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P17980

- PRS6A_HUMAN

UniProt

P17980 - PRS6A_HUMAN

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Protein
26S protease regulatory subunit 6A
Gene
PSMC3, TBP1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

The 26S protease is involved in the ATP-dependent degradation of ubiquitinated proteins. The regulatory (or ATPase) complex confers ATP dependency and substrate specificity to the 26S complex By similarity. In case of HIV-1 infection, suppresses Tat-mediated transactivation.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi227 – 2348ATP Reviewed prediction

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. ATPase activity Source: UniProtKB
  3. protein binding Source: IntAct
  4. transcription coactivator activity Source: ProtInc
  5. transcription corepressor activity Source: ProtInc
Complete GO annotation...

GO - Biological processi

  1. ATP catabolic process Source: GOC
  2. DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest Source: Reactome
  3. G1/S transition of mitotic cell cycle Source: Reactome
  4. RNA metabolic process Source: Reactome
  5. anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process Source: Reactome
  6. antigen processing and presentation of exogenous peptide antigen via MHC class I Source: Reactome
  7. antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent Source: Reactome
  8. antigen processing and presentation of peptide antigen via MHC class I Source: Reactome
  9. apoptotic process Source: Reactome
  10. blastocyst development Source: Ensembl
  11. cellular nitrogen compound metabolic process Source: Reactome
  12. gene expression Source: Reactome
  13. mRNA metabolic process Source: Reactome
  14. mitotic cell cycle Source: Reactome
  15. negative regulation of apoptotic process Source: Reactome
  16. negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
  17. positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
  18. protein polyubiquitination Source: Reactome
  19. regulation of RNA biosynthetic process Source: GOC
  20. regulation of apoptotic process Source: Reactome
  21. regulation of cellular amino acid metabolic process Source: Reactome
  22. regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
  23. small molecule metabolic process Source: Reactome
  24. viral process Source: Reactome
Complete GO annotation...

Keywords - Biological processi

Host-virus interaction

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_111056. Cross-presentation of soluble exogenous antigens (endosomes).
REACT_111178. ER-Phagosome pathway.
REACT_1156. Orc1 removal from chromatin.
REACT_118656. Activation of NF-kappaB in B cells.
REACT_1221. CDK-mediated phosphorylation and removal of Cdc6.
REACT_13464. Regulation of activated PAK-2p34 by proteasome mediated degradation.
REACT_13565. Regulation of ornithine decarboxylase (ODC).
REACT_150471. Separation of Sister Chromatids.
REACT_1614. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
REACT_172638. Asymmetric localization of PCP proteins.
REACT_1949. CDT1 association with the CDC6:ORC:origin complex.
REACT_200766. degradation of AXIN.
REACT_200841. degradation of DVL.
REACT_20549. Autodegradation of the E3 ubiquitin ligase COP1.
REACT_25325. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_4. Ubiquitin-dependent degradation of Cyclin D1.
REACT_6761. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
REACT_6785. Autodegradation of Cdh1 by Cdh1:APC/C.
REACT_6821. SCF-beta-TrCP mediated degradation of Emi1.
REACT_6871. APC/C:Cdc20 mediated degradation of Securin.
REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_9003. SCF(Skp2)-mediated degradation of p27/p21.
REACT_9031. Vpu mediated degradation of CD4.
REACT_9453. Vif-mediated degradation of APOBEC3G.

Names & Taxonomyi

Protein namesi
Recommended name:
26S protease regulatory subunit 6A
Alternative name(s):
26S proteasome AAA-ATPase subunit RPT5
Proteasome 26S subunit ATPase 3
Proteasome subunit P50
Tat-binding protein 1
Short name:
TBP-1
Gene namesi
Name:PSMC3
Synonyms:TBP1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:9549. PSMC3.

Subcellular locationi

Cytoplasm Reviewed prediction. Nucleus Reviewed prediction. CytoplasmP-body By similarity
Note: Colocalizes with TRIM5 in the cytoplasmic bodies By similarity.

