O60506 (HNRPQ_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Heterogeneous nuclear ribonucleoprotein Q
Short name=hnRNP Q

Alternative name(s):
Glycine- and tyrosine-rich RNA-binding protein
Short name=GRY-RBP
NS1-associated protein 1
Synaptotagmin-binding, cytoplasmic RNA-interacting protein

Gene names

Name:	SYNCRIP
Synonyms:	HNRPQ, NSAP1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	623 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Heterogenous nuclear ribonucleoprotein (hnRNP) implicated in mRNA processing mechanisms. Component of the CRD-mediated complex that promotes MYC mRNA stability. Isoform 1, isoform 2 and isoform 3 are associated in vitro with pre-mRNA, splicing intermediates and mature mRNA protein complexes. Isoform 1 binds to apoB mRNA AU-rich sequences. Isoform 1 is part of the APOB mRNA editosome complex and may modulate the postranscriptional C to U RNA-editing of the APOB mRNA through either by binding to A1CF (APOBEC1 complementation factor), to APOBEC1 or to RNA itself. May be involved in translationally coupled mRNA turnover. Implicated with other RNA-binding proteins in the cytoplasmic deadenylation/translational and decay interplay of the FOS mRNA mediated by the major coding-region determinant of instability (mCRD) domain. Interacts in vitro preferentially with poly(A) and poly(U) RNA sequences. Isoform 3 may be involved in cytoplasmic vesicle-based mRNA transport through interaction with synaptotagmins. Component of the GAIT (gamma interferon-activated inhibitor of translation) complex which mediates interferon-gamma-induced transcript-selective translation inhibition in inflammation processes. Upon interferon-gamma activation assembles into the GAIT complex which binds to stem loop-containing GAIT elements in the 3'-UTR of diverse inflammatory mRNAs (such as ceruplasmin) and suppresses their translation; seems not to be essential for GAIT complex function. Ref.3 Ref.10 Ref.11 Ref.12 Ref.22 Ref.26
Subunit structure	Isoform 1 is a component of the APOB mRNA editosome complex and interacts with APOBEC1 and A1CF (APOBEC1 complementation factor). Part of a complex associated with the FOS mCRD domain and consisting of PABPC1, PAIP1, CSDE1/UNR, HNRPD and SYNCRIP. Isoform 3 interacts with HNRPR. Interacts with POLR2A hyperphosphorylated C-terminal domain. Interacts with minute virus of mice (MVM) NS1 protein. Isoform 1, isoform 2 and isoform 3 interact with SMN. Isoform 3 interacts through its C-terminal domain with SYT7, SYT8 and SYT9 By similarity. The non-phosphorylated and phosphorylated forms are colocalized with PAIP1 in polysomes By similarity. Identified in a histone pre-mRNA complex, at least composed of ERI1, LSM11, SLBP, SNRPB, SYNCRIP and YBX1 By similarity. Identified in the spliceosome C complex. Component of the coding region determinant (CRD)-mediated complex, composed of DHX9, HNRNPU, IGF2BP1, SYNCRIP and YBX1. Identified in a mRNP complex, at least composed of DHX9, DDX3X, ELAVL1, HNRNPU, IGF2BP1, ILF3, PABPC1, PCBP2, PTBP2, STAU1, STAU2, SYNCRIP and YBX1. Identified in a mRNP granule complex, at least composed of ACTB, ACTN4, DHX9, ERG, HNRNPA1, HNRNPA2B1, HNRNPAB, HNRNPD, HNRNPL, HNRNPR, HNRNPU, HSPA1, HSPA8, IGF2BP1, ILF2, ILF3, NCBP1, NCL, PABPC1, PABPC4, PABPN1, RPLP0, RPS3, RPS3A, RPS4X, RPS8, RPS9, SYNCRIP, TROVE2, YBX1 and untranslated mRNAs. Interacts with GTPBP1. Component of the GAIT complex; in humans the complex assembly seems to be a two-step process in which EPRS first associates with SYNCRIP to form a pre-GAIT complex which is deficient in GAIT element binding. Ref.1 Ref.3 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.18 Ref.21 Ref.22 Ref.25
Subcellular location	Cytoplasm. Microsome By similarity. Endoplasmic reticulum By similarity. Nucleus By similarity. Note: The tyrosine phosphorylated form bound to RNA is found in microsomes By similarity. Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Ref.3 Ref.18 Ref.22 Isoform 1: Nucleus › nucleoplasm By similarity. Note: Expressed predominantly in the nucleoplasm By similarity. Ref.3 Ref.18 Ref.22 Isoform 2: Nucleus › nucleoplasm By similarity. Note: Expressed predominantly in the nucleoplasm By similarity. Ref.3 Ref.18 Ref.22 Isoform 3: Nucleus › nucleoplasm By similarity. Note: Expressed predominantly in the nucleoplasm By similarity. Ref.3 Ref.18 Ref.22
Tissue specificity	Ubiquitously expressed. Detected in heart, brain, pancreas, placenta, spleen, lung, liver, skeletal muscle, kidney, thymus, prostate, uterus, small intestine, colon, peripheral blood and testis. Ref.11
Domain	The domain containing eight Arg-Gly-Gly repeats (RGG/RXR-box) may be involved in RNA-binding and protein-protein interactions. It is methylated by PRMT1, and essential for nuclear localization.
Post-translational modification	Phosphorylated on tyrosine. The membrane-bound form found in microsomes is phosphorylated in vitro by insulin receptor tyrosine kinase (INSR). Phosphorylation is inhibited upon binding to RNA, whereas the cytoplasmic form is poorly phosphorylated By similarity. Ref.9
Sequence similarities	Contains 3 RRM (RNA recognition motif) domains.
Sequence caution	The sequence AAH15575.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence starting in position 413.

