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O55201

- SPT5H_MOUSE

UniProt

O55201 - SPT5H_MOUSE

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Protein

Transcription elongation factor SPT5

Gene

Supt5h

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Component of the DRB sensitivity-inducing factor complex (DSIF complex), which regulates mRNA processing and transcription elongation by RNA polymerase II. DSIF positively regulates mRNA capping by stimulating the mRNA guanylyltransferase activity of RNGTT/CAP1A. DSIF also acts cooperatively with the negative elongation factor complex (NELF complex) to enhance transcriptional pausing at sites proximal to the promoter. Transcriptional pausing may facilitate the assembly of an elongation competent RNA polymerase II complex. DSIF and NELF promote pausing by inhibition of the transcription elongation factor TFIIS/S-II. TFIIS/S-II binds to RNA polymerase II at transcription pause sites and stimulates the weak intrinsic nuclease activity of the enzyme. Cleavage of blocked transcripts by RNA polymerase II promotes the resumption of transcription from the new 3' terminus and may allow repeated attempts at transcription through natural pause sites (By similarity).By similarity

GO - Molecular functioni

  1. chromatin binding Source: MGI
  2. poly(A) RNA binding Source: Ensembl

GO - Biological processi

  1. negative regulation of DNA-templated transcription, elongation Source: Ensembl
  2. negative regulation of transcription from RNA polymerase II promoter Source: Ensembl
  3. positive regulation of DNA-templated transcription, elongation Source: Ensembl
  4. positive regulation of macroautophagy Source: Ensembl
  5. positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
  6. transcription elongation from RNA polymerase II promoter Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Activator, Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Enzyme and pathway databases

ReactomeiREACT_203462. Formation of the Early Elongation Complex.
REACT_226490. RNA Polymerase II Transcription Elongation.

Names & Taxonomyi

Protein namesi
Recommended name:
Transcription elongation factor SPT5
Alternative name(s):
DRB sensitivity-inducing factor large subunit
Short name:
DSIF large subunit
Gene namesi
Name:Supt5h
Synonyms:Supt5
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 7

Organism-specific databases

MGIiMGI:1202400. Supt5.

Subcellular locationi

Nucleus By similarity

GO - Cellular componenti

  1. DSIF complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10821082Transcription elongation factor SPT5PRO_0000208469Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei664 – 6641Phosphoserine1 Publication
Modified residuei690 – 6901Asymmetric dimethylarginine; alternateBy similarity
Modified residuei690 – 6901Omega-N-methylarginine; alternateBy similarity
Modified residuei690 – 6901Omega-N-methylated arginine; alternateBy similarity
Modified residuei692 – 6921Asymmetric dimethylarginine; alternateBy similarity
Modified residuei692 – 6921Omega-N-methylarginine; alternateBy similarity
Modified residuei692 – 6921Omega-N-methylated arginine; alternateBy similarity
Modified residuei692 – 6921Symmetric dimethylarginine; alternateBy similarity
Modified residuei712 – 7121N6-acetyllysine1 Publication
Modified residuei769 – 7691Phosphothreonine; by CDK9By similarity
Modified residuei778 – 7781Phosphothreonine; by CDK9By similarity
Modified residuei1028 – 10281PhosphothreonineBy similarity

Post-translational modificationi

Methylated by PRMT1/HRMT1L2 and PRMT5/SKB1. Methylation negatively regulates interaction with P-TEFb and RNA polymerase II (By similarity).By similarity
Phosphorylated by CDK7 and CDK9. Phosphorylation by P-TEFb alleviates transcriptional pausing. Phosphorylation may also stimulate interaction with PIN1. Bulk phosphorylation occurs predominantly in mitosis (By similarity).By similarity

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Proteomic databases

MaxQBiO55201.
PaxDbiO55201.
PRIDEiO55201.

PTM databases

PhosphoSiteiO55201.

Expressioni

Gene expression databases

BgeeiO55201.
CleanExiMM_SUPT5H.
GenevestigatoriO55201.

