Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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
  • C-rich single-stranded DNA binding Source: Ensembl
  • mRNA 3'-UTR binding Source: Ensembl
  • mRNA CDS binding Source: Ensembl
  • poly(A) RNA binding Source: UniProtKB
  • pre-mRNA 3'-splice site binding Source: Ensembl
  • ribonucleoprotein complex binding Source: Ensembl
  • 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

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

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

  • axon terminus Source: Ensembl
  • catalytic step 2 spliceosome Source: UniProtKB
  • cell-cell adherens junction Source: BHF-UCL
  • cell cortex Source: Ensembl
  • cytoplasm Source: ProtInc
  • cytosol Source: Ensembl
  • dendritic spine Source: Ensembl
  • extracellular exosome Source: UniProtKB
  • extracellular matrix Source: BHF-UCL
  • focal adhesion Source: UniProtKB
  • membrane Source: UniProtKB
  • mitochondrion Source: Ensembl
  • nuclear chromatin Source: BHF-UCL
  • nucleoplasm Source: Reactome
  • nucleus Source: ProtInc
  • podosome Source: UniProtKB-SubCell
  • postsynaptic density Source: Ensembl
  • protein-DNA complex Source: Ensembl
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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi422 – 4221K → R: Loss of sumoylation. Loss of TP53 transcriptional stimulation. 1 Publication
Mutagenesisi424 – 4241D → A: Loss of sumoylation. 1 Publication

Keywords - Diseasei

Mental retardation

Organism-specific databases

MIMi616580. phenotype.
PharmGKBiPA162391350.

Polymorphism and mutation databases

BioMutaiHNRNPK.
DMDMi48429103.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 463463Heterogeneous nuclear ribonucleoprotein KPRO_0000050096Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineCombined sources1 Publication
Modified residuei34 – 341N6-acetyllysine; alternateBy similarity
Cross-linki34 – 34Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateCombined sources
Cross-linki34 – 34Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residuei36 – 361PhosphoserineCombined sources
Modified residuei39 – 391PhosphothreonineBy similarity
Modified residuei75 – 751PhosphoserineCombined sources
Modified residuei116 – 1161PhosphoserineCombined sources
Cross-linki163 – 163Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Combined sources
Modified residuei198 – 1981N6-acetyllysineBy similarity
Modified residuei214 – 2141PhosphoserineCombined sources
Modified residuei216 – 2161PhosphoserineCombined sources
Modified residuei219 – 2191N6-succinyllysineBy similarity
Modified residuei284 – 2841PhosphoserineCombined sources1 Publication
Modified residuei379 – 3791PhosphoserineCombined sources
Modified residuei380 – 3801PhosphotyrosineCombined sources
Modified residuei405 – 4051N6-acetyllysine; alternateBy similarity
Cross-linki405 – 405Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residuei420 – 4201PhosphoserineCombined sources
Cross-linki422 – 422Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate
Cross-linki422 – 422Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateCombined sources
Cross-linki422 – 422Glycyl 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, Phosphoprotein, Ubl conjugation

Proteomic databases

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

2D gel databases

SWISS-2DPAGEP61978.

PTM databases

iPTMnetiP61978.
PhosphoSiteiP61978.
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
PRR3P795223EBI-304185,EBI-2803328
QKIQ96PU83EBI-304185,EBI-945792
RASD1Q9Y2723EBI-304185,EBI-740818
RBM3P981793EBI-304185,EBI-2949699
RBMXP381596EBI-304185,EBI-743526
SPG7Q9UQ903EBI-304185,EBI-717201
SRCP129316EBI-304185,EBI-621482
TERF2IPQ9NYB02EBI-304185,EBI-750109
TP53P046372EBI-304185,EBI-366083
TP63Q9H3D42EBI-304185,EBI-2337775
ZNF385CQ66K413EBI-304185,EBI-10219231
ZNF792Q3KQV33EBI-304185,EBI-10240849

GO - Molecular functioni

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

Protein-protein interaction databases

BioGridi109431. 267 interactions.
DIPiDIP-31805N.
IntActiP61978. 131 interactions.
MINTiMINT-225422.
STRINGi9606.ENSP00000365439.

Structurei

Secondary structure

1
463
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi381 – 3844Combined sources
Beta strandi388 – 3958Combined sources
Turni396 – 3983Combined sources
Helixi399 – 4024Combined sources
Helixi405 – 4073Combined sources
Helixi408 – 41710Combined sources
Beta strandi420 – 4234Combined sources
Beta strandi430 – 43910Combined sources
Helixi441 – 45919Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 45-216, 385-463.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP61978.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini42 – 10463KH 1PROSITE-ProRule annotationAdd
BLAST
Repeati54 – 76231-1Add
BLAST
Repeati59 – 6243-1
Domaini144 – 20966KH 2PROSITE-ProRule annotationAdd
BLAST
Repeati245 – 25062-1
Repeati257 – 26043-2
Repeati267 – 27043-3
Repeati295 – 29843-4
Repeati324 – 32962-2
Domaini387 – 45165KH 3PROSITE-ProRule annotationAdd
BLAST
Repeati399 – 421231-2Add
BLAST
Repeati404 – 40743-5

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 276276Necessary for interaction with DDX1Add
BLAST
Regioni35 – 197163Interaction with ASFV p30Add
BLAST
Regioni54 – 4213682 X 22 AA approximate repeatsAdd
BLAST
Regioni59 – 4073495 X 4 AA repeats of G-X-G-GAdd
BLAST
Regioni209 – 337129Interaction with ZIK1By similarityAdd
BLAST
Regioni236 – 27338RNA-binding RGG-boxAdd
BLAST
Regioni245 – 329852 X 6 AA approximate repeatsAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi289 – 2946Poly-Pro
Compositional biasi310 – 3156Poly-Pro

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti32 – 321A → D in CAA51267 (PubMed:8107114).Curated

Mass spectrometryi

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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei111 – 13424Missing in isoform 3. 1 PublicationVSP_021669Add
BLAST
Alternative sequencei459 – 4635SGKFF → ADVEGF in isoform 2 and isoform 3. 2 PublicationsVSP_002822

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]
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]
UniGeneiHs.522257.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 45-216, 385-463.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109431. 267 interactions.
DIPiDIP-31805N.
IntActiP61978. 131 interactions.
MINTiMINT-225422.
STRINGi9606.ENSP00000365439.

PTM databases

iPTMnetiP61978.
PhosphoSiteiP61978.
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.
GeneCardsiHNRNPK.
HGNCiHGNC:5044. HNRNPK.
HPAiCAB004435.
CAB016225.
HPA007644.
HPA044105.
MIMi600712. gene.
616580. phenotype.
neXtProtiNX_P61978.
PharmGKBiPA162391350.
GenAtlasiSearch...

Phylogenomic databases

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

Enzyme and pathway databases

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: September 7, 2016
This is version 162 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.