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P09838

- TDT_MOUSE

UniProt

P09838 - TDT_MOUSE

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Protein

DNA nucleotidylexotransferase

Gene

Dntt

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

Functioni

Template-independent DNA polymerase which catalyzes the random addition of deoxynucleoside 5'-triphosphate to the 3'-end of a DNA initiator. One of the in vivo functions of this enzyme is the addition of nucleotides at the junction (N region) of rearranged Ig heavy chain and T-cell receptor gene segments during the maturation of B- and T-cells.

Catalytic activityi

Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).

Cofactori

Magnesium.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi253 – 2531Sodium; via carbonyl oxygen
Metal bindingi255 – 2551Sodium; via carbonyl oxygen
Metal bindingi343 – 3431Magnesium
Metal bindingi345 – 3451Magnesium
Metal bindingi434 – 4341Magnesium

GO - Molecular functioni

  1. DNA binding Source: InterPro
  2. DNA-directed DNA polymerase activity Source: InterPro
  3. DNA nucleotidylexotransferase activity Source: MGI
  4. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. DNA metabolic process Source: MGI
  2. DNA modification Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Nucleotidyltransferase, Transferase

Keywords - Biological processi

Terminal addition

Keywords - Ligandi

Magnesium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
DNA nucleotidylexotransferase (EC:2.7.7.31)
Alternative name(s):
Terminal addition enzyme
Terminal deoxynucleotidyltransferase
Short name:
TDT
Short name:
Terminal transferase
Gene namesi
Name:Dntt
Synonyms:Tdt
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 19

Organism-specific databases

MGIiMGI:98659. Dntt.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
  2. nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 530530DNA nucleotidylexotransferasePRO_0000218792Add
BLAST

Proteomic databases

PRIDEiP09838.

PTM databases

PhosphoSiteiP09838.

Expressioni

Gene expression databases

BgeeiP09838.
CleanExiMM_DNTT.
ExpressionAtlasiP09838. baseline and differential.
GenevestigatoriP09838.

Interactioni

Subunit structurei

Interacts with PRP19 and DNTTIP1. Forms a ternary complex with DNTTIP2 and core histone. Released from this complex by PCNA (By similarity).By similarity

Structurei

Secondary structure

1
530
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi154 – 1563
Helixi166 – 18116
Helixi185 – 19915
Helixi208 – 2114
Helixi219 – 23113
Helixi235 – 2428
Helixi244 – 25310
Helixi260 – 2689
Helixi274 – 2796
Helixi287 – 2948
Helixi296 – 3005
Helixi305 – 32218
Beta strandi327 – 3304
Helixi332 – 3354
Beta strandi339 – 3424
Beta strandi344 – 3496
Helixi355 – 37218
Beta strandi375 – 3817
Beta strandi394 – 3963
Beta strandi401 – 41111
Helixi412 – 4143
Beta strandi425 – 43713
Helixi440 – 4423
Helixi443 – 4519
Helixi454 – 46815
Beta strandi470 – 4723
Beta strandi477 – 4793
Turni480 – 4823
Beta strandi504 – 5063
Helixi511 – 5188
Helixi525 – 5273

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1JMSX-ray2.36A130-530[»]
1KDHX-ray3.00A148-530[»]
1KEJX-ray3.00A148-530[»]
4I27X-ray2.60A132-530[»]
4I28X-ray2.15A132-530[»]
4I29X-ray2.20A132-530[»]
4I2AX-ray1.90A132-530[»]
4I2BX-ray2.20A132-530[»]
4I2CX-ray2.10A132-530[»]
4I2DX-ray2.30A132-530[»]
4I2EX-ray2.00A132-530[»]
4I2FX-ray2.10A132-530[»]
4I2GX-ray2.50A132-530[»]
4I2HX-ray2.75A132-530[»]
4I2IX-ray2.50A132-530[»]
4I2JX-ray2.70A132-530[»]
4IQTX-ray2.60A132-530[»]
4IQUX-ray2.40A132-530[»]
4IQVX-ray2.90A132-530[»]
4IQWX-ray2.60A132-530[»]
ProteinModelPortaliP09838.
SMRiP09838. Positions 23-125, 149-530.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP09838.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini27 – 12498BRCTPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni151 – 530380Mediates interaction with DNTTIP2By similarityAdd
BLAST
Regioni336 – 34510Involved in ssDNA bindingBy similarity

Sequence similaritiesi

Belongs to the DNA polymerase type-X family.Curated
Contains 1 BRCT domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG1796.
GeneTreeiENSGT00530000063002.
HOGENOMiHOG000263600.
HOVERGENiHBG003670.
InParanoidiP09838.
KOiK00977.
OMAiRRTTLNN.
OrthoDBiEOG7BS4BH.
PhylomeDBiP09838.
TreeFamiTF103012.

