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Protein

Heterogeneous nuclear ribonucleoprotein U

Gene

HNRNPU

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

Functioni

DNA- and RNA-binding protein involved in several cellular processes such as nuclear chromatin organization, telomere-length regulation, transcription, mRNA alternative splicing and stability, Xist-mediated transcriptional silencing and mitotic cell progression (PubMed:10490622, PubMed:18082603, PubMed:19029303, PubMed:22325991, PubMed:25986610, PubMed:28622508). Plays a role in the regulation of interphase large-scale gene-rich chromatin organization through chromatin-associated RNAs (caRNAs) in a transcription-dependent manner, and thereby maintains genomic stability (PubMed:1324173, PubMed:8174554, PubMed:28622508). Required for the localization of the long non-coding Xist RNA on the inactive chromosome X (Xi) and the subsequent initiation and maintenance of X-linked transcriptional gene silencing during X-inactivation (By similarity). Plays a role as a RNA polymerase II (Pol II) holoenzyme transcription regulator (PubMed:8174554, PubMed:9353307, PubMed:10490622, PubMed:15711563, PubMed:19617346, PubMed:23811339). Promotes transcription initiation by direct association with the core-TFIIH basal transcription factor complex for the assembly of a functional pre-initiation complex with Pol II in a actin-dependent manner (PubMed:10490622, PubMed:15711563). Blocks Pol II transcription elongation activity by inhibiting the C-terminal domain (CTD) phosphorylation of Pol II and dissociates from Pol II pre-initiation complex prior to productive transcription elongation (PubMed:10490622). Positively regulates CBX5-induced transcriptional gene silencing and retention of CBX5 in the nucleus (PubMed:19617346). Negatively regulates glucocorticoid-mediated transcriptional activation (PubMed:9353307). Key regulator of transcription initiation and elongation in embryonic stem cells upon leukemia inhibitory factor (LIF) signaling (By similarity). Involved in the long non-coding RNA H19-mediated Pol II transcriptional repression (PubMed:23811339). Participates in the circadian regulation of the core clock component ARNTL/BMAL1 transcription (By similarity). Plays a role in the regulation of telomere length (PubMed:18082603). Plays a role as a global pre-mRNA alternative splicing modulator by regulating U2 small nuclear ribonucleoprotein (snRNP) biogenesis (PubMed:22325991). Plays a role in mRNA stability (PubMed:17174306, PubMed:17289661, PubMed:19029303). Component of the CRD-mediated complex that promotes MYC mRNA stabilization (PubMed:19029303). Enhances the expression of specific genes, such as tumor necrosis factor TNFA, by regulating mRNA stability, possibly through binding to the 3'-untranslated region (UTR) (PubMed:17174306). Plays a role in mitotic cell cycle regulation (PubMed:21242313, PubMed:25986610). Involved in the formation of stable mitotic spindle microtubules (MTs) attachment to kinetochore, spindle organization and chromosome congression (PubMed:21242313). Phosphorylation at Ser-59 by PLK1 is required for chromosome alignement and segregation and progression through mitosis (PubMed:25986610). Contributes also to the targeting of AURKA to mitotic spindle MTs (PubMed:21242313). Binds to double- and single-stranded DNA and RNA, poly(A), poly(C) and poly(G) oligoribonucleotides (PubMed:1628625, PubMed:8068679, PubMed:8174554, PubMed:9204873, PubMed:9405365). Binds to chromatin-associated RNAs (caRNAs) (PubMed:28622508). Associates with chromatin to scaffold/matrix attachment region (S/MAR) elements in a chromatin-associated RNAs (caRNAs)-dependent manner (PubMed:7509195, PubMed:1324173, PubMed:9204873, PubMed:9405365, PubMed:10671544, PubMed:11003645, PubMed:11909954, PubMed:28622508). Binds to the Xist RNA (PubMed:26244333). Binds the long non-coding H19 RNA (PubMed:23811339). Binds to SMN1/2 pre-mRNAs at G/U-rich regions (PubMed:22325991). Binds to small nuclear RNAs (snRNAs) (PubMed:22325991). Binds to the 3'-UTR of TNFA mRNA (PubMed:17174306). Binds (via RNA-binding RGG-box region) to the long non-coding Xist RNA; this binding is direct and bridges the Xist RNA and the inactive chromosome X (Xi) (By similarity). Also negatively regulates embryonic stem cell differentiation upon LIF signaling (By similarity). Required for embryonic development (By similarity).By similarity24 Publications
(Microbial infection) Negatively regulates immunodeficiency virus type 1 (HIV-1) replication by preventing the accumulation of viral mRNA transcripts in the cytoplasm.1 Publication

