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Protein

KH domain-containing, RNA-binding, signal transduction-associated protein 1

Gene

KHDRBS1

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

Functioni

Recruited and tyrosine phosphorylated by several receptor systems, for example the T-cell, leptin and insulin receptors. Once phosphorylated, functions as an adapter protein in signal transduction cascades by binding to SH2 and SH3 domain-containing proteins. Role in G2-M progression in the cell cycle. Represses CBP-dependent transcriptional activation apparently by competing with other nuclear factors for binding to CBP. Also acts as a putative regulator of mRNA stability and/or translation rates and mediates mRNA nuclear export. Positively regulates the association of constitutive transport element (CTE)-containing mRNA with large polyribosomes and translation initiation. According to some authors, is not involved in the nucleocytoplasmic export of unspliced (CTE)-containing RNA species according to (PubMed:22253824). RNA-binding protein that plays a role in the regulation of alternative splicing and influences mRNA splice site selection and exon inclusion. Binds to RNA containing 5'-[AU]UAA-3' as a bipartite motif spaced by more than 15 nucleotides. Binds poly(A). Can regulate CD44 alternative splicing in a Ras pathway-dependent manner (By similarity). In cooperation with HNRNPA1 modulates alternative splicing of BCL2L1 by promoting splicing toward isoform Bcl-X(S), and of SMN1 (PubMed:17371836, PubMed:20186123). Can regulate alternative splicing of NRXN1 and NRXN3 in the laminin G-like domain 6 containing the evolutionary conserved neurexin alternative spliced segment 4 (AS4) involved in neurexin selective targeting to postsynaptic partners. In a neuronal activity-dependent manner cooperates synergistically with KHDRBS2/SLIM-1 in regulation of NRXN1 exon skipping at AS4. The cooperation with KHDRBS2/SLIM-1 is antagonistic for regulation of NXRN3 alternative splicing at AS4 (By similarity).By similarity6 Publications
Isoform 3, which is expressed in growth-arrested cells only, inhibits S phase.1 Publication

GO - Molecular functioni

  • DNA binding Source: ProtInc
  • poly(A) binding Source: MGI
  • poly(A) RNA binding Source: UniProtKB
  • poly(U) RNA binding Source: MGI
  • RNA binding Source: UniProtKB
  • SH3/SH2 adaptor activity Source: UniProtKB

GO - Biological processi

  • cell cycle arrest Source: ProtInc
  • cell proliferation Source: ProtInc
  • cell surface receptor signaling pathway Source: UniProtKB
  • G2/M transition of mitotic cell cycle Source: UniProtKB
  • mRNA processing Source: ProtInc
  • negative regulation of transcription, DNA-templated Source: UniProtKB
  • positive regulation of RNA export from nucleus Source: UniProtKB
  • positive regulation of translational initiation Source: UniProtKB
  • regulation of mRNA splicing, via spliceosome Source: Ensembl
  • regulation of RNA export from nucleus Source: UniProtKB
  • signal transduction Source: ProtInc
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Cell cycle, mRNA processing, Transcription, Transcription regulation

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiR-HSA-8849468. PTK6 Regulates Proteins Involved in RNA Processing.
SignaLinkiQ07666.
SIGNORiQ07666.

Names & Taxonomyi

Protein namesi
Recommended name:
KH domain-containing, RNA-binding, signal transduction-associated protein 1
Alternative name(s):
GAP-associated tyrosine phosphoprotein p62
Src-associated in mitosis 68 kDa protein
Short name:
Sam68
p21 Ras GTPase-activating protein-associated p62
p68
Gene namesi
Name:KHDRBS1Imported
Synonyms:SAM681 Publication
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:18116. KHDRBS1.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: Reactome
  • Grb2-Sos complex Source: Ensembl
  • membrane Source: UniProtKB
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi103Y → S: Impairs homodimerization. 1 Publication1
Mutagenesisi110E → A: Impairs homodimerization. 1 Publication1
Mutagenesisi118F → S: Disrupts homodimerization, impairs influence on alternative splicing. 1 Publication1
Mutagenesisi229V → F: Disrupts binding to poly(A), impairs interaction with BCL2L1 modulation of BCL2L1 alternative splicing. 1 Publication1
Mutagenesisi241Y → E: Fails to influence alternative splicing of CD44, NRXN2 and NRXN3. 1 Publication1
Mutagenesisi381E → K: Disrupts interaction with APC. 1 Publication1
Mutagenesisi383Y → K: Impairs interaction with APC. 1 Publication1
Mutagenesisi384E → K: Disrupts interaction with APC. 1 Publication1
Mutagenesisi435Y → F: No effect on the nuclear localization. 1 Publication1
Mutagenesisi440Y → F: Completely blocks nuclear localization. 1 Publication1
Mutagenesisi443Y → F: No effect on the nuclear localization. 1 Publication1

Organism-specific databases

DisGeNETi10657.
OpenTargetsiENSG00000121774.
PharmGKBiPA30092.

