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.

Q13200

- PSMD2_HUMAN

UniProt

Q13200 - PSMD2_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 2

Gene
PSMD2, TRAP2
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.
Binds to the intracellular domain of tumor necrosis factor type 1 receptor. The binding domain of TRAP1 and TRAP2 resides outside the death domain of TNFR1.

GO - Molecular functioni

  1. enzyme regulator activity Source: InterPro
  2. protein binding Source: UniProtKB

GO - Biological processi

  1. anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process Source: Reactome
  2. antigen processing and presentation of exogenous peptide antigen via MHC class I Source: Reactome
  3. antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent Source: Reactome
  4. antigen processing and presentation of peptide antigen via MHC class I Source: Reactome
  5. apoptotic process Source: Reactome
  6. cellular nitrogen compound metabolic process Source: Reactome
  7. DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest Source: Reactome
  8. G1/S transition of mitotic cell cycle Source: Reactome
  9. gene expression Source: Reactome
  10. mitotic cell cycle Source: Reactome
  11. mRNA metabolic process Source: Reactome
  12. negative regulation of apoptotic process Source: Reactome
  13. negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
  14. positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
  15. protein polyubiquitination Source: Reactome
  16. regulation of apoptotic process Source: Reactome
  17. regulation of cellular amino acid metabolic process Source: Reactome
  18. regulation of protein catabolic process Source: InterPro
  19. regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
  20. RNA metabolic process 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 2
Alternative name(s):
26S proteasome regulatory subunit RPN1
26S proteasome regulatory subunit S2
26S proteasome subunit p97
Protein 55.11
Tumor necrosis factor type 1 receptor-associated protein 2
Gene namesi
Name:PSMD2
Synonyms:TRAP2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 3

Organism-specific databases

HGNCiHGNC:9559. PSMD2.

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: UniProtKB-KW
  6. proteasome regulatory particle Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Proteasome

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33905.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 90890826S proteasome non-ATPase regulatory subunit 2PRO_0000173810Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine By similarity
Modified residuei16 – 161Phosphoserine8 Publications
Modified residuei24 – 241Phosphothreonine2 Publications
Modified residuei29 – 291Phosphoserine1 Publication
Modified residuei194 – 1941Phosphotyrosine1 Publication
Modified residuei361 – 3611Phosphoserine3 Publications
Modified residuei551 – 5511N6-acetyllysine By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ13200.
PaxDbiQ13200.
PeptideAtlasiQ13200.
PRIDEiQ13200.

PTM databases

PhosphoSiteiQ13200.

Expressioni

Tissue specificityi

Found in skeletal muscle, liver, heart, brain, kidney, pancreas, lung and placenta.

Gene expression databases

ArrayExpressiQ13200.
BgeeiQ13200.
CleanExiHS_PSMD2.
GenevestigatoriQ13200.

Organism-specific databases

HPAiHPA045192.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
PSMC1P621916EBI-357648,EBI-357598
PSMC5P621959EBI-357648,EBI-357745
UCHL5Q9Y5K55EBI-357648,EBI-1051183

Protein-protein interaction databases

BioGridi111681. 121 interactions.
IntActiQ13200. 35 interactions.
MINTiMINT-1142723.
STRINGi9606.ENSP00000310129.

Structurei

3D structure databases

ProteinModelPortaliQ13200.
SMRiQ13200. Positions 56-908.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati409 – 44234PC 1Add
BLAST
Repeati443 – 47937PC 2Add
BLAST
Repeati480 – 51435PC 3Add
BLAST
Repeati517 – 55135PC 4Add
BLAST
Repeati560 – 58930PC 5Add
BLAST
Repeati692 – 72332PC 6Add
BLAST
Repeati742 – 75716PC 7Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi623 – 64119Glu/Lys-richAdd
BLAST

Sequence similaritiesi

Contains 7 PC repeats.

