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Protein

Uncharacterized protein C11orf84

Gene

C11orf84

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Names & Taxonomyi

Protein namesi
Recommended name:
Uncharacterized protein C11orf84
Gene namesi
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:25115. C11orf84.

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162377769.

Polymorphism and mutation databases

BioMutaiC11orf84.
DMDMi74733196.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 381381Uncharacterized protein C11orf84PRO_0000321528Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei121 – 1211PhosphoserineCombined sources
Modified residuei148 – 1481PhosphoserineCombined sources
Cross-linki220 – 220Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei248 – 2481PhosphoserineCombined sources
Modified residuei251 – 2511PhosphoserineCombined sources
Cross-linki290 – 290Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei308 – 3081PhosphoserineCombined sources1 Publication
Modified residuei310 – 3101PhosphoserineCombined sources
Cross-linki374 – 374Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ9BUA3.
MaxQBiQ9BUA3.
PaxDbiQ9BUA3.
PeptideAtlasiQ9BUA3.
PRIDEiQ9BUA3.

PTM databases

iPTMnetiQ9BUA3.
PhosphoSiteiQ9BUA3.

Expressioni

Gene expression databases

BgeeiQ9BUA3.
CleanExiHS_C11orf84.
ExpressionAtlasiQ9BUA3. baseline and differential.
GenevisibleiQ9BUA3. HS.

Organism-specific databases

HPAiHPA040128.
HPA050313.

Interactioni

Protein-protein interaction databases

BioGridi126827. 13 interactions.
IntActiQ9BUA3. 2 interactions.
STRINGi9606.ENSP00000294244.

Structurei

3D structure databases

ProteinModelPortaliQ9BUA3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi147 – 252106Pro-richAdd
BLAST

Phylogenomic databases

eggNOGiENOG410IS1G. Eukaryota.
ENOG4111DW1. LUCA.
GeneTreeiENSGT00410000025985.
HOGENOMiHOG000111741.
HOVERGENiHBG094884.
InParanoidiQ9BUA3.
OMAiLQDWSKH.
OrthoDBiEOG7MWGXB.
PhylomeDBiQ9BUA3.
TreeFamiTF337165.

Sequencei

Sequence statusi: Complete.

Q9BUA3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALKAEGAAL DCFEVTLKCE EGEDEEEAMV VAVIPRPEPM LRVTQQEKTP
60 70 80 90 100
PPRPSPLEAG SDGCEEPKQQ VSWEQEFLVG SSPGGSGRAL CMVCGAEIRA
110 120 130 140 150
PSADTARSHI LEQHPHTLDL SPSEKSNILE AWSEGVALLQ DVRAEQPSPP
160 170 180 190 200
NSDSGQDAHP DPDANPDAAR MPAEIVVLLD SEDNPSLPKR SRPRGLRPLE
210 220 230 240 250
LPAVPATEPG NKKPRGQRWK EPPGEEPVRK KRGRPMTKNL DPDPEPPSPD
260 270 280 290 300
SPTETFAAPA EVRHFTDGSF PAGFVLQLFS HTQLRGPDSK DSPKDREVAE
310 320 330 340 350
GGLPRAESPS PAPPPGLRGT LDLQVIRVRM EEPPAVSLLQ DWSRHPQGTK
360 370 380
RVGAGDTSDW PTVLSESSTT VAGKPEKGNG V
Length:381
Mass (Da):41,037
Last modified:November 23, 2004 - v3
Checksum:iDC8AB56B1B224D73
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti58 – 581E → Q.
Corresponds to variant rs35875163 [ dbSNP | Ensembl ].
VAR_061607

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CH471076 Genomic DNA. Translation: EAW74172.1.
BC002782 mRNA. Translation: AAH02782.3.
BC007540 mRNA. Translation: AAH07540.2.
BC056402 mRNA. Translation: AAH56402.1.
CR749697 mRNA. Translation: CAH18477.1.
CCDSiCCDS31594.1.
RefSeqiNP_612480.1. NM_138471.2.
UniGeneiHs.502793.