Polymorphism and mutation databases

DMDMi62511098.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000501241 – 443KH domain-containing, RNA-binding, signal transduction-associated protein 1Add BLAST443

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei18PhosphoserineCombined sources1
Modified residuei20PhosphoserineCombined sources1
Modified residuei29PhosphoserineCombined sources1
Modified residuei33PhosphothreonineCombined sources1
Modified residuei45Asymmetric dimethylarginine; by PRMT11 Publication1
Modified residuei52Asymmetric dimethylarginine; partial; by PRMT11 Publication1
Modified residuei58PhosphoserineCombined sources1
Modified residuei84Phosphothreonine; by MAPK1By similarity1
Cross-linki102Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei113PhosphoserineBy similarity1
Modified residuei150PhosphoserineCombined sources1
Modified residuei175N6-acetyllysineCombined sources1
Modified residuei183PhosphothreonineCombined sources1
Modified residuei282Omega-N-methylarginineCombined sources1
Modified residuei284Omega-N-methylarginineCombined sources1
Modified residuei291Omega-N-methylarginineBy similarity1
Modified residuei304Asymmetric dimethylarginine; by PRMT11 Publication1
Modified residuei310Omega-N-methylarginine; by PRMT11 Publication1
Modified residuei315Omega-N-methylarginine; by PRMT11 Publication1
Modified residuei320Dimethylated arginine; in A2780 ovarian carcinoma cell line1 Publication1
Modified residuei320Omega-N-methylarginine; by PRMT11 Publication1
Modified residuei325Omega-N-methylarginine; by PRMT11 Publication1
Modified residuei331Asymmetric dimethylarginine; alternateBy similarity1
Modified residuei331Dimethylated arginine; in A2780 ovarian carcinoma cell line1 Publication1
Modified residuei331Omega-N-methylarginine; alternateCombined sources1
Modified residuei331Omega-N-methylated arginine; by PRMT1; alternate1 Publication1
Modified residuei340Dimethylated arginine; in A2780 ovarian carcinoma cell line1 Publication1
Modified residuei340Omega-N-methylarginine; by PRMT1Combined sources1
Modified residuei387Phosphotyrosine1 Publication1
Modified residuei390PhosphoserineCombined sources1
Modified residuei435Phosphotyrosine; by PTK61 Publication1
Modified residuei440Phosphotyrosine; by PTK61 Publication1
Modified residuei443Phosphotyrosine; by PTK61 Publication1

Post-translational modificationi

Tyrosine phosphorylated by several non-receptor tyrosine kinases, LCK, FYN and JAK3. Negatively correlates with ability to bind RNA but required for many interactions with proteins. Phosphorylation by PTK6 negatively regulates its RNA binding ability. Phosphorylation by PTK6 at Tyr-440 dictates the nulear localization of KHDRBS1. Phosphorylation at Tyr-387 disrupts interaction with APC. Phosphorylation at tyrosine residues by FYN inverts activity on modulation of BCL2L1 alternative splicing.5 Publications
Acetylated. Positively correlates with ability to bind RNA.1 Publication
Arginine methylation is required for nuclear localization. Also can affect interaction with other proteins. Inhibits interaction with Src-like SH3 domains, but not interaction with WW domains of WBP4/FBP21 AND FNBP4/FBP30.3 Publications

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ07666.
MaxQBiQ07666.
PaxDbiQ07666.
PeptideAtlasiQ07666.
PRIDEiQ07666.
TopDownProteomicsiQ07666-1. [Q07666-1]
Q07666-3. [Q07666-3]

PTM databases

iPTMnetiQ07666.
PhosphoSitePlusiQ07666.
SwissPalmiQ07666.

Miscellaneous databases

PMAP-CutDBQ07666.

Expressioni

Tissue specificityi

Ubiquitously expressed in all tissue examined. Isoform 1 is expressed at lower levels in brain, skeletal muscle, and liver whereas isoform 3 is intensified in skeletal muscle and in liver.1 Publication

Developmental stagei

Isoform 3 is only expressed in growth-arrested cells.1 Publication

Gene expression databases

BgeeiENSG00000121774.
CleanExiHS_KHDRBS1.
GenevisibleiQ07666. HS.