Interactioni

Subunit structurei

Interacts with SUPT4H1 to form DSIF. DSIF interacts with the positive transcription elongation factor b complex (P-TEFb complex), which is composed of CDK9 and cyclin-T (CCNT1 or CCNT2). DSIF interacts with RNA polymerase II, and this interaction is reduced by phosphorylation of the C-terminal domain (CTD) of POLR2A by P-TEFb. DSIF also interacts with the NELF complex, which is composed of WHSC2/NELFA, COBRA1/NELFB, TH1L/NELFD and RDBP/NELFE, and this interaction occurs following prior binding of DSIF to RNA polymerase II. Also interacts with PRMT1/HRMT1L2, HTATSF1/TATSF1, RNGTT/CAP1A, PRMT5/SKB1, SUPT6H, and can interact with PIN1. Component of a complex which is at least composed of HTATSF1/Tat-SF1, the P-TEFb complex components CDK9 and CCNT1, RNA polymerase II, SUPT5H, and NCL/nucleolin (By similarity).By similarity

Protein-protein interaction databases

BioGridi203575. 14 interactions.
IntActiO55201. 1 interaction.
MINTiMINT-4105191.

Structurei

3D structure databases

ProteinModelPortaliO55201.
SMRiO55201. Positions 174-309, 411-521, 696-751.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini271 – 30434KOW 1Add
BLAST
Domaini418 – 44932KOW 2Add
BLAST
Domaini470 – 50132KOW 3Add
BLAST
Domaini592 – 62534KOW 4Add
BLAST
Domaini698 – 73134KOW 5Add
BLAST
Repeati748 – 7536CTR1-1; approximate
Repeati754 – 7596CTR1-2
Repeati760 – 7656CTR1-3
Repeati766 – 7727CTR1-4
Repeati775 – 7817CTR1-5
Repeati782 – 7887CTR1-6
Repeati790 – 7967CTR1-7
Repeati797 – 8037CTR1-8
Repeati805 – 8117CTR1-9
Repeati838 – 8458CTR2-1
Repeati848 – 8569CTR2-2; approximate
Repeati857 – 8637CTR2-3; approximate
Repeati875 – 8795CTR2-4; half-length
Repeati890 – 8967CTR2-5; approximate
Repeati898 – 9058CTR2-6
Repeati910 – 9156CTR2-7; approximate
Repeati918 – 9247CTR2-8
Repeati926 – 9338CTR2-9
Repeati937 – 9448CTR2-10

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni174 – 26895Interaction with SUPT4H1 and SUPT4H2By similarityAdd
BLAST
Regioni311 – 418108Interaction with RNA polymerase IIBy similarityAdd
BLAST
Regioni748 – 811649 X 7 AA approximate tandem repeats of G-S-[QR]-T-P-X-[YQ], motif CTR1Add
BLAST
Regioni838 – 94410710 X 8 AA approximate tandem repeats of P-[TS]-P-S-P-[QA]-[SG]-Y, motif CTR2Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi11 – 10494Glu-richAdd
BLAST

Sequence similaritiesi

Belongs to the SPT5 family.Curated
Contains 5 KOW domains.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG0250.
GeneTreeiENSGT00440000037640.
HOVERGENiHBG079775.
InParanoidiO55201.
KOiK15172.
OMAiAFFDIEA.
OrthoDBiEOG7Z3F3Q.
PhylomeDBiO55201.
TreeFamiTF105730.

