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O60506

- HNRPQ_HUMAN

UniProt

O60506 - HNRPQ_HUMAN

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Protein

Heterogeneous nuclear ribonucleoprotein Q

Gene

SYNCRIP

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

Functioni

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.6 Publications

GO - Molecular functioni

  1. nucleotide binding Source: InterPro
  2. poly(A) binding Source: Ensembl
  3. poly(A) RNA binding Source: UniProtKB
  4. RNA binding Source: ProtInc

GO - Biological processi

  1. cellular response to interferon-gamma Source: UniProtKB
  2. CRD-mediated mRNA stabilization Source: UniProtKB
  3. mRNA splicing, via spliceosome Source: UniProtKB
  4. negative regulation of translation Source: UniProtKB
  5. osteoblast differentiation Source: UniProt
  6. RNA processing Source: ProtInc
  7. RNA splicing Source: ProtInc
  8. viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein

Keywords - Biological processi

Host-virus interaction, mRNA processing, mRNA splicing, Translation regulation

Keywords - Ligandi

RNA-binding

Names & Taxonomyi

Protein namesi
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 namesi
Name:SYNCRIP
Synonyms:HNRPQ, NSAP1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 6

Organism-specific databases

HGNCiHGNC:16918. SYNCRIP.

Subcellular locationi

Cytoplasm 3 Publications. 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.By similarity
Isoform 1 : Nucleusnucleoplasm By similarity
Note: Expressed predominantly in the nucleoplasm.By similarity
Isoform 2 : Nucleusnucleoplasm By similarity
Note: Expressed predominantly in the nucleoplasm.By similarity
Isoform 3 : Nucleusnucleoplasm By similarity
Note: Expressed predominantly in the nucleoplasm.By similarity

GO - Cellular componenti

  1. catalytic step 2 spliceosome Source: UniProtKB
  2. CRD-mediated mRNA stability complex Source: UniProtKB
  3. endoplasmic reticulum Source: UniProtKB-KW
  4. GAIT complex Source: UniProtKB
  5. histone pre-mRNA 3'end processing complex Source: UniProtKB
  6. membrane Source: UniProtKB
  7. nucleus Source: ProtInc
  8. ribonucleoprotein complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Microsome, Nucleus, Spliceosome

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134985065.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 623622Heterogeneous nuclear ribonucleoprotein QPRO_0000081867Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Cross-linki123 – 123Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei221 – 2211N6-acetyllysine1 Publication
Modified residuei363 – 3631N6-acetyllysine1 Publication
Modified residuei373 – 3731Phosphotyrosine1 Publication
Modified residuei444 – 4441Asymmetric dimethylarginine; by PRMT1; alternate1 Publication
Modified residuei444 – 4441Omega-N-methylarginine; by PRMT1; alternate1 Publication
Modified residuei496 – 4961Omega-N-methylarginine; by PRMT11 Publication
Modified residuei510 – 5101Asymmetric dimethylarginine; by PRMT11 Publication
Modified residuei518 – 5181Asymmetric dimethylarginine; by PRMT1; alternate1 Publication
Modified residuei518 – 5181Omega-N-methylarginine; by PRMT1; alternate1 Publication
Modified residuei526 – 5261Asymmetric dimethylarginine; by PRMT1; alternate1 Publication
Modified residuei526 – 5261Omega-N-methylarginine; by PRMT1; alternate1 Publication
Modified residuei536 – 5361Asymmetric dimethylarginine; by PRMT1; alternate1 Publication
Modified residuei536 – 5361Omega-N-methylarginine; by PRMT1; alternate1 Publication
Modified residuei539 – 5391Asymmetric dimethylarginine; by PRMT1; alternate1 Publication
Modified residuei539 – 5391Omega-N-methylarginine; by PRMT1; alternate1 Publication
Modified residuei587 – 5871Phosphoserine1 Publication

Post-translational modificationi

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.By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiO60506.
PaxDbiO60506.
PRIDEiO60506.

PTM databases

PhosphoSiteiO60506.