Organism-specific databases

HPAiCAB005355.
HPA051280.
HPA056813.

Interactioni

Subunit structurei

Self-associates to form homooligomers when bound to RNA, oligomerization appears to be limited when binding to proteins; dimerization increases RNA affinity (PubMed:26758068, PubMed:20610388). Interacts with KHDRBS3/SLIM-2 (PubMed:10332027). Interacts with KHDRBS2/SLIM-1; heterooligomer formation of KHDRBS family proteins may modulate RNA substrate specificity (By similarity). Interacts with RASA1, LCK, FYN, PTPN6, PLCG1, GRB2, CBL, JAK3, PIK3R, STAT3, APC, HNRNPA1 (PubMed:1374686, PubMed:9045636, PubMed:10332027, PubMed:11585385, PubMed:17371836, PubMed:22000517). Interacts with PTK6 (via SH3 and SH2 domains) (PubMed:10913193). Forms a complex with ILF2, ILF3, YLPM1, RBMX, NCOA5 and PPP1CA (PubMed:17890166). Does not interact with TPR (PubMed:22253824). Interacts with RBMY1A1, PRMT1 (By similarity). Binds WBP4/FBP21 (via WW domains), FNBP4/FBP30 (via WW domains). Interacts (via Arg/Gly-rich-flanked Pro-rich regions) with FYN (via the SH3 domain) (By similarity).By similarity8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself3EBI-1364,EBI-1364
FYNP062414EBI-1364,EBI-515315
GRB2P629938EBI-1364,EBI-401755
HCKP086314EBI-1364,EBI-346340
HNRNPA1P096519EBI-1364,EBI-352662
JAK3P523332EBI-1364,EBI-518246
LCKP062395EBI-1364,EBI-1348
LckP062402EBI-1364,EBI-1401From a different organism.
PIK3R1P237272EBI-1364,EBI-520244From a different organism.
PLCG1P191742EBI-1364,EBI-79387
SMARCA2P515312EBI-1364,EBI-679562
SRCP129313EBI-1364,EBI-621482
STAT3P407632EBI-1364,EBI-518675
VAV1P154983EBI-1364,EBI-625518
ZBTB7AO953659EBI-1364,EBI-2795384

GO - Molecular functioni

  • SH3/SH2 adaptor activity Source: UniProtKB

Protein-protein interaction databases

BioGridi115900. 170 interactors.
DIPiDIP-29007N.
IntActiQ07666. 78 interactors.
MINTiMINT-102826.
STRINGi9606.ENSP00000313829.

Chemistry databases

BindingDBiQ07666.

Structurei

Secondary structure

1443
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi100 – 113Combined sources14
Helixi119 – 134Combined sources16

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2XA6NMR-A/B97-135[»]
3QHEX-ray2.40B/D365-419[»]
ProteinModelPortaliQ07666.
SMRiQ07666.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ07666.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini171 – 197KHPROSITE-ProRule annotationAdd BLAST27

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni100 – 260Involved in homodimerization1 PublicationAdd BLAST161
Regioni351 – 443Interaction with HNRNPA11 PublicationAdd BLAST93

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi34 – 41Pro-richSequence analysis8
Compositional biasi44 – 55DMA/Gly-richSequence analysisAdd BLAST12
Compositional biasi59 – 89Pro-richSequence analysisAdd BLAST31
Compositional biasi282 – 292DMA/Gly-richSequence analysisAdd BLAST11
Compositional biasi295 – 301Pro-richSequence analysis7
Compositional biasi302 – 332Arg/Gly-richSequence analysisAdd BLAST31
Compositional biasi334 – 363Pro-richSequence analysisAdd BLAST30

Domaini

The KH domain is required for binding to RNA.By similarity
The Pro-rich domains are flanked by Arg/Gly-rich motifs which can be asymmetric dimethylated on arginine residues to give the DMA/Gly-rich regions. Selective methylation on these motifs can modulate protein-protein interactions (By similarity).By similarity

Sequence similaritiesi

Belongs to the KHDRBS family.Sequence analysis
Contains 1 KH domain.PROSITE-ProRule annotation

Keywords - Domaini

SH3-binding

Phylogenomic databases

eggNOGiKOG1588. Eukaryota.
COG5176. LUCA.
GeneTreeiENSGT00550000074434.
HOGENOMiHOG000230771.
HOVERGENiHBG079164.
InParanoidiQ07666.
KOiK13198.
OMAiFLFPDMM.
OrthoDBiEOG091G0EED.
PhylomeDBiQ07666.
TreeFamiTF314878.

