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Protein

Protein FAM195B

Gene

FAM195B

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:
Protein FAM195B
Gene namesi
Name:FAM195B
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:28007. FAM195B.

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA165431912.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 9797Protein FAM195BPRO_0000393954Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei21 – 211Phosphoserine2 Publications
Modified residuei24 – 241Phosphoserine1 Publication
Modified residuei41 – 411PhosphotyrosineBy similarity
Modified residuei79 – 791N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiC9JLW8.
PaxDbiC9JLW8.
PRIDEiC9JLW8.

PTM databases

PhosphoSiteiC9JLW8.

Expressioni

Gene expression databases

BgeeiC9JLW8.
ExpressionAtlasiC9JLW8. baseline and differential.

Organism-specific databases

HPAiHPA045542.

Interactioni

Protein-protein interaction databases

BioGridi131518. 2 interactions.

Structurei

3D structure databases

ProteinModelPortaliC9JLW8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the FAM195 family.Curated

Phylogenomic databases

eggNOGiNOG41066.
GeneTreeiENSGT00530000064168.
HOGENOMiHOG000035119.
InParanoidiC9JLW8.
OrthoDBiEOG7RRF8X.
PhylomeDBiC9JLW8.
TreeFamiTF326620.

Family and domain databases

InterProiIPR029428. FAM195.
[Graphical view]
PfamiPF14799. FAM195. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

C9JLW8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTSSPVSRVV YNGKRTSSPR SPPSSSEIFT PAHEENVRFI YEAWQGVERD
60 70 80 90
LRGQVPGGER GLVEEYVEKV PNPSLKTFKP IDLSDLKRRS TQDAKKS
Length:97
Mass (Da):10,920
Last modified:November 3, 2009 - v1
Checksum:iD92176E755159A81
GO

Sequence cautioni

The sequence BAC86211.1 differs from that shown. Reason: Erroneous translation. Wrong choice of CDS.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK125584 mRNA. Translation: BAC86211.1. Sequence problems.
AC174470 Genomic DNA. No translation available.
CH471099 Genomic DNA. Translation: EAW89687.1.
CCDSiCCDS45814.1.
RefSeqiNP_001087236.1. NM_001093767.2.
NP_997251.2. NM_207368.4.
UniGeneiHs.514632.

Genome annotation databases

EnsembliENST00000455127; ENSP00000409009; ENSG00000225663.
ENST00000538396; ENSP00000445543; ENSG00000225663.
ENST00000574190; ENSP00000458720; ENSG00000225663.
ENST00000576730; ENSP00000458707; ENSG00000225663.
GeneIDi348262.
KEGGihsa:348262.
UCSCiuc010wuy.1. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK125584 mRNA. Translation: BAC86211.1. Sequence problems.
AC174470 Genomic DNA. No translation available.
CH471099 Genomic DNA. Translation: EAW89687.1.
CCDSiCCDS45814.1.
RefSeqiNP_001087236.1. NM_001093767.2.
NP_997251.2. NM_207368.4.
UniGeneiHs.514632.

3D structure databases

ProteinModelPortaliC9JLW8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi131518. 2 interactions.

PTM databases

PhosphoSiteiC9JLW8.

Proteomic databases

MaxQBiC9JLW8.
PaxDbiC9JLW8.
PRIDEiC9JLW8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000455127; ENSP00000409009; ENSG00000225663.
ENST00000538396; ENSP00000445543; ENSG00000225663.
ENST00000574190; ENSP00000458720; ENSG00000225663.
ENST00000576730; ENSP00000458707; ENSG00000225663.
GeneIDi348262.
KEGGihsa:348262.
UCSCiuc010wuy.1. human.

Organism-specific databases

CTDi348262.
GeneCardsiGC17M079783.
H-InvDBHIX0014255.
HGNCiHGNC:28007. FAM195B.
HPAiHPA045542.
neXtProtiNX_C9JLW8.
PharmGKBiPA165431912.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG41066.
GeneTreeiENSGT00530000064168.
HOGENOMiHOG000035119.
InParanoidiC9JLW8.
OrthoDBiEOG7RRF8X.
PhylomeDBiC9JLW8.
TreeFamiTF326620.

Miscellaneous databases

GenomeRNAii348262.
NextBioi99380.
PROiC9JLW8.

Gene expression databases

BgeeiC9JLW8.
ExpressionAtlasiC9JLW8. baseline and differential.

Family and domain databases

InterProiIPR029428. FAM195.
[Graphical view]
PfamiPF14799. FAM195. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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].
    Tissue: Small intestine.
  2. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
    Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
    , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
    Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  5. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-79, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  6. "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-21, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  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-21 AND SER-24, 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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiF195B_HUMAN
AccessioniPrimary (citable) accession number: C9JLW8
Secondary accession number(s): Q6ZUL0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 18, 2010
Last sequence update: November 3, 2009
Last modified: March 4, 2015
This is version 46 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 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.