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Q9UPU5

- UBP24_HUMAN

UniProt

Q9UPU5 - UBP24_HUMAN

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Protein

Ubiquitin carboxyl-terminal hydrolase 24

Gene

USP24

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.1 Publication

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 – 16981NucleophilePROSITE-ProRule annotation
Active sitei1970 – 19701Proton acceptorPROSITE-ProRule annotation

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 – 9421PhosphotyrosineBy similarity
Modified residuei1141 – 11411Phosphoserine1 Publication
Modified residuei2047 – 20471Phosphoserine7 Publications
Modified residuei2077 – 20771PhosphoserineBy 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

BgeeiQ9UPU5.
CleanExiHS_USP24.
GenevestigatoriQ9UPU5.

Organism-specific databases

HPAiHPA026723.
HPA028428.

Interactioni

Protein-protein interaction databases

BioGridi116939. 12 interactions.
IntActiQ9UPU5. 5 interactions.
MINTiMINT-7945132.
STRINGi9606.ENSP00000385700.

Structurei

3D structure databases

ProteinModelPortaliQ9UPU5.
SMRiQ9UPU5. Positions 1677-2043.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini3 – 4442UBAPROSITE-ProRule annotationAdd
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.Curated
Contains 1 UBA domain.PROSITE-ProRule annotation
Contains 1 USP domain.Curated

Phylogenomic databases

eggNOGiCOG5077.
GeneTreeiENSGT00760000119158.
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

