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Protein

Lysine-rich nucleolar protein 1

Gene

KNOP1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

  • poly(A) RNA binding Source: UniProtKB
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Lysine-rich nucleolar protein 1
Alternative name(s):
Protein FAM191A
Testis-specific gene 118 protein
Gene namesi
Name:KNOP1
Synonyms:C16orf88, FAM191A, TSG118
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 16

Organism-specific databases

HGNCiHGNC:34404. KNOP1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162378471.

Polymorphism and mutation databases

BioMutaiKNOP1.
DMDMi121940661.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 458458Lysine-rich nucleolar protein 1PRO_0000321938Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei42 – 421PhosphoserineCombined sources
Modified residuei50 – 501PhosphoserineCombined sources
Modified residuei111 – 1111PhosphoserineCombined sources
Modified residuei265 – 2651PhosphoserineCombined sources
Cross-linki275 – 275Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei308 – 3081PhosphothreonineCombined sources
Modified residuei310 – 3101PhosphothreonineCombined sources
Cross-linki373 – 373Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki407 – 407Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ1ED39.
MaxQBiQ1ED39.
PaxDbiQ1ED39.
PeptideAtlasiQ1ED39.
PRIDEiQ1ED39.

PTM databases

iPTMnetiQ1ED39.
PhosphoSiteiQ1ED39.

Expressioni

Gene expression databases

BgeeiQ1ED39.
CleanExiHS_C16orf88.
ExpressionAtlasiQ1ED39. baseline and differential.
GenevisibleiQ1ED39. HS.

Organism-specific databases

HPAiHPA040848.
HPA041079.

Interactioni

Subunit structurei

Interacts with ZNF106.By similarity

Protein-protein interaction databases

BioGridi134613. 59 interactions.
IntActiQ1ED39. 3 interactions.
MINTiMINT-4992993.
STRINGi9606.ENSP00000219837.

Structurei

3D structure databases

ProteinModelPortaliQ1ED39.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni306 – 458153Interaction with ZNF106By similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi15 – 206Poly-Lys
Compositional biasi65 – 295231Lys-richAdd
BLAST

Phylogenomic databases

eggNOGiENOG410IVRA. Eukaryota.
ENOG41120AA. LUCA.
GeneTreeiENSGT00500000044955.
HOGENOMiHOG000111906.
HOVERGENiHBG107751.
InParanoidiQ1ED39.
OMAiPDPRQGE.
OrthoDBiEOG73NG3T.
PhylomeDBiQ1ED39.
TreeFamiTF336149.

Family and domain databases

InterProiIPR028125. KNOP1.
IPR028124. SMAP_dom.
[Graphical view]
PANTHERiPTHR22426. PTHR22426. 1 hit.
PfamiPF15477. SMAP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q1ED39-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MITKTHKVDL GLPEKKKKKK VVKEPETRYS VLNNDDYFAD VSPLRATSPS
60 70 80 90 100
KSVAHGQAPE MPLVKKKKKK KKGVSTLCEE HVEPETTLPA RRTEKSPSLR
110 120 130 140 150
KQVFGHLEFL SGEKKNKKSP LAMSHASGVK TSPDPRQGEE ETRVGKKLKK
160 170 180 190 200
HKKEKKGAQD PTAFSVQDPW FCEAREARDV GDTCSVGKKD EEQAALGQKR
210 220 230 240 250
KRKSPREHNG KVKKKKKIHQ EGDALPGHSK PSRSMESSPR KGSKKKPVKV
260 270 280 290 300
EAPEYIPISD DPKASAKKKM KSKKKVEQPV IEEPALKRKK KKKRKESGVA
310 320 330 340 350
GDPWKEETDT DLEVVLEKKG NMDEAHIDQV RRKALQEEID RESGKTEASE
360 370 380 390 400
TRKWTGTQFG QWDTAGFENE DQKLKFLRLM GGFKNLSPSF SRPASTIARP
410 420 430 440 450
NMALGKKAAD SLQQNLQRDY DRAMSWKYSR GAGLGFSTAP NKIFYIDRNA

SKSVKLED
Length:458
Mass (Da):51,589
Last modified:July 11, 2006 - v1
Checksum:iF3935374029D61D9
GO

