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Protein

Heterogeneous nuclear ribonucleoprotein D-like

Gene

HNRNPDL

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

Functioni

Acts as a transcriptional regulator. Promotes transcription repression. Promotes transcription activation in differentiated myotubes (By similarity). Binds to double- and single-stranded DNA sequences. Binds to the transcription suppressor CATR sequence of the COX5B promoter (By similarity). Binds with high affinity to RNA molecules that contain AU-rich elements (AREs) found within the 3'-UTR of many proto-oncogenes and cytokine mRNAs. Binds both to nuclear and cytoplasmic poly(A) mRNAs. Binds to poly(G) and poly(A), but not to poly(U) or poly(C) RNA homopolymers. Binds to the 5'-ACUAGC-3' RNA consensus sequence.By similarity1 Publication

GO - Molecular functioni

  • DNA binding Source: UniProtKB-KW
  • double-stranded DNA binding Source: UniProtKB
  • nucleotide binding Source: InterPro
  • poly(A) binding Source: UniProtKB
  • poly(A) RNA binding Source: UniProtKB
  • poly(G) binding Source: UniProtKB
  • single-stranded DNA binding Source: UniProtKB

GO - Biological processi

  • regulation of gene expression Source: UniProtKB
  • regulation of transcription, DNA-templated Source: UniProtKB-KW
  • RNA processing Source: UniProtKB
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator, Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Heterogeneous nuclear ribonucleoprotein D-like
Short name:
hnRNP D-like
Short name:
hnRNP DL
Alternative name(s):
AU-rich element RNA-binding factor
JKT41-binding protein
Protein laAUF1
Gene namesi
Name:HNRNPDL
Synonyms:HNRPDL, JKTBP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 4

Organism-specific databases

HGNCiHGNC:5037. HNRNPDL.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB-SubCell
  • extracellular exosome Source: UniProtKB
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
  • spliceosomal complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Involvement in diseasei

Limb-girdle muscular dystrophy 1G (LGMD1G)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal dominant degenerative myopathy characterized by slowly progressive wasting and weakness of the proximal muscles of arms and legs around the pelvic or shoulder girdles, elevated creatine kinase levels and dystrophic features on muscle biopsy. LGMD1G is characterized by a mild late-onset and is associated with progressive fingers and toes flexion limitation. Affected individuals may also develop cataracts before age 50.
See also OMIM:609115
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti378 – 3781D → H in LGMD1G. 1 Publication
Corresponds to variant rs587777669 [ dbSNP | Ensembl ].
VAR_072567
Natural varianti378 – 3781D → N in LGMD1G. 1 Publication
Corresponds to variant rs587777669 [ dbSNP | Ensembl ].
VAR_072568

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi404 – 4041G → A: Reduces significantly its nuclear localization. 1 Publication

Keywords - Diseasei

Disease mutation, Limb-girdle muscular dystrophy

Organism-specific databases

MalaCardsiHNRNPDL.
MIMi609115. phenotype.
Orphaneti55596. Autosomal dominant limb-girdle muscular dystrophy type 1G.
PharmGKBiPA29362.

Polymorphism and mutation databases

BioMutaiHNRNPDL.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 420420Heterogeneous nuclear ribonucleoprotein D-likePRO_0000287239Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei161 – 1611N6-methyllysine1 Publication
Modified residuei216 – 2161N6-acetyllysineCombined sources
Modified residuei241 – 2411PhosphoserineCombined sources
Modified residuei408 – 4081Dimethylated arginine1 Publication

Post-translational modificationi

Dimethylation of Arg-408 is probably of the asymmetric type.

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Proteomic databases

EPDiO14979.
MaxQBiO14979.
PaxDbiO14979.
PeptideAtlasiO14979.
PRIDEiO14979.

PTM databases

iPTMnetiO14979.
PhosphoSiteiO14979.
SwissPalmiO14979.

Expressioni

Tissue specificityi

Expressed in heart, brain, placenta, lung, liver, skeletal muscle, kidney, pancreas, spleen, thymus, prostate, testis, ovary, small intestine, colon and leukocytes. Expressed in myeloid leukemia, gastric adenocarcinoma, cervical carcinoma, hepatoma, fibrosarcoma, colon adenocarcinoma, epidermoid carcinoma, osteosarcoma and urinary bladder carcinoma cells.2 Publications

Inductioni

Up-regulated by 12-O-tetradecanoylphorbol-13-acetate (TPA) in macrophages and retinoic acid (RA) in granulocytes (at protein level). Down-regulated by IL4/interleukin-4.2 Publications

Gene expression databases

BgeeiO14979.
CleanExiHS_HNRPDL.
ExpressionAtlasiO14979. baseline and differential.
GenevisibleiO14979. HS.

