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Protein

Probable E3 ubiquitin-protein ligase TRIML1

Gene

TRIML1

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

Functioni

Probable E3 ubiquitin-protein ligase which plays an important role in blastocyst development.By similarity

Pathway: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri16 – 5742RING-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Ligase

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable E3 ubiquitin-protein ligase TRIML1 (EC:6.3.2.-)
Alternative name(s):
RING finger protein 209
Tripartite motif family-like protein 1
Gene namesi
Name:TRIML1
Synonyms:RNF209
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 4

Organism-specific databases

HGNCiHGNC:26698. TRIML1.

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162407030.

Polymorphism and mutation databases

BioMutaiTRIML1.
DMDMi74729772.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 468468Probable E3 ubiquitin-protein ligase TRIML1PRO_0000274598Add
BLAST

Proteomic databases

PaxDbiQ8N9V2.
PeptideAtlasiQ8N9V2.
PRIDEiQ8N9V2.

PTM databases

PhosphoSiteiQ8N9V2.

Expressioni

Gene expression databases

BgeeiQ8N9V2.
CleanExiHS_TRIML1.
GenevisibleiQ8N9V2. HS.

Organism-specific databases

HPAiHPA037769.

Interactioni

Subunit structurei

Interacts with USP5.By similarity

Protein-protein interaction databases

BioGridi130974. 4 interactions.
IntActiQ8N9V2. 2 interactions.
STRINGi9606.ENSP00000327738.

Structurei

3D structure databases

ProteinModelPortaliQ8N9V2.
SMRiQ8N9V2. Positions 7-56, 117-263, 288-464.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini267 – 468202B30.2/SPRYPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili133 – 15826Sequence AnalysisAdd
BLAST
Coiled coili184 – 23754Sequence AnalysisAdd
BLAST

Sequence similaritiesi

Contains 1 B30.2/SPRY domain.PROSITE-ProRule annotation
Contains 1 RING-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri16 – 5742RING-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Coiled coil, Zinc-finger

Phylogenomic databases

eggNOGiNOG267050.
GeneTreeiENSGT00760000118893.
HOGENOMiHOG000234133.
HOVERGENiHBG001357.
InParanoidiQ8N9V2.
KOiK12038.
OMAiELTLCRI.
OrthoDBiEOG7M3J02.
PhylomeDBiQ8N9V2.
TreeFamiTF338674.

Family and domain databases

Gene3Di3.30.40.10. 2 hits.
InterProiIPR001870. B30.2/SPRY.
IPR003879. Butyrophylin.
IPR013320. ConA-like_dom.
IPR006574. PRY.
IPR003877. SPRY_dom.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamiPF13765. PRY. 1 hit.
PF00622. SPRY. 1 hit.
[Graphical view]
PRINTSiPR01407. BUTYPHLNCDUF.
SMARTiSM00589. PRY. 1 hit.
SM00184. RING. 1 hit.
SM00449. SPRY. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 1 hit.
PROSITEiPS50188. B302_SPRY. 1 hit.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8N9V2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTADLMENL REELTCFICL DYFSSPVTTE CGHSFCLVCL LRSWEEHNTP
60 70 80 90 100
LSCPECWRTL EGPHFQSNER LGRLASIARQ LRSQVLQSED EQGSYGRMPT
110 120 130 140 150
TAKALSDDEQ GGSAFVAQSH GANRVHLSSE AEEHHREKLQ EILNLLRVRR
160 170 180 190 200
KEAQAVLTHE KERVKLCQEE TKTCKQVVVS EYMKMHQFLK EEEQLQLQLL
210 220 230 240 250
EQEEKENMRK LRNNEIKLTQ QIRSLSKMIA QIESSSQSSA FESLEEVRGA
260 270 280 290 300
LERSEPLLLQ CPEATTTELS LCRITGMKEM LRKFSTEITL DPATANAYLV
310 320 330 340 350
LSEDLKSVKY GGSRQQLPDN PERFDQSATV LGTQIFTSGR HYWEVEVGNK
360 370 380 390 400
TEWEVGICKD SVSRKGNLPK PPGDLFSLIG LKIGDDYSLW VSSPLKGQHV
410 420 430 440 450
REPVCKVGVF LDYESGHIAF YNGTDESLIY SFPQASFQEA LRPIFSPCLP
460
NEGTNTDPLT ICSLNSHV
Length:468
Mass (Da):53,002
Last modified:October 1, 2002 - v1
Checksum:i66F9E2DABC5C96B8
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti21 – 211D → H in a breast cancer sample; somatic mutation. 1 Publication
VAR_035963
Natural varianti132 – 1321E → K.
Corresponds to variant rs13131525 [ dbSNP | Ensembl ].
VAR_052145

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK093499 mRNA. Translation: BAC04185.1.
AC138781 Genomic DNA. No translation available.
BC015684 mRNA. Translation: AAH15684.1.
BC113860 mRNA. Translation: AAI13861.1.
BC114469 mRNA. Translation: AAI14470.1.
CCDSiCCDS3851.1.
RefSeqiNP_848651.2. NM_178556.3.
UniGeneiHs.348618.

Genome annotation databases

EnsembliENST00000332517; ENSP00000327738; ENSG00000184108.
GeneIDi339976.
KEGGihsa:339976.
UCSCiuc003izm.1. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK093499 mRNA. Translation: BAC04185.1.
AC138781 Genomic DNA. No translation available.
BC015684 mRNA. Translation: AAH15684.1.
BC113860 mRNA. Translation: AAI13861.1.
BC114469 mRNA. Translation: AAI14470.1.
CCDSiCCDS3851.1.
RefSeqiNP_848651.2. NM_178556.3.
UniGeneiHs.348618.

3D structure databases

ProteinModelPortaliQ8N9V2.
SMRiQ8N9V2. Positions 7-56, 117-263, 288-464.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi130974. 4 interactions.
IntActiQ8N9V2. 2 interactions.
STRINGi9606.ENSP00000327738.

PTM databases

PhosphoSiteiQ8N9V2.

Polymorphism and mutation databases

BioMutaiTRIML1.
DMDMi74729772.

Proteomic databases

PaxDbiQ8N9V2.
PeptideAtlasiQ8N9V2.
PRIDEiQ8N9V2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000332517; ENSP00000327738; ENSG00000184108.
GeneIDi339976.
KEGGihsa:339976.
UCSCiuc003izm.1. human.

Organism-specific databases

CTDi339976.
GeneCardsiGC04P189060.
HGNCiHGNC:26698. TRIML1.
HPAiHPA037769.
neXtProtiNX_Q8N9V2.
PharmGKBiPA162407030.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG267050.
GeneTreeiENSGT00760000118893.
HOGENOMiHOG000234133.
HOVERGENiHBG001357.
InParanoidiQ8N9V2.
KOiK12038.
OMAiELTLCRI.
OrthoDBiEOG7M3J02.
PhylomeDBiQ8N9V2.
TreeFamiTF338674.

Enzyme and pathway databases

UniPathwayiUPA00143.

Miscellaneous databases

GenomeRNAii339976.
NextBioi97650.
PROiQ8N9V2.

Gene expression databases

BgeeiQ8N9V2.
CleanExiHS_TRIML1.
GenevisibleiQ8N9V2. HS.

Family and domain databases

Gene3Di3.30.40.10. 2 hits.
InterProiIPR001870. B30.2/SPRY.
IPR003879. Butyrophylin.
IPR013320. ConA-like_dom.
IPR006574. PRY.
IPR003877. SPRY_dom.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamiPF13765. PRY. 1 hit.
PF00622. SPRY. 1 hit.
[Graphical view]
PRINTSiPR01407. BUTYPHLNCDUF.
SMARTiSM00589. PRY. 1 hit.
SM00184. RING. 1 hit.
SM00449. SPRY. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 1 hit.
PROSITEiPS50188. B302_SPRY. 1 hit.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 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].
    Tissue: Testis.
  2. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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].
    Tissue: Placenta.
  4. Cited for: VARIANT [LARGE SCALE ANALYSIS] HIS-21.

Entry informationi

Entry nameiTRIML_HUMAN
AccessioniPrimary (citable) accession number: Q8N9V2
Secondary accession number(s): Q96BE5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 6, 2007
Last sequence update: October 1, 2002
Last modified: June 24, 2015
This is version 102 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 4
    Human chromosome 4: 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  5. 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.