Family and domain databases

Gene3Di1.10.150.110. 1 hit.
3.30.210.10. 1 hit.
3.40.50.10190. 1 hit.
InterProiIPR001357. BRCT_dom.
IPR002054. DNA-dir_DNA_pol_X.
IPR019843. DNA_pol-X_BS.
IPR010996. DNA_pol_b-like_N.
IPR018944. DNA_pol_lambd_fingers_domain.
IPR022312. DNA_pol_X.
IPR027421. DNA_pol_X_lyase_dom.
IPR002934. Nucleotidyltransferase.
IPR029398. PolB_thumb.
IPR027292. TdT.
IPR001726. TdT/Mu.
[Graphical view]
PfamiPF00533. BRCT. 1 hit.
PF14791. DNA_pol_B_thumb. 1 hit.
PF10391. DNA_pol_lambd_f. 1 hit.
PF01909. NTP_transf_2. 1 hit.
[Graphical view]
PIRSFiPIRSF000817. DNA_NT. 1 hit.
PIRSF501175. TDT. 1 hit.
PRINTSiPR00869. DNAPOLX.
PR00871. DNAPOLXTDT.
SMARTiSM00292. BRCT. 1 hit.
SM00483. POLXc. 1 hit.
[Graphical view]
SUPFAMiSSF47802. SSF47802. 1 hit.
SSF52113. SSF52113. 1 hit.
PROSITEiPS50172. BRCT. 1 hit.
PS00522. DNA_POLYMERASE_X. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform TDT-L (identifier: P09838-1) [UniParc]FASTAAdd to Basket

Also known as: TDT-Large, TdtL

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
MDPLQAVHLG PRKKRPRQLG TPVASTPYDI RFRDLVLFIL EKKMGTTRRA
60 70 80 90 100
FLMELARRKG FRVENELSDS VTHIVAENNS GSDVLEWLQL QNIKASSELE
110 120 130 140 150
LLDISWLIEC MGAGKPVEMM GRHQLVVNRN SSPSPVPGSQ NVPAPAVKKI
160 170 180 190 200
SQYACQRRTT LNNYNQLFTD ALDILAENDE LRENEGSCLA FMRASSVLKS
210 220 230 240 250
LPFPITSMKD TEGIPCLGDK VKSIIEGIIE DGESSEAKAV LNDERYKSFK
260 270 280 290 300
LFTSVFGVGL KTAEKWFRMG FRTLSKIQSD KSLRFTQMQK AGFLYYEDLV
310 320 330 340 350
SCVNRPEAEA VSMLVKEAVV TFLPDALVTM TGGFRRGKMT GHDVDFLITS
360 370 380 390 400
PEATEDEEQQ LLHKVTDFWK QQGLLLYCDI LESTFEKFKQ PSRKVDALDH
410 420 430 440 450
FQKCFLILKL DHGRVHSEKS GQQEGKGWKA IRVDLVMCPY DRRAFALLGW
460 470 480 490 500
TGSRQFERDL RRYATHERKM MLDNHALYDR TKGKTVTISP LDGKVSKLQK
510 520 530
ALRVFLEAES EEEIFAHLGL DYIEPWERNA

Note: Inactivated at physiological temperature but is stable at lower temperatures.

Length:530
Mass (Da):60,331
Last modified:November 16, 2001 - v3
Checksum:iE6B109DCF39C8107
GO
Isoform TDT-S (identifier: P09838-2) [UniParc]FASTAAdd to Basket

Also known as: TDT-Small, TdtS

The sequence of this isoform differs from the canonical sequence as follows:
     483-502: Missing.

Note: Major form.