Family and domain databases

Gene3Di3.30.1370.10. 1 hit.
InterProiIPR004087. KH_dom.
IPR004088. KH_dom_type_1.
IPR032571. Qua1_dom.
IPR032335. Sam68-YY.
[Graphical view]
PfamiPF00013. KH_1. 1 hit.
PF16274. Qua1. 1 hit.
PF16568. Sam68-YY. 1 hit.
[Graphical view]
SMARTiSM00322. KH. 1 hit.
[Graphical view]
SUPFAMiSSF54791. SSF54791. 1 hit.
PROSITEiPS50084. KH_TYPE_1. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 11 Publication (identifier: Q07666-1) [UniParc]FASTAAdd to basket

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
MQRRDDPAAR MSRSSGRSGS MDPSGAHPSV RQTPSRQPPL PHRSRGGGGG
60 70 80 90 100
SRGGARASPA TQPPPLLPPS ATGPDATVGG PAPTPLLPPS ATASVKMEPE
110 120 130 140 150
NKYLPELMAE KDSLDPSFTH AMQLLTAEIE KIQKGDSKKD DEENYLDLFS
160 170 180 190 200
HKNMKLKERV LIPVKQYPKF NFVGKILGPQ GNTIKRLQEE TGAKISVLGK
210 220 230 240 250
GSMRDKAKEE ELRKGGDPKY AHLNMDLHVF IEVFGPPCEA YALMAHAMEE
260 270 280 290 300
VKKFLVPDMM DDICQEQFLE LSYLNGVPEP SRGRGVPVRG RGAAPPPPPV
310 320 330 340 350
PRGRGVGPPR GALVRGTPVR GAITRGATVT RGVPPPPTVR GAPAPRARTA
360 370 380 390 400
GIQRIPLPPP PAPETYEEYG YDDTYAEQSY EGYEGYYSQS QGDSEYYDYG
410 420 430 440
HGEVQDSYEA YGQDDWNGTR PSLKAPPARP VKGAYREHPY GRY
Length:443
Mass (Da):48,227
Last modified:November 1, 1996 - v1
Checksum:i59FB4DB6FB4DBE98
GO
Isoform 2Curated (identifier: Q07666-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     37-61: Missing.

Note: No experimental confirmation available.Curated
Show »
Length:418
Mass (Da):45,861
Checksum:i36B5B877E35D9A2C
GO
Isoform 31 Publication (identifier: Q07666-3) [UniParc]FASTAAdd to basket
Also known as: DeltaKH1 Publication

The sequence of this isoform differs from the canonical sequence as follows:
     169-207: Missing.

Show »
Length:404
Mass (Da):44,027
Checksum:i0E6334E3447CCA5F
GO

Sequence cautioni

The sequence AAH10132 differs from that shown. Intron retention.Curated

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_05171937 – 61Missing in isoform 2. 1 PublicationAdd BLAST25
Alternative sequenceiVSP_051720169 – 207Missing in isoform 3. 1 PublicationAdd BLAST39

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M88108 mRNA. Translation: AAA59990.1.
U78971 mRNA. Translation: AAB47504.1.
AK091346 mRNA. Translation: BAC03643.1.
AL139249, AL445248 Genomic DNA. Translation: CAI21971.1.
AL139249, AL445248 Genomic DNA. Translation: CAI21972.1.
AL445248, AL139249 Genomic DNA. Translation: CAH71944.1.
AL445248, AL139249 Genomic DNA. Translation: CAH71945.1.
CH471059 Genomic DNA. Translation: EAX07576.1.
CH471059 Genomic DNA. Translation: EAX07577.1.
BC000717 mRNA. Translation: AAH00717.1.
BC010132 mRNA. Translation: AAH10132.1. Sequence problems.
BC019109 mRNA. Translation: AAH19109.1.
CCDSiCCDS350.1. [Q07666-1]
CCDS60067.1. [Q07666-3]
PIRiA38219.
RefSeqiNP_001258807.1. NM_001271878.1. [Q07666-3]
NP_006550.1. NM_006559.2. [Q07666-1]
UniGeneiHs.445893.