Expressioni

Tissue specificityi

Ubiquitously expressed. Detected in heart, brain, pancreas, placenta, spleen, lung, liver, skeletal muscle, kidney, thymus, prostate, uterus, small intestine, colon, peripheral blood and testis.1 Publication

Gene expression databases

BgeeiO60506.
CleanExiHS_SYNCRIP.
ExpressionAtlasiO60506. baseline and differential.
GenevestigatoriO60506.

Organism-specific databases

HPAiCAB010895.
HPA041275.

Interactioni

Subunit structurei

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.By similarity13 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
HABP4Q5JVS02EBI-1024357,EBI-523625
HNRNPDQ14103-43EBI-1024357,EBI-432545
PRMT1Q998732EBI-1024357,EBI-78738
PRMT8Q9NR223EBI-1024357,EBI-745545

Protein-protein interaction databases

BioGridi115755. 140 interactions.
DIPiDIP-35540N.
IntActiO60506. 37 interactions.
MINTiMINT-2796763.

Structurei

Secondary structure

1
623
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi340 – 3434
Helixi351 – 36111
Beta strandi364 – 3696
Beta strandi374 – 3807
Helixi381 – 39111
Beta strandi394 – 3963
Beta strandi399 – 4057

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DGUNMR-A334-423[»]
ProteinModelPortaliO60506.
SMRiO60506. Positions 96-423.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO60506.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini162 – 24180RRM 1PROSITE-ProRule annotationAdd
BLAST
Domaini243 – 32583RRM 2PROSITE-ProRule annotationAdd
BLAST
Domaini338 – 40871RRM 3PROSITE-ProRule annotationAdd
BLAST
Repeati448 – 45031-1
Repeati451 – 45331-2
Repeati460 – 46452-1
Repeati469 – 47242-2
Repeati478 – 48031-3
Repeati485 – 48842-3
Repeati498 – 50031-4
Repeati526 – 52831-5
Repeati539 – 54131-6
Repeati554 – 55631-7
Repeati557 – 55931-8

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni400 – 561162Interaction with APOBEC1Add
BLAST
Regioni448 – 5591128 X 3 AA repeats of R-G-GAdd
BLAST
Regioni460 – 488293 X 4 AA repeats of Y-Y-G-YAdd
BLAST
Regioni518 – 54932Interaction with SMNAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi564 – 57815Bipartite nuclear localization signalSequence AnalysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi431 – 4344Poly-Tyr

Domaini

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.

Sequence similaritiesi

Contains 3 RRM (RNA recognition motif) domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG258596.
GeneTreeiENSGT00550000074366.
HOVERGENiHBG051917.
InParanoidiO60506.
KOiK13160.
OMAiTHMYDEY.
OrthoDBiEOG73JKW2.
PhylomeDBiO60506.
TreeFamiTF314932.

Family and domain databases

Gene3Di3.30.70.330. 2 hits.
InterProiIPR006535. HnRNP_R/Q_splicing_fac.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF00076. RRM_1. 3 hits.
[Graphical view]
SMARTiSM00360. RRM. 3 hits.
[Graphical view]
TIGRFAMsiTIGR01648. hnRNP-R-Q. 1 hit.
PROSITEiPS50102. RRM. 3 hits.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