Ontologies

Keywords
Biological process	Host-virus interaction Translation regulation mRNA processing mRNA splicing
Cellular component	Cytoplasm Endoplasmic reticulum Microsome Nucleus Spliceosome
Coding sequence diversity	Alternative splicing
Domain	Repeat
Ligand	RNA-binding
Molecular function	Ribonucleoprotein
PTM	Acetylation Isopeptide bond Methylation Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	CRD-mediated mRNA stabilization Inferred from mutant phenotype Ref.22. Source: UniProtKB cellular response to interferon-gamma Inferred from direct assay Ref.16. Source: UniProtKB mRNA splicing, via spliceosome Inferred by curator Ref.15. Source: UniProtKB negative regulation of translation Inferred from direct assay Ref.26. Source: UniProtKB virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	CRD-mediated mRNA stability complex Inferred from direct assay Ref.22. Source: UniProtKB catalytic step 2 spliceosome Inferred from direct assay Ref.15. Source: UniProtKB endoplasmic reticulum Inferred from electronic annotation. Source: UniProtKB-SubCell histone pre-mRNA 3'end processing complex Inferred from sequence or structural similarity. Source: UniProtKB nucleoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	RNA binding Traceable author statement Ref.1. Source: ProtInc nucleotide binding Inferred from electronic annotation. Source: InterPro poly(A) RNA binding Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
HNRNPD	Q14103-4	3	EBI-1024357,EBI-432545

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: O60506-1)

Also known as: hnRNP Q3;

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: O60506-2)

Also known as: hnRNP Q2;

The sequence of this isoform differs from the canonical sequence as follows:
     302-336: Missing.

Note: May be due to a competing donor splice site.

Isoform 3 (identifier: O60506-3)

Also known as: hnRNP Q1;

The sequence of this isoform differs from the canonical sequence as follows:
     550-623: VRGARGGRGG...YQDTFGQQWK → QGKGVEAGPDLLQ

Note: May be due to a competing donor splice site and to an exon inclusion.

Isoform 4 (identifier: O60506-4)

The sequence of this isoform differs from the canonical sequence as follows:
     302-336: Missing.
     550-623: VRGARGGRGG...YQDTFGQQWK → QGKGVEAGPDLLQ

Note: May be due to a competing donor splice site and to an exon inclusion. No experimental confirmation available.

