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Q9Y5B9

- SP16H_HUMAN

UniProt

Q9Y5B9 - SP16H_HUMAN

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Protein
FACT complex subunit SPT16
Gene
SUPT16H, FACT140, FACTP140
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Component of the FACT complex, a general chromatin factor that acts to reorganize nucleosomes. The FACT complex is involved in multiple processes that require DNA as a template such as mRNA elongation, DNA replication and DNA repair. During transcription elongation the FACT complex acts as a histone chaperone that both destabilizes and restores nucleosomal structure. It facilitates the passage of RNA polymerase II and transcription by promoting the dissociation of one histone H2A-H2B dimer from the nucleosome, then subsequently promotes the reestablishment of the nucleosome following the passage of RNA polymerase II. The FACT complex is probably also involved in phosphorylation of 'Ser-392' of p53/TP53 via its association with CK2 (casein kinase II). Also involved in vitamin D-coupled transcription regulation via its association with the WINAC complex, a chromatin-remodeling complex recruited by vitamin D receptor (VDR), which is required for the ligand-bound VDR-mediated transrepression of the CYP27B1 gene.7 Publications

GO - Molecular functioni

  1. poly(A) RNA binding Source: UniProtKB
  2. protein binding Source: IntAct

GO - Biological processi

  1. DNA repair Source: UniProtKB-KW
  2. DNA replication Source: UniProtKB-KW
  3. gene expression Source: Reactome
  4. nucleosome disassembly Source: ProtInc
  5. positive regulation of DNA-templated transcription, elongation Source: ProtInc
  6. positive regulation of viral transcription Source: Reactome
  7. transcription elongation from RNA polymerase II promoter Source: Reactome
  8. transcription from RNA polymerase II promoter Source: Reactome
  9. viral process Source: Reactome
Complete GO annotation...

Keywords - Biological processi

DNA damage, DNA repair, DNA replication, Transcription, Transcription regulation

Enzyme and pathway databases

ReactomeiREACT_22107. RNA Polymerase II Pre-transcription Events.
REACT_22201. Formation of HIV elongation complex in the absence of HIV Tat.
REACT_6143. Pausing and recovery of Tat-mediated HIV elongation.
REACT_6162. Tat-mediated elongation of the HIV-1 transcript.
REACT_6244. Pausing and recovery of HIV elongation.
REACT_6259. HIV elongation arrest and recovery.
REACT_6344. Tat-mediated HIV elongation arrest and recovery.
REACT_6346. Formation of HIV-1 elongation complex containing HIV-1 Tat.
REACT_833. RNA Polymerase II Transcription Elongation.

Protein family/group databases

MEROPSiM24.974.

Names & Taxonomyi

Protein namesi
Recommended name:
FACT complex subunit SPT16
Alternative name(s):
Chromatin-specific transcription elongation factor 140 kDa subunit
FACT 140 kDa subunit
FACTp140
Facilitates chromatin transcription complex subunit SPT16
Short name:
hSPT16
Gene namesi
Name:SUPT16H
Synonyms:FACT140, FACTP140
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 14

Organism-specific databases

HGNCiHGNC:11465. SUPT16H.

Subcellular locationi

Nucleus. Chromosome
Note: Colocalizes with RNA polymerase II on chromatin. Recruited to actively transcribed loci.1 Publication

GO - Cellular componenti

  1. chromosome Source: UniProtKB-SubCell
  2. nucleoplasm Source: Reactome
  3. nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA36251.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 10471046FACT complex subunit SPT16
PRO_0000245169Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine4 Publications
Modified residuei139 – 1391N6-acetyllysine1 Publication
Modified residuei188 – 1881Phosphoserine1 Publication
Modified residuei196 – 1961N6-acetyllysine1 Publication
Modified residuei223 – 2231N6-acetyllysine1 Publication
Modified residuei508 – 5081Phosphoserine1 Publication
Modified residuei513 – 5131N6-acetyllysine1 Publication
Modified residuei650 – 6501Phosphoserine2 Publications
Modified residuei658 – 6581Phosphoserine1 Publication
Modified residuei732 – 7321N6-acetyllysine1 Publication
Modified residuei786 – 7861N6-acetyllysine1 Publication
Modified residuei903 – 9031Phosphothreonine1 Publication
Modified residuei904 – 9041N6-acetyllysine1 Publication
Modified residuei979 – 9791Phosphoserine3 Publications
Modified residuei982 – 9821Phosphoserine3 Publications
Modified residuei986 – 9861Phosphoserine1 Publication
Modified residuei1015 – 10151Phosphoserine1 Publication

