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Protein
Submitted name:

Heterogeneous nuclear ribonucleoprotein K

Gene

HNRNPK

Organism
Homo sapiens (Human)
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Names & Taxonomyi

Protein namesi
Submitted name:
Heterogeneous nuclear ribonucleoprotein KImported
Gene namesi
Name:HNRNPKImported
OrganismiHomo sapiens (Human)Imported
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:5044. HNRNPK.

PTM / Processingi

Proteomic databases

EPDiQ5T6W2.
PRIDEiQ5T6W2.

Expressioni

Gene expression databases

BgeeiQ5T6W2.
ExpressionAtlasiQ5T6W2. baseline and differential.

Structurei

3D structure databases

ProteinModelPortaliQ5T6W2.
SMRiQ5T6W2. Positions 40-193, 351-379.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini42 – 10463KHInterPro annotationAdd
BLAST
Domaini120 – 18566KHInterPro annotationAdd
BLAST

Sequence similaritiesi

Contains 2 KH domains.UniRule annotation

Phylogenomic databases

GeneTreeiENSGT00760000119144.
HOGENOMiHOG000019764.
HOVERGENiHBG051916.

Family and domain databases

Gene3Di3.30.1370.10. 2 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. 2 hits.
PF08067. ROKNT. 1 hit.
[Graphical view]
SMARTiSM00322. KH. 2 hits.
[Graphical view]
SUPFAMiSSF54791. SSF54791. 2 hits.
PROSITEiPS50084. KH_TYPE_1. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Fragment.

Q5T6W2-1 [UniParc]FASTAAdd to basket

« 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 YQHYKGSDFD CELRLLIHQS LAGGIIGVKG AKIKELRENT
160 170 180 190 200
QTTIKLFQEC CPHSTDRVVL IGGKPDRVVE CIKIILDLIS ESPIKGRAQP
210 220 230 240 250
YDPNFYDETY DYGGFTMMFD DRRGRPVGFP MRGRGGFDRM PPGRGGRPMP
260 270 280 290 300
PSRRDYDDMS PRRGPPPPPP GRGGRGGSRA RNLPLPPPPP PRGGDLMAYD
310 320 330 340 350
RRGRPGDRYD GMVGFSADET WDSAIDTWSP SEWQMAYEPQ GGSGYDYSYA
360 370
GGRGSYGDLG GPIITTQVTI PKDLAGSII
Length:379
Mass (Da):41,807
Last modified:December 21, 2004 - v1
Checksum:i74D8BFDA2281FE91
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei379 – 3791Imported

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL354733 Genomic DNA. No translation available.

Genome annotation databases

EnsembliENST00000457156; ENSP00000409456; ENSG00000165119.
UCSCiuc064uak.1. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL354733 Genomic DNA. No translation available.

3D structure databases

ProteinModelPortaliQ5T6W2.
SMRiQ5T6W2. Positions 40-193, 351-379.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

EPDiQ5T6W2.
PRIDEiQ5T6W2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000457156; ENSP00000409456; ENSG00000165119.
UCSCiuc064uak.1. human.

Organism-specific databases

HGNCiHGNC:5044. HNRNPK.
GenAtlasiSearch...

Phylogenomic databases

GeneTreeiENSGT00760000119144.
HOGENOMiHOG000019764.
HOVERGENiHBG051916.

Miscellaneous databases

ChiTaRSiHNRNPK. human.

Gene expression databases

BgeeiQ5T6W2.
ExpressionAtlasiQ5T6W2. baseline and differential.

Family and domain databases

Gene3Di3.30.1370.10. 2 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. 2 hits.
PF08067. ROKNT. 1 hit.
[Graphical view]
SMARTiSM00322. KH. 2 hits.
[Graphical view]
SUPFAMiSSF54791. SSF54791. 2 hits.
PROSITEiPS50084. KH_TYPE_1. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "DNA sequence and analysis of human chromosome 9."
    Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
    , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
    Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  2. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  3. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  4. "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
    Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
    J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  5. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. Ensembl
    Submitted (JUL-2011) to UniProtKB
    Cited for: IDENTIFICATION.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "Uncovering global SUMOylation signaling networks in a site-specific manner."
    Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M., Vertegaal A.C.
    Nat. Struct. Mol. Biol. 21:927-936(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "N-terminome analysis of the human mitochondrial proteome."
    Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.
    Proteomics 15:2519-2524(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiQ5T6W2_HUMAN
AccessioniPrimary (citable) accession number: Q5T6W2
Entry historyi
Integrated into UniProtKB/TrEMBL: December 21, 2004
Last sequence update: December 21, 2004
Last modified: May 11, 2016
This is version 86 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)
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

Caution

The sequence shown here is derived from an Ensembl automatic analysis pipeline and should be considered as preliminary data.Imported

Keywords - Technical termi

Complete proteome, Proteomics identificationCombined sources, Reference proteomeImported

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.