Isoform 5 (identifier: O60506-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-152: Missing.
     153-163: YSGQQPSVGTE → MEDHLQIPFIQ
     550-623: VRGARGGRGG...YQDTFGQQWK → QGKGVEAGPDLLQ

Note: May be due to a competing donor splice site and to an exon inclusion.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 623

623

Heterogeneous nuclear ribonucleoprotein Q

PRO_0000081867

Regions

Domain

162 – 241

80

RRM 1

Domain

243 – 325

83

RRM 2

Domain

338 – 408

71

RRM 3

Repeat

448 – 450

3

1-1

Repeat

451 – 453

3

1-2

Repeat

460 – 464

5

2-1

Repeat

469 – 472

4

2-2

Repeat

478 – 480

3

1-3

Repeat

485 – 488

4

2-3

Repeat

498 – 500

3

1-4

Repeat

526 – 528

3

1-5

Repeat

539 – 541

3

1-6

Repeat

554 – 556

3

1-7

Repeat

557 – 559

3

1-8

Region

400 – 561

162

Interaction with APOBEC1

Region

448 – 559

112

8 X 3 AA repeats of R-G-G

Region

460 – 488

29

3 X 4 AA repeats of Y-Y-G-Y

Region

518 – 549

32

Interaction with SMN

Motif

564 – 578

15

Bipartite nuclear localization signal Potential

Compositional bias

431 – 434

4

Poly-Tyr

Amino acid modifications

Modified residue

221

1

N6-acetyllysine Ref.23

Modified residue

363

1

N6-acetyllysine Ref.23

Modified residue

373

1

Phosphotyrosine Ref.9

Modified residue

444

1

Asymmetric dimethylarginine; by PRMT1; alternate Ref.27

Modified residue

444

1

Omega-N-methylarginine; by PRMT1; alternate Ref.27

Modified residue

496

1

Omega-N-methylarginine; by PRMT1 Ref.27

Modified residue

510

1

Asymmetric dimethylarginine; by PRMT1 Ref.27

Modified residue

518

1

Asymmetric dimethylarginine; by PRMT1; alternate Ref.27

Modified residue

518

1

Omega-N-methylarginine; by PRMT1; alternate Ref.27

Modified residue

536

1

Asymmetric dimethylarginine; by PRMT1; alternate Ref.27

Modified residue

536

1

Omega-N-methylarginine; by PRMT1; alternate Ref.27

Modified residue

539

1

Asymmetric dimethylarginine; by PRMT1; alternate Ref.27

Modified residue

539

1

Omega-N-methylarginine; by PRMT1; alternate Ref.27

Modified residue

587

1

Phosphoserine Ref.20

Cross-link

123

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.19

Natural variations

Alternative sequence

1 – 152

152

Missing in isoform 5.

VSP_009581

Alternative sequence

153 – 163

11

YSGQQPSVGTE → MEDHLQIPFIQ in isoform 5.

VSP_009582

Alternative sequence

302 – 336

35

Missing in isoform 2 and isoform 4.

VSP_009583

Alternative sequence

550 – 623

74

VRGAR…GQQWK → QGKGVEAGPDLLQ in isoform 3, isoform 4 and isoform 5.

VSP_009584

Experimental info

Sequence conflict

265

1

K → Q in AAD38198. Ref.1

Sequence conflict

287

1

G → S Ref.2

Sequence conflict

287

1

G → S Ref.3

Sequence conflict

288

1

F → S in AAH40844. Ref.7

Isoform 3:

Sequence conflict

550 – 551

2

QG → V in AAK59705. Ref.5

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

623

Helix Strand Turn

Details...

