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.

Q9UPU5

- UBP24_HUMAN

UniProt

Q9UPU5 - UBP24_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

Ubiquitin carboxyl-terminal hydrolase 24

Gene
USP24, KIAA1057
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

Protease that can remove conjugated ubiquitin from target proteins and polyubiquitin chains. Deubiquitinates DDB2, preventing its proteasomal degradation.

Catalytic activityi

Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei1698 – 16981Nucleophile By similarity
Active sitei1970 – 19701Proton acceptor By similarity

GO - Molecular functioni

  1. cysteine-type peptidase activity Source: UniProtKB-KW
  2. ubiquitinyl hydrolase activity Source: InterPro

GO - Biological processi

  1. ubiquitin-dependent protein catabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Keywords - Biological processi

Ubl conjugation pathway

Protein family/group databases

MEROPSiC19.047.

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquitin carboxyl-terminal hydrolase 24 (EC:3.4.19.12)
Alternative name(s):
Deubiquitinating enzyme 24
Ubiquitin thioesterase 24
Ubiquitin-specific-processing protease 24
Gene namesi
Name:USP24
Synonyms:KIAA1057
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:12623. USP24.

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA37248.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 26202620Ubiquitin carboxyl-terminal hydrolase 24PRO_0000080652Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei63 – 631Phosphoserine2 Publications
Modified residuei942 – 9421Phosphotyrosine By similarity
Modified residuei1141 – 11411Phosphoserine1 Publication
Modified residuei2047 – 20471Phosphoserine7 Publications
Modified residuei2077 – 20771Phosphoserine By similarity
Modified residuei2561 – 25611Phosphoserine1 Publication
Modified residuei2565 – 25651Phosphothreonine3 Publications
Modified residuei2604 – 26041Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9UPU5.
PaxDbiQ9UPU5.
PRIDEiQ9UPU5.

PTM databases

PhosphoSiteiQ9UPU5.

Expressioni

Gene expression databases

ArrayExpressiQ9UPU5.
BgeeiQ9UPU5.
CleanExiHS_USP24.
GenevestigatoriQ9UPU5.

Organism-specific databases

HPAiHPA026723.
HPA028428.

Interactioni

Protein-protein interaction databases

BioGridi116939. 9 interactions.
IntActiQ9UPU5. 5 interactions.
MINTiMINT-7945132.
STRINGi9606.ENSP00000385700.

Structurei

3D structure databases

ProteinModelPortaliQ9UPU5.
SMRiQ9UPU5. Positions 1677-2043.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini3 – 4442UBAAdd
BLAST
Domaini1689 – 2042354USPAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi47 – 9448Gly-richAdd
BLAST
Compositional biasi1035 – 106228Ser-richAdd
BLAST
Compositional biasi1132 – 116433Ser-richAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase C19 family.
Contains 1 UBA domain.
Contains 1 USP domain.

Phylogenomic databases

eggNOGiCOG5077.
HOGENOMiHOG000068011.
HOVERGENiHBG105784.
InParanoidiQ9UPU5.
KOiK11840.
OMAiCMEYFDL.
OrthoDBiEOG712TV9.
PhylomeDBiQ9UPU5.
TreeFamiTF323966.

Family and domain databases

InterProiIPR016024. ARM-type_fold.
IPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19_UCH.
IPR009060. UBA-like.
IPR015940. UBA/transl_elong_EF1B_N_euk.
IPR029071. Ubiquitin-rel_dom.
IPR028889. UCH/PAN2.
[Graphical view]
PfamiPF00443. UCH. 1 hit.
[Graphical view]
SUPFAMiSSF46934. SSF46934. 1 hit.
SSF48371. SSF48371. 2 hits.
SSF54236. SSF54236. 1 hit.
PROSITEiPS50030. UBA. 1 hit.
PS00972. USP_1. 1 hit.
PS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9UPU5-1 [UniParc]FASTAAdd to Basket

« Hide

MESEEEQHMT TLLCMGFSDP ATIRKALRLA KNDINEAVAL LTNERPGLDY     50
GGYEPMDSGG GPSPGPGGGP RGDGGGDGGG GGPSRGGSTG GGGGFDPPPA 100
YHEVVDAEKN DENGNCSGEG IEFPTTNLYE LESRVLTDHW SIPYKREESL 150
GKCLLASTYL ARLGLSESDE NCRRFMDRCM PEAFKKLLTS SAVHKWGTEI 200
HEGIYNMLML LIELVAERIK QDPIPTGLLG VLTMAFNPDN EYHFKNRMKV 250
SQRNWAEVFG EGNMFAVSPV STFQKEPHGW VVDLVNKFGE LGGFAAIQAK 300
LHSEDIELGA VSALIQPLGV CAEYLNSSVV QPMLDPVILT TIQDVRSVEE 350
KDLKDKRLVS IPELLSAVKL LCMRFQPDLV TIVDDLRLDI LLRMLKSPHF 400
SAKMNSLKEV TKLIEDSTLS KSVKNAIDTD RLLDWLVENS VLSIALEGNI 450
DQAQYCDRIK GIIELLGSKL SLDELTKIWK IQSGQSSTVI ENIHTIIAAA 500
AVKFNSDQLN HLFVLIQKSW ETESDRVRQK LLSLIGRIGR EARFETTSGK 550
VLDVLWELAH LPTLPSSLIQ QALEEHLTIL SDAYAVKEAI KRSYIIKCIE 600
DIKRPGEWSG LEKNKKDGFK SSQLNNPQFV WVVPALRQLH EITRSFIKQT 650
YQKQDKSIIQ DLKKNFEIVK LVTGSLIACH RLAAAVAGPG GLSGSTLVDG 700
RYTYREYLEA HLKFLAFFLQ EATLYLGWNR AKEIWECLVT GQDVCELDRE 750
MCFEWFTKGQ HDLESDVQQQ LFKEKILKLE SYEITMNGFN LFKTFFENVN 800
LCDHRLKRQG AQLYVEKLEL IGMDFIWKIA MESPDEEIAN EAIQLIINYS 850
YINLNPRLKK DSVSLHKKFI ADCYTRLEAA SSALGGPTLT HAVTRATKML 900
TATAMPTVAT SVQSPYRSTK LVIIERLLLL AERYVITIED FYSVPRTILP 950
HGASFHGHLL TLNVTYESTK DTFTVEAHSN ETIGSVRWKI AKQLCSPVDN 1000
IQIFTNDSLL TVNKDQKLLH QLGFSDEQIL TVKTSGSGTP SGSSADSSTS 1050
SSSSSSGVFS SSYAMEQEKS LPGVVMALVC NVFDMLYQLA NLEEPRITLR 1100
VRKLLLLIPT DPAIQEALDQ LDSLGRKKTL LSESSSQSSK SPSLSSKQQH 1150
QPSASSILES LFRSFAPGMS TFRVLYNLEV LSSKLMPTAD DDMARSCAKS 1200
FCENFLKAGG LSLVVNVMQR DSIPSEVDYE TRQGVYSICL QLARFLLVGQ 1250
TMPTLLDEDL TKDGIEALSS RPFRNVSRQT SRQMSLCGTP EKSSYRQLSV 1300
SDRSSIRVEE IIPAARVAIQ TMEVSDFTST VACFMRLSWA AAAGRLDLVG 1350
SSQPIKESNS LCPAGIRNRL SSSGSNCSSG SEGEPVALHA GICVRQQSVS 1400
TKDSLIAGEA LSLLVTCLQL RSQQLASFYN LPCVADFIID ILLGSPSAEI 1450
RRVACDQLYT LSQTDTSAHP DVQKPNQFLL GVILTAQLPL WSPTSIMRGV 1500
NQRLLSQCME YFDLRCQLLD DLTTSEMEQL RISPATMLED EITWLDNFEP 1550
NRTAECETSE ADNILLAGHL RLIKTLLSLC GAEKEMLGSS LIKPLLDDFL 1600
FRASRIILNS HSPAGSAAIS QQDFHPKCST ANSRLAAYEV LVMLADSSPS 1650
NLQIIIKELL SMHHQPDPAL TKEFDYLPPV DSRSSSGFVG LRNGGATCYM 1700
NAVFQQLYMQ PGLPESLLSV DDDTDNPDDS VFYQVQSLFG HLMESKLQYY 1750
VPENFWKIFK MWNKELYVRE QQDAYEFFTS LIDQMDEYLK KMGRDQIFKN 1800
TFQGIYSDQK ICKDCPHRYE REEAFMALNL GVTSCQSLEI SLDQFVRGEV 1850
LEGSNAYYCE KCKEKRITVK RTCIKSLPSV LVIHLMRFGF DWESGRSIKY 1900
DEQIRFPWML NMEPYTVSGM ARQDSSSEVG ENGRSVDQGG GGSPRKKVAL 1950
TENYELVGVI VHSGQAHAGH YYSFIKDRRG CGKGKWYKFN DTVIEEFDLN 2000
DETLEYECFG GEYRPKVYDQ TNPYTDVRRR YWNAYMLFYQ RVSDQNSPVL 2050
PKKSRVSVVR QEAEDLSLSA PSSPEISPQS SPRPHRPNND RLSILTKLVK 2100
KGEKKGLFVE KMPARIYQMV RDENLKFMKN RDVYSSDYFS FVLSLASLNA 2150
TKLKHPYYPC MAKVSLQLAI QFLFQTYLRT KKKLRVDTEE WIATIEALLS 2200
KSFDACQWLV EYFISSEGRE LIKIFLLECN VREVRVAVAT ILEKTLDSAL 2250
FYQDKLKSLH QLLEVLLALL DKDVPENCKN CAQYFFLFNT FVQKQGIRAG 2300
DLLLRHSALR HMISFLLGAS RQNNQIRRWS SAQAREFGNL HNTVALLVLH 2350
SDVSSQRNVA PGIFKQRPPI SIAPSSPLLP LHEEVEALLF MSEGKPYLLE 2400
VMFALRELTG SLLALIEMVV YCCFCNEHFS FTMLHFIKNQ LETAPPHELK 2450
NTFQLLHEIL VIEDPIQVER VKFVFETENG LLALMHHSNH VDSSRCYQCV 2500
KFLVTLAQKC PAAKEYFKEN SHHWSWAVQW LQKKMSEHYW TPQSNVSNET 2550
STGKTFQRTI SAQDTLAYAT ALLNEKEQSG SSNGSESSPA NENGDRHLQQ 2600
GSESPMMIGE LRSDLDDVDP 2620
Length:2,620
Mass (Da):294,365
Last modified:November 4, 2008 - v3
Checksum:i2773B7857A8B6633
GO

Sequence cautioni

The sequence AAH29660.1 differs from that shown. Reason: Erroneous initiation.
The sequence BAA91084.1 differs from that shown. Reason: Erroneous initiation.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti226 – 2261T → I.
Corresponds to variant rs1165222 [ dbSNP | Ensembl ].
VAR_047154
Natural varianti1940 – 19401G → S.
Corresponds to variant rs2274540 [ dbSNP | Ensembl ].
VAR_047155
Natural varianti2134 – 21341Y → S.
Corresponds to variant rs12753590 [ dbSNP | Ensembl ].
VAR_047156
Natural varianti2468 – 24681V → A.2 Publications
Corresponds to variant rs487230 [ dbSNP | Ensembl ].
VAR_047157

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti840 – 8401N → S in BAC86814. 1 Publication
Sequence conflicti990 – 9901I → L in BAC86814. 1 Publication
Sequence conflicti1253 – 12531P → S in BAC86814. 1 Publication
Sequence conflicti1776 – 17761E → G in BAC86814. 1 Publication
Sequence conflicti2576 – 25761K → R in BAA91084. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AC091609 Genomic DNA. No translation available.
AK000321 mRNA. Translation: BAA91084.1. Different initiation.
AK127075 mRNA. Translation: BAC86814.1.
AB028980 mRNA. Translation: BAA83009.1.
BC029660 mRNA. Translation: AAH29660.1. Different initiation.
CCDSiCCDS44154.2.
RefSeqiNP_056121.2. NM_015306.2.
UniGeneiHs.477009.

Genome annotation databases

EnsembliENST00000294383; ENSP00000294383; ENSG00000162402.
GeneIDi23358.
KEGGihsa:23358.
UCSCiuc021onw.1. human.

