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Protein

Far upstream element-binding protein 2

Gene

KHSRP

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

Functioni

Binds to the dendritic targeting element and may play a role in mRNA trafficking (By similarity). Part of a ternary complex that binds to the downstream control sequence (DCS) of the pre-mRNA. Mediates exon inclusion in transcripts that are subject to tissue-specific alternative splicing. May interact with single-stranded DNA from the far-upstream element (FUSE). May activate gene expression. Also involved in degradation of inherently unstable mRNAs that contain AU-rich elements (AREs) in their 3'-UTR, possibly by recruiting degradation machinery to ARE-containing mRNAs.By similarity3 Publications

GO - Molecular functioni

  • DNA binding Source: UniProtKB-KW
  • mRNA 3'-UTR AU-rich region binding Source: UniProtKB
  • poly(A) RNA binding Source: UniProtKB

GO - Biological processi

  • 3'-UTR-mediated mRNA destabilization Source: UniProtKB
  • cellular response to cytokine stimulus Source: UniProtKB
  • mRNA catabolic process Source: Ensembl
  • mRNA processing Source: ProtInc
  • mRNA transport Source: UniProtKB-KW
  • negative regulation of nitric oxide biosynthetic process Source: UniProtKB
  • positive regulation of mRNA catabolic process Source: UniProtKB
  • regulation of miRNA metabolic process Source: Ensembl
  • regulation of mRNA stability Source: UniProtKB
  • regulation of transcription, DNA-templated Source: UniProtKB-KW
  • RNA splicing Source: UniProtKB
  • RNA splicing, via transesterification reactions Source: UniProtKB
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

mRNA processing, mRNA splicing, mRNA transport, Transcription, Transcription regulation, Transport

Keywords - Ligandi

DNA-binding, RNA-binding

Enzyme and pathway databases

ReactomeiR-HSA-380994. ATF4 activates genes.
R-HSA-450604. KSRP (KHSRP) binds and destabilizes mRNA.
SIGNORiQ92945.

Names & Taxonomyi

Protein namesi
Recommended name:
Far upstream element-binding protein 2
Short name:
FUSE-binding protein 2
Alternative name(s):
KH type-splicing regulatory protein
Short name:
KSRP
p75
Gene namesi
Name:KHSRP
Synonyms:FUBP2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:6316. KHSRP.

Subcellular locationi

GO - Cellular componenti

  • cytoplasmic stress granule Source: Ensembl
  • cytosol Source: Reactome
  • membrane Source: UniProtKB
  • nucleoplasm Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

DisGeNETi8570.
OpenTargetsiENSG00000088247.
PharmGKBiPA30097.

Chemistry databases

ChEMBLiCHEMBL1795105.

Polymorphism and mutation databases

BioMutaiKHSRP.
DMDMi313104306.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00000501372 – 711Far upstream element-binding protein 2Add BLAST710

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineCombined sources1
Modified residuei40Omega-N-methylarginineBy similarity1
Modified residuei87N6-acetyllysineBy similarity1
Modified residuei99PhosphoserineCombined sources1
Modified residuei100PhosphothreonineCombined sources1
Cross-linki121Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Combined sources
Modified residuei125PhosphoserineCombined sources1
Modified residuei129PhosphoserineCombined sources1
Modified residuei131PhosphoserineCombined sources1
Modified residuei181PhosphoserineCombined sources1
Modified residuei184PhosphoserineCombined sources1
Modified residuei193PhosphoserineCombined sources1 Publication1
Modified residuei274PhosphoserineCombined sources1
Modified residuei411Omega-N-methylarginineCombined sources1
Modified residuei413Omega-N-methylarginineCombined sources1
Modified residuei415Omega-N-methylarginineCombined sources1
Modified residuei442Omega-N-methylarginineCombined sources1
Modified residuei480PhosphoserineCombined sources1

Post-translational modificationi

Phosphorylation at Ser-193 leads to the unfolding of the unstable KH domain 1, creating a site for 14-3-3 YWHAZ binding, which promotes nuclear localization and impairs the RNA degradation function.1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ92945.
MaxQBiQ92945.
PaxDbiQ92945.
PeptideAtlasiQ92945.
PRIDEiQ92945.

2D gel databases

REPRODUCTION-2DPAGEQ92945.

