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Protein

Heterogeneous nuclear ribonucleoprotein K

Gene

HNRNPK

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

Functioni

One of the major pre-mRNA-binding proteins. Binds tenaciously to poly(C) sequences. Likely to play a role in the nuclear metabolism of hnRNAs, particularly for pre-mRNAs that contain cytidine-rich sequences. Can also bind poly(C) single-stranded DNA. Plays an important role in p53/TP53 response to DNA damage, acting at the level of both transcription activation and repression. When sumoylated, acts as a transcriptional coactivator of p53/TP53, playing a role in p21/CDKN1A and 14-3-3 sigma/SFN induction (By similarity). As far as transcription repression is concerned, acts by interacting with long intergenic RNA p21 (lincRNA-p21), a non-coding RNA induced by p53/TP53. This interaction is necessary for the induction of apoptosis, but not cell cycle arrest.By similarity3 Publications

GO - Molecular functioni

  • cadherin binding involved in cell-cell adhesion Source: BHF-UCL
  • poly(A) RNA binding Source: UniProtKB
  • RNA binding Source: ProtInc
  • RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: BHF-UCL
  • single-stranded DNA binding Source: BHF-UCL
  • transcriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific binding Source: BHF-UCL

GO - Biological processi

  • gene expression Source: Reactome
  • mRNA splicing, via spliceosome Source: UniProtKB
  • negative regulation of apoptotic process Source: MGI
  • negative regulation of mRNA splicing, via spliceosome Source: Ensembl
  • positive regulation of low-density lipoprotein particle receptor biosynthetic process Source: BHF-UCL
  • positive regulation of receptor-mediated endocytosis Source: BHF-UCL
  • positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  • protein sumoylation Source: Reactome
  • regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator Source: Ensembl
  • regulation of lipid transport by positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  • regulation of low-density lipoprotein particle clearance Source: BHF-UCL
  • RNA processing Source: ProtInc
  • signal transduction Source: ProtInc
  • viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator, Repressor, Ribonucleoprotein

Keywords - Biological processi

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

Keywords - Ligandi

DNA-binding, RNA-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000165119-MONOMER.
ReactomeiR-HSA-4570464. SUMOylation of RNA binding proteins.
R-HSA-72163. mRNA Splicing - Major Pathway.
R-HSA-72203. Processing of Capped Intron-Containing Pre-mRNA.
SIGNORiP61978.

Names & Taxonomyi

Protein namesi
Recommended name:
Heterogeneous nuclear ribonucleoprotein K
Short name:
hnRNP K
Alternative name(s):
Transformation up-regulated nuclear protein
Short name:
TUNP
Gene namesi
Name:HNRNPK
Synonyms:HNRPK
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:5044. HNRNPK.

Subcellular locationi

GO - Cellular componenti

  • catalytic step 2 spliceosome Source: UniProtKB
  • cell-cell adherens junction Source: BHF-UCL
  • cell projection Source: UniProtKB-KW
  • cytoplasm Source: ProtInc
  • extracellular exosome Source: UniProtKB
  • extracellular matrix Source: BHF-UCL
  • focal adhesion Source: UniProtKB
  • membrane Source: UniProtKB
  • nuclear chromatin Source: BHF-UCL
  • nucleoplasm Source: Reactome
  • nucleus Source: ProtInc
  • podosome Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell projection, Cytoplasm, Nucleus, Spliceosome

Pathology & Biotechi

Involvement in diseasei

Au-Kline syndrome (AUKS)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disorder characterized by intellectual disability, facial dysmorphism, cardiac defects, and connective tissue and skeletal abnormalities. Dysmorphic features include long palpebral fissures, ptosis, a broad prominent nasal bridge, hypoplastic alae nasi, an open downturned mouth, ears with underdeveloped and thick helices, high palate, and a unique tongue with a prominent median crease. Hypotonia, hyporeflexia, and high pain tolerance are additional features.
See also OMIM:616580

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi422K → R: Loss of sumoylation. Loss of TP53 transcriptional stimulation. 1 Publication1
Mutagenesisi424D → A: Loss of sumoylation. 1 Publication1

Keywords - Diseasei

Mental retardation

Organism-specific databases

DisGeNETi3190.
MIMi616580. phenotype.
OpenTargetsiENSG00000165119.
PharmGKBiPA162391350.