Beta strand

340 – 343

4

Helix

351 – 361

11

Beta strand

364 – 369

6

Beta strand

374 – 380

7

Helix

381 – 391

11

Beta strand

394 – 396

3

Beta strand

399 – 405

7

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (hnRNP Q3) [UniParc]. Last modified March 7, 2006. Version 2. Checksum: 0669FA604E8FBBDF	FASTA	623	69,603
	10 20 30 40 50 60 MATEHVNGNG TEEPMDTTSA VIHSENFQTL LDAGLPQKVA EKLDEIYVAG LVAHSDLDER 70 80 90 100 110 120 AIEALKEFNE DGALAVLQQF KDSDLSHVQN KSAFLCGVMK TYRQREKQGT KVADSSKGPD 130 140 150 160 170 180 EAKIKALLER TGYTLDVTTG QRKYGGPPPD SVYSGQQPSV GTEIFVGKIP RDLFEDELVP 190 200 210 220 230 240 LFEKAGPIWD LRLMMDPLTG LNRGYAFVTF CTKEAAQEAV KLYNNHEIRS GKHIGVCISV 250 260 270 280 290 300 ANNRLFVGSI PKSKTKEQIL EEFSKVTEGL TDVILYHQPD DKKKNRGFCF LEYEDHKTAA 310 320 330 340 350 360 QARRRLMSGK VKVWGNVGTV EWADPIEDPD PEVMAKVKVL FVRNLANTVT EEILEKAFSQ 370 380 390 400 410 420 FGKLERVKKL KDYAFIHFDE RDGAVKAMEE MNGKDLEGEN IEIVFAKPPD QKRKERKAQR 430 440 450 460 470 480 QAAKNQMYDD YYYYGPPHMP PPTRGRGRGG RGGYGYPPDY YGYEDYYDYY GYDYHNYRGG 490 500 510 520 530 540 YEDPYYGYED FQVGARGRGG RGARGAAPSR GRGAAPPRGR AGYSQRGGPG SARGVRGARG 550 560 570 580 590 600 GAQQQRGRGV RGARGGRGGN VGGKRKADGY NQPDSKRRQT NNQNWGSQPI AQQPLQGGDH 610 620 SGNYGYKSEN QEFYQDTFGQ QWK
	Isoform 2 (hnRNP Q2) [UniParc]. Checksum: 907A3EFBF5502D3F	FASTA	588	65,682
	10 20 30 40 50 60 MATEHVNGNG TEEPMDTTSA VIHSENFQTL LDAGLPQKVA EKLDEIYVAG LVAHSDLDER 70 80 90 100 110 120 AIEALKEFNE DGALAVLQQF KDSDLSHVQN KSAFLCGVMK TYRQREKQGT KVADSSKGPD 130 140 150 160 170 180 EAKIKALLER TGYTLDVTTG QRKYGGPPPD SVYSGQQPSV GTEIFVGKIP RDLFEDELVP 190 200 210 220 230 240 LFEKAGPIWD LRLMMDPLTG LNRGYAFVTF CTKEAAQEAV KLYNNHEIRS GKHIGVCISV 250 260 270 280 290 300 ANNRLFVGSI PKSKTKEQIL EEFSKVTEGL TDVILYHQPD DKKKNRGFCF LEYEDHKTAA 310 320 330 340 350 360 QVKVLFVRNL ANTVTEEILE KAFSQFGKLE RVKKLKDYAF IHFDERDGAV KAMEEMNGKD 370 380 390 400 410 420 LEGENIEIVF AKPPDQKRKE RKAQRQAAKN QMYDDYYYYG PPHMPPPTRG RGRGGRGGYG 430 440 450 460 470 480 YPPDYYGYED YYDYYGYDYH NYRGGYEDPY YGYEDFQVGA RGRGGRGARG AAPSRGRGAA 490 500 510 520 530 540 PPRGRAGYSQ RGGPGSARGV RGARGGAQQQ RGRGVRGARG GRGGNVGGKR KADGYNQPDS 550 560 570 580 KRRQTNNQNW GSQPIAQQPL QGGDHSGNYG YKSENQEFYQ DTFGQQWK
	Isoform 3 (hnRNP Q1) [UniParc]. Checksum: 32F5C37178197E45	FASTA	562	62,656
	10 20 30 40 50 60 MATEHVNGNG TEEPMDTTSA VIHSENFQTL LDAGLPQKVA EKLDEIYVAG LVAHSDLDER 70 80 90 100 110 120 AIEALKEFNE DGALAVLQQF KDSDLSHVQN KSAFLCGVMK TYRQREKQGT KVADSSKGPD 130 140 150 160 170 180 EAKIKALLER TGYTLDVTTG QRKYGGPPPD SVYSGQQPSV GTEIFVGKIP RDLFEDELVP 190 200 210 220 230 240 LFEKAGPIWD LRLMMDPLTG LNRGYAFVTF CTKEAAQEAV KLYNNHEIRS GKHIGVCISV 250 260 270 280 290 300 ANNRLFVGSI PKSKTKEQIL EEFSKVTEGL TDVILYHQPD DKKKNRGFCF LEYEDHKTAA 310 320 330 340 350 360 QARRRLMSGK VKVWGNVGTV EWADPIEDPD PEVMAKVKVL FVRNLANTVT EEILEKAFSQ 370 380 390 400 410 420 FGKLERVKKL KDYAFIHFDE RDGAVKAMEE MNGKDLEGEN IEIVFAKPPD QKRKERKAQR 430 440 450 460 470 480 QAAKNQMYDD YYYYGPPHMP PPTRGRGRGG RGGYGYPPDY YGYEDYYDYY GYDYHNYRGG 490 500 510 520 530 540 YEDPYYGYED FQVGARGRGG RGARGAAPSR GRGAAPPRGR AGYSQRGGPG SARGVRGARG 550 560 GAQQQRGRGQ GKGVEAGPDL LQ