Genome annotation databases

EnsembliENST00000327300; ENSP00000313829; ENSG00000121774. [Q07666-1]
ENST00000492989; ENSP00000417731; ENSG00000121774. [Q07666-3]
GeneIDi10657.
KEGGihsa:10657.
UCSCiuc001bua.3. human. [Q07666-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M88108 mRNA. Translation: AAA59990.1.
U78971 mRNA. Translation: AAB47504.1.
AK091346 mRNA. Translation: BAC03643.1.
AL139249, AL445248 Genomic DNA. Translation: CAI21971.1.
AL139249, AL445248 Genomic DNA. Translation: CAI21972.1.
AL445248, AL139249 Genomic DNA. Translation: CAH71944.1.
AL445248, AL139249 Genomic DNA. Translation: CAH71945.1.
CH471059 Genomic DNA. Translation: EAX07576.1.
CH471059 Genomic DNA. Translation: EAX07577.1.
BC000717 mRNA. Translation: AAH00717.1.
BC010132 mRNA. Translation: AAH10132.1. Sequence problems.
BC019109 mRNA. Translation: AAH19109.1.
CCDSiCCDS350.1. [Q07666-1]
CCDS60067.1. [Q07666-3]
PIRiA38219.
RefSeqiNP_001258807.1. NM_001271878.1. [Q07666-3]
NP_006550.1. NM_006559.2. [Q07666-1]
UniGeneiHs.445893.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2XA6NMR-A/B97-135[»]
3QHEX-ray2.40B/D365-419[»]
ProteinModelPortaliQ07666.
SMRiQ07666.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115900. 170 interactors.
DIPiDIP-29007N.
IntActiQ07666. 78 interactors.
MINTiMINT-102826.
STRINGi9606.ENSP00000313829.

Chemistry databases

BindingDBiQ07666.

PTM databases

iPTMnetiQ07666.
PhosphoSitePlusiQ07666.
SwissPalmiQ07666.

Polymorphism and mutation databases

DMDMi62511098.

Proteomic databases

EPDiQ07666.
MaxQBiQ07666.
PaxDbiQ07666.
PeptideAtlasiQ07666.
PRIDEiQ07666.
TopDownProteomicsiQ07666-1. [Q07666-1]
Q07666-3. [Q07666-3]

Protocols and materials databases

DNASUi10657.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000327300; ENSP00000313829; ENSG00000121774. [Q07666-1]
ENST00000492989; ENSP00000417731; ENSG00000121774. [Q07666-3]
GeneIDi10657.
KEGGihsa:10657.
UCSCiuc001bua.3. human. [Q07666-1]

Organism-specific databases

CTDi10657.
DisGeNETi10657.
GeneCardsiKHDRBS1.
HGNCiHGNC:18116. KHDRBS1.
HPAiCAB005355.
HPA051280.
HPA056813.
MIMi602489. gene.
neXtProtiNX_Q07666.
OpenTargetsiENSG00000121774.
PharmGKBiPA30092.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1588. Eukaryota.
COG5176. LUCA.
GeneTreeiENSGT00550000074434.
HOGENOMiHOG000230771.
HOVERGENiHBG079164.
InParanoidiQ07666.
KOiK13198.
OMAiFLFPDMM.
OrthoDBiEOG091G0EED.
PhylomeDBiQ07666.
TreeFamiTF314878.

Enzyme and pathway databases

ReactomeiR-HSA-8849468. PTK6 Regulates Proteins Involved in RNA Processing.
SignaLinkiQ07666.
SIGNORiQ07666.

Miscellaneous databases

ChiTaRSiKHDRBS1. human.
EvolutionaryTraceiQ07666.
GeneWikiiKHDRBS1.
GenomeRNAii10657.
PMAP-CutDBQ07666.
PROiQ07666.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000121774.
CleanExiHS_KHDRBS1.
GenevisibleiQ07666. HS.

Family and domain databases

Gene3Di3.30.1370.10. 1 hit.
InterProiIPR004087. KH_dom.
IPR004088. KH_dom_type_1.
IPR032571. Qua1_dom.
IPR032335. Sam68-YY.
[Graphical view]
PfamiPF00013. KH_1. 1 hit.
PF16274. Qua1. 1 hit.
PF16568. Sam68-YY. 1 hit.
[Graphical view]
SMARTiSM00322. KH. 1 hit.
[Graphical view]
SUPFAMiSSF54791. SSF54791. 1 hit.
PROSITEiPS50084. KH_TYPE_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiKHDR1_HUMAN
AccessioniPrimary (citable) accession number: Q07666
Secondary accession number(s): D3DPP3
, Q6PJX7, Q8NB97, Q99760
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 12, 2005
Last sequence update: November 1, 1996
Last modified: November 30, 2016
This is version 170 of the entry and version 1 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 1
    Human chromosome 1: 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.