Genome annotation databases

EnsembliENST00000294244; ENSP00000294244; ENSG00000168005.
GeneIDi144097.
KEGGihsa:144097.
UCSCiuc001nxt.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CH471076 Genomic DNA. Translation: EAW74172.1.
BC002782 mRNA. Translation: AAH02782.3.
BC007540 mRNA. Translation: AAH07540.2.
BC056402 mRNA. Translation: AAH56402.1.
CR749697 mRNA. Translation: CAH18477.1.
CCDSiCCDS31594.1.
RefSeqiNP_612480.1. NM_138471.2.
UniGeneiHs.502793.

3D structure databases

ProteinModelPortaliQ9BUA3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi126827. 13 interactions.
IntActiQ9BUA3. 2 interactions.
STRINGi9606.ENSP00000294244.

PTM databases

iPTMnetiQ9BUA3.
PhosphoSiteiQ9BUA3.

Polymorphism and mutation databases

BioMutaiC11orf84.
DMDMi74733196.

Proteomic databases

EPDiQ9BUA3.
MaxQBiQ9BUA3.
PaxDbiQ9BUA3.
PeptideAtlasiQ9BUA3.
PRIDEiQ9BUA3.

Protocols and materials databases

DNASUi144097.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000294244; ENSP00000294244; ENSG00000168005.
GeneIDi144097.
KEGGihsa:144097.
UCSCiuc001nxt.4. human.

Organism-specific databases

CTDi144097.
GeneCardsiC11orf84.
H-InvDBHIX0201633.
HGNCiHGNC:25115. C11orf84.
HPAiHPA040128.
HPA050313.
neXtProtiNX_Q9BUA3.
PharmGKBiPA162377769.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IS1G. Eukaryota.
ENOG4111DW1. LUCA.
GeneTreeiENSGT00410000025985.
HOGENOMiHOG000111741.
HOVERGENiHBG094884.
InParanoidiQ9BUA3.
OMAiLQDWSKH.
OrthoDBiEOG7MWGXB.
PhylomeDBiQ9BUA3.
TreeFamiTF337165.

Miscellaneous databases

ChiTaRSiC11orf84. human.
GenomeRNAii144097.
PROiQ9BUA3.

Gene expression databases

BgeeiQ9BUA3.
CleanExiHS_C11orf84.
ExpressionAtlasiQ9BUA3. baseline and differential.
GenevisibleiQ9BUA3. HS.

Family and domain databases

ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: Brain and Uterus.
  3. Bienvenut W.V., Calvo F., Matallanas D., Cooper W.N., Zebisch A., Kolch W.
    Submitted (DEC-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 108-143; 171-190; 195-212 AND 295-344, PHOSPHORYLATION AT SER-308, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Cervix carcinoma, Colon carcinoma and Mammary carcinoma.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 291-381.
    Tissue: Melanoma.
  5. "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].
    Tissue: Cervix carcinoma.
  6. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
    Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
    J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-148 AND SER-308, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "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].
  9. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-148 AND SER-248, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  10. "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-308 AND SER-310, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-148 AND SER-308, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-121; SER-148; SER-248; SER-251 AND SER-308, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma and Erythroleukemia.
  13. "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-220; LYS-290 AND LYS-374, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "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-220 AND LYS-374, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "System-wide analysis of SUMOylation dynamics in response to replication stress reveals novel small ubiquitin-like modified target proteins and acceptor lysines relevant for genome stability."
    Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V., Vertegaal A.C.
    Mol. Cell. Proteomics 14:1419-1434(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-220 AND LYS-374, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiCK084_HUMAN
AccessioniPrimary (citable) accession number: Q9BUA3
Secondary accession number(s): Q68CV7, Q6PHS2, Q96IH0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: November 23, 2004
Last modified: July 6, 2016
This is version 111 of the entry and version 3 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: 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.