	Isoform 4 [UniParc]. Checksum: C17388F6F991A127	FASTA	527	58,736
	10 20 30 40 50 60 MATEHVNGNG TEEPMDTTSA VIHSENFQTL LDAGLPQKVA EKLDEIYVAG LVAHSDLDER 70 80 90 100 110 120 AIEALKEFNE DGALAVLQQF KDSDLSHVQN KSAFLCGVMK TYRQREKQGT KVADSSKGPD 130 140 150 160 170 180 EAKIKALLER TGYTLDVTTG QRKYGGPPPD SVYSGQQPSV GTEIFVGKIP RDLFEDELVP 190 200 210 220 230 240 LFEKAGPIWD LRLMMDPLTG LNRGYAFVTF CTKEAAQEAV KLYNNHEIRS GKHIGVCISV 250 260 270 280 290 300 ANNRLFVGSI PKSKTKEQIL EEFSKVTEGL TDVILYHQPD DKKKNRGFCF LEYEDHKTAA 310 320 330 340 350 360 QVKVLFVRNL ANTVTEEILE KAFSQFGKLE RVKKLKDYAF IHFDERDGAV KAMEEMNGKD 370 380 390 400 410 420 LEGENIEIVF AKPPDQKRKE RKAQRQAAKN QMYDDYYYYG PPHMPPPTRG RGRGGRGGYG 430 440 450 460 470 480 YPPDYYGYED YYDYYGYDYH NYRGGYEDPY YGYEDFQVGA RGRGGRGARG AAPSRGRGAA 490 500 510 520 PPRGRAGYSQ RGGPGSARGV RGARGGAQQQ RGRGQGKGVE AGPDLLQ
	Isoform 5 [UniParc]. Checksum: 4F1AD0FE9570F7BD	FASTA	410	46,328
	10 20 30 40 50 60 MEDHLQIPFI QIFVGKIPRD LFEDELVPLF EKAGPIWDLR LMMDPLTGLN RGYAFVTFCT 70 80 90 100 110 120 KEAAQEAVKL YNNHEIRSGK HIGVCISVAN NRLFVGSIPK SKTKEQILEE FSKVTEGLTD 130 140 150 160 170 180 VILYHQPDDK KKNRGFCFLE YEDHKTAAQA RRRLMSGKVK VWGNVGTVEW ADPIEDPDPE 190 200 210 220 230 240 VMAKVKVLFV RNLANTVTEE ILEKAFSQFG KLERVKKLKD YAFIHFDERD GAVKAMEEMN 250 260 270 280 290 300 GKDLEGENIE IVFAKPPDQK RKERKAQRQA AKNQMYDDYY YYGPPHMPPP TRGRGRGGRG 310 320 330 340 350 360 GYGYPPDYYG YEDYYDYYGY DYHNYRGGYE DPYYGYEDFQ VGARGRGGRG ARGAAPSRGR 370 380 390 400 410 GAAPPRGRAG YSQRGGPGSA RGVRGARGGA QQQRGRGQGK GVEAGPDLLQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A novel heterogeneous nuclear ribonucleoprotein-like protein interacts with NS1 of the minute virus of mice." Harris C.E., Boden R.A., Astell C.R. J. Virol. 73:72-80(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), INTERACTION WITH NS1. Tissue: Cervix carcinoma.
[2]	"Cloning of human and mouse GRY-RBP cDNA." Du G., Pan M., Zhou Y., Chen J., Yao H., Yuan J., Qiang B. Chin. Sci. Bull. 45:343-349(2000) Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]	"SMN interacts with a novel family of hnRNP and spliceosomal proteins." Mourelatos Z., Abel L., Yong J., Kataoka N., Dreyfuss G. EMBO J. 20:5443-5452(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), FUNCTION IN MRNA PROCESSING, SUBCELLULAR LOCATION, ASSOCIATION WITH THE SPLICEOSOME, INTERACTION WITH SMN AND HNRPR. Tissue: Cervix carcinoma.
[4]	Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S. Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Liver.
[5]	"The DNA sequence and analysis of human chromosome 6." Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S. Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"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] (ISOFORMS 1/3; 4 AND 5). Tissue: Eye, Lung and Urinary bladder.
[8]	Lubec G., Vishwanath V. Submitted (MAR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 43-60 AND 370-381, MASS SPECTROMETRY. Tissue: Brain and Cajal-Retzius cell.
[9]	"Signaling initiated by overexpression of the fibroblast growth factor receptor-1 investigated by mass spectrometry." Hinsby A.M., Olsen J.V., Bennett K.L., Mann M. Mol. Cell. Proteomics 2:29-36(2003) [PubMed] [Europe PMC] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE, MASS SPECTROMETRY, PHOSPHORYLATION AT TYR-373. Tissue: Kidney.
