SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q99460

- PSMD1_HUMAN

UniProt

Q99460 - PSMD1_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
26S proteasome non-ATPase regulatory subunit 1
Gene
PSMD1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Acts as a regulatory subunit of the 26 proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins.

GO - Molecular functioni

  1. enzyme regulator activity Source: InterPro

GO - Biological processi

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

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 proteasome non-ATPase regulatory subunit 1
Alternative name(s):
26S proteasome regulatory subunit RPN2
26S proteasome regulatory subunit S1
26S proteasome subunit p112
Gene namesi
Name:PSMD1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:9554. PSMD1.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. extracellular vesicular exosome Source: UniProt
  3. nucleoplasm Source: Reactome
  4. proteasome accessory complex Source: UniProtKB
  5. proteasome complex Source: ProtInc
  6. proteasome regulatory particle Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Proteasome

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33899.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 95395326S proteasome non-ATPase regulatory subunit 1
PRO_0000173801Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine2 Publications
Modified residuei273 – 2731Phosphothreonine1 Publication
Modified residuei290 – 2901Phosphoserine1 Publication
Modified residuei310 – 3101N6-acetyllysine1 Publication
Modified residuei311 – 3111Phosphothreonine4 Publications
Modified residuei315 – 3151Phosphoserine4 Publications
Modified residuei720 – 7201N6-acetyllysine By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ99460.
PaxDbiQ99460.
PRIDEiQ99460.

PTM databases

PhosphoSiteiQ99460.

Expressioni

Gene expression databases

ArrayExpressiQ99460.
BgeeiQ99460.
CleanExiHS_PSMD1.
GenevestigatoriQ99460.

Organism-specific databases

HPAiCAB021092.
HPA036736.

Interactioni

Subunit structurei

Interacts with ADRM1.2 Publications

Protein-protein interaction databases

BioGridi111680. 95 interactions.
DIPiDIP-27548N.
IntActiQ99460. 34 interactions.
MINTiMINT-1160606.

Structurei

3D structure databases

ProteinModelPortaliQ99460.
SMRiQ99460. Positions 3-814.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati403 – 43634PC 1
Add
BLAST
Repeati441 – 47434PC 2
Add
BLAST
Repeati476 – 51035PC 3
Add
BLAST
Repeati511 – 54535PC 4
Add
BLAST
Repeati547 – 58034PC 5
Add
BLAST
Repeati581 – 61636PC 6
Add
BLAST
Repeati617 – 64933PC 7
Add
BLAST
Repeati651 – 68535PC 8
Add
BLAST
Repeati686 – 72641PC 9
Add
BLAST
Repeati729 – 76133PC 10
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi936 – 9438Poly-Glu

Sequence similaritiesi

Contains 10 PC repeats.

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG5116.
HOVERGENiHBG007543.
InParanoidiQ99460.
KOiK03032.
OMAiTESCRYQ.
OrthoDBiEOG790G01.
PhylomeDBiQ99460.
TreeFamiTF105742.

Family and domain databases

Gene3Di1.25.10.10. 2 hits.
InterProiIPR016642. 26S_Psome_Rpn2.
IPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR002015. Proteasome/cyclosome_rpt.
[Graphical view]
PfamiPF01851. PC_rep. 4 hits.
[Graphical view]
PIRSFiPIRSF015947. 26S_Psome_Rpn2. 1 hit.
SUPFAMiSSF48371. SSF48371. 3 hits.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q99460-1) [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