        10         20         30         40         50
MESEEEQHMT TLLCMGFSDP ATIRKALRLA KNDINEAVAL LTNERPGLDY
60 70 80 90 100
GGYEPMDSGG GPSPGPGGGP RGDGGGDGGG GGPSRGGSTG GGGGFDPPPA
110 120 130 140 150
YHEVVDAEKN DENGNCSGEG IEFPTTNLYE LESRVLTDHW SIPYKREESL
160 170 180 190 200
GKCLLASTYL ARLGLSESDE NCRRFMDRCM PEAFKKLLTS SAVHKWGTEI
210 220 230 240 250
HEGIYNMLML LIELVAERIK QDPIPTGLLG VLTMAFNPDN EYHFKNRMKV
260 270 280 290 300
SQRNWAEVFG EGNMFAVSPV STFQKEPHGW VVDLVNKFGE LGGFAAIQAK
310 320 330 340 350
LHSEDIELGA VSALIQPLGV CAEYLNSSVV QPMLDPVILT TIQDVRSVEE
360 370 380 390 400
KDLKDKRLVS IPELLSAVKL LCMRFQPDLV TIVDDLRLDI LLRMLKSPHF
410 420 430 440 450
SAKMNSLKEV TKLIEDSTLS KSVKNAIDTD RLLDWLVENS VLSIALEGNI
460 470 480 490 500
DQAQYCDRIK GIIELLGSKL SLDELTKIWK IQSGQSSTVI ENIHTIIAAA
510 520 530 540 550
AVKFNSDQLN HLFVLIQKSW ETESDRVRQK LLSLIGRIGR EARFETTSGK
560 570 580 590 600
VLDVLWELAH LPTLPSSLIQ QALEEHLTIL SDAYAVKEAI KRSYIIKCIE
610 620 630 640 650
DIKRPGEWSG LEKNKKDGFK SSQLNNPQFV WVVPALRQLH EITRSFIKQT
660 670 680 690 700
YQKQDKSIIQ DLKKNFEIVK LVTGSLIACH RLAAAVAGPG GLSGSTLVDG
710 720 730 740 750
RYTYREYLEA HLKFLAFFLQ EATLYLGWNR AKEIWECLVT GQDVCELDRE
760 770 780 790 800
MCFEWFTKGQ HDLESDVQQQ LFKEKILKLE SYEITMNGFN LFKTFFENVN
810 820 830 840 850
LCDHRLKRQG AQLYVEKLEL IGMDFIWKIA MESPDEEIAN EAIQLIINYS
860 870 880 890 900
YINLNPRLKK DSVSLHKKFI ADCYTRLEAA SSALGGPTLT HAVTRATKML
910 920 930 940 950
TATAMPTVAT SVQSPYRSTK LVIIERLLLL AERYVITIED FYSVPRTILP
960 970 980 990 1000
HGASFHGHLL TLNVTYESTK DTFTVEAHSN ETIGSVRWKI AKQLCSPVDN
1010 1020 1030 1040 1050
IQIFTNDSLL TVNKDQKLLH QLGFSDEQIL TVKTSGSGTP SGSSADSSTS
1060 1070 1080 1090 1100
SSSSSSGVFS SSYAMEQEKS LPGVVMALVC NVFDMLYQLA NLEEPRITLR
1110 1120 1130 1140 1150
VRKLLLLIPT DPAIQEALDQ LDSLGRKKTL LSESSSQSSK SPSLSSKQQH
1160 1170 1180 1190 1200
QPSASSILES LFRSFAPGMS TFRVLYNLEV LSSKLMPTAD DDMARSCAKS
1210 1220 1230 1240 1250
FCENFLKAGG LSLVVNVMQR DSIPSEVDYE TRQGVYSICL QLARFLLVGQ
1260 1270 1280 1290 1300
TMPTLLDEDL TKDGIEALSS RPFRNVSRQT SRQMSLCGTP EKSSYRQLSV
1310 1320 1330 1340 1350
SDRSSIRVEE IIPAARVAIQ TMEVSDFTST VACFMRLSWA AAAGRLDLVG
1360 1370 1380 1390 1400
SSQPIKESNS LCPAGIRNRL SSSGSNCSSG SEGEPVALHA GICVRQQSVS
1410 1420 1430 1440 1450
TKDSLIAGEA LSLLVTCLQL RSQQLASFYN LPCVADFIID ILLGSPSAEI
1460 1470 1480 1490 1500
RRVACDQLYT LSQTDTSAHP DVQKPNQFLL GVILTAQLPL WSPTSIMRGV
1510 1520 1530 1540 1550
NQRLLSQCME YFDLRCQLLD DLTTSEMEQL RISPATMLED EITWLDNFEP
1560 1570 1580 1590 1600
NRTAECETSE ADNILLAGHL RLIKTLLSLC GAEKEMLGSS LIKPLLDDFL
1610 1620 1630 1640 1650
FRASRIILNS HSPAGSAAIS QQDFHPKCST ANSRLAAYEV LVMLADSSPS
1660 1670 1680 1690 1700
NLQIIIKELL SMHHQPDPAL TKEFDYLPPV DSRSSSGFVG LRNGGATCYM
1710 1720 1730 1740 1750
NAVFQQLYMQ PGLPESLLSV DDDTDNPDDS VFYQVQSLFG HLMESKLQYY
1760 1770 1780 1790 1800
VPENFWKIFK MWNKELYVRE QQDAYEFFTS LIDQMDEYLK KMGRDQIFKN
1810 1820 1830 1840 1850
TFQGIYSDQK ICKDCPHRYE REEAFMALNL GVTSCQSLEI SLDQFVRGEV
1860 1870 1880 1890 1900
LEGSNAYYCE KCKEKRITVK RTCIKSLPSV LVIHLMRFGF DWESGRSIKY
1910 1920 1930 1940 1950
DEQIRFPWML NMEPYTVSGM ARQDSSSEVG ENGRSVDQGG GGSPRKKVAL
1960 1970 1980 1990 2000
TENYELVGVI VHSGQAHAGH YYSFIKDRRG CGKGKWYKFN DTVIEEFDLN
2010 2020 2030 2040 2050
DETLEYECFG GEYRPKVYDQ TNPYTDVRRR YWNAYMLFYQ RVSDQNSPVL
2060 2070 2080 2090 2100
PKKSRVSVVR QEAEDLSLSA PSSPEISPQS SPRPHRPNND RLSILTKLVK
2110 2120 2130 2140 2150
KGEKKGLFVE KMPARIYQMV RDENLKFMKN RDVYSSDYFS FVLSLASLNA
2160 2170 2180 2190 2200
TKLKHPYYPC MAKVSLQLAI QFLFQTYLRT KKKLRVDTEE WIATIEALLS
2210 2220 2230 2240 2250
KSFDACQWLV EYFISSEGRE LIKIFLLECN VREVRVAVAT ILEKTLDSAL
2260 2270 2280 2290 2300
FYQDKLKSLH QLLEVLLALL DKDVPENCKN CAQYFFLFNT FVQKQGIRAG
2310 2320 2330 2340 2350
DLLLRHSALR HMISFLLGAS RQNNQIRRWS SAQAREFGNL HNTVALLVLH
2360 2370 2380 2390 2400
SDVSSQRNVA PGIFKQRPPI SIAPSSPLLP LHEEVEALLF MSEGKPYLLE
2410 2420 2430 2440 2450
VMFALRELTG SLLALIEMVV YCCFCNEHFS FTMLHFIKNQ LETAPPHELK
2460 2470 2480 2490 2500
NTFQLLHEIL VIEDPIQVER VKFVFETENG LLALMHHSNH VDSSRCYQCV
2510 2520 2530 2540 2550
KFLVTLAQKC PAAKEYFKEN SHHWSWAVQW LQKKMSEHYW TPQSNVSNET
2560 2570 2580 2590 2600
STGKTFQRTI SAQDTLAYAT ALLNEKEQSG SSNGSESSPA NENGDRHLQQ
2610 2620
GSESPMMIGE LRSDLDDVDP
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.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti840 – 8401N → S in BAC86814. (PubMed:14702039)Curated
Sequence conflicti990 – 9901I → L in BAC86814. (PubMed:14702039)Curated
Sequence conflicti1253 – 12531P → S in BAC86814. (PubMed:14702039)Curated
Sequence conflicti1776 – 17761E → G in BAC86814. (PubMed:14702039)Curated
Sequence conflicti2576 – 25761K → R in BAA91084. (PubMed:14702039)Curated

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 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. 12 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 GC01M055543.
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.
GeneTreei ENSGT00760000119158.
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

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: October 29, 2014
This is version 131 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