[10]	"A mechanism for translationally coupled mRNA turnover: interaction between the poly(A) tail and a c-fos RNA coding determinant via a protein complex." Grosset C., Chen C.-Y.A., Xu N., Sonenberg N., Jacquemin-Sablon H., Shyu A.-B. Cell 103:29-40(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN TRANSLATIONALLY COUPLED MRNA TURNOVER, IDENTIFICATION IN A COMPLEX WITH HNRPD; PABPC1; PAIP1 AND CSDE1. Tissue: Placenta.
[11]	"Two-hybrid cloning identifies an RNA-binding protein, GRY-RBP, as a component of apobec-1 editosome." Lau P.P., Chang B.-H., Chan L. Biochem. Biophys. Res. Commun. 282:977-983(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN APOB MRNA EDITING, INTERACTION WITH APOBEC1, TISSUE SPECIFICITY.
[12]	"Identification of GRY-RBP as an apolipoprotein B RNA-binding protein that interacts with both apobec-1 and apobec-1 complementation factor to modulate C to U editing." Blanc V., Navaratnam N., Henderson J.O., Anant S., Kennedy S., Jarmuz A., Scott J., Davidson N.O. J. Biol. Chem. 276:10272-10283(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN APOB MRNA EDITING, RNA-BINDING, INTERACTION WITH A1CF AND APOBEC1.
[13]	"Mass spectrometry and EST-database searching allows characterization of the multi-protein spliceosome complex." Neubauer G., King A., Rappsilber J., Calvio C., Watson M., Ajuh P., Sleeman J., Lamond A.I., Mann M. Nat. Genet. 20:46-50(1998) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN SPLICEOSOME.
[14]	"Hyperphosphorylated C-terminal repeat domain-associating proteins in the nuclear proteome link transcription to DNA/chromatin modification and RNA processing." Carty S.M., Greenleaf A.L. Mol. Cell. Proteomics 1:598-610(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH POLR2A.
[15]	"Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis." Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J. RNA 8:426-439(2002) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE SPLICEOSOMAL C COMPLEX.
[16]	"Noncanonical function of glutamyl-prolyl-tRNA synthetase: gene-specific silencing of translation." Sampath P., Mazumder B., Seshadri V., Gerber C.A., Chavatte L., Kinter M., Ting S.M., Dignam J.D., Kim S., Driscoll D.M., Fox P.L. Cell 119:195-208(2004) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN THE GAIT COMPLEX.
[17]	"The methylation of the C-terminal region of hnRNPQ (NSAP1) is important for its nuclear localization." Passos D.O., Quaresma A.J., Kobarg J. Biochem. Biophys. Res. Commun. 346:517-525(2006) [PubMed] [Europe PMC] [Abstract] Cited for: METHYLATION BY PRMT1.
[18]	"Molecular composition of IMP1 ribonucleoprotein granules." Joeson L., Vikesaa J., Krogh A., Nielsen L.K., Hansen T., Borup R., Johnsen A.H., Christiansen J., Nielsen F.C. Mol. Cell. Proteomics 6:798-811(2007) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN A MRNP GRANULE COMPLEX, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