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG5110.
HOVERGENiHBG001842.
InParanoidiQ13200.
KOiK03028.
OMAiIAQGLTH.
OrthoDBiEOG70KGNV.
PhylomeDBiQ13200.
TreeFamiTF105739.

Family and domain databases

InterProiIPR016643. 26S_Psome_Rpn1.
IPR016024. ARM-type_fold.
IPR002015. Proteasome/cyclosome_rpt.
[Graphical view]
PfamiPF01851. PC_rep. 2 hits.
[Graphical view]
PIRSFiPIRSF015965. 26S_Psome_Rpn1. 1 hit.
SUPFAMiSSF48371. SSF48371. 4 hits.

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q13200-1) [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

MEEGGRDKAP VQPQQSPAAA PGGTDEKPSG KERRDAGDKD KEQELSEEDK    50
QLQDELEMLV ERLGEKDTSL YRPALEELRR QIRSSTTSMT SVPKPLKFLR 100
PHYGKLKEIY ENMAPGENKR FAADIISVLA MTMSGERECL KYRLVGSQEE 150
LASWGHEYVR HLAGEVAKEW QELDDAEKVQ REPLLTLVKE IVPYNMAHNA 200
EHEACDLLME IEQVDMLEKD IDENAYAKVC LYLTSCVNYV PEPENSALLR 250
CALGVFRKFS RFPEALRLAL MLNDMELVED IFTSCKDVVV QKQMAFMLGR 300
HGVFLELSED VEEYEDLTEI MSNVQLNSNF LALARELDIM EPKVPDDIYK 350
THLENNRFGG SGSQVDSARM NLASSFVNGF VNAAFGQDKL LTDDGNKWLY 400
KNKDHGMLSA AASLGMILLW DVDGGLTQID KYLYSSEDYI KSGALLACGI 450
VNSGVRNECD PALALLSDYV LHNSNTMRLG SIFGLGLAYA GSNREDVLTL 500
LLPVMGDSKS SMEVAGVTAL ACGMIAVGSC NGDVTSTILQ TIMEKSETEL 550
KDTYARWLPL GLGLNHLGKG EAIEAILAAL EVVSEPFRSF ANTLVDVCAY 600
AGSGNVLKVQ QLLHICSEHF DSKEKEEDKD KKEKKDKDKK EAPADMGAHQ 650
GVAVLGIALI AMGEEIGAEM ALRTFGHLLR YGEPTLRRAV PLALALISVS 700
NPRLNILDTL SKFSHDADPE VSYNSIFAMG MVGSGTNNAR LAAMLRQLAQ 750
YHAKDPNNLF MVRLAQGLTH LGKGTLTLCP YHSDRQLMSQ VAVAGLLTVL 800
VSFLDVRNII LGKSHYVLYG LVAAMQPRML VTFDEELRPL PVSVRVGQAV 850
DVVGQAGKPK TITGFQTHTT PVLLAHGERA ELATEEFLPV TPILEGFVIL 900
RKNPNYDL 908
Length:908
Mass (Da):100,200
Last modified:July 15, 1999 - v3
Checksum:iFAD71E7B26101BE3
GO
Isoform 2 (identifier: Q13200-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-163: MEEGGRDKAP...WGHEYVRHLA → MSMS

Note: No experimental confirmation available.

Show »
Length:749
Mass (Da):82,193
Checksum:i4007D2AAADF807A6
GO
Isoform 3 (identifier: Q13200-3) [UniParc]FASTAAdd to Basket

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

Note: No experimental confirmation available.