MITSAAGIIS LLDEDEPQLK EFALHKLNAV VNDFWAEISE SVDKIEVLYE    50
DEGFRSRQFA ALVASKVFYH LGAFEESLNY ALGAGDLFNV NDNSEYVETI 100
IAKCIDHYTK QCVENADLPE GEKKPIDQRL EGIVNKMFQR CLDDHKYKQA 150
IGIALETRRL DVFEKTILES NDVPGMLAYS LKLCMSLMQN KQFRNKVLRV 200
LVKIYMNLEK PDFINVCQCL IFLDDPQAVS DILEKLVKED NLLMAYQICF 250
DLYESASQQF LSSVIQNLRT VGTPIASVPG STNTGTVPGS EKDSDSMETE 300
EKTSSAFVGK TPEASPEPKD QTLKMIKILS GEMAIELHLQ FLIRNNNTDL 350
MILKNTKDAV RNSVCHTATV IANSFMHCGT TSDQFLRDNL EWLARATNWA 400
KFTATASLGV IHKGHEKEAL QLMATYLPKD TSPGSAYQEG GGLYALGLIH 450
ANHGGDIIDY LLNQLKNASN DIVRHGGSLG LGLAAMGTAR QDVYDLLKTN 500
LYQDDAVTGE AAGLALGLVM LGSKNAQAIE DMVGYAQETQ HEKILRGLAV 550
GIALVMYGRM EEADALIESL CRDKDPILRR SGMYTVAMAY CGSGNNKAIR 600
RLLHVAVSDV NDDVRRAAVE SLGFILFRTP EQCPSVVSLL SESYNPHVRY 650
GAAMALGICC AGTGNKEAIN LLEPMTNDPV NYVRQGALIA SALIMIQQTE 700
ITCPKVNQFR QLYSKVINDK HDDVMAKFGA ILAQGILDAG GHNVTISLQS 750
RTGHTHMPSV VGVLVFTQFW FWFPLSHFLS LAYTPTCVIG LNKDLKMPKV 800
QYKSNCKPST FAYPAPLEVP KEKEKEKVST AVLSITAKAK KKEKEKEKKE 850
EEKMEVDEAE KKEEKEKKKE PEPNFQLLDN PARVMPAQLK VLTMPETCRY 900
QPFKPLSIGG IIILKDTSED IEELVEPVAA HGPKIEEEEQ EPEPPEPFEY 950
IDD 953
Length:953
Mass (Da):105,836
Last modified:August 31, 2004 - v2
Checksum:iB8682146082D21FA
GO
Isoform 2 (identifier: Q99460-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     797-827: Missing.

Note: No experimental confirmation available.

Show »
Length:922
Mass (Da):102,258
Checksum:i1F727659749D4871
GO

Sequence cautioni

The sequence AAH01053.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.
The sequence AAH14013.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.
The sequence AAH39845.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.
The sequence AAH47897.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.
The sequence AAH64398.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.
The sequence AAH73833.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei797 – 82731Missing in isoform 2.
VSP_011475Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti85 – 851G → R in BAA07918. 1 Publication
Sequence conflicti616 – 6161R → S in BAA07918. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D44466 mRNA. Translation: BAA07918.1.
AC009407 Genomic DNA. Translation: AAX93127.1.
BC001053 mRNA. Translation: AAH01053.1. Sequence problems.
BC014013 mRNA. Translation: AAH14013.1. Sequence problems.
BC039845 mRNA. Translation: AAH39845.1. Sequence problems.
BC047897 mRNA. Translation: AAH47897.1. Sequence problems.
BC064398 mRNA. Translation: AAH64398.1. Sequence problems.
BC073833 mRNA. Translation: AAH73833.1. Sequence problems.
BC094720 mRNA. Translation: AAH94720.1.
BC112344 mRNA. Translation: AAI12345.1.
BC114434 mRNA. Translation: AAI14435.1.
CCDSiCCDS2482.1. [Q99460-1]
CCDS54436.1. [Q99460-2]
RefSeqiNP_001177966.1. NM_001191037.1. [Q99460-2]
NP_002798.2. NM_002807.3. [Q99460-1]
UniGeneiHs.3887.

Genome annotation databases

EnsembliENST00000308696; ENSP00000309474; ENSG00000173692. [Q99460-1]
ENST00000373635; ENSP00000362738; ENSG00000173692. [Q99460-2]
ENST00000409643; ENSP00000386932; ENSG00000173692. [Q99460-2]
GeneIDi5707.
KEGGihsa:5707.
UCSCiuc002vrm.2. human. [Q99460-2]
uc002vrn.2. human. [Q99460-1]

Polymorphism databases

DMDMi51704332.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D44466 mRNA. Translation: BAA07918.1 .
AC009407 Genomic DNA. Translation: AAX93127.1 .
BC001053 mRNA. Translation: AAH01053.1 . Sequence problems.
BC014013 mRNA. Translation: AAH14013.1 . Sequence problems.
BC039845 mRNA. Translation: AAH39845.1 . Sequence problems.
BC047897 mRNA. Translation: AAH47897.1 . Sequence problems.
BC064398 mRNA. Translation: AAH64398.1 . Sequence problems.
BC073833 mRNA. Translation: AAH73833.1 . Sequence problems.
BC094720 mRNA. Translation: AAH94720.1 .
BC112344 mRNA. Translation: AAI12345.1 .
BC114434 mRNA. Translation: AAI14435.1 .
CCDSi CCDS2482.1. [Q99460-1 ]
CCDS54436.1. [Q99460-2 ]
RefSeqi NP_001177966.1. NM_001191037.1. [Q99460-2 ]
NP_002798.2. NM_002807.3. [Q99460-1 ]
UniGenei Hs.3887.

