P54103 (DNJC2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
DnaJ homolog subfamily C member 2

Alternative name(s):
Mouse Id associate 1
Short name=MIDA1
Zuotin-related factor 1

Gene names

Name:	Dnajc2
Synonyms:	Mida1, Zrf1

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	621 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Acts both as a chaperone in the cytosol and as a chromatin regulator in the nucleus. When cytosolic, acts as a molecular chaperone: component of the ribosome-associated complex (RAC), a complex involved in folding or maintaining nascent polypeptides in a folding-competent state. In the RAC complex, stimulates the ATPase activity of the ribosome-associated pool of Hsp70-type chaperones HSPA14 that bind to the nascent polypeptide chain. When nuclear, mediates the switching from polycomb-repressed genes to an active state: specifically recruited at histone H2A ubiquitinated at 'Lys-119' (H2AK119ub), and promotes the displacement of the polycomb PRC1 complex from chromatin, thereby facilitating transcription activation By similarity. Specifically binds DNA sequence 5'-GTCAAGC-3'.
Subunit structure	Component of ribosome-associated complex (RAC), a heterodimer composed of Hsp70/DnaK-type chaperone HSPA14 and Hsp40/DnaJ-type chaperone DNAJC2 By similarity. Interacts (via ZRF1-UBD region) with ID1. Ref.1 Ref.5
Subcellular location	Nucleus. Cytoplasm › cytosol By similarity Ref.4.
Tissue specificity	Expressed in all tissues. Ref.4
Domain	The ZRF1-UBD region specifically recognizes and binds H2AK119ub. The ZRF1-UBD region is also involved in protein-protein interactions with other proteins, suggesting that it may be masked by some regulator, thereby preventing its association with H2AK119ub By similarity.
Post-translational modification	Phosphorylated in M (mitotic) phase By similarity. Ref.7 Ref.8
Sequence similarities	Contains 1 J domain. Contains 2 SANT domains.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Domain	Repeat
Molecular function	Activator Chaperone Chromatin regulator
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	DNA replication Inferred from mutant phenotype Ref.1. Source: MGI G2 phase of mitotic cell cycle Inferred from mutant phenotype Ref.1. Source: MGI chromatin modification Inferred from electronic annotation. Source: UniProtKB-KW positive regulation of transcription, DNA-dependent Inferred from sequence or structural similarity. Source: UniProtKB transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytosol Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	DNA binding Inferred from electronic annotation. Source: InterPro chromatin binding Inferred from sequence or structural similarity. Source: UniProtKB histone binding Inferred from sequence or structural similarity. Source: UniProtKB ubiquitin 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
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 621	620	DnaJ homolog subfamily C member 2		PRO_0000071124
Regions
	Domain	88 – 161	74	J
	Domain	449 – 511	63	SANT 1
	Domain	549 – 604	56	SANT 2
	Region	160 – 250	91	ZRF1-UBD
Amino acid modifications
	Modified residue	47	1	Phosphoserine Ref.7 Ref.8
	Modified residue	48	1	Phosphothreonine Ref.7
	Modified residue	49	1	Phosphoserine Ref.7
	Modified residue	60	1	Phosphoserine Ref.7
	Modified residue	63	1	Phosphoserine Ref.7
Experimental info
	Sequence conflict	473	1	T → R in AAC52486. Ref.4
	Sequence conflict	478	1	E → D in AAC52486. Ref.4
	Sequence conflict	502 – 514	13	KAKSL…DPHQK → EVRGPKSWGSSKR in AAC52486. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	P54103 [UniParc]. Last modified March 6, 2007. Version 2. Checksum: 0FFC511028EA1C41	FASTA	621	71,722
	10 20 30 40 50 60 MLLLPSAAEG QGTAITHALT SASSVCQVEP VGRWFEAFVK RRNRNASTSF QELEDKKELS 70 80 90 100 110 120 EESEDEELQL EEFPMLKTLD PKDWKNQDHY AVLGLGHVRY TATQRQIKAA HKAMVLKHHP 130 140 150 160 170 180 DKRKAAGEPI KEGDNDYFTC ITKAYEMLSD PVKRRAFNSV DPTFDNSVPS KSEAKDNFFQ 190 200 210 220 230 240 VFSPVFERNS RWSNKKNVPK LGDMNSSFED VDAFYSFWYN FDSWREFSYL DEEEKEKAEC 250 260 270 280 290 300 RDERKWIEKQ NRATRAQRKK EEMNRIRTLV DNAYSCDPRI KKFKEEEKAK KEAEKKAKAE 310 320 330 340 350 360 ARRKEQEAKE KQRQAELEAV RLAKEKEEEE VRQQALLAKK EKDIQKKAIK KERQKLRNSC 370 380 390 400 410 420 KSWNHFSDNE ADRVKMMEEV EKLCDRLELA SLQGLNEILA SSTREVGKAA LEKQIEEVNE 430 440 450 460 470 480 QMRREKEEAD ARMRQASKNA EKSTGGSGSG SKNWSEDDLQ LLIKAVNLFP AGTNSRWEVI 490 500 510 520 530 540 ANYMNIHSSS GVKRTAKDVI SKAKSLQKLD PHQKDDINKK AFDKFKKEHG VASQADSAAP 550 560 570 580 590 600 SERFEGPCID STPWTTEEQK LLEQALKTYP VNTPERWEKI AEAVPGRTKK DCMRRYKELV 610 620 EMVKAKKAAQ EQVLNASRAR K