[19]	"Tryptic digestion of ubiquitin standards reveals an improved strategy for identifying ubiquitinated proteins by mass spectrometry." Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D. Proteomics 7:868-874(2007) [PubMed] [Europe PMC] [Abstract] Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-123, MASS SPECTROMETRY. Tissue: Mammary cancer.
[20]	"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-587, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[21]	"Two-site phosphorylation of EPRS coordinates multimodal regulation of noncanonical translational control activity." Arif A., Jia J., Mukhopadhyay R., Willard B., Kinter M., Fox P.L. Mol. Cell 35:164-180(2009) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH EPRS.
[22]	"Control of c-myc mRNA stability by IGF2BP1-associated cytoplasmic RNPs." Weidensdorfer D., Stoehr N., Baude A., Lederer M., Koehn M., Schierhorn A., Buchmeier S., Wahle E., Huettelmaiery S. RNA 15:104-115(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, COMPONENT OF THE CRD-MEDIATED MRNA STABILIZATION COMPLEX, IDENTIFICATION IN A MRNP COMPLEX, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
[23]	"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-221 AND LYS-363, MASS SPECTROMETRY.
[24]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[25]	"Modulation of exosome-mediated mRNA turnover by interaction of GTP-binding protein 1 (GTPBP1) with its target mRNAs." Woo K.C., Kim T.D., Lee K.H., Kim D.Y., Kim S., Lee H.R., Kang H.J., Chung S.J., Senju S., Nishimura Y., Kim K.T. FASEB J. 25:2757-2769(2011) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH GTPBP1.
[26]	"Heterotrimeric GAIT complex drives transcript-selective translation inhibition in murine macrophages." Arif A., Chatterjee P., Moodt R.A., Fox P.L. Mol. Cell. Biol. 32:5046-5055(2012) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, RECONSTITUTION OF THE GAIT COMPLEX.
[27]	"A Y2H-seq approach defines the human protein methyltransferase interactome." Weimann M., Grossmann A., Woodsmith J., Ozkan Z., Birth P., Meierhofer D., Benlasfer N., Valovka T., Timmermann B., Wanker E.E., Sauer S., Stelzl U. Nat. Methods 0:0-0(2013) [PubMed] [Europe PMC] [Abstract] Cited for: METHYLATION AT ARG-444; ARG-496; ARG-510; ARG-518; ARG-526; ARG-536 AND ARG-539 BY PRMT1, MASS SPECTROMETRY.
[28]	"Solution structure of the RNA binding domain in heterogeneous nuclear ribonucleoprotein Q." RIKEN structural genomics initiative (RSGI) Submitted (SEP-2006) to the PDB data bank Cited for: STRUCTURE BY NMR OF 334-423.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF155568 mRNA. Translation: AAD38198.1.
AF037448 mRNA. Translation: AAC12926.1.
AY034481 mRNA. Translation: AAK59703.1.
AY034482 mRNA. Translation: AAK59704.1.
AY034483 mRNA. Translation: AAK59705.1.
AK222776 mRNA. Translation: BAD96496.1.
AL136082 Genomic DNA. Translation: CAI20446.1.
AL136082 Genomic DNA. Translation: CAI20447.1.
CH471051 Genomic DNA. Translation: EAW48625.1.
CH471051 Genomic DNA. Translation: EAW48626.1.
CH471051 Genomic DNA. Translation: EAW48629.1.
CH471051 Genomic DNA. Translation: EAW48630.1.
BC015575 mRNA. Translation: AAH15575.1. Sequence problems.
BC032643 mRNA. Translation: AAH32643.1.
BC040844 mRNA. Translation: AAH40844.1.