Family and domain databases

InterProiIPR005824. KOW.
IPR006645. NGN_dom.
IPR024945. Spt5_C_dom.
IPR022581. Spt5_N.
IPR017071. TF_Spt5.
IPR005100. TF_Spt5_NGN-domain.
IPR008991. Translation_prot_SH3-like.
[Graphical view]
PfamiPF00467. KOW. 2 hits.
PF03439. Spt5-NGN. 1 hit.
PF11942. Spt5_N. 1 hit.
[Graphical view]
PIRSFiPIRSF036945. Spt5. 1 hit.
SMARTiSM01104. CTD. 1 hit.
SM00739. KOW. 6 hits.
SM00738. NGN. 1 hit.
[Graphical view]
SUPFAMiSSF50104. SSF50104. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O55201-1) [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
MSDSEDSNFS EEEDSERSSE AEEAEVEEDQ RSAAGSEKEE EPEEEEEEEE
60 70 80 90 100
EYDEEEEEED DDRPPKKPRH GGFILDEADV DDEYEDEDQW EDGAEDILEK
110 120 130 140 150
EEIEASNIDN VVLDEDRSGA RRLQNLWRDQ REEELGEYYM KKYAKSSVGE
160 170 180 190 200
TVYGGSDELS DDITQQQLLP GVKDPNLWTV KCKIGEERAT AISLMRKFIA
210 220 230 240 250
YQFTDTPLQI KSVVAPEHVK GYIYVEAYKQ THVKQAIEGV GNLRLGYWNQ
260 270 280 290 300
QMVPIKEMTD VLKVVKEVAN LKPKSWVRLK RGIYKDDIAQ VDYVEPSQNT
310 320 330 340 350
ISLKMIPRID YDRIKARMSL KDWFAKRKKF KRPPQRLFDA EKIRSLGGDV
360 370 380 390 400
ASDGDFLIFE GNRYSRKGFL FKSFAMSAVI TEGVKPTLSE LEKFEDQPEG
410 420 430 440 450
IDLEVVTEST GKEREHNFQP GDNVEVCEGE LINLQGKVLS VDGNKITIMP
460 470 480 490 500
KHEDLKDMLE FPAQELRKYF KMGDHVKVIA GRFEGDTGLI VRVEENFVIL
510 520 530 540 550
FSDLTMHELK VLPRDLQLCS ETASGVDVGG QHEWGELVQL DPRTVGVIVR
560 570 580 590 600
LERETFQVLN MHGKVVTVRH QAVTQKKDNR FAVALDSDQN NIHVKDIVKV
610 620 630 640 650
IDGPHSGREG EIRHLYRSFA FLHCKKLVEN GGMFVCKARH LVLAGGSKPR
660 670 680 690 700
DVTNLTVGGF TPMSPRISSP MHPSAEGQHG GFGSPGGMSR GRGRRDNELI
710 720 730 740 750
GQTVRISQGP YKGYIGVVKD ATESTARVEL HSTCQTISVD RQRLTTVDSQ
760 770 780 790 800
RPGGMTSTYG RTPMYGSQTP MYGSGSRTPM YGSQTPLQDG SRTPHYGSQT
810 820 830 840 850
PLHDGSRTPA QSGAWDPNNP NTPSRAEEEY EYAFDDEPTP SPQAYGGTPN
860 870 880 890 900
PQTPGYPDPS SPQVNPQYNP QTPGTPAMYN TDQFSPYAAP SPQGSYQPSP
910 920 930 940 950
SPQSYHQVAP SPAGYQNTHS PASYHPTPSP MAYQASPSPS PVGYSPMTPG
960 970 980 990 1000
APSPGGYNPH TPGSGIEQNS SDWVTTDIQV KVRDTYLDTQ IVGQTGVIRS
1010 1020 1030 1040 1050
VTGGMCSVYL KDSEKVVSIS SEHLEPITPT KNNKVKVILG EDREATGVLL
1060 1070 1080
SIDGEDGIIR MDLEDQQIKI LNLRFLGKLL EA
Length:1,082
Mass (Da):120,664
Last modified:June 1, 1998 - v1
Checksum:i109D0D8D2D71DDE7
GO
Isoform 2 (identifier: O55201-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-194: Missing.

Note: No experimental confirmation available.

Show »
Length:888
Mass (Da):98,310
Checksum:i30E132908E6A5F03
GO

Sequence cautioni

The sequence AAH57449.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti30 – 301Q → R in BAE26244. (PubMed:16141072)Curated
Sequence conflicti51 – 511E → EE in BAE26244. (PubMed:16141072)Curated
Sequence conflicti111 – 1111V → L in BAE27278. (PubMed:16141072)Curated
Sequence conflicti229 – 2291K → E in BAE27184. (PubMed:16141072)Curated
Sequence conflicti265 – 2651V → E in BAE26864. (PubMed:16141072)Curated
Sequence conflicti416 – 4161H → N in AAH58598. (PubMed:15489334)Curated
Sequence conflicti775 – 7751G → D in BAE26864. (PubMed:16141072)Curated
Sequence conflicti1063 – 10631L → I in BAE26864. (PubMed:16141072)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 194194Missing in isoform 2. 1 PublicationVSP_016283Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U88539 mRNA. Translation: AAC40052.1.
AK145117 mRNA. Translation: BAE26244.1.
AK146055 mRNA. Translation: BAE26864.1.
AK146453 mRNA. Translation: BAE27184.1.
AK146583 mRNA. Translation: BAE27278.1.
AK146650 mRNA. Translation: BAE27330.1.
BC007132 mRNA. Translation: AAH07132.1.
BC057449 mRNA. Translation: AAH57449.1. Different initiation.
BC058598 mRNA. Translation: AAH58598.1.
BC059849 mRNA. Translation: AAH59849.1.
CCDSiCCDS39857.1. [O55201-1]
PIRiT42204.
RefSeqiNP_038704.1. NM_013676.1. [O55201-1]
UniGeneiMm.285906.