PTM databases

iPTMnetiQ92945.
PhosphoSitePlusiQ92945.
SwissPalmiQ92945.

Miscellaneous databases

PMAP-CutDBQ92945.

Expressioni

Tissue specificityi

Detected in neural and non-neural cell lines.

Gene expression databases

BgeeiENSG00000088247.
CleanExiHS_KHSRP.
ExpressionAtlasiQ92945. baseline and differential.
GenevisibleiQ92945. HS.

Organism-specific databases

HPAiHPA034739.
HPA056518.

Interactioni

Subunit structurei

Part of a ternary complex containing FUBP2, PTBP1, PTBP2 and HNRPH1. Interacts with PARN.2 Publications

Protein-protein interaction databases

BioGridi114139. 78 interactors.
DIPiDIP-48484N.
IntActiQ92945. 21 interactors.
MINTiMINT-2813544.
STRINGi9606.ENSP00000381216.

Structurei

Secondary structure

1711
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi132 – 134Combined sources3
Helixi141 – 144Combined sources4
Beta strandi146 – 151Combined sources6
Helixi153 – 159Combined sources7
Turni161 – 163Combined sources3
Helixi165 – 174Combined sources10
Beta strandi179 – 183Combined sources5
Beta strandi188 – 194Combined sources7
Helixi198 – 216Combined sources19
Beta strandi234 – 240Combined sources7
Turni242 – 244Combined sources3
Turni245 – 249Combined sources5
Turni251 – 253Combined sources3
Helixi254 – 261Combined sources8
Beta strandi265 – 269Combined sources5
Beta strandi271 – 273Combined sources3
Beta strandi275 – 279Combined sources5
Beta strandi281 – 287Combined sources7
Helixi289 – 302Combined sources14
Beta strandi306 – 308Combined sources3
Turni317 – 319Combined sources3
Beta strandi325 – 330Combined sources6
Turni331 – 333Combined sources3
Helixi334 – 338Combined sources5
Beta strandi340 – 342Combined sources3
Helixi343 – 352Combined sources10
Beta strandi355 – 358Combined sources4
Beta strandi363 – 375Combined sources13
Helixi376 – 393Combined sources18
Beta strandi400 – 405Combined sources6
Turni413 – 415Combined sources3
Beta strandi427 – 432Combined sources6
Helixi433 – 435Combined sources3
Turni436 – 438Combined sources3
Turni441 – 444Combined sources4
Helixi446 – 453Combined sources8
Beta strandi454 – 460Combined sources7
Beta strandi472 – 479Combined sources8
Helixi481 – 494Combined sources14

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2HH2NMR-A424-525[»]
2HH3NMR-A318-418[»]
2JVZNMR-A233-396[»]
2OPUNMR-A130-218[»]
2OPVNMR-A221-305[»]
4B8TNMR-A317-418[»]
ProteinModelPortaliQ92945.
SMRiQ92945.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ92945.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini144 – 208KH 1PROSITE-ProRule annotationAdd BLAST65
Domaini233 – 299KH 2PROSITE-ProRule annotationAdd BLAST67
Domaini322 – 386KH 3PROSITE-ProRule annotationAdd BLAST65
Domaini424 – 491KH 4PROSITE-ProRule annotationAdd BLAST68
Repeati571 – 5821Add BLAST12
Repeati617 – 6282Add BLAST12
Repeati643 – 6543Add BLAST12
Repeati673 – 6844Add BLAST12

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni571 – 6844 X 12 AA imperfect repeatsAdd BLAST114

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi7 – 67Gly/Pro-richAdd BLAST61
Compositional biasi68 – 496Gly-richAdd BLAST429
Compositional biasi498 – 612Ala/Gly/Pro-richAdd BLAST115

Domaini

KH domains KH 3 and KH 4 behave as independent binding modules and can interact with different regions of the AU-rich RNA targets of degradation.

Sequence similaritiesi

Belongs to the KHSRP family.Curated
Contains 4 KH domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG1676. Eukaryota.
ENOG410XZYE. LUCA.
GeneTreeiENSGT00730000110664.
HOGENOMiHOG000231552.
HOVERGENiHBG000625.
InParanoidiQ92945.
KOiK13210.
PhylomeDBiQ92945.
TreeFamiTF313654.

