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Protein

Pre-mRNA-splicing factor ATP-dependent RNA helicase PRP16

Gene

DHX38

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

Functioni

Probable ATP-binding RNA helicase involved in pre-mRNA splicing.

Catalytic activityi

ATP + H2O = ADP + phosphate.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi555 – 5628ATPPROSITE-ProRule annotation

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • ATP-dependent RNA helicase activity Source: GO_Central
  • poly(A) RNA binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase

Keywords - Biological processi

mRNA processing, mRNA splicing

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-HSA-109688. Cleavage of Growing Transcript in the Termination Region.
R-HSA-159236. Transport of Mature mRNA derived from an Intron-Containing Transcript.
R-HSA-72163. mRNA Splicing - Major Pathway.
R-HSA-72187. mRNA 3'-end processing.

Names & Taxonomyi

Protein namesi
Recommended name:
Pre-mRNA-splicing factor ATP-dependent RNA helicase PRP16 (EC:3.6.4.13)
Alternative name(s):
ATP-dependent RNA helicase DHX38
DEAH box protein 38
Gene namesi
Name:DHX38
Synonyms:DDX38, KIAA0224, PRP16
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 16

Organism-specific databases

HGNCiHGNC:17211. DHX38.

Subcellular locationi

GO - Cellular componenti

  • catalytic step 2 spliceosome Source: UniProtKB
  • membrane Source: UniProtKB
  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus, Spliceosome

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27225.

Polymorphism and mutation databases

BioMutaiDHX38.
DMDMi85700389.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources1 Publication
Chaini2 – 12271226Pre-mRNA-splicing factor ATP-dependent RNA helicase PRP16PRO_0000055147Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylglycineCombined sources1 Publication
Modified residuei199 – 1991PhosphoserineCombined sources
Modified residuei260 – 2601N6-acetyllysineCombined sources
Cross-linki482 – 482Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei1194 – 11941PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ92620.
MaxQBiQ92620.
PaxDbiQ92620.
PeptideAtlasiQ92620.
PRIDEiQ92620.

PTM databases

iPTMnetiQ92620.
PhosphoSiteiQ92620.

Expressioni

Gene expression databases

BgeeiQ92620.
CleanExiHS_DHX38.
ExpressionAtlasiQ92620. baseline and differential.
GenevisibleiQ92620. HS.

Organism-specific databases

HPAiHPA041347.

Interactioni

Subunit structurei

Identified in the spliceosome C complex.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
DHX16O602312EBI-1043041,EBI-311446
GPKOWQ929172EBI-1043041,EBI-746309
NUDCD1Q96RS62EBI-1043041,EBI-2512429
RBM10P981752EBI-1043041,EBI-721525
TERF2IPQ9NYB02EBI-1043041,EBI-750109

Protein-protein interaction databases

BioGridi115129. 51 interactions.
IntActiQ92620. 14 interactions.
MINTiMINT-2813093.
STRINGi9606.ENSP00000268482.

Structurei

3D structure databases

ProteinModelPortaliQ92620.
SMRiQ92620. Positions 493-704, 916-1155.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini542 – 705164Helicase ATP-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini727 – 902176Helicase C-terminalPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi652 – 6554DEAH box

Sequence similaritiesi

Contains 1 helicase ATP-binding domain.PROSITE-ProRule annotation
Contains 1 helicase C-terminal domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0925. Eukaryota.
COG1643. LUCA.
GeneTreeiENSGT00840000129715.
HOGENOMiHOG000175261.
HOVERGENiHBG039428.
InParanoidiQ92620.
KOiK12815.
OMAiKNEMLTT.
OrthoDBiEOG7FXZXR.
PhylomeDBiQ92620.
TreeFamiTF105793.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR011545. DEAD/DEAH_box_helicase_dom.
IPR002464. DNA/RNA_helicase_DEAH_CS.
IPR011709. DUF1605.
IPR007502. Helicase-assoc_dom.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00270. DEAD. 1 hit.
PF04408. HA2. 1 hit.
PF00271. Helicase_C. 1 hit.
PF07717. OB_NTP_bind. 1 hit.
[Graphical view]
SMARTiSM00487. DEXDc. 1 hit.
SM00847. HA2. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS00690. DEAH_ATP_HELICASE. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q92620-1) [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

