Q9UPU5 (UBP24_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ubiquitin carboxyl-terminal hydrolase 24
EC=3.4.19.12

Alternative name(s):
Deubiquitinating enzyme 24
Ubiquitin thiolesterase 24
Ubiquitin-specific-processing protease 24

Gene names

Name:	USP24
Synonyms:	KIAA1057

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	2620 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Involved in the ubiquitin-dependent proteolytic pathway in conjunction with the 26S proteasome By similarity.
Catalytic activity	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).
Post-translational modification	Phosphorylated upon DNA damage, probably by ATM or ATR. Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18
Sequence similarities	Belongs to the peptidase C19 family. Contains 1 UBA domain.
Sequence caution	The sequence AAH29660.1 differs from that shown. Reason: Erroneous initiation. The sequence BAA91084.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Ubl conjugation pathway
Coding sequence diversity	Polymorphism
Molecular function	Hydrolase Protease Thiol protease
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	ubiquitin-dependent protein catabolic process Inferred from electronic annotation. Source: InterPro
Molecular function	binding Inferred from electronic annotation. Source: InterPro cysteine-type peptidase activity Inferred from electronic annotation. Source: UniProtKB-KW ubiquitin thiolesterase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 2620	2620	Ubiquitin carboxyl-terminal hydrolase 24		PRO_0000080652
Regions
	Domain	3 – 44	42	UBA
	Compositional bias	47 – 94	48	Gly-rich
	Compositional bias	1035 – 1062	28	Ser-rich
	Compositional bias	1132 – 1164	33	Ser-rich
Sites
	Active site	1698	1	Nucleophile By similarity
	Active site	1970	1	Proton acceptor By similarity
Amino acid modifications
	Modified residue	1141	1	Phosphoserine Ref.11 Ref.15
	Modified residue	1616	1	Phosphoserine Ref.7
	Modified residue	1620	1	Phosphoserine Ref.9
	Modified residue	1943	1	Phosphoserine Ref.6
	Modified residue	2024	1	Phosphotyrosine Ref.5 Ref.6
	Modified residue	2047	1	Phosphoserine Ref.7 Ref.8 Ref.10 Ref.11 Ref.12 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18
	Modified residue	2077	1	Phosphoserine Ref.14
	Modified residue	2559	1	Phosphothreonine Ref.6
	Modified residue	2561	1	Phosphoserine Ref.18
	Modified residue	2565	1	Phosphothreonine Ref.15 Ref.18
	Modified residue	2604	1	Phosphoserine Ref.13 Ref.14 Ref.15
Natural variations
	Natural variant	226	1	T → I. Corresponds to variant rs1165222 [ dbSNP | Ensembl ].		VAR_047154
	Natural variant	1940	1	G → S. Corresponds to variant rs2274540 [ dbSNP | Ensembl ].		VAR_047155
	Natural variant	2134	1	Y → S. Corresponds to variant rs12753590 [ dbSNP | Ensembl ].		VAR_047156
	Natural variant	2468	1	V → A. Ref.2 Ref.3 Corresponds to variant rs487230 [ dbSNP | Ensembl ].		VAR_047157
Experimental info
	Sequence conflict	840	1	N → S in BAC86814. Ref.2
	Sequence conflict	990	1	I → L in BAC86814. Ref.2
	Sequence conflict	1253	1	P → S in BAC86814. Ref.2
	Sequence conflict	1776	1	E → G in BAC86814. Ref.2
	Sequence conflict	2576	1	K → R in BAA91084. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q9UPU5 [UniParc]. Last modified November 4, 2008. Version 3. Checksum: 2773B7857A8B6633	FASTA	2,620	294,365