Family and domain databases

Gene3Di3.30.1370.10. 4 hits.
InterProiIPR015096. DUF1897.
IPR004087. KH_dom.
IPR004088. KH_dom_type_1.
[Graphical view]
PfamiPF09005. DUF1897. 2 hits.
PF00013. KH_1. 4 hits.
[Graphical view]
SMARTiSM00322. KH. 4 hits.
[Graphical view]
SUPFAMiSSF54791. SSF54791. 4 hits.
PROSITEiPS50084. KH_TYPE_1. 4 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q92945-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSDYSTGGPP PGPPPPAGGG GGAGGAGGGP PPGPPGAGDR GGGGPGGGGP
60 70 80 90 100
GGGSAGGPSQ PPGGGGPGIR KDAFADAVQR ARQIAAKIGG DAATTVNNST
110 120 130 140 150
PDFGFGGQKR QLEDGDQPES KKLASQGDSI SSQLGPIHPP PRTSMTEEYR
160 170 180 190 200
VPDGMVGLII GRGGEQINKI QQDSGCKVQI SPDSGGLPER SVSLTGAPES
210 220 230 240 250
VQKAKMMLDD IVSRGRGGPP GQFHDNANGG QNGTVQEIMI PAGKAGLVIG
260 270 280 290 300
KGGETIKQLQ ERAGVKMILI QDGSQNTNVD KPLRIIGDPY KVQQACEMVM
310 320 330 340 350
DILRERDQGG FGDRNEYGSR IGGGIDVPVP RHSVGVVIGR SGEMIKKIQN
360 370 380 390 400
DAGVRIQFKQ DDGTGPEKIA HIMGPPDRCE HAARIINDLL QSLRSGPPGP
410 420 430 440 450
PGGPGMPPGG RGRGRGQGNW GPPGGEMTFS IPTHKCGLVI GRGGENVKAI
460 470 480 490 500
NQQTGAFVEI SRQLPPNGDP NFKLFIIRGS PQQIDHAKQL IEEKIEGPLC
510 520 530 540 550
PVGPGPGGPG PAGPMGPFNP GPFNQGPPGA PPHAGGPPPH QYPPQGWGNT
560 570 580 590 600
YPQWQPPAPH DPSKAAAAAA DPNAAWAAYY SHYYQQPPGP VPGPAPAPAA
610 620 630 640 650
PPAQGEPPQP PPTGQSDYTK AWEEYYKKIG QQPQQPGAPP QQDYTKAWEE
660 670 680 690 700
YYKKQAQVAT GGGPGAPPGS QPDYSAAWAE YYRQQAAYYG QTPGPGGPQP
710
PPTQQGQQQA Q
Length:711
Mass (Da):73,115
Last modified:November 30, 2010 - v4
Checksum:iAB0B7C0B5B938114
GO

Sequence cautioni

The sequence AAC50892 differs from that shown. Reason: Frameshift at positions 304, 309, 466 and 473.Curated
The sequence AAH85004 differs from that shown. Aberrant splicing.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti46G → C in AAB53222 (PubMed:9136930).Curated1
Sequence conflicti46G → C in AAD29861 (PubMed:10087204).Curated1
Sequence conflicti96V → G in AAC50892 (PubMed:8940189).Curated1
Sequence conflicti406 – 407MP → I in AAC50892 (PubMed:8940189).Curated2
Sequence conflicti422Missing in AAC50892 (PubMed:8940189).Curated1
Sequence conflicti487 – 488AK → CR in AAC50892 (PubMed:8940189).Curated2
Sequence conflicti694 – 696GPG → VP in AAC50892 (PubMed:8940189).Curated3

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U94832 mRNA. Translation: AAB53222.1.
AC011491 Genomic DNA. No translation available.
AC011539 Genomic DNA. No translation available.
BC085004 mRNA. Translation: AAH85004.1. Sequence problems.
AF093747, AF093745 Genomic DNA. Translation: AAD29861.1.
AF093748 Genomic DNA. Translation: AAD29862.1.
U69126 mRNA. Translation: AAC50892.1. Frameshift.
AB209662 mRNA. Translation: BAD92899.1.
CCDSiCCDS45936.1.
RefSeqiNP_003676.2. NM_003685.2.
UniGeneiHs.727344.