3D structure databases

ProteinModelPortali Q99460.
SMRi Q99460. Positions 3-814.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111680. 95 interactions.
DIPi DIP-27548N.
IntActi Q99460. 34 interactions.
MINTi MINT-1160606.

Chemistry

DrugBanki DB00188. Bortezomib.

PTM databases

PhosphoSitei Q99460.

Polymorphism databases

DMDMi 51704332.

Proteomic databases

MaxQBi Q99460.
PaxDbi Q99460.
PRIDEi Q99460.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000308696 ; ENSP00000309474 ; ENSG00000173692 . [Q99460-1 ]
ENST00000373635 ; ENSP00000362738 ; ENSG00000173692 . [Q99460-2 ]
ENST00000409643 ; ENSP00000386932 ; ENSG00000173692 . [Q99460-2 ]
GeneIDi 5707.
KEGGi hsa:5707.
UCSCi uc002vrm.2. human. [Q99460-2 ]
uc002vrn.2. human. [Q99460-1 ]

Organism-specific databases

CTDi 5707.
GeneCardsi GC02P231921.
HGNCi HGNC:9554. PSMD1.
HPAi CAB021092.
HPA036736.
neXtProti NX_Q99460.
PharmGKBi PA33899.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5116.
HOVERGENi HBG007543.
InParanoidi Q99460.
KOi K03032.
OMAi TESCRYQ.
OrthoDBi EOG790G01.
PhylomeDBi Q99460.
TreeFami TF105742.

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 PSMD1. human.
GeneWikii PSMD1.
GenomeRNAii 5707.
NextBioi 22174.
PROi Q99460.

Gene expression databases

ArrayExpressi Q99460.
Bgeei Q99460.
CleanExi HS_PSMD1.
Genevestigatori Q99460.

Family and domain databases

Gene3Di 1.25.10.10. 2 hits.
InterProi IPR016642. 26S_Psome_Rpn2.
IPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR002015. Proteasome/cyclosome_rpt.
[Graphical view ]
Pfami PF01851. PC_rep. 4 hits.
[Graphical view ]
PIRSFi PIRSF015947. 26S_Psome_Rpn2. 1 hit.
SUPFAMi SSF48371. SSF48371. 3 hits.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "cDNA cloning of p112, the largest regulatory subunit of the human 26s proteasome, and functional analysis of its yeast homologue, sen3p."
    Yokota K., Kagawa S., Shimizu Y., Akioka H., Tsurumi C., Noda C., Fujimuro M., Yokosawa H., Fujiwara T., Takahashi E., Ohba M., Yamasaki M., DeMartino G.N., Slaughter C.A., Toh-e A., Tanaka K.
    Mol. Biol. Cell 7:853-870(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "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] (ISOFORMS 1 AND 2).
    Tissue: Cervix, Liver, Lymph, Placenta, Testis and Uterus.
  4. "A novel proteasome-interacting protein recruits the deubiquitinating enzyme UCH37 to 26S proteasomes."
    Hamazaki J., Iemura S., Natsume T., Yashiroda H., Tanaka K., Murata S.
    EMBO J. 25:4524-4536(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ADRM1.
  5. "Proteasome recruitment and activation of the Uch37 deubiquitinating enzyme by Adrm1."
    Yao T., Song L., Xu W., DeMartino G.N., Florens L., Swanson S.K., Washburn M.P., Conaway R.C., Conaway J.W., Cohen R.E.
    Nat. Cell Biol. 8:994-1002(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ADRM1.
  6. "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 THR-273; SER-290; THR-311 AND SER-315, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-311 AND SER-315, 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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, 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 THR-311 AND SER-315, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  10. "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-310, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "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 THR-311 AND SER-315, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPSMD1_HUMAN
AccessioniPrimary (citable) accession number: Q99460
Secondary accession number(s): B8ZZH9
, Q24JU0, Q53TI2, Q6GMU5, Q6P2P4, Q6PJM7, Q6PKG9, Q86VU1, Q8IV79
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: August 31, 2004
Last modified: September 3, 2014
This is version 136 of the entry and version 2 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 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi