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Protein

tRNA dimethylallyltransferase, mitochondrial

Gene

TRIT1

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

Functioni

Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 of both cytosolic and mitochondrial tRNAs, leading to the formation of N6-(dimethylallyl)adenosine (i6A).1 Publication

Catalytic activityi

Dimethylallyl diphosphate + adenine(37) in tRNA = diphosphate + N(6)-dimethylallyladenine(37) in tRNA.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri395 – 42531Matrin-typeAdd
BLAST

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • nucleic acid binding Source: InterPro
  • tRNA dimethylallyltransferase activity Source: UniProtKB
  • zinc ion binding Source: InterPro

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

tRNA processing

Keywords - Ligandi

ATP-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

BRENDAi2.5.1.75. 2681.
ReactomeiR-HSA-6782315. tRNA modification in the nucleus and cytosol.
R-HSA-6787450. tRNA modification in the mitochondrion.

Names & Taxonomyi

Protein namesi
Recommended name:
tRNA dimethylallyltransferase, mitochondrial (EC:2.5.1.75)
Alternative name(s):
Isopentenyl-diphosphate:tRNA isopentenyltransferase
Short name:
IPP transferase
Short name:
IPPT
hGRO1
tRNA isopentenyltransferase
Short name:
IPTase
Gene namesi
Name:TRIT1
Synonyms:IPT, MOD5
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:20286. TRIT1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Mitochondrion

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134943037.

Polymorphism and mutation databases

BioMutaiTRIT1.
DMDMi56405066.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4747MitochondrionSequence analysisAdd
BLAST
Chaini48 – 467420tRNA dimethylallyltransferase, mitochondrialPRO_0000019023Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei455 – 4551PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9H3H1.
MaxQBiQ9H3H1.
PaxDbiQ9H3H1.
PRIDEiQ9H3H1.

PTM databases

iPTMnetiQ9H3H1.
PhosphoSiteiQ9H3H1.

Expressioni

Gene expression databases

BgeeiQ9H3H1.
CleanExiHS_TRIT1.
ExpressionAtlasiQ9H3H1. baseline and differential.
GenevisibleiQ9H3H1. HS.

Organism-specific databases

HPAiHPA024174.
HPA053686.

Interactioni

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei122 – 1221Interaction with substrate tRNABy similarity
Sitei206 – 2061Interaction with substrate tRNABy similarity

Protein-protein interaction databases

BioGridi120161. 4 interactions.
IntActiQ9H3H1. 4 interactions.
MINTiMINT-1409659.
STRINGi9606.ENSP00000321810.

Structurei

3D structure databases

ProteinModelPortaliQ9H3H1.
SMRiQ9H3H1. Positions 21-428.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni32 – 376Substrate bindingBy similarity
Regioni55 – 584Interaction with substrate tRNABy similarity
Regioni183 – 1875Interaction with substrate tRNABy similarity
Regioni233 – 25523Interaction with isopentenylpyrophosphate transferaseBy similarityAdd
BLAST
Regioni281 – 2833Interaction with substrate tRNABy similarity
Regioni313 – 33119Interaction with substrate tRNABy similarityAdd
BLAST
Regioni323 – 3308Interaction with substrate tRNABy similarity

Sequence similaritiesi

Belongs to the IPP transferase family.Curated
Contains 1 matrin-type zinc finger.Curated

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri395 – 42531Matrin-typeAdd
BLAST

Keywords - Domaini

Transit peptide, Zinc-finger

Phylogenomic databases

eggNOGiKOG1384. Eukaryota.
COG0324. LUCA.
GeneTreeiENSGT00390000015214.
HOVERGENiHBG052492.
InParanoidiQ9H3H1.
KOiK00791.
OMAiKWINNRF.
PhylomeDBiQ9H3H1.
TreeFamiTF315069.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_00185. IPP_trans.
InterProiIPR018022. IPP_trans.
IPR030666. IPP_transferase_euk.
IPR027417. P-loop_NTPase.
IPR022755. Znf_C2H2_jaz.
IPR003604. Znf_U1.
[Graphical view]
PfamiPF01715. IPPT. 1 hit.
PF12171. zf-C2H2_jaz. 1 hit.
[Graphical view]
PIRSFiPIRSF039110. IPP_transferase. 1 hit.
SMARTiSM00451. ZnF_U1. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 2 hits.
TIGRFAMsiTIGR00174. miaA. 1 hit.

Sequences (6)i

Sequence statusi: Complete.

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

This entry describes 6 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9H3H1-1) [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
MASVAAARAV PVGSGLRGLQ RTLPLVVILG ATGTGKSTLA LQLGQRLGGE
60 70 80 90 100
IVSADSMQVY EGLDIITNKV SAQEQRICRH HMISFVDPLV TNYTVVDFRN
110 120 130 140 150
RATALIEDIF ARDKIPIVVG GTNYYIESLL WKVLVNTKPQ EMGTEKVIDR
160 170 180 190 200
KVELEKEDGL VLHKRLSQVD PEMAAKLHPH DKRKVARSLQ VFEETGISHS
210 220 230 240 250
EFLHRQHTEE GGGPLGGPLK FSNPCILWLH ADQAVLDERL DKRVDDMLAA
260 270 280 290 300
GLLEELRDFH RRYNQKNVSE NSQDYQHGIF QSIGFKEFHE YLITEGKCTL
310 320 330 340 350
ETSNQLLKKG IEALKQVTKR YARKQNRWVK NRFLSRPGPI VPPVYGLEVS
360 370 380 390 400
DVSKWEESVL EPALEIVQSF IQGHKPTATP IKMPYNEAEN KRSYHLCDLC
410 420 430 440 450
DRIIIGDREW AAHIKSKSHL NQLKKRRRLD SDAVNTIESQ SVSPDHNKEP
460
KEKGSPGQND QELKCSV
Length:467
Mass (Da):52,725
Last modified:March 1, 2001 - v1
Checksum:i634469919D7F56A5
GO
Isoform 2 (identifier: Q9H3H1-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-141: Missing.

Note: No experimental confirmation available.
Show »
Length:326
Mass (Da):37,435
Checksum:iEAB3F0F9664B7ACE
GO
Isoform 3 (identifier: Q9H3H1-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-141: Missing.
     235-236: Missing.

Note: No experimental confirmation available.
Show »
Length:324
Mass (Da):37,223
Checksum:i1E6835D7C09126A9
GO
Isoform 4 (identifier: Q9H3H1-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     311-336: Missing.

Show »
Length:441
Mass (Da):49,453
Checksum:i28DB69A67BD6C4B8
GO
Isoform 5 (identifier: Q9H3H1-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     59-138: Missing.
     235-236: Missing.

Note: No experimental confirmation available.
Show »
Length:385
Mass (Da):43,305
Checksum:iD1282514B2CDCF8A
GO
Isoform 6 (identifier: Q9H3H1-6) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-5: MASVA → MFRKI
     6-309: Missing.

Show »
Length:163
Mass (Da):18,758
Checksum:iF66F2BFD015B21F5
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti303 – 3031S → G in CAG33507 (Ref. 5) Curated
Sequence conflicti446 – 4461H → Y in AAL14107 (PubMed:11560893).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti202 – 2021F → L.1 Publication
Corresponds to variant rs3738671 [ dbSNP | Ensembl ].
VAR_020486

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 141141Missing in isoform 2 and isoform 3. 2 PublicationsVSP_010719Add
BLAST
Alternative sequencei1 – 55MASVA → MFRKI in isoform 6. 1 PublicationVSP_053746
Alternative sequencei6 – 309304Missing in isoform 6. 1 PublicationVSP_053747Add
BLAST
Alternative sequencei59 – 13880Missing in isoform 5. 1 PublicationVSP_012415Add
BLAST
Alternative sequencei235 – 2362Missing in isoform 3 and isoform 5. 2 PublicationsVSP_010720
Alternative sequencei311 – 33626Missing in isoform 4. 1 PublicationVSP_010721Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF074918 Transcribed RNA. Translation: AAG31324.1.
AY702944 mRNA. Translation: AAW63405.1.
AY702945 mRNA. Translation: AAW63406.1.
AY303390 mRNA. Translation: AAP60111.1.
AK000068 mRNA. Translation: BAA90923.1.
CR457226 mRNA. Translation: CAG33507.1.
AL033527 Genomic DNA. Translation: CAI19405.1.
AL033527 Genomic DNA. Translation: CAI19406.1.
BC010741 mRNA. Translation: AAH10741.2.
BC107569 mRNA. Translation: AAI07570.1.
BC128155 mRNA. Translation: AAI28156.1.
AY052768 mRNA. Translation: AAL14107.1.
CCDSiCCDS30681.1. [Q9H3H1-1]
RefSeqiNP_001299620.1. NM_001312691.1. [Q9H3H1-4]
NP_001299621.1. NM_001312692.1. [Q9H3H1-5]
NP_060116.2. NM_017646.5. [Q9H3H1-1]
XP_006710769.1. XM_006710706.1. [Q9H3H1-2]
UniGeneiHs.356554.

Genome annotation databases

EnsembliENST00000316891; ENSP00000321810; ENSG00000043514. [Q9H3H1-1]
ENST00000372818; ENSP00000361905; ENSG00000043514. [Q9H3H1-4]
ENST00000441669; ENSP00000388333; ENSG00000043514. [Q9H3H1-5]
ENST00000537440; ENSP00000437700; ENSG00000043514. [Q9H3H1-6]
GeneIDi54802.
KEGGihsa:54802.
UCSCiuc001cem.5. human. [Q9H3H1-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF074918 Transcribed RNA. Translation: AAG31324.1.
AY702944 mRNA. Translation: AAW63405.1.
AY702945 mRNA. Translation: AAW63406.1.
AY303390 mRNA. Translation: AAP60111.1.
AK000068 mRNA. Translation: BAA90923.1.
CR457226 mRNA. Translation: CAG33507.1.
AL033527 Genomic DNA. Translation: CAI19405.1.
AL033527 Genomic DNA. Translation: CAI19406.1.
BC010741 mRNA. Translation: AAH10741.2.
BC107569 mRNA. Translation: AAI07570.1.
BC128155 mRNA. Translation: AAI28156.1.
AY052768 mRNA. Translation: AAL14107.1.
CCDSiCCDS30681.1. [Q9H3H1-1]
RefSeqiNP_001299620.1. NM_001312691.1. [Q9H3H1-4]
NP_001299621.1. NM_001312692.1. [Q9H3H1-5]
NP_060116.2. NM_017646.5. [Q9H3H1-1]
XP_006710769.1. XM_006710706.1. [Q9H3H1-2]
UniGeneiHs.356554.

