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Q5VTL8

- PR38B_HUMAN

UniProt

Q5VTL8 - PR38B_HUMAN

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Protein
Pre-mRNA-splicing factor 38B
Gene
PRPF38B
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

May be required for pre-mRNA splicing Reviewed prediction.

GO - Molecular functioni

  1. poly(A) RNA binding Source: UniProtKB

GO - Biological processi

  1. RNA splicing Source: UniProtKB-KW
  2. mRNA processing 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: Chromosome 1

Organism-specific databases

HGNCiHGNC:25512. PRPF38B.

Subcellular locationi

Nucleus Reviewed prediction

GO - Cellular componenti

  1. spliceosomal complex Source: UniProtKB-KW
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 38B
PRO_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. 3 interactions.
IntActiQ5VTL8. 7 interactions.
MINTiMINT-4654815.

Structurei

3D structure databases

ProteinModelPortaliQ5VTL8.

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili292 – 32130 Reviewed prediction
Add
BLAST

Compositional bias

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

Sequence similaritiesi

Belongs to the PRP38 family.

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG266713.
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. Align

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

MANNSPALTG NSQPQHQAAA AAAQQQQQCG GGGATKPAVS GKQGNVLPLW    50
GNEKTMNLNP MILTNILSSP YFKVQLYELK TYHEVVDEIY FKVTHVEPWE 100
KGSRKTAGQT GMCGGVRGVG TGGIVSTAFC LLYKLFTLKL TRKQVMGLIT 150
HTDSPYIRAL GFMYIRYTQP PTDLWDWFES FLDDEEDLDV KAGGGCVMTI 200
GEMLRSFLTK LEWFSTLFPR IPVPVQKNID QQIKTRPRKI KKDGKEGAEE 250
IDRHVERRRS RSPRRSLSPR RSPRRSRSRS HHREGHGSSS FDRELEREKE 300
RQRLEREAKE REKERRRSRS IDRGLERRRS RSRERHRSRS RSRDRKGDRR 350
DRDREREKEN ERGRRRDRDY DKERGNEREK ERERSRERSK EQRSRGEVEE 400
KKHKEDKDDR RHRDDKRDSK KEKKHSRSRS RERKHRSRSR SRNAGKRSRS 450
RSKEKSSKHK NESKEKSNKR SRSGSQGRTD SVEKSKKREH SPSKEKSRKR 500
SRSKERSHKR DHSDSKDQSD KHDRRRSQSI EQESQEKQHK NKDETV 546
Length:546
Mass (Da):64,468
Last modified:December 7, 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.
The sequence CAH72070.1 differs from that shown. Reason: Erroneous gene model prediction.
The sequence CAI12934.1 differs from that shown. Reason: Erroneous gene model prediction.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei187 – 1904DLDV → FFTL in isoform 2.
VSP_025408
Alternative sequencei191 – 546356Missing in isoform 2.
VSP_025409Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti52 – 521N → S in BAA91546. 1 Publication
Sequence conflicti294 – 2952EL → DR in AAH40127. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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.
CCDSi CCDS788.1. [Q5VTL8-1 ]
RefSeqi NP_060531.2. NM_018061.2. [Q5VTL8-1 ]
UniGenei Hs.342307.

3D structure databases

ProteinModelPortali Q5VTL8.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 120428. 3 interactions.
IntActi Q5VTL8. 7 interactions.
MINTi MINT-4654815.

PTM databases

PhosphoSitei Q5VTL8.

Polymorphism databases

DMDMi 74746965.

Proteomic databases

MaxQBi Q5VTL8.
PaxDbi Q5VTL8.
PRIDEi Q5VTL8.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000370022 ; ENSP00000359039 ; ENSG00000134186 . [Q5VTL8-2 ]
ENST00000370025 ; ENSP00000359042 ; ENSG00000134186 . [Q5VTL8-1 ]
GeneIDi 55119.
KEGGi hsa:55119.
UCSCi uc001dvv.4. human. [Q5VTL8-1 ]

Organism-specific databases

CTDi 55119.
GeneCardsi GC01P109234.
HGNCi HGNC:25512. PRPF38B.
HPAi HPA053255.
neXtProti NX_Q5VTL8.
PharmGKBi PA142671126.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG266713.
HOVERGENi HBG101033.
InParanoidi Q5VTL8.
KOi K12850.
OMAi QIKSRPR.
OrthoDBi EOG7XH6R2.
PhylomeDBi Q5VTL8.
TreeFami TF313626.

Miscellaneous databases

ChiTaRSi PRPF38B. human.
GenomeRNAii 55119.
NextBioi 58764.
PROi Q5VTL8.

Gene expression databases

Bgeei Q5VTL8.
CleanExi HS_PRPF38B.
Genevestigatori Q5VTL8.

Family and domain databases

InterProi IPR005037. PRP38.
[Graphical view ]
PANTHERi PTHR23142. PTHR23142. 1 hit.
Pfami PF03371. PRP38. 1 hit.
[Graphical view ]
ProtoNeti Search...

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(2004) [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(2006) [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(2004) [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(2006) [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(2006) [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(2009) [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(2009) [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(2010) [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(2011) [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 15, 2007
Last sequence update: December 7, 2004
Last modified: July 9, 2014
This is version 84 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

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