GO - Cellular componenti

  1. cytoplasmic mRNA processing body Source: UniProtKB
  2. cytosol Source: Reactome
  3. nucleoplasm Source: Reactome
  4. nucleus Source: UniProt
  5. perinuclear region of cytoplasm Source: Ensembl
  6. proteasome accessory complex Source: UniProtKB
  7. proteasome complex Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Proteasome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi233 – 2331K → H: Loss of function.
Mutagenesisi289 – 2891D → A: Loss of function.

Organism-specific databases

PharmGKBiPA33894.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 43943926S protease regulatory subunit 6A
PRO_0000084698Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine4 Publications
Modified residuei9 – 91Phosphoserine3 Publications

Post-translational modificationi

Sumoylated by UBE2I in response to MEKK1-mediated stimuli.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP17980.
PaxDbiP17980.
PeptideAtlasiP17980.
PRIDEiP17980.

2D gel databases

REPRODUCTION-2DPAGEIPI00018398.

PTM databases

PhosphoSiteiP17980.

Miscellaneous databases

PMAP-CutDBP17980.

Expressioni

Gene expression databases

ArrayExpressiP17980.
BgeeiP17980.
CleanExiHS_PSMC3.
GenevestigatoriP17980.

Organism-specific databases

HPAiHPA006065.

Interactioni

Subunit structurei

May form a heterodimer with a related family member. Interacts with PAAF1. Interacts with HIV-1 Tat.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
P03255-12EBI-359720,EBI-6692439From a different organism.
PSMC6P623335EBI-359720,EBI-357669
PSMD9O002334EBI-359720,EBI-750973

Protein-protein interaction databases

BioGridi111675. 92 interactions.
DIPiDIP-27555N.
IntActiP17980. 26 interactions.
MINTiMINT-1149785.
STRINGi9606.ENSP00000298852.

Structurei

3D structure databases

ProteinModelPortaliP17980.
SMRiP17980. Positions 52-439.

Family & Domainsi

Sequence similaritiesi

Belongs to the AAA ATPase family.

Phylogenomic databases

eggNOGiCOG1222.
HOVERGENiHBG000109.
InParanoidiP17980.
KOiK03065.
OMAiATELNHE.
OrthoDBiEOG7TMZRN.
PhylomeDBiP17980.
TreeFamiTF105648.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR005937. 26S_Psome_P45.
IPR003593. AAA+_ATPase.
IPR003959. ATPase_AAA_core.
IPR003960. ATPase_AAA_CS.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00004. AAA. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR01242. 26Sp45. 1 hit.
PROSITEiPS00674. AAA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P17980-1 [UniParc]FASTAAdd to Basket

« Hide

MNLLPNIESP VTRQEKMATV WDEAEQDGIG EEVLKMSTEE IIQRTRLLDS    50
EIKIMKSEVL RVTHELQAMK DKIKENSEKI KVNKTLPYLV SNVIELLDVD 100
PNDQEEDGAN IDLDSQRKGK CAVIKTSTRQ TYFLPVIGLV DAEKLKPGDL 150
VGVNKDSYLI LETLPTEYDS RVKAMEVDER PTEQYSDIGG LDKQIQELVE 200
AIVLPMNHKE KFENLGIQPP KGVLMYGPPG TGKTLLARAC AAQTKATFLK 250
LAGPQLVQMF IGDGAKLVRD AFALAKEKAP SIIFIDELDA IGTKRFDSEK 300
AGDREVQRTM LELLNQLDGF QPNTQVKVIA ATNRVDILDP ALLRSGRLDR 350
KIEFPMPNEE ARARIMQIHS RKMNVSPDVN YEELARCTDD FNGAQCKAVC 400
VEAGMIALRR GATELTHEDY MEGILEVQAK KKANLQYYA 439
Length:439
Mass (Da):49,204
Last modified:May 10, 2002 - v3
Checksum:i0E443465DDDEBB0B
GO