Post-translational modificationi

ADP-ribosylated. ADP-ribosylation by PARP1 is induced by genotoxic stress and correlates with dissociation of FACT from chromatin.

Keywords - PTMi

Acetylation, ADP-ribosylation, Phosphoprotein

Proteomic databases

MaxQBiQ9Y5B9.
PaxDbiQ9Y5B9.
PeptideAtlasiQ9Y5B9.
PRIDEiQ9Y5B9.

PTM databases

PhosphoSiteiQ9Y5B9.

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Gene expression databases

ArrayExpressiQ9Y5B9.
BgeeiQ9Y5B9.
CleanExiHS_SUPT16H.
GenevestigatoriQ9Y5B9.

Organism-specific databases

HPAiCAB022551.
HPA049787.

Interactioni

Subunit structurei

Interacts with MYOG (via C-terminal region) By similarity. Component of the FACT complex, a stable heterodimer of SSRP1 and SUPT16H. Also component of a CK2-SPT16-SSRP1 complex which forms following UV irradiation, composed of SSRP1, SUPT16H, CSNK2A1, CSNK2A2 and CSNK2B. Component of the WINAC complex, at least composed of SMARCA2, SMARCA4, SMARCB1, SMARCC1, SMARCC2, SMARCD1, SMARCE1, ACTL6A, BAZ1B/WSTF, ARID1A, SUPT16H, CHAF1A and TOP2B. Interacts with NEK9. Binds to histone H2A-H2B. Interacts with GTF2E2.6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
MCM4P339913EBI-1046849,EBI-374938
SSRP1Q089453EBI-1046849,EBI-353771

Protein-protein interaction databases

BioGridi116367. 80 interactions.
DIPiDIP-42757N.
IntActiQ9Y5B9. 25 interactions.
MINTiMINT-2823866.
STRINGi9606.ENSP00000216297.

Structurei

3D structure databases

ProteinModelPortaliQ9Y5B9.
SMRiQ9Y5B9. Positions 5-432, 511-604, 645-926.

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili432 – 50776 Reviewed prediction
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi926 – 101186Glu-rich (acidic)
Add
BLAST

Domaini

The C-terminal Glu-rich acidic region is essential for FACT activity.1 Publication

Sequence similaritiesi

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiCOG5406.
HOGENOMiHOG000209079.
HOVERGENiHBG092544.
InParanoidiQ9Y5B9.
OMAiYILTTQK.
OrthoDBiEOG7VQJC8.
PhylomeDBiQ9Y5B9.
TreeFamiTF300341.

Family and domain databases

Gene3Di3.40.350.10. 1 hit.
3.90.230.10. 1 hit.
InterProiIPR029149. Creatin/AminoP/Spt16_NTD.
IPR013719. DUF1747.
IPR029148. FACT-Spt16_Nlobe.
IPR013953. FACT_Spt16p.
IPR000994. Pept_M24_structural-domain.
[Graphical view]
PfamiPF14826. FACT-Spt16_Nlob. 1 hit.
PF00557. Peptidase_M24. 1 hit.
PF08512. Rtt106. 1 hit.
PF08644. SPT16. 1 hit.
[Graphical view]
SUPFAMiSSF55920. SSF55920. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q9Y5B9-1 [UniParc]FASTAAdd to Basket

« Hide

MAVTLDKDAY YRRVKRLYSN WRKGEDEYAN VDAIVVSVGV DEEIVYAKST     50
ALQTWLFGYE LTDTIMVFCD DKIIFMASKK KVEFLKQIAN TKGNENANGA 100
PAITLLIREK NESNKSSFDK MIEAIKESKN GKKIGVFSKD KFPGEFMKSW 150
NDCLNKEGFD KIDISAVVAY TIAVKEDGEL NLMKKAASIT SEVFNKFFKE 200
RVMEIVDADE KVRHSKLAES VEKAIEEKKY LAGADPSTVE MCYPPIIQSG 250
GNYNLKFSVV SDKNHMHFGA ITCAMGIRFK SYCSNLVRTL MVDPSQEVQE 300
NYNFLLQLQE ELLKELRHGV KICDVYNAVM DVVKKQKPEL LNKITKNLGF 350
GMGIEFREGS LVINSKNQYK LKKGMVFSIN LGFSDLTNKE GKKPEEKTYA 400
LFIGDTVLVD EDGPATVLTS VKKKVKNVGI FLKNEDEEEE EEEKDEAEDL 450
LGRGSRAALL TERTRNEMTA EEKRRAHQKE LAAQLNEEAK RRLTEQKGEQ 500
QIQKARKSNV SYKNPSLMPK EPHIREMKIY IDKKYETVIM PVFGIATPFH 550
IATIKNISMS VEGDYTYLRI NFYCPGSALG RNEGNIFPNP EATFVKEITY 600
RASNIKAPGE QTVPALNLQN AFRIIKEVQK RYKTREAEEK EKEGIVKQDS 650
LVINLNRSNP KLKDLYIRPN IAQKRMQGSL EAHVNGFRFT SVRGDKVDIL 700
YNNIKHALFQ PCDGEMIIVL HFHLKNAIMF GKKRHTDVQF YTEVGEITTD 750
LGKHQHMHDR DDLYAEQMER EMRHKLKTAF KNFIEKVEAL TKEELEFEVP 800
FRDLGFNGAP YRSTCLLQPT SSALVNATEW PPFVVTLDEV ELIHFERVQF 850
HLKNFDMVIV YKDYSKKVTM INAIPVASLD PIKEWLNSCD LKYTEGVQSL 900
NWTKIMKTIV DDPEGFFEQG GWSFLEPEGE GSDAEEGDSE SEIEDETFNP 950
SEDDYEEEEE DSDEDYSSEA EESDYSKESL GSEEESGKDW DELEEEARKA 1000
DRESRYEEEE EQSRSMSRKR KASVHSSGRG SNRGSRHSSA PPKKKRK 1047
Length:1,047
Mass (Da):119,914
Last modified:November 1, 1999 - v1
Checksum:i3E1B23C45BDC61C2
GO

Sequence cautioni

The sequence AAH64561.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.
The sequence AAH73849.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF152961 mRNA. Translation: AAD43978.1.
BC000565 mRNA. Translation: AAH00565.1.
BC014046 mRNA. Translation: AAH14046.1.
BC064561 mRNA. Translation: AAH64561.1. Sequence problems.
BC073849 mRNA. Translation: AAH73849.1. Sequence problems.
AF164924 mRNA. Translation: AAF28231.1.
CCDSiCCDS9569.1.
RefSeqiNP_009123.1. NM_007192.3.
UniGeneiHs.213724.

Genome annotation databases

EnsembliENST00000216297; ENSP00000216297; ENSG00000092201.
GeneIDi11198.
KEGGihsa:11198.
UCSCiuc001wao.2. human.

Polymorphism databases

DMDMi74753511.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF152961 mRNA. Translation: AAD43978.1 .
BC000565 mRNA. Translation: AAH00565.1 .
BC014046 mRNA. Translation: AAH14046.1 .
BC064561 mRNA. Translation: AAH64561.1 . Sequence problems.
BC073849 mRNA. Translation: AAH73849.1 . Sequence problems.
AF164924 mRNA. Translation: AAF28231.1 .
CCDSi CCDS9569.1.
RefSeqi NP_009123.1. NM_007192.3.
UniGenei Hs.213724.

3D structure databases

ProteinModelPortali Q9Y5B9.
SMRi Q9Y5B9. Positions 5-432, 511-604, 645-926.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116367. 80 interactions.
DIPi DIP-42757N.
IntActi Q9Y5B9. 25 interactions.
MINTi MINT-2823866.
STRINGi 9606.ENSP00000216297.

Protein family/group databases

MEROPSi M24.974.

PTM databases

PhosphoSitei Q9Y5B9.

Polymorphism databases

DMDMi 74753511.

Proteomic databases

MaxQBi Q9Y5B9.
PaxDbi Q9Y5B9.
PeptideAtlasi Q9Y5B9.
PRIDEi Q9Y5B9.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000216297 ; ENSP00000216297 ; ENSG00000092201 .
GeneIDi 11198.
KEGGi hsa:11198.
UCSCi uc001wao.2. human.

Organism-specific databases

CTDi 11198.
GeneCardsi GC14M021819.
HGNCi HGNC:11465. SUPT16H.
HPAi CAB022551.
HPA049787.
MIMi 605012. gene.
neXtProti NX_Q9Y5B9.
PharmGKBi PA36251.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5406.
HOGENOMi HOG000209079.
HOVERGENi HBG092544.
InParanoidi Q9Y5B9.
OMAi YILTTQK.
OrthoDBi EOG7VQJC8.
PhylomeDBi Q9Y5B9.
TreeFami TF300341.

Enzyme and pathway databases

Reactomei REACT_22107. RNA Polymerase II Pre-transcription Events.
REACT_22201. Formation of HIV elongation complex in the absence of HIV Tat.
REACT_6143. Pausing and recovery of Tat-mediated HIV elongation.
REACT_6162. Tat-mediated elongation of the HIV-1 transcript.
REACT_6244. Pausing and recovery of HIV elongation.
REACT_6259. HIV elongation arrest and recovery.
REACT_6344. Tat-mediated HIV elongation arrest and recovery.
REACT_6346. Formation of HIV-1 elongation complex containing HIV-1 Tat.
REACT_833. RNA Polymerase II Transcription Elongation.

Miscellaneous databases

ChiTaRSi SUPT16H. human.
GeneWikii SUPT16H.
GenomeRNAii 11198.
NextBioi 42621.
PROi Q9Y5B9.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9Y5B9.
Bgeei Q9Y5B9.
CleanExi HS_SUPT16H.
Genevestigatori Q9Y5B9.

