Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

O60506

- HNRPQ_HUMAN

UniProt

O60506 - HNRPQ_HUMAN

Protein

Heterogeneous nuclear ribonucleoprotein Q

Gene

SYNCRIP

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 144 (01 Oct 2014)
      Sequence version 2 (07 Mar 2006)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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. protein binding Source: IntAct
    5. 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

    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-SubCell
    4. GAIT complex Source: UniProtKB
    5. histone pre-mRNA 3'end processing complex Source: UniProtKB
    6. membrane Source: UniProtKB
    7. nucleoplasm Source: UniProtKB-SubCell
    8. nucleus Source: ProtInc
    9. ribonucleoprotein complex Source: UniProtKB

    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; alternate2 Publications
    Modified residuei444 – 4441Omega-N-methylarginine; by PRMT1; alternate2 Publications
    Modified residuei496 – 4961Omega-N-methylarginine; by PRMT12 Publications
    Modified residuei510 – 5101Asymmetric dimethylarginine; by PRMT12 Publications
    Modified residuei518 – 5181Asymmetric dimethylarginine; by PRMT1; alternate2 Publications
    Modified residuei518 – 5181Omega-N-methylarginine; by PRMT1; alternate2 Publications
    Modified residuei526 – 5261Asymmetric dimethylarginine; by PRMT1; alternate2 Publications
    Modified residuei526 – 5261Omega-N-methylarginine; by PRMT1; alternate2 Publications
    Modified residuei536 – 5361Asymmetric dimethylarginine; by PRMT1; alternate2 Publications
    Modified residuei536 – 5361Omega-N-methylarginine; by PRMT1; alternate2 Publications
    Modified residuei539 – 5391Asymmetric dimethylarginine; by PRMT1; alternate2 Publications
    Modified residuei539 – 5391Omega-N-methylarginine; by PRMT1; alternate2 Publications
    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

    ArrayExpressiO60506.
    BgeeiO60506.
    CleanExiHS_SYNCRIP.
    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. 137 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.
    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

    MATEHVNGNG TEEPMDTTSA VIHSENFQTL LDAGLPQKVA EKLDEIYVAG    50
    LVAHSDLDER AIEALKEFNE DGALAVLQQF KDSDLSHVQN KSAFLCGVMK 100
    TYRQREKQGT KVADSSKGPD EAKIKALLER TGYTLDVTTG QRKYGGPPPD 150
    SVYSGQQPSV GTEIFVGKIP RDLFEDELVP LFEKAGPIWD LRLMMDPLTG 200
    LNRGYAFVTF CTKEAAQEAV KLYNNHEIRS GKHIGVCISV ANNRLFVGSI 250
    PKSKTKEQIL EEFSKVTEGL TDVILYHQPD DKKKNRGFCF LEYEDHKTAA 300
    QARRRLMSGK VKVWGNVGTV EWADPIEDPD PEVMAKVKVL FVRNLANTVT 350
    EEILEKAFSQ FGKLERVKKL KDYAFIHFDE RDGAVKAMEE MNGKDLEGEN 400
    IEIVFAKPPD QKRKERKAQR QAAKNQMYDD YYYYGPPHMP PPTRGRGRGG 450
    RGGYGYPPDY YGYEDYYDYY GYDYHNYRGG YEDPYYGYED FQVGARGRGG 500
    RGARGAAPSR GRGAAPPRGR AGYSQRGGPG SARGVRGARG GAQQQRGRGV 550
    RGARGGRGGN VGGKRKADGY NQPDSKRRQT NNQNWGSQPI AQQPLQGGDH 600
    SGNYGYKSEN QEFYQDTFGQ QWK 623
    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. 137 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.
    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

    ArrayExpressi O60506.
    Bgeei O60506.
    CleanExi HS_SYNCRIP.
    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

    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 1, 2014
    This is version 144 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