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Q8TEB7

- RN128_HUMAN

UniProt

Q8TEB7 - RN128_HUMAN

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Protein

E3 ubiquitin-protein ligase RNF128

Gene

RNF128

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

Functioni

E3 ubiquitin-protein ligase that catalyzes 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains formation. Functions as an inhibitor of cytokine gene transcription. Inhibits IL2 and IL4 transcription, thereby playing an important role in the induction of the anergic phenotype, a long-term stable state of T-lymphocyte unresponsiveness to antigenic stimulation associated with the blockade of interleukin production. Ubiquitinates ARPC5 with 'Lys-48' linkages and COR1A with 'Lys-63' linkages leading to their degradation, down-regulation of these cytosleletal components results in impaired lamellipodium formation and reduced accumulation of F-actin at the immunological synapse. Functions in the patterning of the dorsal ectoderm; sensitizes ectoderm to respond to neural-inducing signals.2 Publications

Pathwayi

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri277 – 31842RING-type; atypicalPROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. ligase activity Source: UniProtKB-KW
  2. ubiquitin-protein transferase activity Source: Ensembl
  3. zinc ion binding Source: InterPro

GO - Biological processi

  1. negative regulation of cytokine biosynthetic process Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase RNF128 (EC:6.3.2.-)
Alternative name(s):
Gene related to anergy in lymphocytes protein
Short name:
GRAIL
RING finger protein 128
Gene namesi
Name:RNF128
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome X

Organism-specific databases

HGNCiHGNC:21153. RNF128.

Subcellular locationi

Endomembrane system By similarity; Single-pass membrane protein By similarity. Cytoplasmcytoskeleton 2 Publications. Cytoplasmperinuclear region By similarity
Note: Localized in an asymmetric perinuclear punctate manner. Localizes to the internal pool of the transferrin recycling endosomal pathway. Partially colocalized with the endoplasmic reticulum resident HSPA5, with Golgi resident STX5, and with the late endosomal GTPase RAB7A (By similarity).By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei208 – 22821HelicalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. cytoskeleton Source: UniProtKB-KW
  2. endoplasmic reticulum Source: Ensembl
  3. Golgi apparatus Source: Ensembl
  4. integral component of membrane Source: UniProtKB-KW
  5. late endosome Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134868457.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3838Sequence AnalysisAdd
BLAST
Chaini39 – 428390E3 ubiquitin-protein ligase RNF128PRO_0000261412Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi48 – 481N-linked (GlcNAc...)Sequence Analysis
Glycosylationi59 – 591N-linked (GlcNAc...)Sequence Analysis
Glycosylationi101 – 1011N-linked (GlcNAc...)1 Publication

Post-translational modificationi

Auto-ubiquitinated. Controls the development of T-cell clonal anergy by ubiquitination.

Keywords - PTMi

Glycoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ8TEB7.
PaxDbiQ8TEB7.
PRIDEiQ8TEB7.

PTM databases

PhosphoSiteiQ8TEB7.

Expressioni

Inductioni

Induced under anergic conditions. Up-regulated during T-cell anergy induction following signaling through the T-cell antigen receptor.1 Publication

Gene expression databases

BgeeiQ8TEB7.
CleanExiHS_RNF128.
ExpressionAtlasiQ8TEB7. baseline and differential.
GenevestigatoriQ8TEB7.

Organism-specific databases

HPAiHPA019675.

Interactioni

Protein-protein interaction databases

BioGridi122731. 13 interactions.
IntActiQ8TEB7. 2 interactions.
STRINGi9606.ENSP00000255499.

Structurei

Secondary structure

1
428
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi42 – 5211Combined sources
Beta strandi61 – 7111Combined sources
Beta strandi80 – 856Combined sources
Beta strandi116 – 1227Combined sources
Helixi128 – 13710Combined sources
Beta strandi141 – 1466Combined sources
Beta strandi165 – 1717Combined sources
Helixi173 – 18412Combined sources
Beta strandi189 – 19911Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3ICUX-ray2.10A38-204[»]
ProteinModelPortaliQ8TEB7.
SMRiQ8TEB7. Positions 38-204, 277-320.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8TEB7.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini75 – 183109PAAdd
BLAST

Domaini

Binding to E2 ubiquitin-conjugating enzyme requires an intact RING finger domain.