Polymorphism and mutation databases

BioMutaiHNRNPK.
DMDMi48429103.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000500961 – 463Heterogeneous nuclear ribonucleoprotein KAdd BLAST463

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineCombined sources1 Publication1
Modified residuei34N6-acetyllysine; alternateBy similarity1
Cross-linki34Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateCombined sources
Cross-linki34Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residuei36PhosphoserineCombined sources1
Modified residuei39PhosphothreonineBy similarity1
Modified residuei75PhosphoserineCombined sources1
Modified residuei116PhosphoserineCombined sources1
Cross-linki163Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Combined sources
Modified residuei198N6-acetyllysineBy similarity1
Modified residuei214PhosphoserineCombined sources1
Modified residuei216PhosphoserineCombined sources1
Modified residuei219N6-succinyllysineBy similarity1
Modified residuei284PhosphoserineCombined sources1 Publication1
Modified residuei316Omega-N-methylarginineCombined sources1
Modified residuei377Omega-N-methylarginineBy similarity1
Modified residuei379PhosphoserineCombined sources1
Modified residuei380PhosphotyrosineCombined sources1
Modified residuei405N6-acetyllysine; alternateBy similarity1
Cross-linki405Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residuei420PhosphoserineCombined sources1
Cross-linki422Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate
Cross-linki422Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateCombined sources
Cross-linki422Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources

Post-translational modificationi

Arg-296 and Arg-299 are dimethylated, probably to asymmetric dimethylarginine.
Sumoylated by CBX4. Sumoylation is increased upon DNA damage, such as that produced by doxorubicin, etoposide, UV light and camptothecin, due to enhanced CBX4 phosphorylation by HIPK2 under these conditions.3 Publications
Ubiquitinated by MDM2. Doxorubicin treatment does not affect monoubiquitination, but slightly decreases HNRNPK poly-ubiquitination.2 Publications
O-glycosylated (O-GlcNAcylated), in a cell cycle-dependent manner.1 Publication

Keywords - PTMi

Acetylation, Glycoprotein, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP61978.
PaxDbiP61978.
PeptideAtlasiP61978.
PRIDEiP61978.
TopDownProteomicsiP61978-1. [P61978-1]

2D gel databases

SWISS-2DPAGEP61978.

PTM databases

iPTMnetiP61978.
PhosphoSitePlusiP61978.
SwissPalmiP61978.

Miscellaneous databases

PMAP-CutDBP61978.

Expressioni

Inductioni

By DNA damage, including ionizing radiations and phleomycin treatment or UV irradiation. This induction requires ATM kinase activity (ionizing radiations and phleomycin) or ATR activity (UV irradiation). Up-regulation is due to protein stabilization. Constitutive protein levels are controlled by MDM2-mediated ubiquitination and degradation via the proteasome pathway.1 Publication

Gene expression databases

BgeeiENSG00000165119.
CleanExiHS_HNRNPK.
ExpressionAtlasiP61978. baseline and differential.
GenevisibleiP61978. HS.

Organism-specific databases

HPAiCAB004435.
CAB016225.
HPA007644.
HPA044105.

Interactioni

Subunit structurei

Interacts with RBM42 and ZIK1. Interacts with BRDT (By similarity). Identified in the spliceosome C complex. Interacts with ANKRD28. Interacts with HCV core protein. Interacts with ASFV p30 protein. Interacts with DDX1. Interacts with MDM2; this interaction leads to ubiquitination and proteasomal degradation. Interacts with p53/TP53.By similarity7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
P298469EBI-304185,EBI-8847394From a different organism.
Q8N9J23EBI-304185,EBI-10268244
AURKAO149652EBI-304185,EBI-448680
C'204LQ8V1E75EBI-304185,EBI-8068745From a different organism.
C6orf226Q5I0X43EBI-304185,EBI-10244057
CIRBPQ140115EBI-304185,EBI-538850
DALRD3Q5D0E63EBI-304185,EBI-2871865
DOCK2Q926083EBI-304185,EBI-448771
EBNA-LPQ8AZK72EBI-304185,EBI-1185167From a different organism.
FBXL18Q96D163EBI-304185,EBI-744419
GRB2P629935EBI-304185,EBI-401755
HNRNPLLQ8WVV93EBI-304185,EBI-535849
MARK4Q6IPE93EBI-304185,EBI-10250211
MDM2Q009872EBI-304185,EBI-389668
PCDHB14Q9Y5E93EBI-304185,EBI-10329013
PRMT1Q998733EBI-304185,EBI-78738
PRPF31F1T0A53EBI-304185,EBI-10177194
PRPF31Q8WWY34EBI-7060731,EBI-1567797
PRR3P795223EBI-304185,EBI-2803328
QKIQ96PU83EBI-304185,EBI-945792
RASD1Q9Y2723EBI-304185,EBI-740818
RBM3P981793EBI-304185,EBI-2949699
RBMXP381596EBI-304185,EBI-743526
RBMY1JQ154154EBI-7060731,EBI-8642021
RBPMS2Q6ZRY44EBI-7060731,EBI-11987469
SPG7Q9UQ903EBI-304185,EBI-717201
SRCP129316EBI-304185,EBI-621482
TERF2IPQ9NYB02EBI-304185,EBI-750109
TP53P046372EBI-7060731,EBI-366083
TP63Q9H3D42EBI-304185,EBI-2337775
ZNF385CQ66K413EBI-304185,EBI-10219231
ZNF408Q9H9D44EBI-7060731,EBI-347633
ZNF792Q3KQV33EBI-304185,EBI-10240849