Genome annotation databases

EnsembliENSMUST00000003527; ENSMUSP00000003527; ENSMUSG00000003435. [O55201-1]
GeneIDi20924.
KEGGimmu:20924.
UCSCiuc009fyh.1. mouse. [O55201-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U88539 mRNA. Translation: AAC40052.1 .
AK145117 mRNA. Translation: BAE26244.1 .
AK146055 mRNA. Translation: BAE26864.1 .
AK146453 mRNA. Translation: BAE27184.1 .
AK146583 mRNA. Translation: BAE27278.1 .
AK146650 mRNA. Translation: BAE27330.1 .
BC007132 mRNA. Translation: AAH07132.1 .
BC057449 mRNA. Translation: AAH57449.1 . Different initiation.
BC058598 mRNA. Translation: AAH58598.1 .
BC059849 mRNA. Translation: AAH59849.1 .
CCDSi CCDS39857.1. [O55201-1 ]
PIRi T42204.
RefSeqi NP_038704.1. NM_013676.1. [O55201-1 ]
UniGenei Mm.285906.

3D structure databases

ProteinModelPortali O55201.
SMRi O55201. Positions 174-309, 411-521, 696-751.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 203575. 14 interactions.
IntActi O55201. 1 interaction.
MINTi MINT-4105191.

PTM databases

PhosphoSitei O55201.

Proteomic databases

MaxQBi O55201.
PaxDbi O55201.
PRIDEi O55201.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000003527 ; ENSMUSP00000003527 ; ENSMUSG00000003435 . [O55201-1 ]
GeneIDi 20924.
KEGGi mmu:20924.
UCSCi uc009fyh.1. mouse. [O55201-1 ]

Organism-specific databases

CTDi 20924.
MGIi MGI:1202400. Supt5.

Phylogenomic databases

eggNOGi COG0250.
GeneTreei ENSGT00440000037640.
HOVERGENi HBG079775.
InParanoidi O55201.
KOi K15172.
OMAi AFFDIEA.
OrthoDBi EOG7Z3F3Q.
PhylomeDBi O55201.
TreeFami TF105730.

Enzyme and pathway databases

Reactomei REACT_203462. Formation of the Early Elongation Complex.
REACT_226490. RNA Polymerase II Transcription Elongation.

Miscellaneous databases

ChiTaRSi SUPT5H. mouse.
NextBioi 299833.
PROi O55201.
SOURCEi Search...

Gene expression databases

Bgeei O55201.
CleanExi MM_SUPT5H.
Genevestigatori O55201.

Family and domain databases

InterProi IPR005824. KOW.
IPR006645. NGN_dom.
IPR024945. Spt5_C_dom.
IPR022581. Spt5_N.
IPR017071. TF_Spt5.
IPR005100. TF_Spt5_NGN-domain.
IPR008991. Translation_prot_SH3-like.
[Graphical view ]
Pfami PF00467. KOW. 2 hits.
PF03439. Spt5-NGN. 1 hit.
PF11942. Spt5_N. 1 hit.
[Graphical view ]
PIRSFi PIRSF036945. Spt5. 1 hit.
SMARTi SM01104. CTD. 1 hit.
SM00739. KOW. 6 hits.
SM00738. NGN. 1 hit.
[Graphical view ]
SUPFAMi SSF50104. SSF50104. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation of murine SPT5 homologue: completion of the isolation and characterization of human and murine homologues of yeast chromatin structural protein complex SPT4, SPT5, and SPT6."
    Chiang P.-W., Stubbs L., Zhang L., Kurnit D.M.
    Genomics 47:426-428(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: C57BL/6J.
    Tissue: Heart, Mammary gland and Placenta.
  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).
    Strain: C57BL/6 and FVB/N.
    Tissue: Brain, Mammary tumor, Olfactory epithelium and Salivary gland.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-664, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  5. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-712, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiSPT5H_MOUSE
AccessioniPrimary (citable) accession number: O55201
Secondary accession number(s): Q3UJ77
, Q3UJH1, Q3UKD7, Q3UM54, Q6PB73, Q6PDP0, Q6PFR4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: June 1, 1998
Last modified: October 29, 2014
This is version 118 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3