3D structure databases

ProteinModelPortaliQ9H3H1.
SMRiQ9H3H1. Positions 21-428.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120161. 4 interactions.
IntActiQ9H3H1. 4 interactions.
MINTiMINT-1409659.
STRINGi9606.ENSP00000321810.

PTM databases

iPTMnetiQ9H3H1.
PhosphoSiteiQ9H3H1.

Polymorphism and mutation databases

BioMutaiTRIT1.
DMDMi56405066.

Proteomic databases

EPDiQ9H3H1.
MaxQBiQ9H3H1.
PaxDbiQ9H3H1.
PRIDEiQ9H3H1.

Protocols and materials databases

DNASUi54802.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000316891; ENSP00000321810; ENSG00000043514. [Q9H3H1-1]
ENST00000372818; ENSP00000361905; ENSG00000043514. [Q9H3H1-4]
ENST00000441669; ENSP00000388333; ENSG00000043514. [Q9H3H1-5]
ENST00000537440; ENSP00000437700; ENSG00000043514. [Q9H3H1-6]
GeneIDi54802.
KEGGihsa:54802.
UCSCiuc001cem.5. human. [Q9H3H1-1]

Organism-specific databases

CTDi54802.
GeneCardsiTRIT1.
HGNCiHGNC:20286. TRIT1.
HPAiHPA024174.
HPA053686.
neXtProtiNX_Q9H3H1.
PharmGKBiPA134943037.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1384. Eukaryota.
COG0324. LUCA.
GeneTreeiENSGT00390000015214.
HOVERGENiHBG052492.
InParanoidiQ9H3H1.
KOiK00791.
OMAiKWINNRF.
PhylomeDBiQ9H3H1.
TreeFamiTF315069.

Enzyme and pathway databases

BRENDAi2.5.1.75. 2681.
ReactomeiR-HSA-6782315. tRNA modification in the nucleus and cytosol.
R-HSA-6787450. tRNA modification in the mitochondrion.

Miscellaneous databases

ChiTaRSiTRIT1. human.
GeneWikiiTRIT1.
GenomeRNAii54802.
PROiQ9H3H1.

Gene expression databases

BgeeiQ9H3H1.
CleanExiHS_TRIT1.
ExpressionAtlasiQ9H3H1. baseline and differential.
GenevisibleiQ9H3H1. HS.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_00185. IPP_trans.
InterProiIPR018022. IPP_trans.
IPR030666. IPP_transferase_euk.
IPR027417. P-loop_NTPase.
IPR022755. Znf_C2H2_jaz.
IPR003604. Znf_U1.
[Graphical view]
PfamiPF01715. IPPT. 1 hit.
PF12171. zf-C2H2_jaz. 1 hit.
[Graphical view]
PIRSFiPIRSF039110. IPP_transferase. 1 hit.
SMARTiSM00451. ZnF_U1. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 2 hits.
TIGRFAMsiTIGR00174. miaA. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning of a human tRNA isopentenyl transferase."
    Golovko A., Hjalm G., Sitbon F., Nicander B.
    Gene 258:85-93(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION.
  2. "Identification and functional characterization of the candidate tumor suppressor gene TRIT1 in human lung cancer."
    Spinola M., Galvan A., Pignatiello C., Conti B., Pastorino U., Nicander B., Paroni R., Dragani T.A.
    Oncogene 24:5502-5509(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6), ALTERNATIVE SPLICING.
    Tissue: Lung.
  3. "Human MOD5 cDNA sequence."
    Peters J.L., Yan Q., Guan M.X.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  4. "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 2).
    Tissue: Colon.
  5. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
  6. "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].
  7. "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] (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 7-467 (ISOFORM 5), VARIANT LEU-202.
    Tissue: Kidney and Uterus.
  8. "Regulation of physiological rates in Caenorhabditis elegans by a tRNA-modifying enzyme in the mitochondria."
    Lemieux J., Lakowski B., Webb A., Meng Y., Ubach A., Bussiere F., Barnes T., Hekimi S.
    Genetics 159:147-157(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 7-467 (ISOFORM 4).
  9. "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.
  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-455, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiMOD5_HUMAN
AccessioniPrimary (citable) accession number: Q9H3H1
Secondary accession number(s): A1A4X7
, Q3T7B5, Q5QPK5, Q5QPK6, Q6IAC9, Q96FJ3, Q96L45, Q9NXT7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 5, 2004
Last sequence update: March 1, 2001
Last modified: June 8, 2016
This is version 126 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. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. SIMILARITY comments
    Index of protein domains and families

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 one 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.