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Protein

Uncharacterized protein C1orf198

Gene

C1orf198

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

Names & Taxonomyi

Protein namesi
Recommended name:
Uncharacterized protein C1orf198
Gene namesi
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:25900. C1orf198.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA143485319.

Polymorphism and mutation databases

BioMutaiC1orf198.
DMDMi74752632.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources1 Publication
Chaini2 – 327326Uncharacterized protein C1orf198PRO_0000280342Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineCombined sources1 Publication
Modified residuei37 – 371PhosphoserineCombined sources
Modified residuei129 – 1291PhosphoserineBy similarity
Modified residuei175 – 1751PhosphoserineCombined sources
Modified residuei289 – 2891PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9H425.
MaxQBiQ9H425.
PaxDbiQ9H425.
PeptideAtlasiQ9H425.
PRIDEiQ9H425.

PTM databases

iPTMnetiQ9H425.
PhosphoSiteiQ9H425.

Expressioni

Gene expression databases

BgeeiQ9H425.
CleanExiHS_C1orf198.
ExpressionAtlasiQ9H425. baseline and differential.
GenevisibleiQ9H425. HS.

Organism-specific databases

HPAiHPA004798.

Interactioni

Protein-protein interaction databases

BioGridi124327. 14 interactions.
IntActiQ9H425. 7 interactions.
STRINGi9606.ENSP00000355623.

Structurei

3D structure databases

ProteinModelPortaliQ9H425.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Phylogenomic databases

eggNOGiENOG410IQUY. Eukaryota.
ENOG4111F2J. LUCA.
GeneTreeiENSGT00390000018361.
HOGENOMiHOG000013173.
HOVERGENiHBG080980.
InParanoidiQ9H425.
OMAiRCLVGPR.
OrthoDBiEOG7D59QP.
PhylomeDBiQ9H425.
TreeFamiTF334642.

Family and domain databases

InterProiIPR031600. DUF4706.
[Graphical view]
PfamiPF15797. DUF4706. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

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

Isoform 1 (identifier: Q9H425-1) [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
MASMAAAIAA SRSAVMSGNR PLDDRERKRF TYFSSLSPMA RKIMQDKEKI
60 70 80 90 100
REKYGPEWAR LPPAQQDEII DRCLVGPRAP APRDPGDSEE LTRFPGLRGP
110 120 130 140 150
TGQKVVRFGD EDLTWQDEHS APFSWETKSQ MEFSISALSI QEPSNGTAAS
160 170 180 190 200
EPRPLSKASQ GSQALKSSQG SRSSSLDALG PTRKEEEASF WKINAERSRG
210 220 230 240 250
EGPEAEFQSL TPSQIKSMEK GEKVLPPCYR QEPAPKDREA KVERPSTLRQ
260 270 280 290 300
EQRPLPNVST ERERPQPVQA FSSALHEAAP SQLEGKLPSP DVRQDDGEDT
310 320
LFSEPKFAQV SSSNVVLKTG FDFLDNW
Length:327
Mass (Da):36,346
Last modified:March 1, 2001 - v1
Checksum:i769AFAB47FE287C4
GO
Isoform 2 (identifier: Q9H425-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-130: Missing.

Show »
Length:197
Mass (Da):21,657
Checksum:i7B74BC2D70AC50D7
GO
Isoform 3 (identifier: Q9H425-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-38: Missing.

Note: No experimental confirmation available.
Show »
Length:289
Mass (Da):32,215
Checksum:iCBC03D53C1807240
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti163 – 1631Q → L in BAG53223 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti274 – 2741A → S.
Corresponds to variant rs34864456 [ dbSNP | Ensembl ].
VAR_050707
Natural varianti306 – 3061K → R.
Corresponds to variant rs35115679 [ dbSNP | Ensembl ].
VAR_050708

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 130130Missing in isoform 2. 1 PublicationVSP_044252Add
BLAST
Alternative sequencei1 – 3838Missing in isoform 3. 1 PublicationVSP_046926Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK027431 mRNA. Translation: BAB55105.1.
AK096166 mRNA. Translation: BAG53223.1.
AK292433 mRNA. Translation: BAF85122.1.
AL118511 Genomic DNA. No translation available.
CH471098 Genomic DNA. Translation: EAW69926.1.
BC066649 mRNA. Translation: AAH66649.1.
CCDSiCCDS1587.1. [Q9H425-1]
CCDS44330.1. [Q9H425-3]
CCDS44331.1. [Q9H425-2]
RefSeqiNP_001129966.1. NM_001136494.1. [Q9H425-3]
NP_001129967.1. NM_001136495.1. [Q9H425-2]
NP_116189.1. NM_032800.2. [Q9H425-1]
UniGeneiHs.520494.