Organism-specific databases

HPAiHPA056820.
HPA063147.

Interactioni

Subunit structurei

Interacts with ZNF148 (By similarity). Interacts with TNPO1.By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
SF1Q156374EBI-299727,EBI-744603

Protein-protein interaction databases

BioGridi115308. 116 interactions.
IntActiO14979. 37 interactions.
MINTiMINT-2998491.
STRINGi9606.ENSP00000295470.

Structurei

3D structure databases

ProteinModelPortaliO14979.
SMRiO14979. Positions 135-323.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini148 – 23083RRM 1PROSITE-ProRule annotationAdd
BLAST
Domaini233 – 31280RRM 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni342 – 42079Necessary for interaction with TNPO1Add
BLAST
Regioni396 – 42025Necessary for its nuclear import and exportAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi79 – 824Poly-Arg
Compositional biasi316 – 3216Poly-Gln
Compositional biasi323 – 41189Gly-richAdd
BLAST
Compositional biasi353 – 39644Tyr-richAdd
BLAST

Sequence similaritiesi

Contains 2 RRM (RNA recognition motif) domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG410IQWX. Eukaryota.
ENOG4111SPT. LUCA.
GeneTreeiENSGT00760000118873.
HOGENOMiHOG000234441.
HOVERGENiHBG002295.
InParanoidiO14979.
KOiK13044.
OMAiGPGYTDY.
OrthoDBiEOG715Q6V.
PhylomeDBiO14979.
TreeFamiTF314808.

Family and domain databases

Gene3Di3.30.70.330. 2 hits.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF00076. RRM_1. 2 hits.
[Graphical view]
SMARTiSM00360. RRM. 2 hits.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 2 hits.
PROSITEiPS50102. RRM. 2 hits.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O14979-1) [UniParc]FASTAAdd to basket

Also known as: JKTBP1

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
MEVPPRLSHV PPPLFPSAPA TLASRSLSHW RPRPPRQLAP LLPSLAPSSA
60 70 80 90 100
RQGARRAQRH VTAQQPSRLA GGAAIKGGRR RRPDLFRRHF KSSSIQRSAA
110 120 130 140 150
AAAATRTARQ HPPADSSVTM EDMNEYSNIE EFAEGSKINA SKNQQDDGKM
160 170 180 190 200
FIGGLSWDTS KKDLTEYLSR FGEVVDCTIK TDPVTGRSRG FGFVLFKDAA
210 220 230 240 250
SVDKVLELKE HKLDGKLIDP KRAKALKGKE PPKKVFVGGL SPDTSEEQIK
260 270 280 290 300
EYFGAFGEIE NIELPMDTKT NERRGFCFIT YTDEEPVKKL LESRYHQIGS
310 320 330 340 350
GKCEIKVAQP KEVYRQQQQQ QKGGRGAAAG GRGGTRGRGR GQGQNWNQGF
360 370 380 390 400
NNYYDQGYGN YNSAYGGDQN YSGYGGYDYT GYNYGNYGYG QGYADYSGQQ
410 420
STYGKASRGG GNHQNNYQPY
Length:420
Mass (Da):46,438
Last modified:August 1, 1999 - v3
Checksum:i00F631863859D0CA
GO
Isoform 2 (identifier: O14979-2) [UniParc]FASTAAdd to basket

Also known as: JKTBP2

The sequence of this isoform differs from the canonical sequence as follows:
     1-119: Missing.

Show »
Length:301
Mass (Da):33,589
Checksum:i6BF76C3AEB682BAD
GO
Isoform 3 (identifier: O14979-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-119: Missing.
     341-397: Missing.

Show »
Length:244
Mass (Da):27,191
Checksum:i977B204371D65D76
GO

Sequence cautioni

The sequence BAA22860.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti378 – 3781D → H in LGMD1G. 1 Publication
Corresponds to variant rs587777669 [ dbSNP | Ensembl ].
VAR_072567
Natural varianti378 – 3781D → N in LGMD1G. 1 Publication
Corresponds to variant rs587777669 [ dbSNP | Ensembl ].
VAR_072568