GO - Molecular functioni

  • cadherin binding involved in cell-cell adhesion Source: BHF-UCL

Protein-protein interaction databases

BioGridi109431. 267 interactors.
DIPiDIP-31805N.
IntActiP61978. 161 interactors.
MINTiMINT-225422.
STRINGi9606.ENSP00000365439.

Structurei

Secondary structure

1463
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi381 – 384Combined sources4
Beta strandi388 – 395Combined sources8
Turni396 – 398Combined sources3
Helixi399 – 402Combined sources4
Helixi405 – 407Combined sources3
Helixi408 – 417Combined sources10
Beta strandi420 – 423Combined sources4
Beta strandi430 – 439Combined sources10
Helixi441 – 459Combined sources19

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1J5KNMR-A379-463[»]
1KHMNMR-A379-463[»]
1ZZIX-ray1.80A/B385-463[»]
1ZZJX-ray2.30A/B/C385-463[»]
1ZZKX-ray0.95A385-463[»]
ProteinModelPortaliP61978.
SMRiP61978.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP61978.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini42 – 104KH 1PROSITE-ProRule annotationAdd BLAST63
Repeati54 – 761-1Add BLAST23
Repeati59 – 623-14
Domaini144 – 209KH 2PROSITE-ProRule annotationAdd BLAST66
Repeati245 – 2502-16
Repeati257 – 2603-24
Repeati267 – 2703-34
Repeati295 – 2983-44
Repeati324 – 3292-26
Domaini387 – 451KH 3PROSITE-ProRule annotationAdd BLAST65
Repeati399 – 4211-2Add BLAST23
Repeati404 – 4073-54

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 276Necessary for interaction with DDX11 PublicationAdd BLAST276
Regioni35 – 197Interaction with ASFV p30Add BLAST163
Regioni54 – 4212 X 22 AA approximate repeatsAdd BLAST368
Regioni59 – 4075 X 4 AA repeats of G-X-G-GAdd BLAST349
Regioni209 – 337Interaction with ZIK1By similarityAdd BLAST129
Regioni236 – 273RNA-binding RGG-boxAdd BLAST38
Regioni245 – 3292 X 6 AA approximate repeatsAdd BLAST85

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi289 – 294Poly-Pro6
Compositional biasi310 – 315Poly-Pro6

Sequence similaritiesi

Contains 3 KH domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG2192. Eukaryota.
ENOG4111GSB. LUCA.
GeneTreeiENSGT00760000119144.
HOVERGENiHBG051916.
InParanoidiP61978.
KOiK12886.
OMAiKALRTDX.
PhylomeDBiP61978.
TreeFamiTF316335.

Family and domain databases

Gene3Di3.30.1370.10. 3 hits.
InterProiIPR033090. hnRNP_K.
IPR004087. KH_dom.
IPR004088. KH_dom_type_1.
IPR012987. ROK_N.
[Graphical view]
PANTHERiPTHR10288:SF167. PTHR10288:SF167. 1 hit.
PfamiPF00013. KH_1. 3 hits.
PF08067. ROKNT. 1 hit.
[Graphical view]
SMARTiSM00322. KH. 3 hits.
[Graphical view]
SUPFAMiSSF54791. SSF54791. 3 hits.
PROSITEiPS50084. KH_TYPE_1. 3 hits.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

