Reviewed, UniProtKB/Swiss-Prot O60506 (HNRPQ_HUMAN)

Names and origin

Protein names

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

Gene names

Name:	SYNCRIP
Synonyms:	HNRPQ, NSAP1

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	623 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	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. Ref.3 Ref.10 Ref.11 Ref.12 Ref.21
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, at least composed of AQR, ASCC3L1, C19orf29, CDC40, CDC5L, CRNKL1, DDX23, DDX41, DDX48, DDX5, DGCR14, DHX35, DHX38, DHX8, EFTUD2, FRG1, GPATC1, HNRPA1, HNRPA2B1, HNRPA3, HNRPC, HNRPF, HNRPH1, HNRPK, HNRPM, HNRPR, HNRPU, KIAA1160, KIAA1604, LSM2, LSM3, MAGOH, MORG1, PABPC1, PLRG1, PNN, PPIE, PPIL1, PPIL3, PPWD1, PRPF19, PRPF4B, PRPF6, PRPF8, RALY, RBM22, RBM8A, RBMX, SART1, SF3A1, SF3A2, SF3A3, SF3B1, SF3B2, SF3B3, SFRS1, SKIV2L2, SNRPA1, SNRPB, SNRPB2, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF, SNRPG, SNW1, SRRM1, SRRM2, SYF2, SYNCRIP, TFIP11, THOC4, U2AF1, WDR57, XAB2 and ZCCHC8. 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. Ref.3 Ref.11 Ref.12 Ref.1 Ref.14
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.21 Ref.16 Isoform 1: Nucleus › nucleoplasm By similarity. Note: Expressed predominantly in the nucleoplasm By similarity. Ref.3 Ref.21 Ref.16 Isoform 2: Nucleus › nucleoplasm By similarity. Note: Expressed predominantly in the nucleoplasm By similarity. Ref.3 Ref.21 Ref.16 Isoform 3: Nucleus › nucleoplasm By similarity. Note: Expressed predominantly in the nucleoplasm By similarity. Ref.3 Ref.21 Ref.16
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 may be involved in RNA-binding and protein-protein interactions.
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. Phosphorylated upon DNA damage, probably by ATM or ATR. Ref.9 Ref.18
Sequence similarities	Contains 3 RRM (RNA recognition motif) domains.
Sequence caution	The sequence AAH15575.1 differs from that shown. Reason: Miscellaneous discrepancy. Contaminating sequence. Potential poly-A sequence starting in position 413.

Ontologies

Keywords
Biological process	Host-virus interaction 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 Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	CRD-mediated mRNA stabilization Ref.21 Inferred from mutant phenotype. Source: UniProtKB RNA splicing Ref.1 Traceable author statement. Source: ProtInc interspecies interaction between organisms Inferred from electronic annotation. Source: UniProtKB-KW mRNA processing Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	CRD-mediated mRNA stability complex Ref.21 Inferred from direct assay. 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 microsome Inferred from electronic annotation. Source: UniProtKB-SubCell nucleoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell spliceosomal complex Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	nucleotide binding Inferred from electronic annotation. Source: InterPro protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CNBP	P62633	1	EBI-1024357,EBI-1047529
HNRNPD	Q14103-4	3	EBI-1024357,EBI-432545
HNRNPD	Q14103-4	1	EBI-1024377,EBI-432545
PRKRA	O75569	1	EBI-1024357,EBI-713955
PUF60	Q9UHX1	1	EBI-1024357,EBI-1053259
STK24	Q5T5B3	1	EBI-1024357,EBI-1054809

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.
Note: Expressed predominantly in the nucleoplasm (By similarity). Ref.3 Ref.21 Ref.16
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: Expressed predominantly in the nucleoplasm (By similarity). Ref.3 Ref.21 Ref.16 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: Expressed predominantly in the nucleoplasm (By similarity). Ref.3 Ref.21 Ref.16 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
	Sequence conflict	550 – 551	2	QG → V in AAK59705. Ref.5
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

Initiator methionine

1

1

Removed

Chain

2 – 623

622

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

2

1

N-acetylalanine Ref.20

Modified residue

221

1

N6-acetyllysine Ref.22

Modified residue

363

1

N6-acetyllysine Ref.22

Modified residue

373

1

Phosphotyrosine Ref.9

Modified residue

587

1

Phosphoserine Ref.18

Cross-link

123

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.17

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

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

623

Helix Strand Turn

Details...

Beta strand

340 – 343

4

Helix

351 – 360

10

Beta strand

364 – 369

6

Beta strand

374 – 380

7

Helix

385 – 391

7

Beta strand

402 – 405

4

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). 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). 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. 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. 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: 9847309] [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: 11574476] [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: 14574404] [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: 15489334] [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: 12601080] [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: 11051545] [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: 11352648] [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: 11134005] [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: 9731529] [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: 12376575] [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: 11991638] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE SPICEOSOMAL C COMPLEX.
[16]	"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: 17289661] [Abstract] Cited for: IDENTIFICATION IN A MRNP GRANULE COMPLEX, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
[17]	"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: 17370265] [Abstract] Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-123, MASS SPECTROMETRY.
[18]	"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: 17525332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-587, MASS SPECTROMETRY.
[19]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[20]	"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY.
[21]	"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: 19029303] [Abstract] Cited for: FUNCTION, COMPONENT OF THE CRD-MEDIATED MRNA STABILIZATION COMPLEX, IDENTIFICATION IN A MRNP COMPLEX, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
[22]	"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-221 AND LYS-363, MASS SPECTROMETRY.
[23]	"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.
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.
NP_001153146.1.
NP_001153147.1.
NP_001153148.1.
NP_001153149.1.
NP_006363.4.

UniGene

Hs.571177

3D structure databases

PDBe
RCSB PDB
PDBj

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

SMR

O60506. Positions 162-408.

ModBase

Search...

Protein-protein interaction databases

IntAct

O60506. 15 interactions.

STRING

O60506.

PTM databases

PhosphoSite

O60506.

Proteomic databases

PRIDE

O60506.

Genome annotation databases

Ensembl

ENST00000369622; ENSP00000358635; ENSG00000135316; Homo sapiens. [Genome view]

GeneID

10492.

KEGG

hsa:10492.

UCSC

uc003pkw.1. human.
uc003pkx.1. human.
uc003pkz.1. human.
uc003pla.1. human.

Organism-specific databases

CTD

10492.

GeneCards

GC06M086377.

H-InvDB

HIX0006046.

HGNC

HGNC:16918. SYNCRIP.

HPA

CAB010895.

PharmGKB

PA134985065.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG19478.

HOVERGEN

O60506.

InParanoid

O60506.

OMA

THMYDEY.

OrthoDB

EOG9TF351.

PhylomeDB

O60506.

Gene expression databases

ArrayExpress

O60506.

Bgee

O60506.

CleanEx

HS_SYNCRIP.

Genevestigator

O60506.

GermOnline

ENSG00000135316. Homo sapiens.

Family and domain databases

InterPro

IPR012677. a_b_plait_nuc_bd.
IPR006535. HnRNP_R/Q_splicing_fac.
IPR000504. RRM_RNP1.
[Graphical view]

Gene3D

G3DSA:3.30.70.330. a_b_plait_nuc_bd. 3 hits.

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 Resources

NextBio

39814.

Entry information

Entry name

HNRPQ_HUMAN

Accession

Primary (citable) accession number: O60506
Secondary accession number(s): 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:	February 9, 2010
This is version 98 of the entry and version 2 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.