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi504 – 511ATPSequence analysis8

GO - Molecular functioni

  • actin binding Source: UniProtKB
  • ATP binding Source: UniProtKB
  • chromatin binding Source: UniProtKB
  • chromatin DNA binding Source: UniProtKB
  • core promoter binding Source: UniProtKB
  • DNA binding Source: UniProtKB
  • double-stranded DNA binding Source: UniProtKB
  • double-stranded RNA binding Source: UniProtKB
  • enhancer binding Source: Ensembl
  • identical protein binding Source: UniProtKB
  • macromolecular complex binding Source: UniProtKB
  • mRNA 3'-UTR binding Source: UniProtKB
  • poly(A) binding Source: UniProtKB
  • poly(C) RNA binding Source: UniProtKB
  • poly(G) binding Source: UniProtKB
  • pre-mRNA binding Source: UniProtKB
  • promoter-specific chromatin binding Source: UniProtKB
  • ribonucleoprotein complex binding Source: UniProtKB
  • RNA binding Source: UniProtKB
  • RNA polymerase II core binding Source: UniProtKB
  • RNA polymerase II C-terminal domain binding Source: UniProtKB
  • sequence-specific double-stranded DNA binding Source: UniProtKB
  • single-stranded DNA binding Source: UniProtKB
  • single-stranded RNA binding Source: UniProtKB
  • snRNA binding Source: UniProtKB
  • telomerase RNA binding Source: BHF-UCL
  • TFIIH-class transcription factor binding Source: UniProtKB
  • transcription corepressor activity Source: UniProtKB

GO - Biological processi

  • cardiac muscle cell development Source: Ensembl
  • cellular response to dexamethasone stimulus Source: Ensembl
  • cellular response to glucocorticoid stimulus Source: UniProtKB
  • cellular response to leukemia inhibitory factor Source: UniProtKB
  • circadian regulation of gene expression Source: UniProtKB
  • CRD-mediated mRNA stabilization Source: UniProtKB
  • dosage compensation by inactivation of X chromosome Source: UniProtKB
  • maintenance of protein location in nucleus Source: UniProtKB
  • mRNA splicing, via spliceosome Source: Reactome
  • mRNA stabilization Source: UniProtKB
  • negative regulation of kinase activity Source: UniProtKB
  • negative regulation of stem cell differentiation Source: UniProtKB
  • negative regulation of telomere maintenance via telomerase Source: BHF-UCL
  • negative regulation of transcription elongation from RNA polymerase II promoter Source: UniProtKB
  • negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • osteoblast differentiation Source: UniProtKB
  • positive regulation of attachment of mitotic spindle microtubules to kinetochore Source: UniProtKB
  • positive regulation of DNA topoisomerase (ATP-hydrolyzing) activity Source: UniProtKB
  • positive regulation of stem cell proliferation Source: UniProtKB
  • positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • protein localization to spindle microtubule Source: UniProtKB
  • regulation of alternative mRNA splicing, via spliceosome Source: UniProtKB
  • regulation of chromatin organization Source: UniProtKB
  • regulation of mitotic cell cycle Source: UniProtKB
  • regulation of mitotic spindle assembly Source: UniProtKB
  • RNA localization to chromatin Source: UniProtKB
  • RNA metabolic process Source: Reactome
  • RNA processing Source: ProtInc

Keywordsi

Molecular functionActivator, Chromatin regulator, Developmental protein, DNA-binding, Repressor, Ribonucleoprotein, RNA-binding
Biological processBiological rhythms, Cell cycle, Cell division, Differentiation, Mitosis, mRNA processing, mRNA splicing, Transcription, Transcription regulation
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-HSA-72163. mRNA Splicing - Major Pathway.
R-HSA-72203. Processing of Capped Intron-Containing Pre-mRNA.
SIGNORiQ00839.

