Reviewed, UniProtKB/Swiss-Prot O14979 (HNRDL_HUMAN)

Names and origin

Protein names

Recommended name:
    Heterogeneous nuclear ribonucleoprotein D-like
      Short name=hnRPD-like protein
      Short name=hnHNRP-DL
Alternative name(s):
    JKT41-binding protein
    AU-rich element RNA-binding factor
    Protein laAUF1

Gene names

Name:	HNRPDL
Synonyms:	JKTBP

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	420 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	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. Ref.1
Subunit structure	Interacts with ZNF148 By similarity. Interacts with TNPO1. Ref.8
Subcellular location	Nucleus. Cytoplasm. Note: Shuttles between the nucleus and the cytoplasm in a TNPO1-dependent manner. Ref.3 Ref.11
Tissue specificity	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. Ref.1 Ref.2
Induction	Up-regulated by 12-O-tetradecanoylphorbol 13-acetate (TPA) in macrophages and retinoic acid (RA) in granulocytes (at protein level). Down-regulated by interleukin-4 (IL-4). Ref.8 Ref.2
Post-translational modification	Dimethylation of Arg-408 is probably of the asymmetric type.
Sequence similarities	Contains 2 RRM (RNA recognition motif) domains.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing
Domain	Repeat
Ligand	DNA-binding RNA-binding
Molecular function	Activator Repressor
PTM	Acetylation Methylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	RNA processing Ref.1 Traceable author statement. Source: ProtInc regulation of transcription Inferred from electronic annotation. Source: UniProtKB-KW transcription Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell heterogeneous nuclear ribonucleoprotein complex Ref.1 Traceable author statement. Source: ProtInc
Molecular function	double-stranded DNA binding Ref.1 Traceable author statement. Source: ProtInc nucleotide binding Inferred from electronic annotation. Source: InterPro poly(A) RNA binding Ref.1 Traceable author statement. Source: ProtInc protein binding Inferred from physical interaction. Source: IntAct single-stranded DNA binding Ref.1 Traceable author statement. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ATIC	P31939	1	EBI-299727,EBI-1048599

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: O14979-1)

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.

Isoform 2 (identifier: O14979-2)

Also known as: JKTBP2;

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

Isoform 3 (identifier: O14979-3)

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

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 420	420	Heterogeneous nuclear ribonucleoprotein D-like		PRO_0000287239
Regions
	Domain	148 – 230	83	RRM 1
	Domain	233 – 312	80	RRM 2
	Region	342 – 420	79	Necessary for interaction with TNPO1
	Region	396 – 420	25	Necessary for its nuclear import and export
	Compositional bias	79 – 82	4	Poly-Arg
	Compositional bias	316 – 321	6	Poly-Gln
	Compositional bias	323 – 411	89	Gly-rich
	Compositional bias	353 – 396	44	Tyr-rich
Amino acid modifications
	Modified residue	161	1	N6-methyllysine Ref.9
	Modified residue	216	1	N6-acetyllysine Ref.17
	Modified residue	241	1	Phosphoserine Ref.13 Ref.15 Ref.16
	Modified residue	408	1	Dimethylated arginine Ref.9 Ref.12
Natural variations
	Alternative sequence	1 – 119	119	Missing in isoform 2 and isoform 3.		VSP_025410
	Alternative sequence	341 – 397	57	Missing in isoform 3.		VSP_025411
Experimental info
	Mutagenesis	404	1	G → A: Reduces significantly its nuclear localization. Ref.8