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

Isoform 1 (identifier: P61978-1) [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
METEQPEETF PNTETNGEFG KRPAEDMEEE QAFKRSRNTD EMVELRILLQ
60 70 80 90 100
SKNAGAVIGK GGKNIKALRT DYNASVSVPD SSGPERILSI SADIETIGEI
110 120 130 140 150
LKKIIPTLEE GLQLPSPTAT SQLPLESDAV ECLNYQHYKG SDFDCELRLL
160 170 180 190 200
IHQSLAGGII GVKGAKIKEL RENTQTTIKL FQECCPHSTD RVVLIGGKPD
210 220 230 240 250
RVVECIKIIL DLISESPIKG RAQPYDPNFY DETYDYGGFT MMFDDRRGRP
260 270 280 290 300
VGFPMRGRGG FDRMPPGRGG RPMPPSRRDY DDMSPRRGPP PPPPGRGGRG
310 320 330 340 350
GSRARNLPLP PPPPPRGGDL MAYDRRGRPG DRYDGMVGFS ADETWDSAID
360 370 380 390 400
TWSPSEWQMA YEPQGGSGYD YSYAGGRGSY GDLGGPIITT QVTIPKDLAG
410 420 430 440 450
SIIGKGGQRI KQIRHESGAS IKIDEPLEGS EDRIITITGT QDQIQNAQYL
460
LQNSVKQYSG KFF
Length:463
Mass (Da):50,976
Last modified:June 7, 2004 - v1
Checksum:i0F70EE169B2A064A
GO
Isoform 2 (identifier: P61978-2) [UniParc] [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     459-463: SGKFF → ADVEGF

Show »
Length:464
Mass (Da):51,028
Checksum:i0B4EC22FE4534A06
GO
Isoform 3 (identifier: P61978-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     111-134: Missing.
     459-463: SGKFF → ADVEGF

Note: No experimental confirmation available.
Show »
Length:440
Mass (Da):48,562
Checksum:iC98A78A7462BF776
GO

Sequence cautioni

The sequence BAD92799 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti32A → D in CAA51267 (PubMed:8107114).Curated1

Mass spectrometryi

Isoform 1 : Molecular mass is 50976.25 Da from positions 1 - 463. Determined by MALDI. 1 Publication

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_021669111 – 134Missing in isoform 3. 1 PublicationAdd BLAST24
Alternative sequenceiVSP_002822459 – 463SGKFF → ADVEGF in isoform 2 and isoform 3. 2 Publications5

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S74678 mRNA. Translation: AAB20770.1.
X72727 mRNA. Translation: CAA51267.1.
AB209562 mRNA. Translation: BAD92799.1. Different initiation.
AL354733 Genomic DNA. Translation: CAI16020.1.
CH471089 Genomic DNA. Translation: EAW62675.1.
BC000355 mRNA. Translation: AAH00355.1.
BC014980 mRNA. Translation: AAH14980.1.
CCDSiCCDS6667.1.
CCDS6668.1. [P61978-2]
PIRiS43363.
RefSeqiNP_001305115.1. NM_001318186.1.
NP_001305116.1. NM_001318187.1. [P61978-3]
NP_001305117.1. NM_001318188.1. [P61978-1]
NP_002131.2. NM_002140.4. [P61978-2]
NP_112552.1. NM_031262.3. [P61978-1]
NP_112553.1. NM_031263.3. [P61978-2]
XP_005252017.1. XM_005251960.2. [P61978-2]
XP_005252020.1. XM_005251963.3. [P61978-3]
XP_005252022.1. XM_005251965.2. [P61978-3]
XP_016870157.1. XM_017014668.1. [P61978-1]
UniGeneiHs.522257.