Sequence cautioni

The sequence AAC05805.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAH89430.1 differs from that shown.Contaminating sequence. Potential poly-A sequence.Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti28 – 281R → Q.
Corresponds to variant rs11640454 [ dbSNP | Ensembl ].
VAR_061716
Natural varianti266 – 2661A → V.
Corresponds to variant rs2074036 [ dbSNP | Ensembl ].
VAR_039387
Natural varianti276 – 2761V → A.
Corresponds to variant rs28424569 [ dbSNP | Ensembl ].
VAR_061717

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC002550 Genomic DNA. Translation: AAC05805.1. Different initiation.
BC089430 mRNA. Translation: AAH89430.1. Sequence problems.
BC117562 mRNA. Translation: AAI17563.1.
CCDSiCCDS42127.1.
RefSeqiNP_001013009.2. NM_001012991.2.
XP_005255374.1. XM_005255317.3.
XP_006721109.1. XM_006721046.2.
UniGeneiHs.585209.

Genome annotation databases

EnsembliENST00000219837; ENSP00000219837; ENSG00000103550.
GeneIDi400506.
KEGGihsa:400506.
UCSCiuc002dgq.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC002550 Genomic DNA. Translation: AAC05805.1. Different initiation.
BC089430 mRNA. Translation: AAH89430.1. Sequence problems.
BC117562 mRNA. Translation: AAI17563.1.
CCDSiCCDS42127.1.
RefSeqiNP_001013009.2. NM_001012991.2.
XP_005255374.1. XM_005255317.3.
XP_006721109.1. XM_006721046.2.
UniGeneiHs.585209.

3D structure databases

ProteinModelPortaliQ1ED39.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi134613. 59 interactions.
IntActiQ1ED39. 3 interactions.
MINTiMINT-4992993.
STRINGi9606.ENSP00000219837.

PTM databases

iPTMnetiQ1ED39.
PhosphoSiteiQ1ED39.

Polymorphism and mutation databases

BioMutaiKNOP1.
DMDMi121940661.

Proteomic databases

EPDiQ1ED39.
MaxQBiQ1ED39.
PaxDbiQ1ED39.
PeptideAtlasiQ1ED39.
PRIDEiQ1ED39.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000219837; ENSP00000219837; ENSG00000103550.
GeneIDi400506.
KEGGihsa:400506.
UCSCiuc002dgq.4. human.

Organism-specific databases

CTDi400506.
GeneCardsiKNOP1.
H-InvDBHIX0037256.
HIX0038620.
HGNCiHGNC:34404. KNOP1.
HPAiHPA040848.
HPA041079.
neXtProtiNX_Q1ED39.
PharmGKBiPA162378471.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IVRA. Eukaryota.
ENOG41120AA. LUCA.
GeneTreeiENSGT00500000044955.
HOGENOMiHOG000111906.
HOVERGENiHBG107751.
InParanoidiQ1ED39.
OMAiPDPRQGE.
OrthoDBiEOG73NG3T.
PhylomeDBiQ1ED39.
TreeFamiTF336149.

Miscellaneous databases

ChiTaRSiKNOP1. human.
GenomeRNAii400506.
PROiQ1ED39.

Gene expression databases

BgeeiQ1ED39.
CleanExiHS_C16orf88.
ExpressionAtlasiQ1ED39. baseline and differential.
GenevisibleiQ1ED39. HS.

Family and domain databases

InterProiIPR028125. KNOP1.
IPR028124. SMAP_dom.
[Graphical view]
PANTHERiPTHR22426. PTHR22426. 1 hit.
PfamiPF15477. SMAP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Embryonic stem cell and Lymph.
  3. "Quantitative phosphoproteome profiling of Wnt3a-mediated signaling network: indicating the involvement of ribonucleoside-diphosphate reductase M2 subunit phosphorylation at residue serine 20 in canonical Wnt signal transduction."
    Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S., Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.
    Mol. Cell. Proteomics 6:1952-1967(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42; SER-50; SER-265; THR-308 AND THR-310, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  5. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42 AND SER-111, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  9. "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: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-275 AND LYS-407, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "SUMO-2 orchestrates chromatin modifiers in response to DNA damage."
    Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V., Vertegaal A.C.
    Cell Rep. 10:1778-1791(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-373, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiKNOP1_HUMAN
AccessioniPrimary (citable) accession number: Q1ED39
Secondary accession number(s): O43328, Q5FWF3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: July 11, 2006
Last modified: June 8, 2016
This is version 84 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations

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.