Show »
Length:778
Mass (Da):85,606
Checksum:i5564271C57A5959D
GO

Sequence cautioni

The sequence AAA87705.1 differs from that shown. Reason: Erroneous initiation.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti176 – 1761A → T.
Corresponds to variant rs11545172 [ dbSNP | Ensembl ].
VAR_051554
Natural varianti313 – 3131E → D.1 Publication
Corresponds to variant rs11545169 [ dbSNP | Ensembl ].
VAR_051555
Natural varianti724 – 7241N → Y.2 Publications
Corresponds to variant rs17856236 [ dbSNP | Ensembl ].
VAR_067451

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 163163MEEGG…VRHLA → MSMS in isoform 2. VSP_055065Add
BLAST
Alternative sequencei1 – 130130Missing in isoform 3. VSP_055066Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti10 – 101P → R in CAA60167. 1 Publication
Sequence conflicti21 – 211P → S1 Publication
Sequence conflicti32 – 321E → G1 Publication
Sequence conflicti43 – 431Q → L1 Publication
Sequence conflicti57 – 571E → V1 Publication
Sequence conflicti60 – 601V → A in BAA11226. 1 Publication
Sequence conflicti226 – 2261Y → S in AAA87705. 1 Publication
Sequence conflicti260 – 2601S → T in CAA60167. 1 Publication
Sequence conflicti281 – 2833IFT → SS in AAA87705. 1 Publication
Sequence conflicti415 – 4151G → A in BAA11226. 1 Publication
Sequence conflicti731 – 7311M → MGM1 Publication
Sequence conflicti776 – 7761L → P in BAG63219. 1 Publication
Sequence conflicti900 – 9089LRKNPNYDL → FGRTPIMISK1 Publication
Sequence conflicti900 – 9089LRKNPNYDL → FGRTPIMISK1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D78151 mRNA. Translation: BAA11226.1.
BT009736 mRNA. Translation: AAP88738.1.
AK301759 mRNA. Translation: BAG63219.1.
AK302177 mRNA. Translation: BAG63543.1.
AC078797 Genomic DNA. No translation available.
BC002368 mRNA. Translation: AAH02368.1.
BC002997 mRNA. Translation: AAH02997.1.
BC007897 mRNA. Translation: AAH07897.1.
U12596 mRNA. Translation: AAA87705.1. Different initiation.
X86446 mRNA. Translation: CAA60167.1.
CCDSiCCDS3258.1. [Q13200-1]
RefSeqiNP_001265637.1. NM_001278708.1.
NP_001265638.1. NM_001278709.1.
NP_002799.3. NM_002808.4.
UniGeneiHs.518464.

Genome annotation databases

EnsembliENST00000310118; ENSP00000310129; ENSG00000175166.
ENST00000435761; ENSP00000402618; ENSG00000175166.
ENST00000439383; ENSP00000416028; ENSG00000175166.
GeneIDi5708.
KEGGihsa:5708.
UCSCiuc003fnn.1. human. [Q13200-1]

Polymorphism databases

DMDMi6174930.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D78151 mRNA. Translation: BAA11226.1 .
BT009736 mRNA. Translation: AAP88738.1 .
AK301759 mRNA. Translation: BAG63219.1 .
AK302177 mRNA. Translation: BAG63543.1 .
AC078797 Genomic DNA. No translation available.
BC002368 mRNA. Translation: AAH02368.1 .
BC002997 mRNA. Translation: AAH02997.1 .
BC007897 mRNA. Translation: AAH07897.1 .
U12596 mRNA. Translation: AAA87705.1 . Different initiation.
X86446 mRNA. Translation: CAA60167.1 .
CCDSi CCDS3258.1. [Q13200-1 ]
RefSeqi NP_001265637.1. NM_001278708.1.
NP_001265638.1. NM_001278709.1.
NP_002799.3. NM_002808.4.
UniGenei Hs.518464.

3D structure databases

ProteinModelPortali Q13200.
SMRi Q13200. Positions 56-908.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111681. 121 interactions.
IntActi Q13200. 35 interactions.
MINTi MINT-1142723.
STRINGi 9606.ENSP00000310129.

Chemistry

DrugBanki DB00188. Bortezomib.

PTM databases

PhosphoSitei Q13200.

Polymorphism databases

DMDMi 6174930.