IPI

IPI00018140.
IPI00402182.
IPI00402183.
IPI00402184.
IPI00402185.

RefSeq

NP_001153145.1. NM_001159673.1.
NP_001153146.1. NM_001159674.1.
NP_001153147.1. NM_001159675.1.
NP_001153148.1. NM_001159676.1.
NP_001153149.1. NM_001159677.1.
NP_001240700.1. NM_001253771.1.
NP_006363.4. NM_006372.4.

UniGene

Hs.571177.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2DGU	NMR	-	A	334-423	[»]

ProteinModelPortal

O60506.

ModBase

Search...

Protein-protein interaction databases

IntAct

O60506. 26 interactions.

MINT

MINT-2796763.

PTM databases

PhosphoSite

O60506.

Proteomic databases

PaxDb

O60506.

PRIDE

O60506.

Protocols and materials databases

DNASU

10492.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000355238; ENSP00000347380; ENSG00000135316.
ENST00000369622; ENSP00000358635; ENSG00000135316.

GeneID

10492.

KEGG

hsa:10492.

UCSC

uc003pku.3. human.
uc003pkv.3. human.
uc003pkw.3. human.
uc003pkx.3. human.
uc003pkz.2. human.

Organism-specific databases

CTD

10492.

GeneCards

GC06M086267.

HGNC

HGNC:16918. SYNCRIP.

HPA

CAB010895.

neXtProt

NX_O60506.

PharmGKB

PA134985065.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG258596.

HOVERGEN

HBG051917.

InParanoid

O60506.

KO

K13160.

OMA

GNMATEH.

OrthoDB

EOG4FN4HM.

PhylomeDB

O60506.

Gene expression databases

ArrayExpress

O60506.

Bgee

O60506.

CleanEx

HS_SYNCRIP.

Genevestigator

O60506.

GermOnline

ENSG00000135316. Homo sapiens.

Family and domain databases

Gene3D

3.30.70.330. 2 hits.

InterPro

IPR006535. HnRNP_R/Q_splicing_fac.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]

Pfam

PF00076. RRM_1. 3 hits.
[Graphical view]

SMART

SM00360. RRM. 3 hits.
[Graphical view]

TIGRFAMs

TIGR01648. hnRNP-R-Q. 1 hit.

PROSITE

PS50102. RRM. 3 hits.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

SYNCRIP. human.

EvolutionaryTrace

O60506.

GenomeRNAi

10492.

NextBio

39814.

Entry information

Entry name

HNRPQ_HUMAN

Accession

Primary (citable) accession number: O60506
Secondary accession number(s): E1P501 , E1P502, Q53H05, Q5TCG2, Q5TCG3, Q8IW78, Q8N599, Q96LC1, Q96LC2, Q9Y583

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 1, 2004
Last sequence update:	March 7, 2006
Last modified:	May 1, 2013
This is version 131 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

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.