Sequence cautioni

The sequence AAI07805.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti356 – 3561M → T in BAD96205. 1 Publication
Sequence conflicti409 – 4091R → A in AAA36666. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK313518 mRNA. Translation: BAG36298.1.
CH471064 Genomic DNA. Translation: EAW67916.1.
BC008713 mRNA. Translation: AAH08713.4.
BC073165 mRNA. Translation: AAH73165.3.
BC106920 mRNA. Translation: AAI06921.1.
BC107804 mRNA. Translation: AAI07805.1. Different initiation.
AK222485 mRNA. Translation: BAD96205.1.
M34079 mRNA. Translation: AAA36666.1.
CR456731 mRNA. Translation: CAG33012.1.
CCDSiCCDS7935.1.
PIRiA34832.
RefSeqiNP_002795.2. NM_002804.4.
UniGeneiHs.250758.

Genome annotation databases

EnsembliENST00000298852; ENSP00000298852; ENSG00000165916.
GeneIDi5702.
KEGGihsa:5702.
UCSCiuc001nfh.2. human.

Polymorphism databases

DMDMi20532406.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK313518 mRNA. Translation: BAG36298.1 .
CH471064 Genomic DNA. Translation: EAW67916.1 .
BC008713 mRNA. Translation: AAH08713.4 .
BC073165 mRNA. Translation: AAH73165.3 .
BC106920 mRNA. Translation: AAI06921.1 .
BC107804 mRNA. Translation: AAI07805.1 . Different initiation.
AK222485 mRNA. Translation: BAD96205.1 .
M34079 mRNA. Translation: AAA36666.1 .
CR456731 mRNA. Translation: CAG33012.1 .
CCDSi CCDS7935.1.
PIRi A34832.
RefSeqi NP_002795.2. NM_002804.4.
UniGenei Hs.250758.

3D structure databases

ProteinModelPortali P17980.
SMRi P17980. Positions 52-439.
ModBasei Search...

Protein-protein interaction databases

BioGridi 111675. 92 interactions.
DIPi DIP-27555N.
IntActi P17980. 26 interactions.
MINTi MINT-1149785.
STRINGi 9606.ENSP00000298852.

PTM databases

PhosphoSitei P17980.

Polymorphism databases

DMDMi 20532406.

2D gel databases

REPRODUCTION-2DPAGE IPI00018398.

Proteomic databases

MaxQBi P17980.
PaxDbi P17980.
PeptideAtlasi P17980.
PRIDEi P17980.

Protocols and materials databases

DNASUi 5702.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000298852 ; ENSP00000298852 ; ENSG00000165916 .
GeneIDi 5702.
KEGGi hsa:5702.
UCSCi uc001nfh.2. human.

Organism-specific databases

CTDi 5702.
GeneCardsi GC11M047440.
HGNCi HGNC:9549. PSMC3.
HPAi HPA006065.
MIMi 186852. gene.
neXtProti NX_P17980.
PharmGKBi PA33894.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1222.
HOVERGENi HBG000109.
InParanoidi P17980.
KOi K03065.
OMAi ATELNHE.
OrthoDBi EOG7TMZRN.
PhylomeDBi P17980.
TreeFami TF105648.

Enzyme and pathway databases

Reactomei REACT_111056. Cross-presentation of soluble exogenous antigens (endosomes).
REACT_111178. ER-Phagosome pathway.
REACT_1156. Orc1 removal from chromatin.
REACT_118656. Activation of NF-kappaB in B cells.
REACT_1221. CDK-mediated phosphorylation and removal of Cdc6.
REACT_13464. Regulation of activated PAK-2p34 by proteasome mediated degradation.
REACT_13565. Regulation of ornithine decarboxylase (ODC).
REACT_150471. Separation of Sister Chromatids.
REACT_1614. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
REACT_172638. Asymmetric localization of PCP proteins.
REACT_1949. CDT1 association with the CDC6:ORC:origin complex.
REACT_200766. degradation of AXIN.
REACT_200841. degradation of DVL.
REACT_20549. Autodegradation of the E3 ubiquitin ligase COP1.
REACT_25325. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_4. Ubiquitin-dependent degradation of Cyclin D1.
REACT_6761. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
REACT_6785. Autodegradation of Cdh1 by Cdh1:APC/C.
REACT_6821. SCF-beta-TrCP mediated degradation of Emi1.
REACT_6871. APC/C:Cdc20 mediated degradation of Securin.
REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_9003. SCF(Skp2)-mediated degradation of p27/p21.
REACT_9031. Vpu mediated degradation of CD4.
REACT_9453. Vif-mediated degradation of APOBEC3G.