Sequence similaritiesi

Contains 1 RING-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri277 – 31842RING-type; atypicalPROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix, Zinc-finger

Phylogenomic databases

eggNOGiNOG271676.
GeneTreeiENSGT00760000119057.
HOGENOMiHOG000231432.
HOVERGENiHBG057659.
InParanoidiQ8TEB7.
KOiK10629.
OMAiTVPGDWG.
PhylomeDBiQ8TEB7.
TreeFamiTF317486.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR003137. Protease-assoc_domain.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF02225. PA. 1 hit.
PF13639. zf-RING_2. 1 hit.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
[Graphical view]
PROSITEiPS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q8TEB7-1) [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
MGPPPGAGVS CRGGCGFSRL LAWCFLLALS PQAPGSRGAE AVWTAYLNVS
60 70 80 90 100
WRVPHTGVNR TVWELSEEGV YGQDSPLEPV AGVLVPPDGP GALNACNPHT
110 120 130 140 150
NFTVPTVWGS TVQVSWLALI QRGGGCTFAD KIHLAYERGA SGAVIFNFPG
160 170 180 190 200
TRNEVIPMSH PGAVDIVAIM IGNLKGTKIL QSIQRGIQVT MVIEVGKKHG
210 220 230 240 250
PWVNHYSIFF VSVSFFIITA ATVGYFIFYS ARRLRNARAQ SRKQRQLKAD
260 270 280 290 300
AKKAIGRLQL RTLKQGDKEI GPDGDSCAVC IELYKPNDLV RILTCNHIFH
310 320 330 340 350
KTCVDPWLLE HRTCPMCKCD ILKALGIEVD VEDGSVSLQV PVSNEISNSA
360 370 380 390 400
SSHEEDNRSE TASSGYASVQ GTDEPPLEEH VQSTNESLQL VNHEANSVAV
410 420
DVIPHVDNPT FEEDETPNQE TAVREIKS
Length:428
Mass (Da):46,521
Last modified:June 1, 2002 - v1
Checksum:i32F9CDB32BF208FA
GO
Isoform 2 (identifier: Q8TEB7-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-161: MGPPPGAGVS...RNEVIPMSHP → MNQENRSSFF...GNQTIQMANF

Note: No experimental confirmation available.

Show »
Length:402
Mass (Da):44,617
Checksum:iCCE3A965DB2F4F2E
GO

Sequence cautioni

The sequence BAB15682.1 differs from that shown. Reason: Frameshift at position 291. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti4 – 41P → L in AAK77554. (PubMed:12705856)Curated
Sequence conflicti214 – 2141S → P in AAK77554. (PubMed:12705856)Curated
Sequence conflicti223 – 2231V → G in AAK77554. (PubMed:12705856)Curated
Sequence conflicti255 – 2551I → L in BAB15682. (PubMed:14702039)Curated
Sequence conflicti257 – 2571R → G in AAH56677. (PubMed:15489334)Curated
Sequence conflicti261 – 2611R → L in BAB15682. (PubMed:14702039)Curated
Sequence conflicti336 – 3361V → A in BAB15682. (PubMed:14702039)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 161161MGPPP…PMSHP → MNQENRSSFFWLLVIFTFLL KITASFSMSAYVTVTYYNET SNYTAIETCECGVYGLASPV ANAMGVVGIPKNNNYQACDH NTEFSNTKKPWIALIERGNC TFSEKIQTAGRRNADAVVIY NAPETGNQTIQMANF in isoform 2. 1 PublicationVSP_021685Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF394689 mRNA. Translation: AAK77554.1.
AK027169 mRNA. Translation: BAB15682.1. Frameshift.
AK074264 mRNA. Translation: BAB85033.1.
AK126553 mRNA. Translation: BAC86589.1.
AL391315 Genomic DNA. Translation: CAI39545.1.
AL391315, AL606833 Genomic DNA. Translation: CAI39546.1.
AL606833, AL391315 Genomic DNA. Translation: CAI41228.1.
BC030951 mRNA. Translation: AAH30951.1.
BC056677 mRNA. Translation: AAH56677.1.
BC063404 mRNA. Translation: AAH63404.1.
CCDSiCCDS14520.1. [Q8TEB7-2]
CCDS14521.1. [Q8TEB7-1]
RefSeqiNP_078815.3. NM_024539.3. [Q8TEB7-2]
NP_919445.1. NM_194463.1. [Q8TEB7-1]
UniGeneiHs.496542.

Genome annotation databases

EnsembliENST00000255499; ENSP00000255499; ENSG00000133135. [Q8TEB7-1]
ENST00000324342; ENSP00000316127; ENSG00000133135. [Q8TEB7-2]
GeneIDi79589.
KEGGihsa:79589.
UCSCiuc004emk.3. human. [Q8TEB7-2]
uc004eml.3. human. [Q8TEB7-1]

Polymorphism databases

DMDMi74751443.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF394689 mRNA. Translation: AAK77554.1 .
AK027169 mRNA. Translation: BAB15682.1 . Frameshift.
AK074264 mRNA. Translation: BAB85033.1 .
AK126553 mRNA. Translation: BAC86589.1 .
AL391315 Genomic DNA. Translation: CAI39545.1 .
AL391315 , AL606833 Genomic DNA. Translation: CAI39546.1 .
AL606833 , AL391315 Genomic DNA. Translation: CAI41228.1 .
BC030951 mRNA. Translation: AAH30951.1 .
BC056677 mRNA. Translation: AAH56677.1 .
BC063404 mRNA. Translation: AAH63404.1 .
CCDSi CCDS14520.1. [Q8TEB7-2 ]
CCDS14521.1. [Q8TEB7-1 ]
RefSeqi NP_078815.3. NM_024539.3. [Q8TEB7-2 ]
NP_919445.1. NM_194463.1. [Q8TEB7-1 ]
UniGenei Hs.496542.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3ICU X-ray 2.10 A 38-204 [» ]
ProteinModelPortali Q8TEB7.
SMRi Q8TEB7. Positions 38-204, 277-320.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 122731. 13 interactions.
IntActi Q8TEB7. 2 interactions.
STRINGi 9606.ENSP00000255499.

PTM databases

PhosphoSitei Q8TEB7.

Polymorphism databases

DMDMi 74751443.

Proteomic databases

MaxQBi Q8TEB7.
PaxDbi Q8TEB7.
PRIDEi Q8TEB7.

Protocols and materials databases

DNASUi 79589.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000255499 ; ENSP00000255499 ; ENSG00000133135 . [Q8TEB7-1 ]
ENST00000324342 ; ENSP00000316127 ; ENSG00000133135 . [Q8TEB7-2 ]
GeneIDi 79589.
KEGGi hsa:79589.
UCSCi uc004emk.3. human. [Q8TEB7-2 ]
uc004eml.3. human. [Q8TEB7-1 ]

Organism-specific databases

CTDi 79589.
GeneCardsi GC0XP105937.
HGNCi HGNC:21153. RNF128.
HPAi HPA019675.
MIMi 300439. gene.
neXtProti NX_Q8TEB7.
PharmGKBi PA134868457.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG271676.
GeneTreei ENSGT00760000119057.
HOGENOMi HOG000231432.
HOVERGENi HBG057659.
InParanoidi Q8TEB7.
KOi K10629.
OMAi TVPGDWG.
PhylomeDBi Q8TEB7.
TreeFami TF317486.

Enzyme and pathway databases

UniPathwayi UPA00143 .

Miscellaneous databases

ChiTaRSi RNF128. human.
EvolutionaryTracei Q8TEB7.
GeneWikii RNF128.
GenomeRNAii 79589.
NextBioi 35460171.
PROi Q8TEB7.
SOURCEi Search...

Gene expression databases

Bgeei Q8TEB7.
CleanExi HS_RNF128.
ExpressionAtlasi Q8TEB7. baseline and differential.
Genevestigatori Q8TEB7.

Family and domain databases

Gene3Di 3.30.40.10. 1 hit.
InterProi IPR003137. Protease-assoc_domain.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view ]
Pfami PF02225. PA. 1 hit.
PF13639. zf-RING_2. 1 hit.
[Graphical view ]
SMARTi SM00184. RING. 1 hit.
[Graphical view ]
PROSITEi PS50089. ZF_RING_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "GRAIL: an E3 ubiquitin ligase that inhibits cytokine gene transcription is expressed in anergic CD4+ T cells."
    Anandasabapathy N., Ford G.S., Bloom D., Holness C., Paragas V., Seroogy C., Skrenta H., Hollenhorst M., Fathman C.G., Soares L.
    Immunity 18:535-547(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, INDUCTION, MUTAGENESIS.
  2. "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] (ISOFORMS 1 AND 2).
    Tissue: Hepatoma, Lung and Mammary gland.
  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. "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).
    Tissue: Brain.
  5. "GRAIL (gene related to anergy in lymphocytes) regulates cytoskeletal reorganization through ubiquitination and degradation of Arp2/3 subunit 5 and coronin 1A."
    Ichikawa D., Mizuno M., Yamamura T., Miyake S.
    J. Biol. Chem. 286:43465-43474(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  6. "PA domain of the E3 ligase GRAIL."
    Structural genomics consortium (SGC)
    Submitted (OCT-2009) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 38-204, GLYCOSYLATION AT ASN-101.

Entry informationi

Entry nameiRN128_HUMAN
AccessioniPrimary (citable) accession number: Q8TEB7
Secondary accession number(s): A0PJI4
, Q6PH80, Q6ZTJ8, Q96RF3, Q9H5E4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: June 1, 2002
Last modified: November 26, 2014
This is version 113 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3