Names & Taxonomyi

Protein namesi
Recommended name:
Heterogeneous nuclear ribonucleoprotein U1 Publication
Short name:
hnRNP U1 Publication
Alternative name(s):
GRIP1201 Publication
Nuclear p120 ribonucleoprotein1 Publication
Scaffold-attachment factor A2 Publications
Short name:
SAF-A2 Publications
p1201 Publication
pp1201 Publication
Gene namesi
Name:HNRNPUImported
Synonyms:C1orf199Imported, HNRPUImported, SAFA, U21.1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

EuPathDBiHostDB:ENSG00000153187.16.
HGNCiHGNC:5048. HNRNPU.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Centromere, Chromosome, Cytoplasm, Cytoskeleton, Kinetochore, Nucleus, Spliceosome

Pathology & Biotechi

Involvement in diseasei

Epileptic encephalopathy, early infantile, 54 (EIEE54)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of epileptic encephalopathy, a heterogeneous group of severe childhood onset epilepsies characterized by refractory seizures, neurodevelopmental impairment, and poor prognosis. Development is normal prior to seizure onset, after which cognitive and motor delays become apparent.
See also OMIM:617391
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_078622171 – 825Missing in EIEE54. 1 PublicationAdd BLAST655
Natural variantiVAR_078623805 – 825Missing in EIEE54; unknown pathological significance. 1 PublicationAdd BLAST21

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi59S → A: No change in interaction with AURKA, PLK1 and TPX2. Increases mitotic chromosome misalignment and chromosome segregation defects and time required to progress through mitosis. 1 Publication1
Mutagenesisi59S → E: Increases mitotic chromosome misalignment and chromosome segregation defects and decreases time required to progress through mitosis. 1 Publication1
Mutagenesisi100D → A: No cleavage by caspases during apoptosis. Inhibits CASP3-induced cleavage in vitro. 1 Publication1
Mutagenesisi616 – 620RTQKK → ATQAA: Loss of actin-binding. 1 Publication5

Keywords - Diseasei

Disease mutation, Epilepsy

Organism-specific databases

DisGeNETi3192.
MIMi617391. phenotype.
OpenTargetsiENSG00000153187.
PharmGKBiPA162391486.

Polymorphism and mutation databases

BioMutaiHNRNPU.
DMDMi254763463.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources3 Publications
ChainiPRO_00000818722 – 825Heterogeneous nuclear ribonucleoprotein UAdd BLAST824

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserine; partialCombined sources2 Publications1
Modified residuei4PhosphoserineCombined sources1
Modified residuei17N6-acetyllysineBy similarity1
Modified residuei21N6-acetyllysineBy similarity1
Modified residuei59Phosphoserine; by PLK1Combined sources1 Publication1
Modified residuei66PhosphoserineCombined sources1
Modified residuei186N6-acetyllysineBy similarity1
Modified residuei187ADP-ribosylserine1 Publication1
Modified residuei255CitrullineBy similarity1
Modified residuei265N6-acetyllysine; alternateCombined sources1
Cross-linki265Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateCombined sources
Cross-linki265Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residuei266PhosphotyrosineBy similarity1
Modified residuei267PhosphoserineCombined sources1
Modified residuei271PhosphoserineCombined sources1
Modified residuei286PhosphothreonineCombined sources1
Modified residuei352N6-acetyllysineCombined sources1
Cross-linki495Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei516N6-acetyllysine; alternateCombined sources1
Cross-linki516Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residuei524N6-acetyllysine; alternateCombined sources1
Cross-linki524Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residuei532PhosphothreonineCombined sources1
Cross-linki536Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei551N6-acetyllysineCombined sources1
Modified residuei565N6-acetyllysine; alternateCombined sources1
Cross-linki565Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Cross-linki574Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei582PhosphothreonineCombined sources1
Cross-linki609Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki626Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei635N6-acetyllysine; alternateCombined sources1
Cross-linki635Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Cross-linki664Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki670Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei702Omega-N-methylarginineCombined sources1
Modified residuei715Asymmetric dimethylarginineBy similarity1
Modified residuei720Asymmetric dimethylarginineBy similarity1
Modified residuei727Asymmetric dimethylarginineBy similarity1
Modified residuei733Asymmetric dimethylarginine; alternateCombined sources1
Modified residuei733Omega-N-methylarginine; alternateBy similarity1
Modified residuei739Asymmetric dimethylarginine; alternateCombined sources1
Modified residuei739Dimethylated arginine; in A2780 ovarian carcinoma cell line1 Publication1
Modified residuei739Omega-N-methylarginine; alternateCombined sources1
Modified residuei755Asymmetric dimethylarginineCombined sources1
Modified residuei762Asymmetric dimethylarginineCombined sources1
Modified residuei814N6-acetyllysine; alternateCombined sources1
Cross-linki814Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Isoform 2 (identifier: Q00839-2)
Modified residuei215N6-acetyllysineCombined sources1

Post-translational modificationi

Cleaved at Asp-100 by CASP3 during T-cell apoptosis, resulting in a loss of DNA- and chromatin-binding activities (PubMed:9405365, PubMed:10671544).2 Publications
Extensively phosphorylated (PubMed:7993898). Phosphorylated on Ser-59 by PLK1 and dephosphorylated by protein phosphatase 2A (PP2A) in mitosis (PubMed:25986610).2 Publications
Arg-739 is dimethylated, probably to asymmetric dimethylarginine (Ref. 8). Arg-733 is dimethylated, probably to asymmetric dimethylarginine (By similarity).By similarity1 Publication
Citrullinated by PADI4.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei100Cleavage; by CASP32 Publications1

Keywords - PTMi

Acetylation, ADP-ribosylation, Citrullination, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ00839.
MaxQBiQ00839.
PaxDbiQ00839.
PeptideAtlasiQ00839.
PRIDEiQ00839.

PTM databases

iPTMnetiQ00839.
PhosphoSitePlusiQ00839.
SwissPalmiQ00839.

Expressioni

Tissue specificityi

Widely expressed.1 Publication

Gene expression databases

BgeeiENSG00000153187.
CleanExiHS_HNRNPU.
ExpressionAtlasiQ00839. baseline and differential.
GenevisibleiQ00839. HS.

Organism-specific databases

HPAiCAB011532.
HPA041057.
HPA058707.

Interactioni

Subunit structurei

Oligomer (via ATPase domain and RNA-binding RGG-box region); oligomerization occurs upon ATP-binding in a chromatin-associated RNAs (caRNAs)- and transcription-dependent manner and is required for chromatin decompaction (PubMed:28622508). ATP hydrolysis is required to cycle from an oligomeric to monomeric state to compact chromatin (PubMed:28622508). Component of the coding region determinant (CRD)-mediated complex, composed of DHX9, HNRNPU, IGF2BP1, SYNCRIP and YBX1 (PubMed:19029303). Identified in the spliceosome C complex (PubMed:11991638). Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs (PubMed:17289661, PubMed:19029303). Associates with heterogeneous nuclear ribonucleoprotein (hnRNP) particles (PubMed:8174554, PubMed:9204873, PubMed:9405365, PubMed:11909954). Associates (via middle region) with the C-terminal domain (CTD) RNA polymerase II (Pol II) holoenzyme; this association occurs in a RNA-independent manner (PubMed:10490622). Associates (via middle region) with the core-TFIIH basal transcription factor complex; this association inhibits the CTD phosphorylation of RNA polymerase II holoenzyme by downregulating TFIIH kinase activity (PubMed:10490622). Associates with the telomerase holoenzyme complex (PubMed:18082603). Associates with spindle microtubules (MTs) in a TPX2-dependent manner (PubMed:21242313). Interacts (via C-terminus) with actin; this interaction is direct and mediates association with the phosphorylated CTD of RNA polymerase II and is disrupted in presence of the long non-coding H19 RNA (PubMed:15711563, PubMed:23811339). Interacts with AURKA (PubMed:21242313, PubMed:25986610). Interacts (via C-terminus) with CBX5; this interaction is, at least in part, RNA-dependent (PubMed:19617346). Interacts with CR2 (PubMed:7753047). Interacts with CRY1 (By similarity). Interacts (via C-terminus) with EP300; this interaction enhances DNA-binding to nuclear scaffold/matrix attachment region (S/MAR) elements (PubMed:11909954). Interacts with ERBB4 (PubMed:20858735). Interacts with GEMIN5 (PubMed:25911097). Interacts with IGF2BP1 (PubMed:17289661, PubMed:23640942). Interacts with IGF2BP2 and IGF2BP3 (PubMed:23640942). Interacts with NCL; this interaction occurs during mitosis (PubMed:21242313). Interacts (via C-terminus) with NR3C1 (via C-terminus) (PubMed:9353307). Interacts with PLK1; this interaction induces phosphorylation of HNRNPU at Ser-59 in mitosis (PubMed:25986610). Interacts with POU3F4 (PubMed:9105675). Interacts with SMARCA4; this interaction occurs in embryonic stem cells and stimulates global Pol II-mediated transcription. Interacts (via C-terminus) with TOP2A; this interaction protects the topoisomerase TOP2A from degradation and positively regulates the relaxation of supercoiled DNA by TOP2A in a RNA-dependent manner (By similarity). Interacts with TPX2; this interaction recruits HNRNPU to spindle microtubules (MTs) (PubMed:21242313, PubMed:25986610). Interacts with UBQLN2 (PubMed:25616961).By similarity22 Publications
(Microbial infection) Interacts with HIV-1 protein Rev.1 Publication

Binary interactionsi

Show more details

GO - Molecular functioni

  • actin binding Source: UniProtKB
  • identical protein binding Source: UniProtKB
  • RNA polymerase II core binding Source: UniProtKB
  • RNA polymerase II C-terminal domain binding Source: UniProtKB
  • TFIIH-class transcription factor binding Source: UniProtKB

Protein-protein interaction databases

BioGridi109433. 524 interactors.
CORUMiQ00839.
DIPiDIP-684N.
IntActiQ00839. 319 interactors.
MINTiMINT-1654412.
STRINGi9606.ENSP00000283179.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ZRJNMR-A23-42[»]
ProteinModelPortaliQ00839.
SMRiQ00839.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ00839.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini8 – 42SAPPROSITE-ProRule annotation2 PublicationsAdd BLAST35
Domaini267 – 464B30.2/SPRYPROSITE-ProRule annotationAdd BLAST198

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni488 – 672ATPase domain1 PublicationAdd BLAST185
Regioni611 – 626Actin-binding1 PublicationAdd BLAST16
Regioni714 – 739RNA-binding RGG-box2 PublicationsAdd BLAST26

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi2 – 160Asp/Glu-rich (acidic)Add BLAST159
Compositional biasi84 – 94Poly-GluAdd BLAST11
Compositional biasi161 – 209Gln-richAdd BLAST49
Compositional biasi703 – 825Gly-richAdd BLAST123
Compositional biasi740 – 750Poly-GlyAdd BLAST11

Domaini

The SAP domain is necessary for specific binding to nuclear scaffold/matrix attachment region (S/MAR) elements in DNA (PubMed:9405365, PubMed:11003645). The RNA-binding RGG-box region is necessary for its association with inactive X chromosome (Xi) regions and to chromatin-associated RNAs (caRNAs) (PubMed:14608463, PubMed:28622508). Both the DNA-binding domain SAP and the RNA-binding RGG-box region are necessary for the localization of Xist RNA on the Xi (By similarity). The ATPase and RNA-binding RGG-box regions are necessary for oligomerization (PubMed:28622508).By similarity4 Publications

Phylogenomic databases

eggNOGiENOG410IR1W. Eukaryota.
ENOG410Y1WQ. LUCA.
GeneTreeiENSGT00390000020210.
HOGENOMiHOG000253920.
HOVERGENiHBG061101.
InParanoidiQ00839.
KOiK12888.
OMAiQAFNQSW.
OrthoDBiEOG091G041T.
PhylomeDBiQ00839.
TreeFamiTF317301.

Family and domain databases

CDDicd12884. SPRY_hnRNP. 1 hit.
Gene3Di1.10.720.30. 1 hit.
InterProiView protein in InterPro
IPR001870. B30.2/SPRY.
IPR013320. ConA-like_dom_sf.
IPR026745. hnRNP_U.
IPR027417. P-loop_NTPase.
IPR003034. SAP_dom.
IPR036361. SAP_dom_sf.
IPR003877. SPRY_dom.
IPR035778. SPRY_hnRNP_U.
PANTHERiPTHR12381:SF11. PTHR12381:SF11. 1 hit.
PfamiView protein in Pfam
PF02037. SAP. 1 hit.
PF00622. SPRY. 1 hit.
SMARTiView protein in SMART
SM00513. SAP. 1 hit.
SM00449. SPRY. 1 hit.
SUPFAMiSSF49899. SSF49899. 1 hit.
SSF52540. SSF52540. 1 hit.
SSF68906. SSF68906. 1 hit.
PROSITEiView protein in PROSITE
PS50188. B302_SPRY. 1 hit.
PS50800. SAP. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q00839-1) [UniParc]FASTAAdd to basket
Also known as: Long