Genome annotation databases

EnsembliENST00000398148; ENSP00000381216; ENSG00000088247.
GeneIDi8570.
KEGGihsa:8570.
UCSCiuc002mer.5. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U94832 mRNA. Translation: AAB53222.1.
AC011491 Genomic DNA. No translation available.
AC011539 Genomic DNA. No translation available.
BC085004 mRNA. Translation: AAH85004.1. Sequence problems.
AF093747, AF093745 Genomic DNA. Translation: AAD29861.1.
AF093748 Genomic DNA. Translation: AAD29862.1.
U69126 mRNA. Translation: AAC50892.1. Frameshift.
AB209662 mRNA. Translation: BAD92899.1.
CCDSiCCDS45936.1.
RefSeqiNP_003676.2. NM_003685.2.
UniGeneiHs.727344.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2HH2NMR-A424-525[»]
2HH3NMR-A318-418[»]
2JVZNMR-A233-396[»]
2OPUNMR-A130-218[»]
2OPVNMR-A221-305[»]
4B8TNMR-A317-418[»]
ProteinModelPortaliQ92945.
SMRiQ92945.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114139. 78 interactors.
DIPiDIP-48484N.
IntActiQ92945. 21 interactors.
MINTiMINT-2813544.
STRINGi9606.ENSP00000381216.

Chemistry databases

ChEMBLiCHEMBL1795105.

PTM databases

iPTMnetiQ92945.
PhosphoSitePlusiQ92945.
SwissPalmiQ92945.

Polymorphism and mutation databases

BioMutaiKHSRP.
DMDMi313104306.

2D gel databases

REPRODUCTION-2DPAGEQ92945.

Proteomic databases

EPDiQ92945.
MaxQBiQ92945.
PaxDbiQ92945.
PeptideAtlasiQ92945.
PRIDEiQ92945.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000398148; ENSP00000381216; ENSG00000088247.
GeneIDi8570.
KEGGihsa:8570.
UCSCiuc002mer.5. human.

Organism-specific databases

CTDi8570.
DisGeNETi8570.
GeneCardsiKHSRP.
H-InvDBHIX0040083.
HGNCiHGNC:6316. KHSRP.
HPAiHPA034739.
HPA056518.
MIMi603445. gene.
neXtProtiNX_Q92945.
OpenTargetsiENSG00000088247.
PharmGKBiPA30097.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1676. Eukaryota.
ENOG410XZYE. LUCA.
GeneTreeiENSGT00730000110664.
HOGENOMiHOG000231552.
HOVERGENiHBG000625.
InParanoidiQ92945.
KOiK13210.
PhylomeDBiQ92945.
TreeFamiTF313654.

Enzyme and pathway databases

ReactomeiR-HSA-380994. ATF4 activates genes.
R-HSA-450604. KSRP (KHSRP) binds and destabilizes mRNA.
SIGNORiQ92945.

Miscellaneous databases

ChiTaRSiKHSRP. human.
EvolutionaryTraceiQ92945.
GeneWikiiKHSRP.
GenomeRNAii8570.
PMAP-CutDBQ92945.
PROiQ92945.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000088247.
CleanExiHS_KHSRP.
ExpressionAtlasiQ92945. baseline and differential.
GenevisibleiQ92945. HS.

Family and domain databases

Gene3Di3.30.1370.10. 4 hits.
InterProiIPR015096. DUF1897.
IPR004087. KH_dom.
IPR004088. KH_dom_type_1.
[Graphical view]
PfamiPF09005. DUF1897. 2 hits.
PF00013. KH_1. 4 hits.
[Graphical view]
SMARTiSM00322. KH. 4 hits.
[Graphical view]
SUPFAMiSSF54791. SSF54791. 4 hits.
PROSITEiPS50084. KH_TYPE_1. 4 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiFUBP2_HUMAN
AccessioniPrimary (citable) accession number: Q92945
Secondary accession number(s): O00301
, Q59EZ9, Q5U4P6, Q9UNT5, Q9UQH5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 26, 2003
Last sequence update: November 30, 2010
Last modified: November 2, 2016
This is version 162 of the entry and version 4 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 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.