Polymorphism databases

DMDMi212276491.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AC091609 Genomic DNA. No translation available.
AK000321 mRNA. Translation: BAA91084.1 . Different initiation.
AK127075 mRNA. Translation: BAC86814.1 .
AB028980 mRNA. Translation: BAA83009.1 .
BC029660 mRNA. Translation: AAH29660.1 . Different initiation.
CCDSi CCDS44154.2.
RefSeqi NP_056121.2. NM_015306.2.
UniGenei Hs.477009.

3D structure databases

ProteinModelPortali Q9UPU5.
SMRi Q9UPU5. Positions 1677-2043.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116939. 9 interactions.
IntActi Q9UPU5. 5 interactions.
MINTi MINT-7945132.
STRINGi 9606.ENSP00000385700.

Protein family/group databases

MEROPSi C19.047.

PTM databases

PhosphoSitei Q9UPU5.

Polymorphism databases

DMDMi 212276491.

Proteomic databases

MaxQBi Q9UPU5.
PaxDbi Q9UPU5.
PRIDEi Q9UPU5.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000294383 ; ENSP00000294383 ; ENSG00000162402 .
GeneIDi 23358.
KEGGi hsa:23358.
UCSCi uc021onw.1. human.

Organism-specific databases

CTDi 23358.
GeneCardsi GC01M055536.
H-InvDB HIX0000626.
HGNCi HGNC:12623. USP24.
HPAi HPA026723.
HPA028428.
MIMi 610569. gene.
neXtProti NX_Q9UPU5.
PharmGKBi PA37248.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5077.
HOGENOMi HOG000068011.
HOVERGENi HBG105784.
InParanoidi Q9UPU5.
KOi K11840.
OMAi CMEYFDL.
OrthoDBi EOG712TV9.
PhylomeDBi Q9UPU5.
TreeFami TF323966.

Miscellaneous databases

ChiTaRSi USP24. human.
GeneWikii USP24.
GenomeRNAii 23358.
NextBioi 45380.
PROi Q9UPU5.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9UPU5.
Bgeei Q9UPU5.
CleanExi HS_USP24.
Genevestigatori Q9UPU5.

Family and domain databases

InterProi IPR016024. ARM-type_fold.
IPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19_UCH.
IPR009060. UBA-like.
IPR015940. UBA/transl_elong_EF1B_N_euk.
IPR029071. Ubiquitin-rel_dom.
IPR028889. UCH/PAN2.
[Graphical view ]
Pfami PF00443. UCH. 1 hit.
[Graphical view ]
SUPFAMi SSF46934. SSF46934. 1 hit.
SSF48371. SSF48371. 2 hits.
SSF54236. SSF54236. 1 hit.
PROSITEi PS50030. UBA. 1 hit.
PS00972. USP_1. 1 hit.
PS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "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].
  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] OF 751-2082 AND 2256-2620, VARIANT ALA-2468.
  3. "Prediction of the coding sequences of unidentified human genes. XIV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
    Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    DNA Res. 6:197-205(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2233-2620, VARIANT ALA-2468.
    Tissue: Brain.
  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] OF 1483-2620.
    Tissue: Placenta.
  5. "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry."
    Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C.
    Anal. Chem. 76:2763-2772(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2047, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2047, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Platelet.
  8. "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-2047, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63; SER-1141; SER-2047; THR-2565 AND SER-2604, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "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].
  11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2047, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "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-2561, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  13. "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-2047 AND THR-2565, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "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-2047 AND THR-2565, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "The deubiquitinating protein USP24 interacts with DDB2 and regulates DDB2 stability."
    Zhang L., Lubin A., Chen H., Sun Z., Gong F.
    Cell Cycle 11:4378-4384(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiUBP24_HUMAN
AccessioniPrimary (citable) accession number: Q9UPU5
Secondary accession number(s): Q6ZSY2, Q8N2Y4, Q9NXD1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 20, 2001
Last sequence update: November 4, 2008
Last modified: September 3, 2014
This is version 129 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, 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
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. Peptidase families
    Classification of peptidase families and list of entries
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi