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Q7Z5B4

- RIC3_HUMAN

UniProt

Q7Z5B4 - RIC3_HUMAN

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Protein

Protein RIC-3

Gene

RIC3

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

Functioni

Promotes functional expression of homomeric alpha-7 and alpha-8 nicotinic acetylcholine receptors at the cell surface. May also promote functional expression of homomeric serotoninergic 5-HT3 receptors, and of heteromeric acetylcholine receptors alpha-3/beta-2, alpha-3/beta-4, alpha-4/beta-2 and alpha-4/beta-4.7 Publications

GO - Biological processi

  1. cellular protein complex assembly Source: Ensembl
  2. positive regulation of cytosolic calcium ion concentration Source: Ensembl
  3. protein folding Source: Ensembl
  4. synaptic transmission, cholinergic Source: Ensembl
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Protein RIC-3
Alternative name(s):
Resistant to inhibitor of cholinesterase 3
Gene namesi
Name:RIC3
ORF Names:UNQ720/PRO1385
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:30338. RIC3.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini29 – 9567LumenalSequence AnalysisAdd
BLAST
Transmembranei96 – 11621HelicalSequence AnalysisAdd
BLAST
Topological domaini117 – 369253CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum Source: UniProtKB-KW
  2. Golgi apparatus Source: UniProtKB-KW
  3. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Golgi apparatus, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA142671066.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2828By similarityAdd
BLAST
Chaini29 – 369341Protein RIC-3PRO_0000302731Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei202 – 2021N6-acetyllysine; alternate1 Publication
Cross-linki202 – 202Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Ubl conjugation

Proteomic databases

MaxQBiQ7Z5B4.
PaxDbiQ7Z5B4.
PRIDEiQ7Z5B4.

PTM databases

PhosphoSiteiQ7Z5B4.

Expressioni

Tissue specificityi

Broadly expressed, with high levels in muscle, brain, heart, pancreas and testis. In the central nervous system, highest levels are detected in the cerebellum and pituitary gland. Over-expressed in brains from patients with bipolar disease or schizophrenia. Isoform 5 is predominantly expressed in the brain.3 Publications

Gene expression databases

BgeeiQ7Z5B4.
CleanExiHS_RIC3.
ExpressionAtlasiQ7Z5B4. baseline and differential.
GenevestigatoriQ7Z5B4.

Interactioni

Subunit structurei

Monomer and homodimer. Interacts with CHRNA7, CHRNA3, CHRNA4, CHRNB2, CHRNB4 and HTR3A.3 Publications

Protein-protein interaction databases

BioGridi122743. 34 interactions.
IntActiQ7Z5B4. 1 interaction.
MINTiMINT-8343009.
STRINGi9606.ENSP00000344904.

Structurei

3D structure databases

ProteinModelPortaliQ7Z5B4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili140 – 16930By similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi81 – 9414Poly-GlyAdd
BLAST
Compositional biasi269 – 2724Poly-Glu

Domaini

The coiled-coil domain mediates transient homodimerization with other acetylcholine receptor-bound RIC3 molecules, promoting stepwise ACHR homomeric assembly at the membrane.By similarity

Sequence similaritiesi

Belongs to the ric-3 family.Curated

Keywords - Domaini

Coiled coil, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG46432.
GeneTreeiENSGT00440000034107.
HOVERGENiHBG106009.
InParanoidiQ7Z5B4.
OMAiHRKITNF.
OrthoDBiEOG7MKW7H.
PhylomeDBiQ7Z5B4.
TreeFamiTF333291.

Family and domain databases

InterProiIPR026160. Ric3.
[Graphical view]
PANTHERiPTHR21723. PTHR21723. 1 hit.

Sequences (5)i

Sequence statusi: Complete.

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

This entry describes 5 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q7Z5B4-1) [UniParc]FASTAAdd to Basket

Also known as: a

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
MAYSTVQRVA LASGLVLALS LLLPKAFLSR GKRQEPPPTP EGKLGRFPPM
60 70 80 90 100
MHHHQAPSDG QTPGARFQRS HLAEAFAKAK GSGGGAGGGG SGRGLMGQII
110 120 130 140 150
PIYGFGIFLY ILYILFKLSK GKTTAEDGKC YTAMPGNTHR KITSFELAQL
160 170 180 190 200
QEKLKETEAA MEKLINRVGP NGESRAQTVT SDQEKRLLHQ LREITRVMKE
210 220 230 240 250
GKFIDRFSPE KEAEEAPYME DWEGYPEETY PIYDLSDCIK RRQETILVDY
260 270 280 290 300
PDPKELSAEE IAERMGMIEE EESDHLGWES LPTDPRAQED NSVTSCDPKP
310 320 330 340 350
ETCSCCFHED EDPAVLAENA GFSADSYPEQ EETTKEEWSQ DFKDEGLGIS
360
TDKAYTGSML RKRNPQGLE
Length:369
Mass (Da):41,092
Last modified:October 1, 2003 - v1
Checksum:i15FD70384070345D
GO
Isoform 2 (identifier: Q7Z5B4-2) [UniParc]FASTAAdd to Basket

Also known as: d

The sequence of this isoform differs from the canonical sequence as follows:
     118-128: LSKGKTTAEDG → VSRIILIILHQ
     129-369: Missing.

Show »
Length:128
Mass (Da):13,663
Checksum:i01D76A36CC9F0C2F
GO
Isoform 3 (identifier: Q7Z5B4-3) [UniParc]FASTAAdd to Basket

Also known as: c

The sequence of this isoform differs from the canonical sequence as follows:
     41-222: Missing.

Note: No experimental confirmation available.

Show »
Length:187
Mass (Da):20,954
Checksum:iC51C0B8B8F21B4B2
GO
Isoform 4 (identifier: Q7Z5B4-5) [UniParc]FASTAAdd to Basket

Also known as: b

The sequence of this isoform differs from the canonical sequence as follows:
     174-174: Missing.

Show »
Length:368
Mass (Da):41,005
Checksum:iC66CFFD8641778DA
GO
Isoform 5 (identifier: Q7Z5B4-6) [UniParc]FASTAAdd to Basket

Also known as: e

The sequence of this isoform differs from the canonical sequence as follows:
     143-224: TSFELAQLQE...EAPYMEDWEG → S

Show »
Length:288
Mass (Da):31,643
Checksum:i2D0010517F3E6E20
GO

Sequence cautioni

The sequence BAB13871.1 differs from that shown. Reason: Probable cloning artifact.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti23 – 231Missing in AAP92163. (PubMed:12821669)Curated
Sequence conflicti165 – 1651I → F in AAH22455. (PubMed:15489334)Curated
Isoform 2 (identifier: Q7Z5B4-2)
Sequence conflicti124 – 1241I → T in AAP92163. (PubMed:12821669)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti57 – 571P → H.1 Publication
Corresponds to variant rs17855498 [ dbSNP | Ensembl ].
VAR_034943
Natural varianti130 – 1301C → Y.
Corresponds to variant rs55990541 [ dbSNP | Ensembl ].
VAR_062208
Natural varianti346 – 3461G → V in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_036391

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei41 – 222182Missing in isoform 3. 1 PublicationVSP_027939Add
BLAST
Alternative sequencei118 – 12811LSKGKTTAEDG → VSRIILIILHQ in isoform 2. 2 PublicationsVSP_027940Add
BLAST
Alternative sequencei129 – 369241Missing in isoform 2. 2 PublicationsVSP_027941Add
BLAST
Alternative sequencei143 – 22482TSFEL…EDWEG → S in isoform 5. 1 PublicationVSP_043786Add
BLAST
Alternative sequencei174 – 1741Missing in isoform 4. 2 PublicationsVSP_027943

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY326435 mRNA. Translation: AAP92162.1.
AY326436 mRNA. Translation: AAP92163.1.
AM422214 mRNA. Translation: CAM12309.1.
AY358475 mRNA. Translation: AAQ88839.1.
AK021670 mRNA. Translation: BAB13871.1. Sequence problems.
AK315379 mRNA. Translation: BAG37772.1.
AL832601 mRNA. Translation: CAD89943.1.
AC091013 Genomic DNA. No translation available.
AC116456 Genomic DNA. No translation available.
AC129895 Genomic DNA. No translation available.
CH471064 Genomic DNA. Translation: EAW68628.1.
CH471064 Genomic DNA. Translation: EAW68630.1.
BC022455 mRNA. Translation: AAH22455.1.
CCDSiCCDS44533.1. [Q7Z5B4-3]
CCDS55741.1. [Q7Z5B4-6]
CCDS55742.1. [Q7Z5B4-1]
CCDS7788.1. [Q7Z5B4-5]
RefSeqiNP_001128581.1. NM_001135109.2. [Q7Z5B4-3]
NP_001193600.1. NM_001206671.2. [Q7Z5B4-1]
NP_001193601.1. NM_001206672.2. [Q7Z5B4-6]
NP_078833.3. NM_024557.4. [Q7Z5B4-5]
XP_006718381.1. XM_006718318.1. [Q7Z5B4-5]
XP_006718383.1. XM_006718320.1.
UniGeneiHs.231850.
Hs.568986.