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

This entry describes 5 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O60506-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MATEHVNGNG TEEPMDTTSA VIHSENFQTL LDAGLPQKVA EKLDEIYVAG
60 70 80 90 100
LVAHSDLDER AIEALKEFNE DGALAVLQQF KDSDLSHVQN KSAFLCGVMK
110 120 130 140 150
TYRQREKQGT KVADSSKGPD EAKIKALLER TGYTLDVTTG QRKYGGPPPD
160 170 180 190 200
SVYSGQQPSV GTEIFVGKIP RDLFEDELVP LFEKAGPIWD LRLMMDPLTG
210 220 230 240 250
LNRGYAFVTF CTKEAAQEAV KLYNNHEIRS GKHIGVCISV ANNRLFVGSI
260 270 280 290 300
PKSKTKEQIL EEFSKVTEGL TDVILYHQPD DKKKNRGFCF LEYEDHKTAA
310 320 330 340 350
QARRRLMSGK VKVWGNVGTV EWADPIEDPD PEVMAKVKVL FVRNLANTVT
360 370 380 390 400
EEILEKAFSQ FGKLERVKKL KDYAFIHFDE RDGAVKAMEE MNGKDLEGEN
410 420 430 440 450
IEIVFAKPPD QKRKERKAQR QAAKNQMYDD YYYYGPPHMP PPTRGRGRGG
460 470 480 490 500
RGGYGYPPDY YGYEDYYDYY GYDYHNYRGG YEDPYYGYED FQVGARGRGG
510 520 530 540 550
RGARGAAPSR GRGAAPPRGR AGYSQRGGPG SARGVRGARG GAQQQRGRGV
560 570 580 590 600
RGARGGRGGN VGGKRKADGY NQPDSKRRQT NNQNWGSQPI AQQPLQGGDH
610 620
SGNYGYKSEN QEFYQDTFGQ QWK
Length:623
Mass (Da):69,603
Last modified:March 7, 2006 - v2
Checksum:i0669FA604E8FBBDF
GO
Isoform 2 (identifier: O60506-2) [UniParc]FASTAAdd to Basket

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.

Show »
Length:588
Mass (Da):65,682
Checksum:i907A3EFBF5502D3F
GO
Isoform 3 (identifier: O60506-3) [UniParc]FASTAAdd to Basket

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.Curated

Show »
Length:562
Mass (Da):62,656
Checksum:i32F5C37178197E45
GO
Isoform 4 (identifier: O60506-4) [UniParc]FASTAAdd to Basket

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.

Show »
Length:527
Mass (Da):58,736
Checksum:iC17388F6F991A127
GO
Isoform 5 (identifier: O60506-5) [UniParc]FASTAAdd to Basket

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.

Show »
Length:410
Mass (Da):46,328
Checksum:i4F1AD0FE9570F7BD
GO

Sequence cautioni

The sequence AAH15575.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence starting in position 413.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti265 – 2651K → Q in AAD38198. (PubMed:9847309)Curated
Sequence conflicti287 – 2871G → S1 PublicationCurated
Sequence conflicti287 – 2871G → S(PubMed:11574476)Curated
Sequence conflicti288 – 2881F → S in AAH40844. (PubMed:15489334)Curated
Isoform 3 (identifier: O60506-3)
Sequence conflicti550 – 5512QG → V in AAK59705. (PubMed:14574404)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 152152Missing in isoform 5. 1 PublicationVSP_009581Add
BLAST
Alternative sequencei153 – 16311YSGQQPSVGTE → MEDHLQIPFIQ in isoform 5. 1 PublicationVSP_009582Add
BLAST
Alternative sequencei302 – 33635Missing in isoform 2 and isoform 4. 2 PublicationsVSP_009583Add
BLAST
Alternative sequencei550 – 62374VRGAR…GQQWK → QGKGVEAGPDLLQ in isoform 3, isoform 4 and isoform 5. 3 PublicationsVSP_009584Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS5005.1. [O60506-1]
CCDS55041.1. [O60506-3]
RefSeqiNP_001153145.1. NM_001159673.1.
NP_001153146.1. NM_001159674.1. [O60506-4]
NP_001153147.1. NM_001159675.1. [O60506-2]
NP_001153148.1. NM_001159676.1.
NP_001153149.1. NM_001159677.1. [O60506-3]
NP_001240700.1. NM_001253771.1. [O60506-5]
NP_006363.4. NM_006372.4. [O60506-1]
XP_005248694.1. XM_005248637.1. [O60506-1]
UniGeneiHs.571177.

