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Protein

Pre-mRNA-splicing factor 38B

Gene

PRPF38B

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

Functioni

May be required for pre-mRNA splicing.Curated

GO - Molecular functioni

  1. poly(A) RNA binding Source: UniProtKB

GO - Biological processi

  1. mRNA processing Source: UniProtKB-KW
  2. RNA splicing Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

mRNA processing, mRNA splicing

Names & Taxonomyi

Protein namesi
Recommended name:
Pre-mRNA-splicing factor 38B
Alternative name(s):
Sarcoma antigen NY-SAR-27
Gene namesi
Name:PRPF38B
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:25512. PRPF38B.

Subcellular locationi

Nucleus Curated

GO - Cellular componenti

  1. precatalytic spliceosome Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Nucleus, Spliceosome

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA142671126.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 546545Pre-mRNA-splicing factor 38BPRO_0000287235Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei227 – 2271N6-acetyllysine1 Publication
Modified residuei320 – 3201Phosphoserine1 Publication
Modified residuei448 – 4481Phosphoserine1 Publication
Modified residuei473 – 4731Phosphoserine1 Publication
Modified residuei475 – 4751Phosphoserine1 Publication
Modified residuei481 – 4811Phosphoserine1 Publication
Modified residuei527 – 5271Phosphoserine4 Publications
Modified residuei529 – 5291Phosphoserine4 Publications
Modified residuei534 – 5341Phosphoserine2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ5VTL8.
PaxDbiQ5VTL8.
PRIDEiQ5VTL8.

PTM databases

PhosphoSiteiQ5VTL8.

Expressioni

Gene expression databases

BgeeiQ5VTL8.
CleanExiHS_PRPF38B.
GenevestigatoriQ5VTL8.

Organism-specific databases

HPAiHPA053255.

Interactioni

Protein-protein interaction databases

BioGridi120428. 5 interactions.
IntActiQ5VTL8. 7 interactions.
MINTiMINT-4654815.

Structurei

3D structure databases

ProteinModelPortaliQ5VTL8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili292 – 32130Sequence AnalysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi253 – 451199Arg-richAdd
BLAST

Sequence similaritiesi

Belongs to the PRP38 family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG266713.
GeneTreeiENSGT00730000111145.
HOVERGENiHBG101033.
InParanoidiQ5VTL8.
KOiK12850.
OMAiQIKSRPR.
OrthoDBiEOG7XH6R2.
PhylomeDBiQ5VTL8.
TreeFamiTF313626.

Family and domain databases

InterProiIPR005037. PRP38.
[Graphical view]
PANTHERiPTHR23142. PTHR23142. 1 hit.
PfamiPF03371. PRP38. 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: Q5VTL8-1) [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
MANNSPALTG NSQPQHQAAA AAAQQQQQCG GGGATKPAVS GKQGNVLPLW
60 70 80 90 100
GNEKTMNLNP MILTNILSSP YFKVQLYELK TYHEVVDEIY FKVTHVEPWE
110 120 130 140 150
KGSRKTAGQT GMCGGVRGVG TGGIVSTAFC LLYKLFTLKL TRKQVMGLIT
160 170 180 190 200
HTDSPYIRAL GFMYIRYTQP PTDLWDWFES FLDDEEDLDV KAGGGCVMTI
210 220 230 240 250
GEMLRSFLTK LEWFSTLFPR IPVPVQKNID QQIKTRPRKI KKDGKEGAEE
260 270 280 290 300
IDRHVERRRS RSPRRSLSPR RSPRRSRSRS HHREGHGSSS FDRELEREKE
310 320 330 340 350
RQRLEREAKE REKERRRSRS IDRGLERRRS RSRERHRSRS RSRDRKGDRR
360 370 380 390 400
DRDREREKEN ERGRRRDRDY DKERGNEREK ERERSRERSK EQRSRGEVEE
410 420 430 440 450
KKHKEDKDDR RHRDDKRDSK KEKKHSRSRS RERKHRSRSR SRNAGKRSRS
460 470 480 490 500
RSKEKSSKHK NESKEKSNKR SRSGSQGRTD SVEKSKKREH SPSKEKSRKR
510 520 530 540
SRSKERSHKR DHSDSKDQSD KHDRRRSQSI EQESQEKQHK NKDETV
Length:546
Mass (Da):64,468
Last modified:December 6, 2004 - v1
Checksum:iA3082DCF491F88F8
GO
Isoform 2 (identifier: Q5VTL8-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     187-190: DLDV → FFTL
     191-546: Missing.