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (JKTBP1) [UniParc]. Last modified August 1, 1999. Version 3. Checksum: 00F631863859D0CA	FASTA	420	46,438
	10 20 30 40 50 60 MEVPPRLSHV PPPLFPSAPA TLASRSLSHW RPRPPRQLAP LLPSLAPSSA RQGARRAQRH 70 80 90 100 110 120 VTAQQPSRLA GGAAIKGGRR RRPDLFRRHF KSSSIQRSAA AAAATRTARQ HPPADSSVTM 130 140 150 160 170 180 EDMNEYSNIE EFAEGSKINA SKNQQDDGKM FIGGLSWDTS KKDLTEYLSR FGEVVDCTIK 190 200 210 220 230 240 TDPVTGRSRG FGFVLFKDAA SVDKVLELKE HKLDGKLIDP KRAKALKGKE PPKKVFVGGL 250 260 270 280 290 300 SPDTSEEQIK EYFGAFGEIE NIELPMDTKT NERRGFCFIT YTDEEPVKKL LESRYHQIGS 310 320 330 340 350 360 GKCEIKVAQP KEVYRQQQQQ QKGGRGAAAG GRGGTRGRGR GQGQNWNQGF NNYYDQGYGN 370 380 390 400 410 420 YNSAYGGDQN YSGYGGYDYT GYNYGNYGYG QGYADYSGQQ STYGKASRGG GNHQNNYQPY
	Isoform 2 (JKTBP2). Checksum: 6BF76C3AEB682BAD	FASTA	301	33,589
	10 20 30 40 50 60 MEDMNEYSNI EEFAEGSKIN ASKNQQDDGK MFIGGLSWDT SKKDLTEYLS RFGEVVDCTI 70 80 90 100 110 120 KTDPVTGRSR GFGFVLFKDA ASVDKVLELK EHKLDGKLID PKRAKALKGK EPPKKVFVGG 130 140 150 160 170 180 LSPDTSEEQI KEYFGAFGEI ENIELPMDTK TNERRGFCFI TYTDEEPVKK LLESRYHQIG 190 200 210 220 230 240 SGKCEIKVAQ PKEVYRQQQQ QQKGGRGAAA GGRGGTRGRG RGQGQNWNQG FNNYYDQGYG 250 260 270 280 290 300 NYNSAYGGDQ NYSGYGGYDY TGYNYGNYGY GQGYADYSGQ QSTYGKASRG GGNHQNNYQP Y
	Isoform 3. Checksum: 977B204371D65D76	FASTA	244	27,191
	10 20 30 40 50 60 MEDMNEYSNI EEFAEGSKIN ASKNQQDDGK MFIGGLSWDT SKKDLTEYLS RFGEVVDCTI 70 80 90 100 110 120 KTDPVTGRSR GFGFVLFKDA ASVDKVLELK EHKLDGKLID PKRAKALKGK EPPKKVFVGG 130 140 150 160 170 180 LSPDTSEEQI KEYFGAFGEI ENIELPMDTK TNERRGFCFI TYTDEEPVKK LLESRYHQIG 190 200 210 220 230 240 SGKCEIKVAQ PKEVYRQQQQ QQKGGRGAAA GGRGGTRGRG RGQQSTYGKA SRGGGNHQNN YQPY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 9538234] [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: 10072754] [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: 11705999] [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: 15815621] [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: 15489334] [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: 15190078] [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: 9524220] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 131-420, INTERACTION WITH TNPO1, MUTAGENESIS OF GLY-404, INDUCTION, RNA-BINDING.
[9]	Bienvenut W.V., Zebisch A., Lilla S., von Kriegsheim A., Lempens A., Kolch W. Submitted (DEC-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 150-180; 190-209; 234-269; 275-289 AND 406-420, METHYLATION AT LYS-161 AND ARG-408, 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: 12406575] [Abstract] Cited for: SUBCELLULAR LOCATION, RNA-BINDING.
[12]	"Identifying and quantifying in vivo methylation sites by heavy methyl SILAC." Ong S.E., Mittler G., Mann M. Nat. Methods 1:119-126(2004) [PubMed: 15782174] [Abstract] Cited for: METHYLATION [LARGE SCALE ANALYSIS] AT ARG-408, MASS SPECTROMETRY.
[13]	"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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-241, MASS SPECTROMETRY. Tissue: Epithelium.
[14]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[15]	"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: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-241, MASS SPECTROMETRY.
[16]	"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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-241, MASS SPECTROMETRY. Tissue: T-cell.
[17]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-216, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
IPI	IPI00011274. IPI00045498. IPI00845282.
PIR	JW0079.
RefSeq	NP_112740.1.
UniGene	Hs.527105
3D structure databases
HSSP	HSSP built from PDB template 1HD1 based on UniProtKB Q14103.
SMR	O14979. Positions 145-311.
ModBase	Search...
Protein-protein interaction databases
IntAct	O14979. 2 interactions.
STRING	O14979.
PTM databases
PhosphoSite	O14979.
Proteomic databases
PRIDE	O14979.
Genome annotation databases
Ensembl	ENST00000295470; ENSP00000295470; ENSG00000152795; Homo sapiens. [Genome view]
GeneID	9987.
KEGG	hsa:9987.
UCSC	uc003hmr.1. human. uc003hmt.1. human.
Organism-specific databases
CTD	9987.
GeneCards	GC04M083563.
HGNC	HGNC:5037. HNRPDL.
MIM	607137. gene.
PharmGKB	PA29362.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG10620.
HOGENOM	HBG756718.
HOVERGEN	O14979.
InParanoid	O14979.
OMA	SAAMEDM.
OrthoDB	EOG9PCDBG.
PhylomeDB	O14979.
Gene expression databases
ArrayExpress	O14979.
Bgee	O14979.
CleanEx	HS_HNRPDL.
Genevestigator	O14979.
Family and domain databases
InterPro	IPR012677. a_b_plait_nuc_bd. IPR000504. RRM_RNP1. [Graphical view]
Gene3D	G3DSA:3.30.70.330. a_b_plait_nuc_bd. 2 hits.
Pfam	PF00076. RRM_1. 2 hits. [Graphical view]
SMART	SM00360. RRM. 2 hits. [Graphical view]
PROSITE	PS50102. RRM. 2 hits. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	37714.
SOURCE	Search...

Entry information

Entry name

HNRDL_HUMAN

Accession

Primary (citable) accession number: O14979
Secondary accession number(s): Q6SPF2 , Q7KZ74, Q7KZ75, Q96IM0, Q96S43

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 15, 2007
Last sequence update:	August 1, 1999
Last modified:	January 19, 2010
This is version 85 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any 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.