Genome annotation databases

EnsembliENST00000355238; ENSP00000347380; ENSG00000135316. [O60506-3]
ENST00000369622; ENSP00000358635; ENSG00000135316. [O60506-1]
GeneIDi10492.
KEGGihsa:10492.
UCSCiuc003pku.3. human. [O60506-1]
uc003pkv.3. human. [O60506-3]
uc003pkw.3. human. [O60506-4]
uc003pkx.3. human. [O60506-5]
uc003pkz.2. human. [O60506-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS5005.1. [O60506-1 ]
CCDS55041.1. [O60506-3 ]
RefSeqi NP_001153145.1. NM_001159673.1.
NP_001153146.1. NM_001159674.1. [O60506-4 ]
NP_001153147.1. NM_001159675.1. [O60506-2 ]
NP_001153148.1. NM_001159676.1.
NP_001153149.1. NM_001159677.1. [O60506-3 ]
NP_001240700.1. NM_001253771.1. [O60506-5 ]
NP_006363.4. NM_006372.4. [O60506-1 ]
XP_005248694.1. XM_005248637.1. [O60506-1 ]
UniGenei Hs.571177.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2DGU NMR - A 334-423 [» ]
ProteinModelPortali O60506.
SMRi O60506. Positions 96-423.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115755. 140 interactions.
DIPi DIP-35540N.
IntActi O60506. 37 interactions.
MINTi MINT-2796763.

PTM databases

PhosphoSitei O60506.

Proteomic databases

MaxQBi O60506.
PaxDbi O60506.
PRIDEi O60506.

Protocols and materials databases

DNASUi 10492.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000355238 ; ENSP00000347380 ; ENSG00000135316 . [O60506-3 ]
ENST00000369622 ; ENSP00000358635 ; ENSG00000135316 . [O60506-1 ]
GeneIDi 10492.
KEGGi hsa:10492.
UCSCi uc003pku.3. human. [O60506-1 ]
uc003pkv.3. human. [O60506-3 ]
uc003pkw.3. human. [O60506-4 ]
uc003pkx.3. human. [O60506-5 ]
uc003pkz.2. human. [O60506-2 ]

Organism-specific databases

CTDi 10492.
GeneCardsi GC06M086317.
HGNCi HGNC:16918. SYNCRIP.
HPAi CAB010895.
HPA041275.
neXtProti NX_O60506.
PharmGKBi PA134985065.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG258596.
GeneTreei ENSGT00550000074366.
HOVERGENi HBG051917.
InParanoidi O60506.
KOi K13160.
OMAi THMYDEY.
OrthoDBi EOG73JKW2.
PhylomeDBi O60506.
TreeFami TF314932.

Miscellaneous databases

ChiTaRSi SYNCRIP. human.
EvolutionaryTracei O60506.
GeneWikii SYNCRIP.
GenomeRNAii 10492.
NextBioi 39814.
PROi O60506.

Gene expression databases

Bgeei O60506.
CleanExi HS_SYNCRIP.
ExpressionAtlasi O60506. baseline and differential.
Genevestigatori O60506.

Family and domain databases

Gene3Di 3.30.70.330. 2 hits.
InterProi IPR006535. HnRNP_R/Q_splicing_fac.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view ]
Pfami PF00076. RRM_1. 3 hits.
[Graphical view ]
SMARTi SM00360. RRM. 3 hits.
[Graphical view ]
TIGRFAMsi TIGR01648. hnRNP-R-Q. 1 hit.
PROSITEi PS50102. RRM. 3 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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, IDENTIFICATION BY 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, IDENTIFICATION BY 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. 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.
    Tissue: Mammary cancer.
  20. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-587, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  21. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  22. "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.
  23. "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.
  24. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  25. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  26. "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.
  27. "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.
  28. Cited for: METHYLATION AT ARG-444; ARG-496; ARG-510; ARG-518; ARG-526; ARG-536 AND ARG-539 BY PRMT1, IDENTIFICATION BY MASS SPECTROMETRY.
  29. "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.

Entry informationi

Entry nameiHNRPQ_HUMAN
AccessioniPrimary (citable) accession number: O60506
Secondary accession number(s): E1P501
, E1P502, Q53H05, Q5TCG2, Q5TCG3, Q8IW78, Q8N599, Q96LC1, Q96LC2, Q9Y583
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 2004
Last sequence update: March 7, 2006
Last modified: October 29, 2014
This is version 145 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3