        10         20         30         40         50
MGDTSEDASI HRLEGTDLDC QVGGLICKSK SAASEQHVFK APAPRPSLLG
60 70 80 90 100
LDLLASLKRR EREEKDDGED KKKSKVSSYK DWEESKDDQK DAEEEGGDQA
110 120 130 140 150
GQNIRKDRHY RSARVETPSH PGGVSEEFWE RSRQRERERR EHGVYASSKE
160 170 180 190 200
EKDWKKEKSR DRDYDRKRDR DERDRSRHSS RSERDGGSER SSRRNEPESP
210 220 230 240 250
RHRPKDAATP SRSTWEEEDS GYGSSRRSQW ESPSPTPSYR DSERSHRLST
260 270 280 290 300
RDRDRSVRGK YSDDTPLPTP SYKYNEWADD RRHLGSTPRL SRGRGRREEG
310 320 330 340 350
EEGISFDTEE ERQQWEDDQR QADRDWYMMD EGYDEFHNPL AYSSEDYVRR
360 370 380 390 400
REQHLHKQKQ KRISAQRRQI NEDNERWETN RMLTSGVVHR LEVDEDFEED
410 420 430 440 450
NAAKVHLMVH NLVPPFLDGR IVFTKQPEPV IPVKDATSDL AIIARKGSQT
460 470 480 490 500
VRKHREQKER KKAQHKHWEL AGTKLGDIMG VKKEEEPDKA VTEDGKVDYR
510 520 530 540 550
TEQKFADHMK RKSEASSEFA KKKSILEQRQ YLPIFAVQQE LLTIIRDNSI
560 570 580 590 600
VIVVGETGSG KTTQLTQYLH EDGYTDYGMI GCTQPRRVAA MSVAKRVSEE
610 620 630 640 650
MGGNLGEEVG YAIRFEDCTS ENTLIKYMTD GILLRESLRE ADLDHYSAII
660 670 680 690 700
MDEAHERSLN TDVLFGLLRE VVARRSDLKL IVTSATMDAE KFAAFFGNVP
710 720 730 740 750
IFHIPGRTFP VDILFSKTPQ EDYVEAAVKQ SLQVHLSGAP GDILIFMPGQ
760 770 780 790 800
EDIEVTSDQI VEHLEELENA PALAVLPIYS QLPSDLQAKI FQKAPDGVRK
810 820 830 840 850
CIVATNIAET SLTVDGIMFV IDSGYCKLKV FNPRIGMDAL QIYPISQANA
860 870 880 890 900
NQRSGRAGRT GPGQCFRLYT QSAYKNELLT TTVPEIQRTN LANVVLLLKS
910 920 930 940 950
LGVQDLLQFH FMDPPPEDNM LNSMYQLWIL GALDNTGGLT STGRLMVEFP
960 970 980 990 1000
LDPALSKMLI VSCDMGCSSE ILLIVSMLSV PAIFYRPKGR EEESDQIREK
1010 1020 1030 1040 1050
FAVPESDHLT YLNVYLQWKN NNYSTIWCND HFIHAKAMRK VREVRAQLKD
1060 1070 1080 1090 1100
IMVQQRMSLA SCGTDWDIVR KCICAAYFHQ AAKLKGIGEY VNIRTGMPCH
1110 1120 1130 1140 1150
LHPTSSLFGM GYTPDYIVYH ELVMTTKEYM QCVTAVDGEW LAELGPMFYS
1160 1170 1180 1190 1200
VKQAGKSRQE NRRRAKEEAS AMEEEMALAE EQLRARRQEQ EKRSPLGSVR
1210 1220
STKIYTPGRK EQGEPMTPRR TPARFGL
Length:1,227
Mass (Da):140,503
Last modified:January 24, 2006 - v2
Checksum:i80D06118D0D465E5
GO
Isoform 2 (identifier: Q92620-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     99-786: Missing.

Note: No experimental confirmation available.
Show »
Length:539
Mass (Da):60,743
Checksum:i4BE6EB5D8640A4A9
GO

Sequence cautioni

The sequence BAA13213.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti1217 – 12171T → A.2 Publications
VAR_015518

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei99 – 786688Missing in isoform 2. 1 PublicationVSP_056045Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF038391 mRNA. Translation: AAC39729.1.
D86977 mRNA. Translation: BAA13213.2. Different initiation.
AK301074 mRNA. Translation: BAG62680.1.
AC009087 Genomic DNA. No translation available.
AC004682 Genomic DNA. Translation: AAC27431.1.
CH471166 Genomic DNA. Translation: EAW59180.1.
CH471166 Genomic DNA. Translation: EAW59190.1.
BC004235 mRNA. Translation: AAH04235.1.
BC008340 mRNA. Translation: AAH08340.1.
CCDSiCCDS10907.1. [Q92620-1]
RefSeqiNP_054722.2. NM_014003.3. [Q92620-1]
XP_011521786.1. XM_011523484.1. [Q92620-1]
XP_011521787.1. XM_011523485.1. [Q92620-1]
UniGeneiHs.151218.