Show »
Length:510
Mass (Da):58,266
Checksum:iCF6E850EE36EE3BF
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti26 – 261T → M in CAA48634. (PubMed:8464703)Curated
Sequence conflicti99 – 991L → F in CAA48634. (PubMed:8464703)Curated
Sequence conflicti193 – 1931R → G in CAA27735. (PubMed:3755527)Curated
Sequence conflicti287 – 2871Q → K in CAA27735. (PubMed:3755527)Curated
Sequence conflicti309 – 3091E → Q in CAA27735. (PubMed:3755527)Curated
Sequence conflicti367 – 3671D → H in CAA27735. (PubMed:3755527)Curated
Sequence conflicti441 – 4455DRRAF → ECAC in CAA27735. (PubMed:3755527)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei483 – 50220Missing in isoform TDT-S. 1 PublicationVSP_001309Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X04123 mRNA. Translation: CAA27735.1.
X68670 mRNA. Translation: CAA48634.2.
AF316014 mRNA. Translation: AAK07884.1.
AF316015 mRNA. Translation: AAK07885.1.
AK087978 mRNA. Translation: BAC40071.1.
AK088709 mRNA. Translation: BAC40518.1.
CCDSiCCDS29807.1. [P09838-1]
CCDS37984.1. [P09838-2]
PIRiB23595.
RefSeqiNP_001036693.1. NM_001043228.1. [P09838-2]
NP_033371.2. NM_009345.2. [P09838-1]
UniGeneiMm.25620.

Genome annotation databases

EnsembliENSMUST00000051806; ENSMUSP00000062078; ENSMUSG00000025014. [P09838-1]
ENSMUST00000112200; ENSMUSP00000107819; ENSMUSG00000025014. [P09838-2]
GeneIDi21673.
KEGGimmu:21673.
UCSCiuc008hlo.1. mouse. [P09838-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X04123 mRNA. Translation: CAA27735.1 .
X68670 mRNA. Translation: CAA48634.2 .
AF316014 mRNA. Translation: AAK07884.1 .
AF316015 mRNA. Translation: AAK07885.1 .
AK087978 mRNA. Translation: BAC40071.1 .
AK088709 mRNA. Translation: BAC40518.1 .
CCDSi CCDS29807.1. [P09838-1 ]
CCDS37984.1. [P09838-2 ]
PIRi B23595.
RefSeqi NP_001036693.1. NM_001043228.1. [P09838-2 ]
NP_033371.2. NM_009345.2. [P09838-1 ]
UniGenei Mm.25620.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1JMS X-ray 2.36 A 130-530 [» ]
1KDH X-ray 3.00 A 148-530 [» ]
1KEJ X-ray 3.00 A 148-530 [» ]
4I27 X-ray 2.60 A 132-530 [» ]
4I28 X-ray 2.15 A 132-530 [» ]
4I29 X-ray 2.20 A 132-530 [» ]
4I2A X-ray 1.90 A 132-530 [» ]
4I2B X-ray 2.20 A 132-530 [» ]
4I2C X-ray 2.10 A 132-530 [» ]
4I2D X-ray 2.30 A 132-530 [» ]
4I2E X-ray 2.00 A 132-530 [» ]
4I2F X-ray 2.10 A 132-530 [» ]
4I2G X-ray 2.50 A 132-530 [» ]
4I2H X-ray 2.75 A 132-530 [» ]
4I2I X-ray 2.50 A 132-530 [» ]
4I2J X-ray 2.70 A 132-530 [» ]
4IQT X-ray 2.60 A 132-530 [» ]
4IQU X-ray 2.40 A 132-530 [» ]
4IQV X-ray 2.90 A 132-530 [» ]
4IQW X-ray 2.60 A 132-530 [» ]
ProteinModelPortali P09838.
SMRi P09838. Positions 23-125, 149-530.
ModBasei Search...
MobiDBi Search...

PTM databases

PhosphoSitei P09838.

Proteomic databases

PRIDEi P09838.

Protocols and materials databases

DNASUi 21673.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000051806 ; ENSMUSP00000062078 ; ENSMUSG00000025014 . [P09838-1 ]
ENSMUST00000112200 ; ENSMUSP00000107819 ; ENSMUSG00000025014 . [P09838-2 ]
GeneIDi 21673.
KEGGi mmu:21673.
UCSCi uc008hlo.1. mouse. [P09838-1 ]

Organism-specific databases

CTDi 1791.
MGIi MGI:98659. Dntt.

Phylogenomic databases

eggNOGi COG1796.
GeneTreei ENSGT00530000063002.
HOGENOMi HOG000263600.
HOVERGENi HBG003670.
InParanoidi P09838.
KOi K00977.
OMAi RRTTLNN.
OrthoDBi EOG7BS4BH.
PhylomeDBi P09838.
TreeFami TF103012.

Miscellaneous databases

EvolutionaryTracei P09838.
NextBioi 300956.
PROi P09838.
SOURCEi Search...