	10 20 30 40 50 60 MESEEEQHMT TLLCMGFSDP ATIRKALRLA KNDINEAVAL LTNERPGLDY GGYEPMDSGG 70 80 90 100 110 120 GPSPGPGGGP RGDGGGDGGG GGPSRGGSTG GGGGFDPPPA YHEVVDAEKN DENGNCSGEG 130 140 150 160 170 180 IEFPTTNLYE LESRVLTDHW SIPYKREESL GKCLLASTYL ARLGLSESDE NCRRFMDRCM 190 200 210 220 230 240 PEAFKKLLTS SAVHKWGTEI HEGIYNMLML LIELVAERIK QDPIPTGLLG VLTMAFNPDN 250 260 270 280 290 300 EYHFKNRMKV SQRNWAEVFG EGNMFAVSPV STFQKEPHGW VVDLVNKFGE LGGFAAIQAK 310 320 330 340 350 360 LHSEDIELGA VSALIQPLGV CAEYLNSSVV QPMLDPVILT TIQDVRSVEE KDLKDKRLVS 370 380 390 400 410 420 IPELLSAVKL LCMRFQPDLV TIVDDLRLDI LLRMLKSPHF SAKMNSLKEV TKLIEDSTLS 430 440 450 460 470 480 KSVKNAIDTD RLLDWLVENS VLSIALEGNI DQAQYCDRIK GIIELLGSKL SLDELTKIWK 490 500 510 520 530 540 IQSGQSSTVI ENIHTIIAAA AVKFNSDQLN HLFVLIQKSW ETESDRVRQK LLSLIGRIGR 550 560 570 580 590 600 EARFETTSGK VLDVLWELAH LPTLPSSLIQ QALEEHLTIL SDAYAVKEAI KRSYIIKCIE 610 620 630 640 650 660 DIKRPGEWSG LEKNKKDGFK SSQLNNPQFV WVVPALRQLH EITRSFIKQT YQKQDKSIIQ 670 680 690 700 710 720 DLKKNFEIVK LVTGSLIACH RLAAAVAGPG GLSGSTLVDG RYTYREYLEA HLKFLAFFLQ 730 740 750 760 770 780 EATLYLGWNR AKEIWECLVT GQDVCELDRE MCFEWFTKGQ HDLESDVQQQ LFKEKILKLE 790 800 810 820 830 840 SYEITMNGFN LFKTFFENVN LCDHRLKRQG AQLYVEKLEL IGMDFIWKIA MESPDEEIAN 850 860 870 880 890 900 EAIQLIINYS YINLNPRLKK DSVSLHKKFI ADCYTRLEAA SSALGGPTLT HAVTRATKML 910 920 930 940 950 960 TATAMPTVAT SVQSPYRSTK LVIIERLLLL AERYVITIED FYSVPRTILP HGASFHGHLL 970 980 990 1000 1010 1020 TLNVTYESTK DTFTVEAHSN ETIGSVRWKI AKQLCSPVDN IQIFTNDSLL TVNKDQKLLH 1030 1040 1050 1060 1070 1080 QLGFSDEQIL TVKTSGSGTP SGSSADSSTS SSSSSSGVFS SSYAMEQEKS LPGVVMALVC 1090 1100 1110 1120 1130 1140 NVFDMLYQLA NLEEPRITLR VRKLLLLIPT DPAIQEALDQ LDSLGRKKTL LSESSSQSSK 1150 1160 1170 1180 1190 1200 SPSLSSKQQH QPSASSILES LFRSFAPGMS TFRVLYNLEV LSSKLMPTAD DDMARSCAKS 1210 1220 1230 1240 1250 1260 FCENFLKAGG LSLVVNVMQR DSIPSEVDYE TRQGVYSICL QLARFLLVGQ TMPTLLDEDL 1270 1280 1290 1300 1310 1320 TKDGIEALSS RPFRNVSRQT SRQMSLCGTP EKSSYRQLSV SDRSSIRVEE IIPAARVAIQ 1330 1340 1350 1360 1370 1380 TMEVSDFTST VACFMRLSWA AAAGRLDLVG SSQPIKESNS LCPAGIRNRL SSSGSNCSSG 1390 1400 1410 1420 1430 1440 SEGEPVALHA GICVRQQSVS TKDSLIAGEA LSLLVTCLQL RSQQLASFYN LPCVADFIID 1450 1460 1470 1480 1490 1500 ILLGSPSAEI RRVACDQLYT LSQTDTSAHP DVQKPNQFLL GVILTAQLPL WSPTSIMRGV 1510 1520 1530 1540 1550 1560 NQRLLSQCME YFDLRCQLLD DLTTSEMEQL RISPATMLED EITWLDNFEP NRTAECETSE 1570 1580 1590 1600 1610 1620 ADNILLAGHL RLIKTLLSLC GAEKEMLGSS LIKPLLDDFL FRASRIILNS HSPAGSAAIS 1630 1640 1650 1660 1670 1680 QQDFHPKCST ANSRLAAYEV LVMLADSSPS NLQIIIKELL SMHHQPDPAL TKEFDYLPPV 1690 1700 1710 1720 1730 1740 DSRSSSGFVG LRNGGATCYM NAVFQQLYMQ PGLPESLLSV DDDTDNPDDS VFYQVQSLFG 1750 1760 1770 1780 1790 1800 HLMESKLQYY VPENFWKIFK MWNKELYVRE QQDAYEFFTS LIDQMDEYLK KMGRDQIFKN 1810 1820 1830 1840 1850 1860 TFQGIYSDQK ICKDCPHRYE REEAFMALNL GVTSCQSLEI SLDQFVRGEV LEGSNAYYCE 1870 1880 1890 1900 1910 1920 KCKEKRITVK RTCIKSLPSV LVIHLMRFGF DWESGRSIKY DEQIRFPWML NMEPYTVSGM 1930 1940 1950 1960 1970 1980 ARQDSSSEVG ENGRSVDQGG GGSPRKKVAL TENYELVGVI VHSGQAHAGH YYSFIKDRRG 1990 2000 2010 2020 2030 2040 CGKGKWYKFN DTVIEEFDLN DETLEYECFG GEYRPKVYDQ TNPYTDVRRR YWNAYMLFYQ 2050 2060 2070 2080 2090 2100 RVSDQNSPVL PKKSRVSVVR QEAEDLSLSA PSSPEISPQS SPRPHRPNND RLSILTKLVK 2110 2120 2130 2140 2150 2160 KGEKKGLFVE KMPARIYQMV RDENLKFMKN RDVYSSDYFS FVLSLASLNA TKLKHPYYPC 2170 2180 2190 2200 2210 2220 MAKVSLQLAI QFLFQTYLRT KKKLRVDTEE WIATIEALLS KSFDACQWLV EYFISSEGRE 2230 2240 2250 2260 2270 2280 LIKIFLLECN VREVRVAVAT ILEKTLDSAL FYQDKLKSLH QLLEVLLALL DKDVPENCKN 2290 2300 2310 2320 2330 2340 CAQYFFLFNT FVQKQGIRAG DLLLRHSALR HMISFLLGAS RQNNQIRRWS SAQAREFGNL 2350 2360 2370 2380 2390 2400 HNTVALLVLH SDVSSQRNVA PGIFKQRPPI SIAPSSPLLP LHEEVEALLF MSEGKPYLLE 2410 2420 2430 2440 2450 2460 VMFALRELTG SLLALIEMVV YCCFCNEHFS FTMLHFIKNQ LETAPPHELK NTFQLLHEIL 2470 2480 2490 2500 2510 2520 VIEDPIQVER VKFVFETENG LLALMHHSNH VDSSRCYQCV KFLVTLAQKC PAAKEYFKEN 2530 2540 2550 2560 2570 2580 SHHWSWAVQW LQKKMSEHYW TPQSNVSNET STGKTFQRTI SAQDTLAYAT ALLNEKEQSG 2590 2600 2610 2620 SSNGSESSPA NENGDRHLQQ GSESPMMIGE LRSDLDDVDP