Proteomic databases

MaxQBi Q13200.
PaxDbi Q13200.
PeptideAtlasi Q13200.
PRIDEi Q13200.

Protocols and materials databases

DNASUi 5708.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000310118 ; ENSP00000310129 ; ENSG00000175166 .
ENST00000435761 ; ENSP00000402618 ; ENSG00000175166 .
ENST00000439383 ; ENSP00000416028 ; ENSG00000175166 .
GeneIDi 5708.
KEGGi hsa:5708.
UCSCi uc003fnn.1. human. [Q13200-1 ]

Organism-specific databases

CTDi 5708.
GeneCardsi GC03P184016.
HGNCi HGNC:9559. PSMD2.
HPAi HPA045192.
MIMi 606223. gene.
neXtProti NX_Q13200.
PharmGKBi PA33905.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5110.
HOVERGENi HBG001842.
InParanoidi Q13200.
KOi K03028.
OMAi IAQGLTH.
OrthoDBi EOG70KGNV.
PhylomeDBi Q13200.
TreeFami TF105739.

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 PSMD2. human.
GeneWikii PSMD2.
GenomeRNAii 5708.
NextBioi 22178.
PROi Q13200.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q13200.
Bgeei Q13200.
CleanExi HS_PSMD2.
Genevestigatori Q13200.

Family and domain databases

InterProi IPR016643. 26S_Psome_Rpn1.
IPR016024. ARM-type_fold.
IPR002015. Proteasome/cyclosome_rpt.
[Graphical view ]
Pfami PF01851. PC_rep. 2 hits.
[Graphical view ]
PIRSFi PIRSF015965. 26S_Psome_Rpn1. 1 hit.
SUPFAMi SSF48371. SSF48371. 4 hits.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "cDNA cloning and functional analysis of the p97 subunit of the 26S proteasome, a polypeptide identical to the type-1 tumor-necrosis-factor-receptor-associated protein-2/55.11."
    Tsurumi C., Shimizu Y., Saeki M., Kato S., DeMartino G.N., Slaughter C.A., Fujimuro M., Yokosawa H., Yamasaki M., Hendil K.B., Toh-e A., Tanahashi N., Tanaka K.
    Eur. J. Biochem. 239:912-921(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 49-66; 81-85; 91-117; 138-145; 148-158; 182-193; 209-229; 438-441 AND 471-481.
    Tissue: Fibrosarcoma.
  2. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT TYR-724.
  3. "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 2 AND 3), VARIANT ASP-313.
    Tissue: Testis.
  4. "The DNA sequence, annotation and analysis of human chromosome 3."
    Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
    , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
    Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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], VARIANT TYR-724.
    Tissue: Lung, Muscle and Skin.
  6. "Two-hybrid cloning of a gene encoding TNF receptor-associated protein 2, a protein that interacts with the intracellular domain of the type 1 TNF receptor: identity with subunit 2 of the 26S protease."
    Dunbar J.D., Song H.Y., Guo D., Wu L.-W., Donner D.B.
    J. Immunol. 158:4252-4259(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 21-908.
  7. "A protein related to a proteasomal subunit binds to the intracellular domain of the p55 TNF receptor upstream to its 'death domain'."
    Boldin M.P., Mett I.L., Wallach D.
    FEBS Lett. 367:39-44(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 10-908.
    Tissue: Liver.
  8. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "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-16; THR-24; SER-29 AND TYR-194, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  10. "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
    Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
    J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "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-16 AND SER-361, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  15. "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-16; THR-24 AND SER-361, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "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-16 AND SER-361, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPSMD2_HUMAN
AccessioniPrimary (citable) accession number: Q13200
Secondary accession number(s): B4DX07
, B4DXY1, E7EW34, E9PCS3, Q12932, Q15321, Q53XQ4, Q96I12
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 15, 1999
Last modified: September 3, 2014
This is version 147 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 3
    Human chromosome 3: 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
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi