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Protein

tRNA (uracil(54)-C(5))-methyltransferase homolog

Gene

TRMT2B

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Probable S-adenosyl-L-methionine-dependent methyltransferase that catalyzes the formation of 5-methyl-uridine at position 54 (m5U54) in all tRNA. May also have a role in tRNA stabilization or maturation (By similarity).By similarity

Catalytic activityi

S-adenosyl-L-methionine + uracil(54) in tRNA = S-adenosyl-L-homocysteine + 5-methyluracil(54) in tRNA.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei323 – 3231S-adenosyl-L-methioninePROSITE-ProRule annotation
Binding sitei373 – 3731S-adenosyl-L-methioninePROSITE-ProRule annotation
Binding sitei423 – 4231S-adenosyl-L-methioninePROSITE-ProRule annotation
Active sitei451 – 4511NucleophilePROSITE-ProRule annotation
Active sitei497 – 4971Proton acceptorBy similarity

GO - Molecular functioni

  1. S-adenosylmethionine-dependent tRNA (m5U54) methyltransferase activity Source: UniProtKB-EC

GO - Biological processi

  1. RNA processing Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Biological processi

tRNA processing

Keywords - Ligandi

S-adenosyl-L-methionine

Names & Taxonomyi

Protein namesi
Recommended name:
tRNA (uracil(54)-C(5))-methyltransferase homolog (EC:2.1.1.35)
Alternative name(s):
TRM2 homolog
Gene namesi
Name:TRMT2B
Synonyms:CXorf34
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:25748. TRMT2B.

Subcellular locationi

GO - Cellular componenti

  1. mitochondrion Source: Ensembl
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA164726782.

Polymorphism and mutation databases

BioMutaiTRMT2B.
DMDMi74762656.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 504504tRNA (uracil(54)-C(5))-methyltransferase homologPRO_0000311932Add
BLAST

Proteomic databases

MaxQBiQ96GJ1.
PaxDbiQ96GJ1.
PRIDEiQ96GJ1.

PTM databases

PhosphoSiteiQ96GJ1.

Expressioni

Gene expression databases

BgeeiQ96GJ1.
CleanExiHS_TRMT2B.
ExpressionAtlasiQ96GJ1. baseline and differential.
GenevestigatoriQ96GJ1.

Organism-specific databases

HPAiHPA003745.
HPA035120.
HPA040814.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
ERCC1P079923EBI-10195625,EBI-750962

Protein-protein interaction databases

BioGridi123044. 5 interactions.
IntActiQ96GJ1. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliQ96GJ1.
SMRiQ96GJ1. Positions 312-504.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the class I-like SAM-binding methyltransferase superfamily. RNA M5U methyltransferase family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG2265.
GeneTreeiENSGT00530000063723.
HOVERGENiHBG108599.
InParanoidiQ96GJ1.
KOiK15331.
OMAiHEGGYWR.
OrthoDBiEOG7327N9.
PhylomeDBiQ96GJ1.
TreeFamiTF352239.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR025714. Methyltranfer_dom.
IPR029063. SAM-dependent_MTases.
IPR025823. tRNA_(uracil-5-)_MeTrfase_met.
IPR010280. U5_MeTrfase_fam.
[Graphical view]
PfamiPF13847. Methyltransf_31. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 2 hits.
PROSITEiPS51687. SAM_MT_RNA_M5U. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q96GJ1-1) [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
MAGLKRRVPL HSLRYFISMV GLFSKPGLLP WYARNPPGWS QLFLGTVCKG
60 70 80 90 100
DFTRVIATKC QKGQKSQKKP SHLGPLDGSW QERLADVVTP LWRLSYEEQL
110 120 130 140 150
KVKFAAQKKI LQRLESYIQM LNGVSVTTAV PKSERLSCLL HPIIPSPVIN
160 170 180 190 200
GYRNKSTFSV NRGPDGNPKT VGFYLGTWRD GNVVCVQSNH LKNIPEKHSQ
210 220 230 240 250
VAQYYEVFLR QSPLEPCLVF HEGGYWRELT VRTNSQGHTM AIITFHPQKL
260 270 280 290 300
SQEELHVQKE IVKEFFIRGP GAACGLTSLY FQESTMTRCS HQQSPYQLLF
310 320 330 340 350
GEPYIFEELL SLKIRISPDA FFQINTAGAE MLYRTVGELT GVNSDTILLD
360 370 380 390 400
ICCGTGVIGL SLAQHTSRVL GIELLEQAVE DARWTAAFNG ITNSEFHTGQ
410 420 430 440 450
AEKILPGLLK SKEDGQSIVA VVNPARAGLH YKVIQAIRNF RAIHTLVFVS
460 470 480 490 500
CKLHGESTRN VIELCCPPDP AKKLLGEPFV LQQAVPVDLF PHTPHCELVL

LFTR
Length:504
Mass (Da):56,476
Last modified:December 1, 2001 - v1
Checksum:iD7A28E168AC9C366
GO
Isoform 2 (identifier: Q96GJ1-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     464-504: LCCPPDPAKKLLGEPFVLQQAVPVDLFPHTPHCELVLLFTR → RSLILLECSGMVSAHCSLHLPGSSDSPASAS

Note: No experimental confirmation available.

Show »
Length:494
Mass (Da):55,006
Checksum:i22B3CD7F012C136F
GO
Isoform 3 (identifier: Q96GJ1-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     102-146: Missing.

Note: No experimental confirmation available.

Show »
Length:459
Mass (Da):51,485
Checksum:i2000E09C0715483C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti238 – 2381H → R in BAB14223 (PubMed:14702039).Curated
Sequence conflicti451 – 4511C → R in CAI46112 (PubMed:17974005).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti12 – 121S → R.
Corresponds to variant rs7064613 [ dbSNP | Ensembl ].
VAR_037355

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei102 – 14645Missing in isoform 3. 1 PublicationVSP_029643Add
BLAST
Alternative sequencei464 – 50441LCCPP…LLFTR → RSLILLECSGMVSAHCSLHL PGSSDSPASAS in isoform 2. 1 PublicationVSP_029644Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK022749 mRNA. Translation: BAB14223.1.
AL832849 mRNA. Translation: CAI46112.1.
AL133275, AL109952, Z97985 Genomic DNA. Translation: CAI42155.1.
AL133275, AL109952, Z97985 Genomic DNA. Translation: CAI42156.1.
Z97985, AL109952, AL133275 Genomic DNA. Translation: CAI42658.1.
Z97985, AL109952, AL133275 Genomic DNA. Translation: CAI42657.1.
AL109952, AL133275, Z97985 Genomic DNA. Translation: CAI42997.1.
AL109952, AL133275, Z97985 Genomic DNA. Translation: CAI42998.1.
CH471115 Genomic DNA. Translation: EAX02831.1.
CH471115 Genomic DNA. Translation: EAX02837.1.
BC007526 mRNA. Translation: AAH07526.1.
BC008067 mRNA. Translation: AAH08067.2.
BC009437 mRNA. Translation: AAH09437.1.
BC020116 mRNA. Translation: AAH20116.1.
BC034272 mRNA. Translation: AAH34272.1.
CCDSiCCDS14477.1. [Q96GJ1-1]
CCDS55464.1. [Q96GJ1-3]
RefSeqiNP_001161442.1. NM_001167970.1. [Q96GJ1-1]
NP_001161443.1. NM_001167971.1. [Q96GJ1-3]
NP_001161444.1. NM_001167972.1. [Q96GJ1-1]
NP_079193.2. NM_024917.5. [Q96GJ1-1]
XP_005262252.1. XM_005262195.1. [Q96GJ1-1]
XP_005262253.1. XM_005262196.1. [Q96GJ1-1]
XP_006724768.1. XM_006724705.1. [Q96GJ1-1]
UniGeneiHs.496501.

Genome annotation databases

EnsembliENST00000372935; ENSP00000362026; ENSG00000188917. [Q96GJ1-1]
ENST00000372936; ENSP00000362027; ENSG00000188917. [Q96GJ1-1]
ENST00000372939; ENSP00000362030; ENSG00000188917. [Q96GJ1-3]
ENST00000545398; ENSP00000438134; ENSG00000188917. [Q96GJ1-1]
GeneIDi79979.
KEGGihsa:79979.
UCSCiuc004egq.3. human. [Q96GJ1-1]
uc004egv.3. human. [Q96GJ1-3]

Polymorphism and mutation databases

BioMutaiTRMT2B.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK022749 mRNA. Translation: BAB14223.1.
AL832849 mRNA. Translation: CAI46112.1.
AL133275, AL109952, Z97985 Genomic DNA. Translation: CAI42155.1.
AL133275, AL109952, Z97985 Genomic DNA. Translation: CAI42156.1.
Z97985, AL109952, AL133275 Genomic DNA. Translation: CAI42658.1.
Z97985, AL109952, AL133275 Genomic DNA. Translation: CAI42657.1.
AL109952, AL133275, Z97985 Genomic DNA. Translation: CAI42997.1.
AL109952, AL133275, Z97985 Genomic DNA. Translation: CAI42998.1.
CH471115 Genomic DNA. Translation: EAX02831.1.
CH471115 Genomic DNA. Translation: EAX02837.1.
BC007526 mRNA. Translation: AAH07526.1.
BC008067 mRNA. Translation: AAH08067.2.
BC009437 mRNA. Translation: AAH09437.1.
BC020116 mRNA. Translation: AAH20116.1.
BC034272 mRNA. Translation: AAH34272.1.
CCDSiCCDS14477.1. [Q96GJ1-1]
CCDS55464.1. [Q96GJ1-3]
RefSeqiNP_001161442.1. NM_001167970.1. [Q96GJ1-1]
NP_001161443.1. NM_001167971.1. [Q96GJ1-3]
NP_001161444.1. NM_001167972.1. [Q96GJ1-1]
NP_079193.2. NM_024917.5. [Q96GJ1-1]
XP_005262252.1. XM_005262195.1. [Q96GJ1-1]
XP_005262253.1. XM_005262196.1. [Q96GJ1-1]
XP_006724768.1. XM_006724705.1. [Q96GJ1-1]
UniGeneiHs.496501.

3D structure databases

ProteinModelPortaliQ96GJ1.
SMRiQ96GJ1. Positions 312-504.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi123044. 5 interactions.
IntActiQ96GJ1. 1 interaction.

PTM databases

PhosphoSiteiQ96GJ1.

Polymorphism and mutation databases

BioMutaiTRMT2B.
DMDMi74762656.

Proteomic databases

MaxQBiQ96GJ1.
PaxDbiQ96GJ1.
PRIDEiQ96GJ1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000372935; ENSP00000362026; ENSG00000188917. [Q96GJ1-1]
ENST00000372936; ENSP00000362027; ENSG00000188917. [Q96GJ1-1]
ENST00000372939; ENSP00000362030; ENSG00000188917. [Q96GJ1-3]
ENST00000545398; ENSP00000438134; ENSG00000188917. [Q96GJ1-1]
GeneIDi79979.
KEGGihsa:79979.
UCSCiuc004egq.3. human. [Q96GJ1-1]
uc004egv.3. human. [Q96GJ1-3]

Organism-specific databases

CTDi79979.
GeneCardsiGC0XM100264.
H-InvDBHIX0016920.
HIX0029044.
HGNCiHGNC:25748. TRMT2B.
HPAiHPA003745.
HPA035120.
HPA040814.
neXtProtiNX_Q96GJ1.
PharmGKBiPA164726782.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG2265.
GeneTreeiENSGT00530000063723.
HOVERGENiHBG108599.
InParanoidiQ96GJ1.
KOiK15331.
OMAiHEGGYWR.
OrthoDBiEOG7327N9.
PhylomeDBiQ96GJ1.
TreeFamiTF352239.

Miscellaneous databases

ChiTaRSiTRMT2B. human.
GenomeRNAii79979.
NextBioi70009.
PROiQ96GJ1.

Gene expression databases

BgeeiQ96GJ1.
CleanExiHS_TRMT2B.
ExpressionAtlasiQ96GJ1. baseline and differential.
GenevestigatoriQ96GJ1.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR025714. Methyltranfer_dom.
IPR029063. SAM-dependent_MTases.
IPR025823. tRNA_(uracil-5-)_MeTrfase_met.
IPR010280. U5_MeTrfase_fam.
[Graphical view]
PfamiPF13847. Methyltransf_31. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 2 hits.
PROSITEiPS51687. SAM_MT_RNA_M5U. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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).
    Tissue: Teratocarcinoma.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    Tissue: Lymph node.
  3. "The DNA sequence of the human X chromosome."
    Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
    , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
    Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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: Brain, Colon, Lymph, Placenta and Skin.

Entry informationi

Entry nameiTRM2_HUMAN
AccessioniPrimary (citable) accession number: Q96GJ1
Secondary accession number(s): A6NDG5
, A6NEI9, A6NMG6, Q5JPF0, Q5JVY6, Q96HU7, Q96IH9, Q9H9K2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 4, 2007
Last sequence update: December 1, 2001
Last modified: April 29, 2015
This is version 121 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 X
    Human chromosome X: 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

External Data

Dasty 3

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 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.