Gene expression databases

Bgeei P09838.
CleanExi MM_DNTT.
ExpressionAtlasi P09838. baseline and differential.
Genevestigatori P09838.

Family and domain databases

Gene3Di 1.10.150.110. 1 hit.
3.30.210.10. 1 hit.
3.40.50.10190. 1 hit.
InterProi IPR001357. BRCT_dom.
IPR002054. DNA-dir_DNA_pol_X.
IPR019843. DNA_pol-X_BS.
IPR010996. DNA_pol_b-like_N.
IPR018944. DNA_pol_lambd_fingers_domain.
IPR022312. DNA_pol_X.
IPR027421. DNA_pol_X_lyase_dom.
IPR002934. Nucleotidyltransferase.
IPR029398. PolB_thumb.
IPR027292. TdT.
IPR001726. TdT/Mu.
[Graphical view ]
Pfami PF00533. BRCT. 1 hit.
PF14791. DNA_pol_B_thumb. 1 hit.
PF10391. DNA_pol_lambd_f. 1 hit.
PF01909. NTP_transf_2. 1 hit.
[Graphical view ]
PIRSFi PIRSF000817. DNA_NT. 1 hit.
PIRSF501175. TDT. 1 hit.
PRINTSi PR00869. DNAPOLX.
PR00871. DNAPOLXTDT.
SMARTi SM00292. BRCT. 1 hit.
SM00483. POLXc. 1 hit.
[Graphical view ]
SUPFAMi SSF47802. SSF47802. 1 hit.
SSF52113. SSF52113. 1 hit.
PROSITEi PS50172. BRCT. 1 hit.
PS00522. DNA_POLYMERASE_X. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation and characterization of bovine and mouse terminal deoxynucleotidyltransferase cDNAs expressible in mammalian cells."
    Koiwai O., Yokota T., Kageyama T., Hirose T., Yoshida S., Arai K.
    Nucleic Acids Res. 14:5777-5792(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Differential splicing in mouse thymus generates two forms of terminal deoxynucleotidyl transferase."
    Doyen N., Fanton D'Andon M., Bentolila L.A., Nguyen T.Q., Rougeon F.
    Nucleic Acids Res. 21:1187-1191(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: BALB/c.
    Tissue: Thymus.
  3. Doyen N.
    Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION TO 443-445.
  4. "The long isoform of terminal deoxynucleotidyl transferase (TdtL) enters the nucleus and, rather than catalyzing N addition, modulates the catalytic activity of the short isoform."
    Benedict C.L., Gilfillan S., Kearney J.F.
    J. Exp. Med. 193:89-99(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS TDT-L AND TDT-S), CHARACTERIZATION.
    Strain: C57BL/6.
    Tissue: Thymus.
  5. "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].
    Strain: NOD.
    Tissue: Thymus.
  6. Lubec G., Sunyer B., Chen W.-Q.
    Submitted (JAN-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 388-393, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: OF1.
    Tissue: Hippocampus.
  7. "The two isoforms of mouse terminal deoxynucleotidyl transferase differ in both the ability to add N regions and subcellular localization."
    Bentolila L.A., Fanton D'Andon M., Nguyen T.Q., Martinez O., Rougeon F., Doyen N.
    EMBO J. 14:4221-4229(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: PRELIMINARY CHARACTERIZATION OF ALTERNATIVE FORMS.
  8. "Comparison of the two murine terminal deoxynucleotidyltransferase isoforms. A 20-amino acid insertion in the highly conserved carboxyl-terminal region modifies the thermosensitivity but not the catalytic activity."
    Boule J.-B., Rougeon F., Papanicolaou C.
    J. Biol. Chem. 275:28984-28988(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF ALTERNATIVE FORMS.
  9. Erratum
    Boule J.-B., Rougeon F., Papanicolaou C.
    J. Biol. Chem. 275:33184-33184(2000) [PubMed] [Europe PMC] [Abstract]
  10. "Crystal structures of a template-independent DNA polymerase: murine terminal deoxynucleotidyltransferase."
    Delarue M., Boule J.-B., Lescar J., Expert-Bezancon N., Jourdan N., Sukumar N., Rougeon F., Papanicolaou C.
    EMBO J. 21:427-439(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 130-530 (ISOFORM TLT-S).

Entry informationi

Entry nameiTDT_MOUSE
AccessioniPrimary (citable) accession number: P09838
Secondary accession number(s): Q99PD0, Q99PD1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: November 16, 2001
Last modified: October 29, 2014
This is version 155 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

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

External Data

Dasty 3