Genome annotation databases

EnsembliENST00000366663; ENSP00000355623; ENSG00000119280. [Q9H425-1]
ENST00000470540; ENSP00000428172; ENSG00000119280. [Q9H425-3]
ENST00000523410; ENSP00000430967; ENSG00000119280. [Q9H425-2]
GeneIDi84886.
KEGGihsa:84886.
UCSCiuc001hub.4. human. [Q9H425-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK027431 mRNA. Translation: BAB55105.1.
AK096166 mRNA. Translation: BAG53223.1.
AK292433 mRNA. Translation: BAF85122.1.
AL118511 Genomic DNA. No translation available.
CH471098 Genomic DNA. Translation: EAW69926.1.
BC066649 mRNA. Translation: AAH66649.1.
CCDSiCCDS1587.1. [Q9H425-1]
CCDS44330.1. [Q9H425-3]
CCDS44331.1. [Q9H425-2]
RefSeqiNP_001129966.1. NM_001136494.1. [Q9H425-3]
NP_001129967.1. NM_001136495.1. [Q9H425-2]
NP_116189.1. NM_032800.2. [Q9H425-1]
UniGeneiHs.520494.

3D structure databases

ProteinModelPortaliQ9H425.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi124327. 14 interactions.
IntActiQ9H425. 7 interactions.
STRINGi9606.ENSP00000355623.

PTM databases

iPTMnetiQ9H425.
PhosphoSiteiQ9H425.

Polymorphism and mutation databases

BioMutaiC1orf198.
DMDMi74752632.

Proteomic databases

EPDiQ9H425.
MaxQBiQ9H425.
PaxDbiQ9H425.
PeptideAtlasiQ9H425.
PRIDEiQ9H425.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000366663; ENSP00000355623; ENSG00000119280. [Q9H425-1]
ENST00000470540; ENSP00000428172; ENSG00000119280. [Q9H425-3]
ENST00000523410; ENSP00000430967; ENSG00000119280. [Q9H425-2]
GeneIDi84886.
KEGGihsa:84886.
UCSCiuc001hub.4. human. [Q9H425-1]

Organism-specific databases

CTDi84886.
GeneCardsiC1orf198.
H-InvDBHIX0001687.
HGNCiHGNC:25900. C1orf198.
HPAiHPA004798.
neXtProtiNX_Q9H425.
PharmGKBiPA143485319.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IQUY. Eukaryota.
ENOG4111F2J. LUCA.
GeneTreeiENSGT00390000018361.
HOGENOMiHOG000013173.
HOVERGENiHBG080980.
InParanoidiQ9H425.
OMAiRCLVGPR.
OrthoDBiEOG7D59QP.
PhylomeDBiQ9H425.
TreeFamiTF334642.

Miscellaneous databases

ChiTaRSiC1orf198. human.
GenomeRNAii84886.
PROiQ9H425.

Gene expression databases

BgeeiQ9H425.
CleanExiHS_C1orf198.
ExpressionAtlasiQ9H425. baseline and differential.
GenevisibleiQ9H425. HS.

Family and domain databases

InterProiIPR031600. DUF4706.
[Graphical view]
PfamiPF15797. DUF4706. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
    Tissue: Mesangial cell and Testis.
  2. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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] (ISOFORM 1).
    Tissue: Testis.
  5. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
    Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
    Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-12, ACETYLATION AT ALA-2.
  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. "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-37, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  8. "Systematic validation of antibody binding and protein subcellular localization using siRNA and confocal microscopy."
    Stadler C., Hjelmare M., Neumann B., Jonasson K., Pepperkok R., Uhlen M., Lundberg E.
    J. Proteomics 75:2236-2251(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  9. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "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-37 AND SER-175, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma and Erythroleukemia.
  11. "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-175 AND SER-289, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiCA198_HUMAN
AccessioniPrimary (citable) accession number: Q9H425
Secondary accession number(s): A8K8R8, B3KTW1, G5EA08
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 20, 2007
Last sequence update: March 1, 2001
Last modified: July 6, 2016
This is version 99 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: 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.