Genome annotation databases

EnsembliENST00000268482; ENSP00000268482; ENSG00000140829. [Q92620-1]
GeneIDi9785.
KEGGihsa:9785.
UCSCiuc002fcb.4. human. [Q92620-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF038391 mRNA. Translation: AAC39729.1.
D86977 mRNA. Translation: BAA13213.2. Different initiation.
AK301074 mRNA. Translation: BAG62680.1.
AC009087 Genomic DNA. No translation available.
AC004682 Genomic DNA. Translation: AAC27431.1.
CH471166 Genomic DNA. Translation: EAW59180.1.
CH471166 Genomic DNA. Translation: EAW59190.1.
BC004235 mRNA. Translation: AAH04235.1.
BC008340 mRNA. Translation: AAH08340.1.
CCDSiCCDS10907.1. [Q92620-1]
RefSeqiNP_054722.2. NM_014003.3. [Q92620-1]
XP_011521786.1. XM_011523484.1. [Q92620-1]
XP_011521787.1. XM_011523485.1. [Q92620-1]
UniGeneiHs.151218.

3D structure databases

ProteinModelPortaliQ92620.
SMRiQ92620. Positions 493-704, 916-1155.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115129. 51 interactions.
IntActiQ92620. 14 interactions.
MINTiMINT-2813093.
STRINGi9606.ENSP00000268482.

PTM databases

iPTMnetiQ92620.
PhosphoSiteiQ92620.

Polymorphism and mutation databases

BioMutaiDHX38.
DMDMi85700389.

Proteomic databases

EPDiQ92620.
MaxQBiQ92620.
PaxDbiQ92620.
PeptideAtlasiQ92620.
PRIDEiQ92620.

Protocols and materials databases

DNASUi9785.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000268482; ENSP00000268482; ENSG00000140829. [Q92620-1]
GeneIDi9785.
KEGGihsa:9785.
UCSCiuc002fcb.4. human. [Q92620-1]

Organism-specific databases

CTDi9785.
GeneCardsiDHX38.
HGNCiHGNC:17211. DHX38.
HPAiHPA041347.
MIMi605584. gene.
neXtProtiNX_Q92620.
PharmGKBiPA27225.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0925. Eukaryota.
COG1643. LUCA.
GeneTreeiENSGT00840000129715.
HOGENOMiHOG000175261.
HOVERGENiHBG039428.
InParanoidiQ92620.
KOiK12815.
OMAiKNEMLTT.
OrthoDBiEOG7FXZXR.
PhylomeDBiQ92620.
TreeFamiTF105793.

Enzyme and pathway databases

ReactomeiR-HSA-109688. Cleavage of Growing Transcript in the Termination Region.
R-HSA-159236. Transport of Mature mRNA derived from an Intron-Containing Transcript.
R-HSA-72163. mRNA Splicing - Major Pathway.
R-HSA-72187. mRNA 3'-end processing.

Miscellaneous databases

ChiTaRSiDHX38. human.
GeneWikiiDHX38.
GenomeRNAii9785.
NextBioi35475455.
PROiQ92620.
SOURCEiSearch...

Gene expression databases

BgeeiQ92620.
CleanExiHS_DHX38.
ExpressionAtlasiQ92620. baseline and differential.
GenevisibleiQ92620. HS.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR011545. DEAD/DEAH_box_helicase_dom.
IPR002464. DNA/RNA_helicase_DEAH_CS.
IPR011709. DUF1605.
IPR007502. Helicase-assoc_dom.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00270. DEAD. 1 hit.
PF04408. HA2. 1 hit.
PF00271. Helicase_C. 1 hit.
PF07717. OB_NTP_bind. 1 hit.
[Graphical view]
SMARTiSM00487. DEXDc. 1 hit.
SM00847. HA2. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS00690. DEAH_ATP_HELICASE. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Human homologs of yeast prp16 and prp17 reveal conservation of the mechanism for catalytic step II of pre-mRNA splicing."
    Zhou Z., Reed R.
    EMBO J. 17:2095-2106(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ALA-1217.
  2. "Prediction of the coding sequences of unidentified human genes. VI. The coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis of cDNA clones from cell line KG-1 and brain."
    Nagase T., Seki N., Ishikawa K., Ohira M., Kawarabayasi Y., Ohara O., Tanaka A., Kotani H., Miyajima N., Nomura N.
    DNA Res. 3:321-329(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT ALA-1217.
    Tissue: Bone marrow.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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] (ISOFORM 2).
    Tissue: Spleen.
  5. "The sequence and analysis of duplication-rich human chromosome 16."
    Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
    , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
    Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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] (ISOFORM 1).
    Tissue: Brain and Placenta.
  8. Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.
    Submitted (DEC-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-12 AND 692-707, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT GLY-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Ovarian carcinoma.
  9. "Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis."
    Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.
    RNA 8:426-439(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE SPLICEOSOMAL C COMPLEX.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1194, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT GLY-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-260, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  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-199, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "System-wide analysis of SUMOylation dynamics in response to replication stress reveals novel small ubiquitin-like modified target proteins and acceptor lysines relevant for genome stability."
    Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V., Vertegaal A.C.
    Mol. Cell. Proteomics 14:1419-1434(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-482, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPRP16_HUMAN
AccessioniPrimary (citable) accession number: Q92620
Secondary accession number(s): B4DVG8
, D3DWS7, O75212, Q96HN7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 24, 2006
Last modified: May 11, 2016
This is version 163 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.