Family and domain databases

Gene3Di 3.40.350.10. 1 hit.
3.90.230.10. 1 hit.
InterProi IPR029149. Creatin/AminoP/Spt16_NTD.
IPR013719. DUF1747.
IPR029148. FACT-Spt16_Nlobe.
IPR013953. FACT_Spt16p.
IPR000994. Pept_M24_structural-domain.
[Graphical view ]
Pfami PF14826. FACT-Spt16_Nlob. 1 hit.
PF00557. Peptidase_M24. 1 hit.
PF08512. Rtt106. 1 hit.
PF08644. SPT16. 1 hit.
[Graphical view ]
SUPFAMi SSF55920. SSF55920. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The chromatin-specific transcription elongation factor FACT comprises human SPT16 and SSRP1 proteins."
    Orphanides G., Wu W.-H., Lane W.S., Hampsey M., Reinberg D.
    Nature 400:284-288(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, INTERACTION WITH SSRP1; H2A AND H2B.
  2. "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 1-638.
    Tissue: Brain, Eye and Testis.
  3. Bienvenut W.V., Boldt K., von Kriegsheim A.F., Kolch W.
    Submitted (JUL-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-12 AND 480-490, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Hepatoma.
  4. Bienvenut W.V., Vousden K.H., Lukashchuk N.
    Submitted (MAR-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-12; 93-108 AND 582-596, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Lung carcinoma.
  5. "Functional interaction of general transcription initiation factor TFIIE with general chromatin factor SPT16/CDC68."
    Kang S.-W., Kuzuhara T., Horikoshi M.
    Genes Cells 5:251-263(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 801-1047, TISSUE SPECIFICITY, INTERACTION WITH GTF2E2.
  6. "FACT, a factor that facilitates transcript elongation through nucleosomes."
    Orphanides G., LeRoy G., Chang C.-H., Luse D.S., Reinberg D.
    Cell 92:105-116(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "Requirement of RSF and FACT for transcription of chromatin templates in vitro."
    LeRoy G., Orphanides G., Lane W.S., Reinberg D.
    Science 282:1900-1904(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "FACT relieves DSIF/NELF-mediated inhibition of transcriptional elongation and reveals functional differences between P-TEFb and TFIIH."
    Wada T., Orphanides G., Hasegawa J., Kim D.-K., Shima D., Yamaguchi Y., Fukuda A., Hisatake K., Oh S., Reinberg D., Handa H.
    Mol. Cell 5:1067-1072(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. "A DNA damage-induced p53 serine 392 kinase complex contains CK2, hSpt16, and SSRP1."
    Keller D.M., Zeng X., Wang Y., Zhang Q.H., Kapoor M., Shu H., Goodman R., Lozano G., Zhao Y., Lu H.
    Mol. Cell 7:283-292(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH SSRP1; CSNK2A1; CSNK2A2 AND CSNK2B.
  10. "p53 serine 392 phosphorylation increases after UV through induction of the assembly of the CK2.hSPT16.SSRP1 complex."
    Keller D.M., Lu H.
    J. Biol. Chem. 277:50206-50213(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SSRP1; CSNK2A1; CSNK2A2 AND CSNK2B.
  11. "The chromatin-remodeling complex WINAC targets a nuclear receptor to promoters and is impaired in Williams syndrome."
    Kitagawa H., Fujiki R., Yoshimura K., Mezaki Y., Uematsu Y., Matsui D., Ogawa S., Unno K., Okubo M., Tokita A., Nakagawa T., Ito T., Ishimi Y., Nagasawa H., Matsumoto T., Yanagisawa J., Kato S.
    Cell 113:905-917(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE WINAC COMPLEX, FUNCTION.
  12. Cited for: FUNCTION, DOMAIN.
  13. "Nek9, a novel FACT-associated protein, modulates interphase progression."
    Tan B.C.-M., Lee S.-C.
    J. Biol. Chem. 279:9321-9330(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NEK9.
  14. "Histone H2B monoubiquitination functions cooperatively with FACT to regulate elongation by RNA polymerase II."
    Pavri R., Zhu B., Li G., Trojer P., Mandal S., Shilatifard A., Reinberg D.
    Cell 125:703-717(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  15. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-979 AND SER-982, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  16. "Modulation of nucleosome-binding activity of FACT by poly(ADP-ribosyl)ation."
    Huang J.-Y., Chen W.-H., Chang Y.-L., Wang H.-T., Chuang W.-T., Lee S.-C.
    Nucleic Acids Res. 34:2398-2407(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: ADP-RIBOSYLATION.
  17. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-508 AND SER-1015, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  18. "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].
  19. "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-139; LYS-196; LYS-223; LYS-513; LYS-732; LYS-786 AND LYS-904, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. "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-650; THR-903; SER-979 AND SER-982, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  21. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  22. "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-188; SER-650; SER-658; SER-979; SER-982 AND SER-986, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  23. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  24. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiSP16H_HUMAN
AccessioniPrimary (citable) accession number: Q9Y5B9
Secondary accession number(s): Q6GMT8
, Q6P2F1, Q6PJM1, Q9NRX0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2006
Last sequence update: November 1, 1999
Last modified: September 3, 2014
This is version 117 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

Caution

Although related to the peptidase M24 family, this protein lacks conserved active site residues suggesting that it may lack peptidase activity.

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 14
    Human chromosome 14: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. Peptidase families
    Classification of peptidase families and list of entries
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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