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Protein

DnaJ homolog subfamily C member 8

Gene

DNAJC8

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Enzyme and pathway databases

ReactomeiR-HSA-72163. mRNA Splicing - Major Pathway.

Names & Taxonomyi

Protein namesi
Recommended name:
DnaJ homolog subfamily C member 8
Alternative name(s):
Splicing protein spf31
Gene namesi
Name:DNAJC8
Synonyms:SPF31
ORF Names:HSPC315, HSPC331
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:15470. DNAJC8.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27425.

Polymorphism and mutation databases

BioMutaiDNAJC8.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 253252DnaJ homolog subfamily C member 8PRO_0000071060Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineCombined sources
Modified residuei35 – 351PhosphoserineCombined sources
Modified residuei146 – 1461N6-acetyllysineCombined sources
Modified residuei222 – 2221PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiO75937.
MaxQBiO75937.
PaxDbiO75937.
PeptideAtlasiO75937.
PRIDEiO75937.
TopDownProteomicsiO75937.

PTM databases

iPTMnetiO75937.
PhosphoSiteiO75937.

Expressioni

Gene expression databases

BgeeiO75937.
CleanExiHS_DNAJC8.
ExpressionAtlasiO75937. baseline and differential.
GenevisibleiO75937. HS.

Organism-specific databases

HPAiHPA026275.
HPA026283.

Interactioni

Protein-protein interaction databases

BioGridi116501. 37 interactions.
IntActiO75937. 21 interactions.
MINTiMINT-3002069.
STRINGi9606.ENSP00000263697.

Structurei

3D structure databases

ProteinModelPortaliO75937.
SMRiO75937. Positions 57-120.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini57 – 12468JPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 J domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG1150. Eukaryota.
ENOG4110ZJ4. LUCA.
GeneTreeiENSGT00390000012569.
HOVERGENiHBG051377.
InParanoidiO75937.
KOiK09528.
OMAiQNFYTEV.
OrthoDBiEOG7BW0KC.
PhylomeDBiO75937.
TreeFamiTF105167.

Family and domain databases

Gene3Di1.10.287.110. 1 hit.
InterProiIPR001623. DnaJ_domain.
[Graphical view]
PfamiPF00226. DnaJ. 1 hit.
[Graphical view]
PRINTSiPR00625. JDOMAIN.
SMARTiSM00271. DnaJ. 1 hit.
[Graphical view]
SUPFAMiSSF46565. SSF46565. 1 hit.
PROSITEiPS50076. DNAJ_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

O75937-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAASGESGTS GGGGSTEEAF MTFYSEVKQI EKRDSVLTSK NQIERLTRPG
60 70 80 90 100
SSYFNLNPFE VLQIDPEVTD EEIKKRFRQL SILVHPDKNQ DDADRAQKAF
110 120 130 140 150
EAVDKAYKLL LDQEQKKRAL DVIQAGKEYV EHTVKERKKQ LKKEGKPTIV
160 170 180 190 200
EEDDPELFKQ AVYKQTMKLF AELEIKRKER EAKEMHERKR QREEEIEAQE
210 220 230 240 250
KAKREREWQK NFEESRDGRV DSWRNFQANT KGKKEKKNRT FLRPPKVKME

QRE
Length:253
Mass (Da):29,842
Last modified:April 26, 2005 - v2
Checksum:iC69D6189D69D1588
GO

Sequence cautioni

The sequence AAC35352.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence CAG33181.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti253 – 2531E → D in CAG33181 (Ref. 2) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF083190 mRNA. Translation: AAC35352.1. Different initiation.
CR456900 mRNA. Translation: CAG33181.1. Different initiation.
AK300797 mRNA. Translation: BAG62456.1.
AL353354, AL353622 Genomic DNA. Translation: CAI20826.1.
AL353622, AL353354 Genomic DNA. Translation: CAI19135.1.
CH471059 Genomic DNA. Translation: EAX07707.1.
CH471059 Genomic DNA. Translation: EAX07710.1.
BC033159 mRNA. Translation: AAH33159.1.
AF161433 mRNA. Translation: AAF28993.1.
AF161449 mRNA. Translation: AAF29009.1.
CCDSiCCDS41292.1.
RefSeqiNP_055095.2. NM_014280.2.
UniGeneiHs.433540.

Genome annotation databases

EnsembliENST00000263697; ENSP00000263697; ENSG00000126698.
GeneIDi22826.
KEGGihsa:22826.
UCSCiuc001bpn.4. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF083190 mRNA. Translation: AAC35352.1. Different initiation.
CR456900 mRNA. Translation: CAG33181.1. Different initiation.
AK300797 mRNA. Translation: BAG62456.1.
AL353354, AL353622 Genomic DNA. Translation: CAI20826.1.
AL353622, AL353354 Genomic DNA. Translation: CAI19135.1.
CH471059 Genomic DNA. Translation: EAX07707.1.
CH471059 Genomic DNA. Translation: EAX07710.1.
BC033159 mRNA. Translation: AAH33159.1.
AF161433 mRNA. Translation: AAF28993.1.
AF161449 mRNA. Translation: AAF29009.1.
CCDSiCCDS41292.1.
RefSeqiNP_055095.2. NM_014280.2.
UniGeneiHs.433540.

3D structure databases

ProteinModelPortaliO75937.
SMRiO75937. Positions 57-120.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116501. 37 interactions.
IntActiO75937. 21 interactions.
MINTiMINT-3002069.
STRINGi9606.ENSP00000263697.

PTM databases

iPTMnetiO75937.
PhosphoSiteiO75937.

Polymorphism and mutation databases

BioMutaiDNAJC8.

Proteomic databases

EPDiO75937.
MaxQBiO75937.
PaxDbiO75937.
PeptideAtlasiO75937.
PRIDEiO75937.
TopDownProteomicsiO75937.

Protocols and materials databases

DNASUi22826.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000263697; ENSP00000263697; ENSG00000126698.
GeneIDi22826.
KEGGihsa:22826.
UCSCiuc001bpn.4. human.

Organism-specific databases

CTDi22826.
GeneCardsiDNAJC8.
HGNCiHGNC:15470. DNAJC8.
HPAiHPA026275.
HPA026283.
neXtProtiNX_O75937.
PharmGKBiPA27425.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1150. Eukaryota.
ENOG4110ZJ4. LUCA.
GeneTreeiENSGT00390000012569.
HOVERGENiHBG051377.
InParanoidiO75937.
KOiK09528.
OMAiQNFYTEV.
OrthoDBiEOG7BW0KC.
PhylomeDBiO75937.
TreeFamiTF105167.

Enzyme and pathway databases

ReactomeiR-HSA-72163. mRNA Splicing - Major Pathway.

Miscellaneous databases

GenomeRNAii22826.
PROiO75937.

Gene expression databases

BgeeiO75937.
CleanExiHS_DNAJC8.
ExpressionAtlasiO75937. baseline and differential.
GenevisibleiO75937. HS.

Family and domain databases

Gene3Di1.10.287.110. 1 hit.
InterProiIPR001623. DnaJ_domain.
[Graphical view]
PfamiPF00226. DnaJ. 1 hit.
[Graphical view]
PRINTSiPR00625. JDOMAIN.
SMARTiSM00271. DnaJ. 1 hit.
[Graphical view]
SUPFAMiSSF46565. SSF46565. 1 hit.
PROSITEiPS50076. DNAJ_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "spf31: a protein involved in splicing."
    King A., Ajuh P., Schrotz-King P., Lamond A., Mann M.
    Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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: Uterus.
  7. "Human partial CDS from CD34+ stem cells."
    Ye M., Zhang Q.-H., Zhou J., Shen Y., Wu X.-Y., Guan Z.Q., Wang L., Fan H.-Y., Mao Y.-F., Dai M., Huang Q.-H., Chen S.-J., Chen Z.
    Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 96-253.
    Tissue: Umbilical cord blood.
  8. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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-146, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-222, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Erythroleukemia.
  14. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiDNJC8_HUMAN
AccessioniPrimary (citable) accession number: O75937
Secondary accession number(s): B4DUU4
, D3DPM0, Q6IBA4, Q8N4Z5, Q9P051, Q9P067
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 19, 2002
Last sequence update: April 26, 2005
Last modified: July 6, 2016
This is version 125 of the entry and version 2 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, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.