Miscellaneous databases

ChiTaRSi PSMC3. human.
GeneWikii PSMC3.
GenomeRNAii 5702.
NextBioi 22154.
PMAP-CutDB P17980.
PROi P17980.
SOURCEi Search...

Gene expression databases

ArrayExpressi P17980.
Bgeei P17980.
CleanExi HS_PSMC3.
Genevestigatori P17980.

Family and domain databases

Gene3Di 3.40.50.300. 1 hit.
InterProi IPR005937. 26S_Psome_P45.
IPR003593. AAA+_ATPase.
IPR003959. ATPase_AAA_core.
IPR003960. ATPase_AAA_CS.
IPR027417. P-loop_NTPase.
[Graphical view ]
Pfami PF00004. AAA. 1 hit.
[Graphical view ]
SMARTi SM00382. AAA. 1 hit.
[Graphical view ]
SUPFAMi SSF52540. SSF52540. 1 hit.
TIGRFAMsi TIGR01242. 26Sp45. 1 hit.
PROSITEi PS00674. AAA. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The type 1 human immunodeficiency virus Tat binding protein is a transcriptional activator belonging to an additional family of evolutionarily conserved genes."
    Ohana B., Moore P.A., Ruben S.M., Southgate C.D., Green M.R., Rosen C.A.
    Proc. Natl. Acad. Sci. U.S.A. 90:138-142(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "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].
  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].
    Tissue: Kidney, Lung and Peripheral nerve.
  5. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
    Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 16-439.
    Tissue: Adipose tissue.
  6. "A cDNA for a protein that interacts with the human immunodeficiency virus Tat transactivator."
    Nelbock P., Dillion P.J., Perkins A., Rosen C.A.
    Science 248:1650-1653(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 36-439, INTERACTION WITH HIV-1 TAT.
  7. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 36-439.
  8. Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.
    Submitted (DEC-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 130-144; 156-171; 174-233; 251-266; 277-294; 309-327; 335-344; 351-362; 372-386 AND 398-409, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
  9. "Identification, purification, and characterization of a PA700-dependent activator of the proteasome."
    Demartino G.N., Proske R.J., Moomaw C.R., Strong A.A., Song X., Hisamatsu H., Tanaka K., Slaughter C.A.
    J. Biol. Chem. 271:3112-3118(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE.
  10. "Proteasomal ATPase-associated factor 1 negatively regulates proteasome activity by interacting with proteasomal ATPases."
    Park Y., Hwang Y.-P., Lee J.-S., Seo S.-H., Yoon S.K., Yoon J.-B.
    Mol. Cell. Biol. 25:3842-3853(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PAAF1.
  11. "Mass spectrometric characterization of the affinity-purified human 26S proteasome complex."
    Wang X., Chen C.-F., Baker P.R., Chen P.-L., Kaiser P., Huang L.
    Biochemistry 46:3553-3565(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  12. "Ubc9 fusion-directed SUMOylation identifies constitutive and inducible SUMOylation."
    Jakobs A., Himstedt F., Funk M., Korn B., Gaestel M., Niedenthal R.
    Nucleic Acids Res. 35:E109-E109(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION.
  13. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPRS6A_HUMAN
AccessioniPrimary (citable) accession number: P17980
Secondary accession number(s): B2R8V1
, Q3B757, Q3B865, Q53HU5, Q6GPG8, Q6IBS1, Q96HD3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: May 10, 2002
Last modified: September 3, 2014
This is version 159 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. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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