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
MSSSPVNVKK LKVSELKEEL KKRRLSDKGL KAELMERLQA ALDDEEAGGR
60 70 80 90 100
PAMEPGNGSL DLGGDSAGRS GAGLEQEAAA GGDEEEEEEE EEEEGISALD
110 120 130 140 150
GDQMELGEEN GAAGAADSGP MEEEEAASED ENGDDQGFQE GEDELGDEEE
160 170 180 190 200
GAGDENGHGE QQPQPPATQQ QQPQQQRGAA KEAAGKSSGP TSLFAVTVAP
210 220 230 240 250
PGARQGQQQA GGKKKAEGGG GGGRPGAPAA GDGKTEQKGG DKKRGVKRPR
260 270 280 290 300
EDHGRGYFEY IEENKYSRAK SPQPPVEEED EHFDDTVVCL DTYNCDLHFK
310 320 330 340 350
ISRDRLSASS LTMESFAFLW AGGRASYGVS KGKVCFEMKV TEKIPVRHLY
360 370 380 390 400
TKDIDIHEVR IGWSLTTSGM LLGEEEFSYG YSLKGIKTCN CETEDYGEKF
410 420 430 440 450
DENDVITCFA NFESDEVELS YAKNGQDLGV AFKISKEVLA GRPLFPHVLC
460 470 480 490 500
HNCAVEFNFG QKEKPYFPIP EEYTFIQNVP LEDRVRGPKG PEEKKDCEVV
510 520 530 540 550
MMIGLPGAGK TTWVTKHAAE NPGKYNILGT NTIMDKMMVA GFKKQMADTG
560 570 580 590 600
KLNTLLQRAP QCLGKFIEIA ARKKRNFILD QTNVSAAAQR RKMCLFAGFQ
610 620 630 640 650
RKAVVVCPKD EDYKQRTQKK AEVEGKDLPE HAVLKMKGNF TLPEVAECFD
660 670 680 690 700
EITYVELQKE EAQKLLEQYK EESKKALPPE KKQNTGSKKS NKNKSGKNQF
710 720 730 740 750
NRGGGHRGRG GFNMRGGNFR GGAPGNRGGY NRRGNMPQRG GGGGGSGGIG
760 770 780 790 800
YPYPRAPVFP GRGSYSNRGN YNRGGMPNRG NYNQNFRGRG NNRGYKNQSQ
810 820
GYNQWQQGQF WGQKPWSQHY HQGYY
Length:825
Mass (Da):90,584
Last modified:July 28, 2009 - v6
Checksum:i5D4EC4188436831F
GO
Isoform 2 (identifier: Q00839-2) [UniParc]FASTAAdd to basket
Also known as: Short

The sequence of this isoform differs from the canonical sequence as follows:
     213-231: Missing.

Show »
Length:806
Mass (Da):88,980
Checksum:iBCE1AD365501EDC1
GO

Sequence cautioni

The sequence AAC19382 differs from that shown. Aberrant splicing.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti603A → V in AAH07950 (PubMed:15489334).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_078622171 – 825Missing in EIEE54. 1 PublicationAdd BLAST655
Natural variantiVAR_014712712F → L2 PublicationsCorresponds to variant dbSNP:rs1052660Ensembl.1
Natural variantiVAR_078623805 – 825Missing in EIEE54; unknown pathological significance. 1 PublicationAdd BLAST21

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_005846213 – 231Missing in isoform 2. 3 PublicationsAdd BLAST19

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X65488 mRNA. Translation: CAA46472.1.
AF068846 mRNA. Translation: AAC19382.1. Sequence problems.
BX323046 Genomic DNA. No translation available.
BC003367 mRNA. Translation: AAH03367.1.
BC003621 mRNA. Translation: AAH03621.1.
BC007950 mRNA. Translation: AAH07950.2.
BC024767 mRNA. Translation: AAH24767.1.
BC034925 mRNA. Translation: AAH34925.1.
CCDSiCCDS31081.1. [Q00839-2]
CCDS41479.1. [Q00839-1]
PIRiS22765.
RefSeqiNP_004492.2. NM_004501.3. [Q00839-2]
NP_114032.2. NM_031844.2. [Q00839-1]
XP_016856604.1. XM_017001115.1. [Q00839-1]
XP_016856605.1. XM_017001116.1. [Q00839-1]
XP_016856606.1. XM_017001117.1. [Q00839-2]
UniGeneiHs.106212.
Hs.411490.
Hs.743421.

Genome annotation databases

EnsembliENST00000444376; ENSP00000393151; ENSG00000153187. [Q00839-2]
ENST00000640218; ENSP00000491215; ENSG00000153187. [Q00839-1]
GeneIDi3192.
KEGGihsa:3192.
UCSCiuc001iaz.2. human. [Q00839-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Similar proteinsi

Entry informationi

Entry nameiHNRPU_HUMAN
AccessioniPrimary (citable) accession number: Q00839
Secondary accession number(s): O75507
, Q8N174, Q96HY9, Q9BQ09
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: July 28, 2009
Last modified: November 22, 2017
This is version 201 of the entry and version 6 of the sequence. See 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 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references