Genome annotation databases

EnsembliENST00000351839; ENSP00000317788; ENSG00000165119. [P61978-1]
ENST00000360384; ENSP00000353552; ENSG00000165119. [P61978-1]
ENST00000376263; ENSP00000365439; ENSG00000165119. [P61978-2]
ENST00000376281; ENSP00000365458; ENSG00000165119. [P61978-2]
GeneIDi3190.
KEGGihsa:3190.
UCSCiuc004ang.5. human.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S74678 mRNA. Translation: AAB20770.1.
X72727 mRNA. Translation: CAA51267.1.
AB209562 mRNA. Translation: BAD92799.1. Different initiation.
AL354733 Genomic DNA. Translation: CAI16020.1.
CH471089 Genomic DNA. Translation: EAW62675.1.
BC000355 mRNA. Translation: AAH00355.1.
BC014980 mRNA. Translation: AAH14980.1.
CCDSiCCDS6667.1.
CCDS6668.1. [P61978-2]
PIRiS43363.
RefSeqiNP_001305115.1. NM_001318186.1.
NP_001305116.1. NM_001318187.1. [P61978-3]
NP_001305117.1. NM_001318188.1. [P61978-1]
NP_002131.2. NM_002140.4. [P61978-2]
NP_112552.1. NM_031262.3. [P61978-1]
NP_112553.1. NM_031263.3. [P61978-2]
XP_005252017.1. XM_005251960.2. [P61978-2]
XP_005252020.1. XM_005251963.3. [P61978-3]
XP_005252022.1. XM_005251965.2. [P61978-3]
XP_016870157.1. XM_017014668.1. [P61978-1]
UniGeneiHs.522257.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1J5KNMR-A379-463[»]
1KHMNMR-A379-463[»]
1ZZIX-ray1.80A/B385-463[»]
1ZZJX-ray2.30A/B/C385-463[»]
1ZZKX-ray0.95A385-463[»]
ProteinModelPortaliP61978.
SMRiP61978.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109431. 267 interactors.
DIPiDIP-31805N.
IntActiP61978. 161 interactors.
MINTiMINT-225422.
STRINGi9606.ENSP00000365439.

PTM databases

iPTMnetiP61978.
PhosphoSitePlusiP61978.
SwissPalmiP61978.

Polymorphism and mutation databases

BioMutaiHNRNPK.
DMDMi48429103.

2D gel databases

SWISS-2DPAGEP61978.

Proteomic databases

MaxQBiP61978.
PaxDbiP61978.
PeptideAtlasiP61978.
PRIDEiP61978.
TopDownProteomicsiP61978-1. [P61978-1]

Protocols and materials databases

DNASUi3190.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000351839; ENSP00000317788; ENSG00000165119. [P61978-1]
ENST00000360384; ENSP00000353552; ENSG00000165119. [P61978-1]
ENST00000376263; ENSP00000365439; ENSG00000165119. [P61978-2]
ENST00000376281; ENSP00000365458; ENSG00000165119. [P61978-2]
GeneIDi3190.
KEGGihsa:3190.
UCSCiuc004ang.5. human.

Organism-specific databases

CTDi3190.
DisGeNETi3190.
GeneCardsiHNRNPK.
HGNCiHGNC:5044. HNRNPK.
HPAiCAB004435.
CAB016225.
HPA007644.
HPA044105.
MIMi600712. gene.
616580. phenotype.
neXtProtiNX_P61978.
OpenTargetsiENSG00000165119.
PharmGKBiPA162391350.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2192. Eukaryota.
ENOG4111GSB. LUCA.
GeneTreeiENSGT00760000119144.
HOVERGENiHBG051916.
InParanoidiP61978.
KOiK12886.
OMAiKALRTDX.
PhylomeDBiP61978.
TreeFamiTF316335.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000165119-MONOMER.
ReactomeiR-HSA-4570464. SUMOylation of RNA binding proteins.
R-HSA-72163. mRNA Splicing - Major Pathway.
R-HSA-72203. Processing of Capped Intron-Containing Pre-mRNA.
SIGNORiP61978.

Miscellaneous databases

ChiTaRSiHNRNPK. human.
EvolutionaryTraceiP61978.
GeneWikiiHNRPK.
GenomeRNAii3190.
PMAP-CutDBP61978.
PROiP61978.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000165119.
CleanExiHS_HNRNPK.
ExpressionAtlasiP61978. baseline and differential.
GenevisibleiP61978. HS.

Family and domain databases

Gene3Di3.30.1370.10. 3 hits.
InterProiIPR033090. hnRNP_K.
IPR004087. KH_dom.
IPR004088. KH_dom_type_1.
IPR012987. ROK_N.
[Graphical view]
PANTHERiPTHR10288:SF167. PTHR10288:SF167. 1 hit.
PfamiPF00013. KH_1. 3 hits.
PF08067. ROKNT. 1 hit.
[Graphical view]
SMARTiSM00322. KH. 3 hits.
[Graphical view]
SUPFAMiSSF54791. SSF54791. 3 hits.
PROSITEiPS50084. KH_TYPE_1. 3 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiHNRPK_HUMAN
AccessioniPrimary (citable) accession number: P61978
Secondary accession number(s): Q07244
, Q15671, Q59F98, Q5T6W4, Q60577, Q922Y7, Q96J62
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: June 7, 2004
Last modified: November 30, 2016
This is version 165 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 9
    Human chromosome 9: 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.