Genome annotation databases

EnsembliENST00000309737; ENSP00000308820; ENSG00000166405. [Q7Z5B4-1]
ENST00000335425; ENSP00000333988; ENSG00000166405. [Q7Z5B4-3]
ENST00000343202; ENSP00000344904; ENSG00000166405. [Q7Z5B4-5]
ENST00000419822; ENSP00000404415; ENSG00000166405. [Q7Z5B4-2]
ENST00000425599; ENSP00000395320; ENSG00000166405. [Q7Z5B4-6]
GeneIDi79608.
KEGGihsa:79608.
UCSCiuc001mgc.2. human. [Q7Z5B4-5]
uc001mgd.2. human. [Q7Z5B4-1]
uc001mge.2. human. [Q7Z5B4-3]
uc001mgf.4. human. [Q7Z5B4-2]
uc009yfm.2. human. [Q7Z5B4-6]

Polymorphism databases

DMDMi74713638.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY326435 mRNA. Translation: AAP92162.1 .
AY326436 mRNA. Translation: AAP92163.1 .
AM422214 mRNA. Translation: CAM12309.1 .
AY358475 mRNA. Translation: AAQ88839.1 .
AK021670 mRNA. Translation: BAB13871.1 . Sequence problems.
AK315379 mRNA. Translation: BAG37772.1 .
AL832601 mRNA. Translation: CAD89943.1 .
AC091013 Genomic DNA. No translation available.
AC116456 Genomic DNA. No translation available.
AC129895 Genomic DNA. No translation available.
CH471064 Genomic DNA. Translation: EAW68628.1 .
CH471064 Genomic DNA. Translation: EAW68630.1 .
BC022455 mRNA. Translation: AAH22455.1 .
CCDSi CCDS44533.1. [Q7Z5B4-3 ]
CCDS55741.1. [Q7Z5B4-6 ]
CCDS55742.1. [Q7Z5B4-1 ]
CCDS7788.1. [Q7Z5B4-5 ]
RefSeqi NP_001128581.1. NM_001135109.2. [Q7Z5B4-3 ]
NP_001193600.1. NM_001206671.2. [Q7Z5B4-1 ]
NP_001193601.1. NM_001206672.2. [Q7Z5B4-6 ]
NP_078833.3. NM_024557.4. [Q7Z5B4-5 ]
XP_006718381.1. XM_006718318.1. [Q7Z5B4-5 ]
XP_006718383.1. XM_006718320.1.
UniGenei Hs.231850.
Hs.568986.

3D structure databases

ProteinModelPortali Q7Z5B4.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 122743. 34 interactions.
IntActi Q7Z5B4. 1 interaction.
MINTi MINT-8343009.
STRINGi 9606.ENSP00000344904.

PTM databases

PhosphoSitei Q7Z5B4.

Polymorphism databases

DMDMi 74713638.

Proteomic databases

MaxQBi Q7Z5B4.
PaxDbi Q7Z5B4.
PRIDEi Q7Z5B4.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000309737 ; ENSP00000308820 ; ENSG00000166405 . [Q7Z5B4-1 ]
ENST00000335425 ; ENSP00000333988 ; ENSG00000166405 . [Q7Z5B4-3 ]
ENST00000343202 ; ENSP00000344904 ; ENSG00000166405 . [Q7Z5B4-5 ]
ENST00000419822 ; ENSP00000404415 ; ENSG00000166405 . [Q7Z5B4-2 ]
ENST00000425599 ; ENSP00000395320 ; ENSG00000166405 . [Q7Z5B4-6 ]
GeneIDi 79608.
KEGGi hsa:79608.
UCSCi uc001mgc.2. human. [Q7Z5B4-5 ]
uc001mgd.2. human. [Q7Z5B4-1 ]
uc001mge.2. human. [Q7Z5B4-3 ]
uc001mgf.4. human. [Q7Z5B4-2 ]
uc009yfm.2. human. [Q7Z5B4-6 ]

Organism-specific databases

CTDi 79608.
GeneCardsi GC11M008127.
H-InvDB HIX0009421.
HGNCi HGNC:30338. RIC3.
MIMi 610509. gene.
neXtProti NX_Q7Z5B4.
PharmGKBi PA142671066.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG46432.
GeneTreei ENSGT00440000034107.
HOVERGENi HBG106009.
InParanoidi Q7Z5B4.
OMAi HRKITNF.
OrthoDBi EOG7MKW7H.
PhylomeDBi Q7Z5B4.
TreeFami TF333291.

Miscellaneous databases

GeneWikii RIC3.
GenomeRNAii 79608.
NextBioi 68650.
PROi Q7Z5B4.
SOURCEi Search...

Gene expression databases

Bgeei Q7Z5B4.
CleanExi HS_RIC3.
ExpressionAtlasi Q7Z5B4. baseline and differential.
Genevestigatori Q7Z5B4.

Family and domain databases

InterProi IPR026160. Ric3.
[Graphical view ]
PANTHERi PTHR21723. PTHR21723. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Conservation within the RIC-3 gene family. Effectors of mammalian nicotinic acetylcholine receptor expression."
    Halevi S., Yassin L., Eshel M., Sala F., Sala S., Criado M., Treinin M.
    J. Biol. Chem. 278:34411-34417(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), ALTERNATIVE SPLICING (ISOFORMS 1; 2; 3 AND 4), TISSUE SPECIFICITY, FUNCTION.
  2. "Molecular cloning and characterization of a novel human variant of RIC-3, a putative chaperone of nicotinic acetylcholine receptors."
    Seredenina T., Ferraro T., Terstappen G.C., Caricasole A., Roncarati R.
    Biosci. Rep. 28:299-306(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), ALTERNATIVE SPLICING, FUNCTION, TISSUE SPECIFICITY.
    Tissue: Hippocampus.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
  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 4).
    Tissue: Brain and Embryo.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    Tissue: Spinal cord.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "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 4), VARIANT HIS-57.
    Tissue: Brain.
  9. "Ric-3 promotes functional expression of the nicotinic acetylcholine receptor alpha7 subunit in mammalian cells."
    Williams M.E., Burton B., Urrutia A., Shcherbatko A., Chavez-Noriega L.E., Cohen C.J., Aiyar J.
    J. Biol. Chem. 280:1257-1263(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CHRNA7.
  10. "Cell surface expression of 5-hydroxytryptamine type 3 receptors is promoted by RIC-3."
    Cheng A., McDonald N.A., Connolly C.N.
    J. Biol. Chem. 280:22502-22507(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH HTR3A, SUBCELLULAR LOCATION.
  11. "Dual role of the RIC-3 protein in trafficking of serotonin and nicotinic acetylcholine receptors."
    Castillo M., Mulet J., Gutierrez L.M., Ortiz J.A., Castelan F., Gerber S., Sala S., Sala F., Criado M.
    J. Biol. Chem. 280:27062-27068(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  12. "RIC-3 enhances functional expression of multiple nicotinic acetylcholine receptor subtypes in mammalian cells."
    Lansdell S.J., Gee V.J., Harkness P.C., Doward A.I., Baker E.R., Gibb A.J., Millar N.S.
    Mol. Pharmacol. 68:1431-1438(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CHRNA7; CHRNA3; CHRNA4; CHRNB2 AND CHRNB4.
  13. "Differential subcellular localization of RIC-3 isoforms and their role in determining 5-HT3 receptor composition."
    Cheng A., Bollan K.A., Greenwood S.M., Irving A.J., Connolly C.N.
    J. Biol. Chem. 282:26158-26166(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, TOPOLOGY, FUNCTION.
  14. "Lack of RIC-3 congruence with beta2 subunit-containing nicotinic acetylcholine receptors in bipolar disorder."
    Severance E.G., Yolken R.H.
    Neuroscience 148:454-460(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  15. "Tryptic digestion of ubiquitin standards reveals an improved strategy for identifying ubiquitinated proteins by mass spectrometry."
    Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D.
    Proteomics 7:868-874(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-202.
    Tissue: Mammary cancer.
  16. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-202, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. Cited for: VARIANT [LARGE SCALE ANALYSIS] VAL-346.

Entry informationi

Entry nameiRIC3_HUMAN
AccessioniPrimary (citable) accession number: Q7Z5B4
Secondary accession number(s): B0B1U0
, B2RD25, D3DQU5, Q6UX78, Q7Z5B3, Q86T94, Q8TBJ9, Q9HAH8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: October 1, 2003
Last modified: October 29, 2014
This is version 82 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 11
    Human chromosome 11: 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. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3