 20 interactions.
IntActiP38647. 16 interactions.
MINTiMINT-1860030.
STRINGi10090.ENSMUSP00000025217.

Structurei

3D structure databases

ProteinModelPortaliP38647.
SMRiP38647. Positions 54-651.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the heat shock protein 70 family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0443.
GeneTreeiENSGT00750000117237.
HOGENOMiHOG000228136.
HOVERGENiHBG051845.
InParanoidiP38647.
KOiK04043.
OMAiQRDVAIM.
OrthoDBiEOG715Q3K.
TreeFamiTF105046.

Family and domain databases

Gene3Di1.20.1270.10. 1 hit.
2.60.34.10. 1 hit.
HAMAPiMF_00332. DnaK.
InterProiIPR012725. Chaperone_DnaK.
IPR018181. 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. 1 hit.
TIGRFAMsiTIGR02350. prok_dnaK. 1 hit.
PROSITEiPS00297. HSP70_1. 1 hit.
PS00329. HSP70_2. 1 hit.
PS01036. HSP70_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P38647-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MISASRAAAA RLVGTAASRS PAAARPQDGW NGLSHEAFRF VSRRDYASEA
60 70 80 90 100
IKGAVVGIDL GTTNSCVAVM EGKQAKVLEN AEGARTTPSV VAFTADGERL
110 120 130 140 150
VGMPAKRQAV TNPNNTFYAT KRLIGRRYDD PEVQKDTKNV PFKIVRASNG
160 170 180 190 200
DAWVEAHGKL YSPSQIGAFV LMKMKETAEN YLGHTAKNAV ITVPAYFNDS
210 220 230 240 250
QRQATKDAGQ ISGLNVLRVI NEPTAAALAY GLDKSEDKVI AVYDLGGGTF
260 270 280 290 300
DISILEIQKG VFEVKSTNGD TFLGGEDFDQ ALLRHIVKEF KRETGVDLTK
310 320 330 340 350
DNMALQRVRE AAEKAKCELS SSVQTDINLP YLTMDASGPK HLNMKLTRAQ
360 370 380 390 400
FEGIVTDLIK RTIAPCQKAM QDAEVSKSDI GEVILVGGMT RMPKVQQTVQ
410 420 430 440 450
DLFGRAPSKA VNPDEAVAIG AAIQGGVLAG DVTDVLLLDV TPLSLGIETL
460 470 480 490 500
GGVFTKLINR NTTIPTKKSQ VFSTAADGQT QVEIKVCQGE REMAGDNKLL
510 520 530 540 550
GQFTLIGIPP APRGVPQIEV TFDIDANGIV HVSAKDKGTG REQQIVIQSS
560 570 580 590 600
GGLSKDDIEN MVKNAEKYAE EDRRKKERVE AVNMAEGIIH DTETKMEEFK
610 620 630 640 650
DQLPADECNK LKEEISKMRA LLAGKDSETG ENIRQAASSL QQASLKLFEM
660 670
AYKKMASERE GSGSSGTGEQ KEDQKEEKQ
Length:679
Mass (Da):73,461
Last modified:October 3, 2012 - v3
Checksum:iDF1C997775627928
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti5 – 51S → T AA sequence (PubMed:7684501)Curated
Sequence conflicti78 – 781L → Q in BAE21690. (PubMed:16141072)Curated
Sequence conflicti106 – 1061K → R AA sequence (PubMed:7684501)Curated
Sequence conflicti150 – 1501G → S in BAE35373. (PubMed:16141072)Curated
Sequence conflicti522 – 5221F → S AA sequence (PubMed:7684501)Curated

Polymorphismi

Two forms of the protein have been found, MOT-1, found in mortal cells and MOT-2, found in immortal cells. The sequence of MOT-2 is shown here.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti618 – 6181M → V in MOT-1.
Natural varianti624 – 6241G → R in MOT-1.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D11089 mRNA. Translation: BAA01862.2.
L06896 mRNA. No translation available.
D17666 Genomic DNA. Translation: BAA04548.1.
D17556 mRNA. Translation: BAA04493.1.
AK004946 mRNA. Translation: BAB23690.1.
AK002634 mRNA. Translation: BAB22248.1.
AK133501 mRNA. Translation: BAE21690.1.
AK137109 mRNA. Translation: BAE23238.1.
AK145965 mRNA. Translation: BAE26790.1.
AK159791 mRNA. Translation: BAE35373.1.
AK165958 mRNA. Translation: BAE38486.1.
AK167856 mRNA. Translation: BAE39874.1.
AC114820 Genomic DNA. No translation available.
AC131675 Genomic DNA. No translation available.
CH466557 Genomic DNA. Translation: EDK97122.1.
BC052727 mRNA. Translation: AAH52727.1.
BC057343 mRNA. Translation: AAH57343.1.
CCDSiCCDS29138.1.
PIRiS39839. A48127.
RefSeqiNP_034611.2. NM_010481.2.
UniGeneiMm.209419.

Genome annotation databases

EnsembliENSMUST00000025217; ENSMUSP00000025217; ENSMUSG00000024359.
GeneIDi15526.
KEGGimmu:15526.
UCSCiuc008elv.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D11089 mRNA. Translation: BAA01862.2 .
L06896 mRNA. No translation available.
D17666 Genomic DNA. Translation: BAA04548.1 .
D17556 mRNA. Translation: BAA04493.1 .
AK004946 mRNA. Translation: BAB23690.1 .
AK002634 mRNA. Translation: BAB22248.1 .
AK133501 mRNA. Translation: BAE21690.1 .
AK137109 mRNA. Translation: BAE23238.1 .
AK145965 mRNA. Translation: BAE26790.1 .
AK159791 mRNA. Translation: BAE35373.1 .
AK165958 mRNA. Translation: BAE38486.1 .
AK167856 mRNA. Translation: BAE39874.1 .
AC114820 Genomic DNA. No translation available.
AC131675 Genomic DNA. No translation available.
CH466557 Genomic DNA. Translation: EDK97122.1 .
BC052727 mRNA. Translation: AAH52727.1 .
BC057343 mRNA. Translation: AAH57343.1 .
CCDSi CCDS29138.1.
PIRi S39839. A48127.
RefSeqi NP_034611.2. NM_010481.2.
UniGenei Mm.209419.