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"MIDA1, a protein associated with Id, regulates cell growth." Shoji W., Inoue T., Yamamoto T., Obinata M. J. Biol. Chem. 270:24818-24825(1995) [PubMed: 7559602] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH ID1.
[2]	"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: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J.
[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]. Strain: C57BL/6. Tissue: Brain.
[4]	"Cloning and chromosomal localization of a mouse cDNA with homology to the Saccharomyces cerevisiae gene zuotin." Hughes R., Chan F.Y., White R.A., Zon L.I. Genomics 29:546-550(1995) [PubMed: 8666407] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-514, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[5]	"MIDA1, an Id-associating protein, has two distinct DNA binding activities that are converted by the association with Id1: a novel function of Id protein." Inoue T., Shoji W., Obinata M. Biochem. Biophys. Res. Commun. 266:147-151(1999) [PubMed: 10581180] [Abstract] Cited for: INTERACTION WITH ID1.
[6]	"MIDA1 is a sequence specific DNA binding protein with novel DNA binding properties." Inoue T., Shoji W., Obinata M. Genes Cells 5:699-709(2000) [PubMed: 10971652] [Abstract] Cited for: DNA-BINDING.
[7]	"A differential phosphoproteomic analysis of retinoic acid-treated P19 cells." Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D. J. Proteome Res. 6:3174-3186(2007) [PubMed: 17622165] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47; THR-48; SER-49; SER-60 AND SER-63, MASS SPECTROMETRY. Tissue: Teratocarcinoma.
[8]	"Large-scale phosphorylation analysis of mouse liver." Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed: 17242355] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47, MASS SPECTROMETRY. Tissue: Liver.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D63784 mRNA. Translation: BAA09854.1. AK131964 mRNA. Translation: BAE20907.1. BC052027 mRNA. Translation: AAH52027.1. U53208 mRNA. Translation: AAC52486.1.
IPI	IPI00126317.
PIR	A57591.
RefSeq	NP_033610.1. NM_009584.4.
UniGene	Mm.266312.
3D structure databases
ProteinModelPortal	P54103.
SMR	P54103. Positions 85-162, 450-512, 543-601.
ModBase	Search...
Protein-protein interaction databases
STRING	P54103.
PTM databases
PhosphoSite	P54103.
Proteomic databases
PRIDE	P54103.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000030771; ENSMUSP00000030771; ENSMUSG00000029014.
GeneID	22791.
KEGG	mmu:22791.
UCSC	uc008woy.1. mouse.
Organism-specific databases
CTD	27000.
MGI	MGI:99470. Dnajc2.
Phylogenomic databases
eggNOG	roNOG07168.
HOGENOM	HBG383362.
HOVERGEN	HBG008782.
InParanoid	P54103.
OMA	CKTWNHF.
OrthoDB	EOG4D26PN.
PhylomeDB	P54103.
Gene expression databases
ArrayExpress	P54103.
Bgee	P54103.
CleanEx	MM_DNAJC2.
Genevestigator	P54103.
GermOnline	ENSMUSG00000029014. Mus musculus.
Family and domain databases
InterPro	IPR001623. DnaJ_N. IPR018253. Heat_shock_DnaJ_CS. IPR009057. Homeodomain-like. IPR012287. Homeodomain-rel. IPR014778. Myb_DNA-bd. IPR001005. SANT_DNA-bd. IPR017884. SANT_eukarya. IPR017930. Tscrpt_reg_HTH_Myb-type. [Graphical view]
Gene3D	G3DSA:1.10.287.110. DnaJ_N. 1 hit. G3DSA:1.10.10.60. Homeodomain-rel. 1 hit.
KO	K09522.
Pfam	PF00226. DnaJ. 1 hit. PF00249. Myb_DNA-binding. 2 hits. [Graphical view]
SMART	SM00271. DnaJ. 1 hit. SM00717. SANT. 2 hits. [Graphical view]
SUPFAM	SSF46565. DnaJ_N. 1 hit. SSF46689. Homeodomain_like. 2 hits.
PROSITE	PS00636. DNAJ_1. 1 hit. PS50076. DNAJ_2. 1 hit. PS51293. SANT. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	303379.
SOURCE	Search...

Entry information

Entry name

DNJC2_MOUSE

Accession

Primary (citable) accession number: P54103
Secondary accession number(s): Q61866

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	March 6, 2007
Last modified:	November 16, 2011
This is version 88 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program