Show »
Length:190
Mass (Da):21,061
Checksum:iBA711597136F2BBD
GO

Sequence cautioni

The sequence AAO65168.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence CAH72070.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence CAI12934.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti52 – 521N → S in BAA91546 (PubMed:14702039).Curated
Sequence conflicti294 – 2952EL → DR in AAH40127 (PubMed:15489334).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei187 – 1904DLDV → FFTL in isoform 2. 1 PublicationVSP_025408
Alternative sequencei191 – 546356Missing in isoform 2. 1 PublicationVSP_025409Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK001192 mRNA. Translation: BAA91546.1.
AL591719, AL160171 Genomic DNA. Translation: CAH72068.1.
AL591719, AL160171 Genomic DNA. Translation: CAH72069.1.
AL591719, AL160171 Genomic DNA. Translation: CAH72070.1. Sequence problems.
AL160171, AL591719 Genomic DNA. Translation: CAI12932.1.
AL160171, AL591719 Genomic DNA. Translation: CAI12933.1.
AL160171, AL591719 Genomic DNA. Translation: CAI12934.1. Sequence problems.
BC007757 mRNA. Translation: AAH07757.1. Different termination.
BC016296 mRNA. Translation: AAH16296.1. Different termination.
BC024275 mRNA. Translation: AAH24275.1. Different termination.
BC040127 mRNA. Translation: AAH40127.1. Different termination.
BC053838 mRNA. Translation: AAH53838.1.
BC107801 mRNA. Translation: AAI07802.1. Different termination.
BC130346 mRNA. Translation: AAI30347.1.
BC132963 mRNA. Translation: AAI32964.1.
AY211915 mRNA. Translation: AAO65168.1. Different initiation.
CCDSiCCDS788.1. [Q5VTL8-1]
RefSeqiNP_060531.2. NM_018061.2. [Q5VTL8-1]
UniGeneiHs.342307.

Genome annotation databases

EnsembliENST00000370022; ENSP00000359039; ENSG00000134186. [Q5VTL8-2]
ENST00000370025; ENSP00000359042; ENSG00000134186. [Q5VTL8-1]
GeneIDi55119.
KEGGihsa:55119.
UCSCiuc001dvv.4. human. [Q5VTL8-1]

Polymorphism databases

DMDMi74746965.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK001192 mRNA. Translation: BAA91546.1.
AL591719, AL160171 Genomic DNA. Translation: CAH72068.1.
AL591719, AL160171 Genomic DNA. Translation: CAH72069.1.
AL591719, AL160171 Genomic DNA. Translation: CAH72070.1. Sequence problems.
AL160171, AL591719 Genomic DNA. Translation: CAI12932.1.
AL160171, AL591719 Genomic DNA. Translation: CAI12933.1.
AL160171, AL591719 Genomic DNA. Translation: CAI12934.1. Sequence problems.
BC007757 mRNA. Translation: AAH07757.1. Different termination.
BC016296 mRNA. Translation: AAH16296.1. Different termination.
BC024275 mRNA. Translation: AAH24275.1. Different termination.
BC040127 mRNA. Translation: AAH40127.1. Different termination.
BC053838 mRNA. Translation: AAH53838.1.
BC107801 mRNA. Translation: AAI07802.1. Different termination.
BC130346 mRNA. Translation: AAI30347.1.
BC132963 mRNA. Translation: AAI32964.1.
AY211915 mRNA. Translation: AAO65168.1. Different initiation.
CCDSiCCDS788.1. [Q5VTL8-1]
RefSeqiNP_060531.2. NM_018061.2. [Q5VTL8-1]
UniGeneiHs.342307.

3D structure databases

ProteinModelPortaliQ5VTL8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120428. 5 interactions.
IntActiQ5VTL8. 7 interactions.
MINTiMINT-4654815.

PTM databases

PhosphoSiteiQ5VTL8.

Polymorphism databases

DMDMi74746965.

Proteomic databases

MaxQBiQ5VTL8.
PaxDbiQ5VTL8.
PRIDEiQ5VTL8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000370022; ENSP00000359039; ENSG00000134186. [Q5VTL8-2]
ENST00000370025; ENSP00000359042; ENSG00000134186. [Q5VTL8-1]
GeneIDi55119.
KEGGihsa:55119.
UCSCiuc001dvv.4. human. [Q5VTL8-1]

Organism-specific databases

CTDi55119.
GeneCardsiGC01P109234.
HGNCiHGNC:25512. PRPF38B.
HPAiHPA053255.
neXtProtiNX_Q5VTL8.
PharmGKBiPA142671126.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG266713.
GeneTreeiENSGT00730000111145.
HOVERGENiHBG101033.
InParanoidiQ5VTL8.
KOiK12850.
OMAiQIKSRPR.
OrthoDBiEOG7XH6R2.
PhylomeDBiQ5VTL8.
TreeFamiTF313626.

Miscellaneous databases

ChiTaRSiPRPF38B. human.
GenomeRNAii55119.
NextBioi58764.
PROiQ5VTL8.

Gene expression databases

BgeeiQ5VTL8.
CleanExiHS_PRPF38B.
GenevestigatoriQ5VTL8.

Family and domain databases

InterProiIPR005037. PRP38.
[Graphical view]
PANTHERiPTHR23142. PTHR23142. 1 hit.
PfamiPF03371. PRP38. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  2. "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(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Tissue: Lung, Muscle, Skin and Testis.
  4. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 402-546 (ISOFORM 1).
  5. "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(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  6. "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(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-527 AND SER-529, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-527; SER-529 AND SER-534, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "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(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  9. "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(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-227, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "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(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-448; SER-527; SER-529 AND SER-534, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "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(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-320; SER-473; SER-475; SER-481; SER-527 AND SER-529, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPR38B_HUMAN
AccessioniPrimary (citable) accession number: Q5VTL8
Secondary accession number(s): Q05DD6
, Q32Q58, Q5VTL9, Q6PK39, Q7Z6E2, Q86WF3, Q8IWG9, Q9NW40
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 14, 2007
Last sequence update: December 6, 2004
Last modified: February 3, 2015
This is version 88 of the entry and version 1 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.