3D structure databases

ProteinModelPortali P38647.
SMRi P38647. Positions 54-651.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 200457. 20 interactions.
IntActi P38647. 16 interactions.
MINTi MINT-1860030.
STRINGi 10090.ENSMUSP00000025217.

PTM databases

PhosphoSitei P38647.

2D gel databases

COMPLUYEAST-2DPAGE P38647.
REPRODUCTION-2DPAGE IPI00133903.
P38647.
SWISS-2DPAGE P38647.

Proteomic databases

PaxDbi P38647.
PRIDEi P38647.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000025217 ; ENSMUSP00000025217 ; ENSMUSG00000024359 .
GeneIDi 15526.
KEGGi mmu:15526.
UCSCi uc008elv.2. mouse.

Organism-specific databases

CTDi 3313.
MGIi MGI:96245. Hspa9.

Phylogenomic databases

eggNOGi COG0443.
GeneTreei ENSGT00750000117237.
HOGENOMi HOG000228136.
HOVERGENi HBG051845.
InParanoidi P38647.
KOi K04043.
OMAi QRDVAIM.
OrthoDBi EOG715Q3K.
TreeFami TF105046.

Enzyme and pathway databases

Reactomei REACT_199101. Mitochondrial protein import.

Miscellaneous databases

ChiTaRSi Hspa9. mouse.
NextBioi 288444.
PROi P38647.
SOURCEi Search...

Gene expression databases

CleanExi MM_HSPA9.
Genevestigatori P38647.

Family and domain databases

Gene3Di 1.20.1270.10. 1 hit.
2.60.34.10. 1 hit.
HAMAPi MF_00332. DnaK.
InterProi IPR012725. Chaperone_DnaK.
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. 1 hit.
TIGRFAMsi TIGR02350. prok_dnaK. 1 hit.
PROSITEi PS00297. HSP70_1. 1 hit.
PS00329. HSP70_2. 1 hit.
PS01036. HSP70_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of a novel member of mouse hsp70 family. Its association with cellular mortal phenotype."
    Wadhwa R., Kaul S.C., Ikawa Y., Sugimoto Y.
    J. Biol. Chem. 268:6615-6621(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: CD-1-ICR.
    Tissue: Embryonic fibroblast.
  2. Wadhwa R.
    Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION TO 123.
  3. "Induction of cellular senescence by transfection of cytosolic mortalin cDNA in NIH 3T3 cells."
    Wadhwa R., Kaul S.C., Sugimoto Y., Mitsui Y.
    J. Biol. Chem. 268:22239-22242(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: CD-1-ICR.
    Tissue: Embryonic fibroblast.
  4. "Cloning of the gene encoding peptide-binding protein 74 shows that it is a new member of the heat shock protein 70 family."
    Domanico S.Z., Denagel D.C., Dahlseid J.N., Green J.M., Pierce S.K.
    Mol. Cell. Biol. 13:3598-3610(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
    Tissue: B-cell.
  5. "Structure and organization of the gene encoding a mouse mitochondrial stress-70 protein."
    Michikawa Y., Baba T., Arai Y., Sakakura T., Kusakabe M.
    FEBS Lett. 336:27-33(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: BALB/c.
    Tissue: Liver.
  6. "Antigenic protein specific for C3H strain mouse is a mitochondrial stress-70 protein."
    Michikawa Y., Baba T., Arai Y., Sakakura T., Tanaka M., Kusakabe M.
    Biochem. Biophys. Res. Commun. 196:223-232(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C3H/HeN.
    Tissue: Kidney.
  7. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and DBA/2.
    Tissue: Embryo, Kidney and Liver.
  8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  9. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    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].
    Strain: C57BL/6.
    Tissue: Brain.
  11. "Separation and sequencing of familiar and novel murine proteins using preparative two-dimensional gel electrophoresis."
    Merrick B.A., Patterson R.M., Wichter L.L., He C., Selkirk J.K.
    Electrophoresis 15:735-745(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 47-70.
    Tissue: Fibroblast.
  12. Lubec G., Klug S., Yang J.W., Zigmond M.
    Submitted (JUL-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 188-202; 266-284; 349-360; 395-405 AND 499-513, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Brain and Hippocampus.
  13. "PBP74, a new member of the mammalian 70-kDa heat shock protein family, is a mitochondrial protein."
    Dahlseid J.N., Lill R., Green J.M., Xu X., Qiu Y., Pierce S.K.
    Mol. Biol. Cell 5:1265-1275(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  14. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-135; LYS-300; LYS-360 AND LYS-567, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-135; LYS-138; LYS-206; LYS-300; LYS-360; LYS-368; LYS-394; LYS-567; LYS-600; LYS-610 AND LYS-646, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast and Liver.
  15. "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
    Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
    Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-76; LYS-135; LYS-138; LYS-206; LYS-234; LYS-288; LYS-300; LYS-360; LYS-567; LYS-600; LYS-612 AND LYS-646, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiGRP75_MOUSE
AccessioniPrimary (citable) accession number: P38647
Secondary accession number(s): Q3TW93
, Q3UVN1, Q3V015, Q7TSZ0, Q9CQ05
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: October 3, 2012
Last modified: November 26, 2014
This is version 143 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3