References

[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: 16710414] [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: 14702039] [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: 10470851] [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: 15489334] [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: 15144186] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-2024, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[6]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1943; TYR-2024 AND THR-2559, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[7]	"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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1616 AND SER-2047, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[8]	"A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed: 16964243] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2047, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 316:1160-1166(2007) [PubMed: 17525332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1620, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[10]	"Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis." Wang B., Malik R., Nigg E.A., Korner R. Anal. Chem. 80:9526-9533(2008) [PubMed: 19007248] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2047, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column." Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y. Anal. Sci. 24:161-166(2008) [PubMed: 18187866] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1141 AND SER-2047, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"Phosphoproteome of resting human platelets." Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A. J. Proteome Res. 7:526-534(2008) [PubMed: 18088087] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2047, MASS SPECTROMETRY. Tissue: Platelet.
[13]	"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: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2604, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[14]	"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: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2047; SER-2077 AND SER-2604, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[15]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1141; SER-2047; THR-2565 AND SER-2604, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[16]	"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: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2047, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[17]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed: 19369195] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2047, MASS SPECTROMETRY.
[18]	"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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2047; SER-2561 AND THR-2565, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[19]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
IPI	IPI00902614.
RefSeq	NP_056121.2. NM_015306.2.
UniGene	Hs.477009.
3D structure databases
ProteinModelPortal	Q9UPU5.
SMR	Q9UPU5. Positions 960-1032, 1683-2045.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9UPU5. 2 interactions.
STRING	Q9UPU5.
Protein family/group databases
MEROPS	C19.047.
PTM databases
PhosphoSite	Q9UPU5.
Polymorphism databases
DMDM	212276491.
Proteomic databases
PRIDE	Q9UPU5.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000294383; ENSP00000294383; ENSG00000162402.
GeneID	23358.
KEGG	hsa:23358.
UCSC	uc001cyg.2. human.
Organism-specific databases
CTD	23358.
GeneCards	GC01M055533.
HGNC	HGNC:12623. USP24.
HPA	HPA026723. HPA028428.
MIM	610569. gene.
neXtProt	NX_Q9UPU5.
PharmGKB	PA37248.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG15964.
GeneTree	ENSGT00600000084366.
HOGENOM	HBG357761.
HOVERGEN	HBG105784.
InParanoid	Q9UPU5.
OMA	HMISFLL.
OrthoDB	EOG4T782B.
PhylomeDB	Q9UPU5.
Gene expression databases
ArrayExpress	Q9UPU5.
Bgee	Q9UPU5.
CleanEx	HS_USP24.
Genevestigator	Q9UPU5.
GermOnline	ENSG00000162402. Homo sapiens.
Family and domain databases
InterPro	IPR016024. ARM-type_fold. IPR018200. Pept_C19ubi-hydrolase_C_CS. IPR001394. Peptidase_C19. IPR009060. UBA-like. IPR015940. UBA/transl_elong_EF1B_N_euk. [Graphical view]
KO	K11840.
Pfam	PF00443. UCH. 1 hit. [Graphical view]
SUPFAM	SSF48371. ARM-type_fold. 1 hit. SSF46934. UBA_like. 1 hit.
PROSITE	PS50030. UBA. 1 hit. PS00972. UCH_2_1. 1 hit. PS00973. UCH_2_2. 1 hit. PS50235. UCH_2_3. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	45380.
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Entry information

Entry name

UBP24_HUMAN

Accession

Primary (citable) accession number: Q9UPU5
Secondary accession number(s): Q6ZSY2, Q8N2Y4, Q9NXD1

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 20, 2001
Last sequence update:	November 4, 2008
Last modified:	January 25, 2012
This is version 102 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.