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 119119Missing in isoform 2 and isoform 3. 3 PublicationsVSP_025410Add
BLAST
Alternative sequencei341 – 39757Missing in isoform 3. 1 PublicationVSP_025411Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB017019 mRNA. Translation: BAA75241.1.
D89092 mRNA. Translation: BAA24361.1.
AB066484 mRNA. Translation: BAB62188.1.
CR407623 mRNA. Translation: CAG28551.1.
AC124016 Genomic DNA. Translation: AAY40914.1.
AB017018 Genomic DNA. Translation: BAA75239.1.
AB017018 Genomic DNA. Translation: BAA75240.1.
BC007392 mRNA. Translation: AAH07392.2.
BC011714 mRNA. Translation: AAH11714.1.
BC071944 mRNA. Translation: AAH71944.1.
AY453824 mRNA. Translation: AAR17782.1.
D89678 mRNA. Translation: BAA22860.1. Different initiation.
CCDSiCCDS3593.1. [O14979-1]
PIRiJW0079.
RefSeqiNP_001193929.1. NM_001207000.1.
NP_112740.1. NM_031372.3. [O14979-1]
UniGeneiHs.527105.
Hs.707013.

Genome annotation databases

EnsembliENST00000295470; ENSP00000295470; ENSG00000152795. [O14979-1]
ENST00000349655; ENSP00000338552; ENSG00000152795. [O14979-2]
ENST00000502762; ENSP00000422040; ENSG00000152795. [O14979-1]
ENST00000507721; ENSP00000480156; ENSG00000152795. [O14979-2]
ENST00000602300; ENSP00000473677; ENSG00000152795. [O14979-2]
ENST00000621267; ENSP00000483254; ENSG00000152795. [O14979-1]
ENST00000630114; ENSP00000486452; ENSG00000152795. [O14979-2]
ENST00000630827; ENSP00000485954; ENSG00000152795. [O14979-2]
GeneIDi9987.
KEGGihsa:9987.
UCSCiuc003hmr.4. human. [O14979-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB017019 mRNA. Translation: BAA75241.1.
D89092 mRNA. Translation: BAA24361.1.
AB066484 mRNA. Translation: BAB62188.1.
CR407623 mRNA. Translation: CAG28551.1.
AC124016 Genomic DNA. Translation: AAY40914.1.
AB017018 Genomic DNA. Translation: BAA75239.1.
AB017018 Genomic DNA. Translation: BAA75240.1.
BC007392 mRNA. Translation: AAH07392.2.
BC011714 mRNA. Translation: AAH11714.1.
BC071944 mRNA. Translation: AAH71944.1.
AY453824 mRNA. Translation: AAR17782.1.
D89678 mRNA. Translation: BAA22860.1. Different initiation.
CCDSiCCDS3593.1. [O14979-1]
PIRiJW0079.
RefSeqiNP_001193929.1. NM_001207000.1.
NP_112740.1. NM_031372.3. [O14979-1]
UniGeneiHs.527105.
Hs.707013.

3D structure databases

ProteinModelPortaliO14979.
SMRiO14979. Positions 135-323.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115308. 116 interactions.
IntActiO14979. 37 interactions.
MINTiMINT-2998491.
STRINGi9606.ENSP00000295470.

PTM databases

iPTMnetiO14979.
PhosphoSiteiO14979.
SwissPalmiO14979.

Polymorphism and mutation databases

BioMutaiHNRNPDL.

Proteomic databases

EPDiO14979.
MaxQBiO14979.
PaxDbiO14979.
PeptideAtlasiO14979.
PRIDEiO14979.

Protocols and materials databases

DNASUi9987.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000295470; ENSP00000295470; ENSG00000152795. [O14979-1]
ENST00000349655; ENSP00000338552; ENSG00000152795. [O14979-2]
ENST00000502762; ENSP00000422040; ENSG00000152795. [O14979-1]
ENST00000507721; ENSP00000480156; ENSG00000152795. [O14979-2]
ENST00000602300; ENSP00000473677; ENSG00000152795. [O14979-2]
ENST00000621267; ENSP00000483254; ENSG00000152795. [O14979-1]
ENST00000630114; ENSP00000486452; ENSG00000152795. [O14979-2]
ENST00000630827; ENSP00000485954; ENSG00000152795. [O14979-2]
GeneIDi9987.
KEGGihsa:9987.
UCSCiuc003hmr.4. human. [O14979-1]

Organism-specific databases

CTDi9987.
GeneCardsiHNRNPDL.
HGNCiHGNC:5037. HNRNPDL.
HPAiHPA056820.
HPA063147.
MalaCardsiHNRNPDL.
MIMi607137. gene.
609115. phenotype.
neXtProtiNX_O14979.
Orphaneti55596. Autosomal dominant limb-girdle muscular dystrophy type 1G.
PharmGKBiPA29362.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IQWX. Eukaryota.
ENOG4111SPT. LUCA.
GeneTreeiENSGT00760000118873.
HOGENOMiHOG000234441.
HOVERGENiHBG002295.
InParanoidiO14979.
KOiK13044.
OMAiGPGYTDY.
OrthoDBiEOG715Q6V.
PhylomeDBiO14979.
TreeFamiTF314808.

Miscellaneous databases

GeneWikiiHNRPDL.
GenomeRNAii9987.
PROiO14979.
SOURCEiSearch...

Gene expression databases

BgeeiO14979.
CleanExiHS_HNRPDL.
ExpressionAtlasiO14979. baseline and differential.
GenevisibleiO14979. HS.

Family and domain databases

Gene3Di3.30.70.330. 2 hits.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF00076. RRM_1. 2 hits.
[Graphical view]
SMARTiSM00360. RRM. 2 hits.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 2 hits.
PROSITEiPS50102. RRM. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterization of a cDNA encoding a novel heterogeneous nuclear ribonucleoprotein-like protein and its expression in myeloid leukemia cells."
    Tsuchiya N., Kamei D., Takano A., Matsui T., Yamada M.
    J. Biochem. 123:499-507(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, TISSUE SPECIFICITY, RNA-BINDING, DNA-BINDING.
    Tissue: Erythroleukemia and Placenta.
  2. "Two forms of expression and genomic structure of the human heterogeneous nuclear ribonucleoprotein D-like JKTBP gene (HNRPDL)."
    Kamei D., Tsuchiya N., Yamazaki M., Meguro H., Yamada M.
    Gene 228:13-22(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), INDUCTION, TISSUE SPECIFICITY.
    Tissue: Placenta.
  3. "Identification of the nucleocytoplasmic shuttling sequence of heterogeneous nuclear ribonucleoprotein D-like protein JKTBP and its interaction with mRNA."
    Kawamura H., Tomozoe Y., Akagi T., Kamei D., Ochiai M., Yamada M.
    J. Biol. Chem. 277:2732-2739(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), SUBCELLULAR LOCATION, RNA-BINDING.
  4. "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 (MAY-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  5. "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] [Europe PMC] [Abstract]
    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] (ISOFORM 1).
    Tissue: Lung, Ovary and Skin.
  7. "Regulation of murine cytochrome c oxidase Vb gene expression during myogenesis: YY-1 and heterogeneous nuclear ribonucleoprotein D-like protein (JKTBP1) reciprocally regulate transcription activity by physical interaction with the BERF-1/ZBP-89 factor."
    Boopathi E., Lenka N., Prabu S.K., Fang J.-K., Wilkinson F., Atchison M., Giallongo A., Avadhani N.G.
    J. Biol. Chem. 279:35242-35254(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 123-420.
    Tissue: Brain.
  8. "Molecular cloning of the cDNA encoding A + U-rich element RNA binding factor."
    Doi A., Shiosaka T., Takaoka Y., Yanagisawa K., Fujita S.
    Biochim. Biophys. Acta 1396:51-56(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 131-420, INTERACTION WITH TNPO1, MUTAGENESIS OF GLY-404, INDUCTION, RNA-BINDING.
  9. Cited for: PROTEIN SEQUENCE OF 150-180; 190-209; 234-269; 275-289 AND 406-420, METHYLATION AT LYS-161 AND ARG-408, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Colon carcinoma and Ovarian carcinoma.
  10. Lubec G., Chen W.-Q., Sun Y.
    Submitted (DEC-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 235-269 AND 275-289.
    Tissue: Fetal brain cortex.
  11. "Interactions of heterogeneous nuclear ribonucleoprotein D-like protein JKTBP and its domains with high-affinity binding sites."
    Kamei D., Yamada M.
    Gene 298:49-57(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, RNA-BINDING.
  12. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-241, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "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-241, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  15. "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-216, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "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-241, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "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-241, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "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-241, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma and Erythroleukemia.
  20. Cited for: INVOLVEMENT IN LGMD1G, VARIANTS LGMD1G ASN-378 AND HIS-378.
  21. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-241, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiHNRDL_HUMAN
AccessioniPrimary (citable) accession number: O14979
Secondary accession number(s): Q6SPF2
, Q7KZ74, Q7KZ75, Q96IM0, Q96S43
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 15, 2007
Last sequence update: August 1, 1999
Last modified: July 6, 2016
This is version 152 of the entry and version 3 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 4
    Human chromosome 4: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. 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.