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Q66PJ3

- AR6P4_HUMAN

UniProt

Q66PJ3 - AR6P4_HUMAN

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Protein

ADP-ribosylation factor-like protein 6-interacting protein 4

Gene

ARL6IP4

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

Functioni

Involved in modulating alternative pre-mRNA splicing with either 5' distal site activation or preferential use of 3' proximal site. In case of infection by Herpes simplex virus (HSVI), may act as a splicing inhibitor of HSVI pre-mRNA.1 Publication

GO - Molecular functioni

  1. poly(A) RNA binding Source: UniProtKB

GO - Biological processi

  1. mRNA processing Source: UniProtKB-KW
  2. RNA splicing Source: ProtInc
Complete GO annotation...

Keywords - Biological processi

mRNA processing, mRNA splicing

Names & Taxonomyi

Protein namesi
Recommended name:
ADP-ribosylation factor-like protein 6-interacting protein 4
Short name:
ARL-6-interacting protein 4
Short name:
Aip-4
Alternative name(s):
HSP-975
HSVI-binding protein
SR-15
SRp25
Short name:
SR-25
Splicing factor SRrp37
Gene namesi
Name:ARL6IP4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:18076. ARL6IP4.

Subcellular locationi

Nucleusnucleolus 1 Publication. Nucleus speckle 1 Publication

GO - Cellular componenti

  1. nucleus Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134879338.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 421421ADP-ribosylation factor-like protein 6-interacting protein 4PRO_0000312270Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei332 – 3321Phosphoserine6 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ66PJ3.
PaxDbiQ66PJ3.
PRIDEiQ66PJ3.

PTM databases

PhosphoSiteiQ66PJ3.

Expressioni

Tissue specificityi

Isoforms 3 and 7 were identified in brain, pancreas, prostate, and testis, but little or no message could be detected in other tissues.1 Publication

Developmental stagei

Expressed only in G1/S phase.1 Publication

Inductioni

In case of Herpes simplex virus (HSVI)-binding to cells.1 Publication

Gene expression databases

BgeeiQ66PJ3.
CleanExiHS_ARL6IP4.
ExpressionAtlasiQ66PJ3. baseline.
GenevestigatoriQ66PJ3.

Organism-specific databases

HPAiHPA052098.

Interactioni

Subunit structurei

Interacts with ARL6 (By similarity). Interacts with ZCCHC17. Interacts with SRSF2.By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
IKBKGQ9Y6K92EBI-2683099,EBI-81279

Protein-protein interaction databases

BioGridi119477. 21 interactions.
IntActiQ66PJ3. 8 interactions.
MINTiMINT-5010073.
STRINGi9606.ENSP00000313422.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi190 – 28293Ser-richAdd
BLAST
Compositional biasi286 – 31227Lys-richAdd
BLAST

Sequence similaritiesi

Belongs to the ARL6IP4 family.Curated

Phylogenomic databases

eggNOGiNOG83556.
GeneTreeiENSGT00390000009670.
HOVERGENiHBG102109.
InParanoidiQ66PJ3.
OMAiWHRSAEE.
TreeFamiTF350468.

Family and domain databases

InterProiIPR019532. Nucl_RNA-splicing_assoc_SR-25.
[Graphical view]
PfamiPF10500. SR-25. 1 hit.
[Graphical view]

Sequences (7)i

Sequence statusi: Complete.

This entry describes 7 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q66PJ3-1) [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
MPRCTYQLEQ NPGFLPDGPG VHARAHCQDL SGPYGHEFAT SESLGGRVGK
60 70 80 90 100
TRAPQSGARS RMERAGPAGE EGGAREGRLL PRAPGAWVLR ACAERAALEV
110 120 130 140 150
GAASADTGVR GCGARGPAPL LASAGGGRAR DGTWGVRTKG SGAALPSRPA
160 170 180 190 200
SRAAPRPEAS SPPLPLEKAR GGLSGPQGGR ARGAMAHVGS RKRSRSRSRS
210 220 230 240 250
RGRGSEKRKK KSRKDTSRNC SASTSQGRKA STAPGAEASP SPCITERSKQ
260 270 280 290 300
KARRRTRSSS SSSSSSSSSS SSSSSSSSSS SSDGRKKRGK YKDKRRKKKK
310 320 330 340 350
KRKKLKKKGK EKAEAQQVEA LPGPSLDQWH RSAGEEEDGP VLTDEQKSRI
360 370 380 390 400
QAMKPMTKEE WDARQSIIRK VVDPETGRTR LIKGDGEVLE EIVTKERHRE
410 420
INKQATRGDC LAFQMRAGLL P
Length:421
Mass (Da):44,915
Last modified:July 9, 2014 - v2
Checksum:i46C75D66A5181DAC
GO
Isoform 2 (identifier: Q66PJ3-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     238-245: Missing.

Show »
Length:413
Mass (Da):44,159
Checksum:iBC723AA29C3D5E59
GO
Isoform 3 (identifier: Q66PJ3-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     227-245: Missing.

Show »
Length:402
Mass (Da):43,132
Checksum:i13B57EF2169FA844
GO
Isoform 4 (identifier: Q66PJ3-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     227-245: Missing.
     404-421: QATRGDCLAFQMRAGLLP → VGVAPLPAIRPQLCL

Show »
Length:399
Mass (Da):42,731
Checksum:i23D0D604986EE066
GO
Isoform 5 (identifier: Q66PJ3-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     238-245: Missing.
     317-364: Missing.

Show »
Length:365
Mass (Da):38,699
Checksum:i7E2C81AE496AC2D2
GO
Isoform 6 (identifier: Q66PJ3-6) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     238-276: ASPSPCITER...SSSSSSSSSS → VLLAPLLPPR...GGRRRRRGRS
     277-421: Missing.

Show »
Length:276
Mass (Da):28,528
Checksum:i6F944F7B299C9953
GO
Isoform 7 (identifier: Q66PJ3-7) [UniParc]FASTAAdd to Basket

Also known as: SRrp37-2

The sequence of this isoform differs from the canonical sequence as follows:
     1-184: Missing.
     227-237: Missing.

Show »
Length:226
Mass (Da):25,349
Checksum:iC41994822C524656
GO

Sequence cautioni

Isoform 6 : The sequence AAF76892.1 differs from that shown. Reason: Frameshift at position 276.
The sequence AAF76892.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
The sequence AAH01958.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
The sequence AAH15569.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
The sequence AAH15909.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
The sequence AAH94839.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
The sequence ACF07995.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
The sequence BAA94744.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti160 – 1601S → P in AAH94839. (PubMed:15489334)Curated
Sequence conflicti233 – 2331A → V in AAF76892. (PubMed:11884129)Curated

RNA editingi

Partially edited. In the brain, edited at about 68%.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti149 – 1491P → A.
Corresponds to variant rs12825243 [ dbSNP | Ensembl ].
VAR_059583
Natural varianti286 – 2861K → R in RNA edited version.
Corresponds to variant rs3178165 [ dbSNP | Ensembl ].
VAR_058333

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 184184Missing in isoform 7. 1 PublicationVSP_054581Add
BLAST
Alternative sequencei227 – 24519Missing in isoform 3 and isoform 4. 3 PublicationsVSP_029780Add
BLAST
Alternative sequencei227 – 23711Missing in isoform 7. 1 PublicationVSP_054582Add
BLAST
Alternative sequencei238 – 27639ASPSP…SSSSS → VLLAPLLPPRPPPLPPVMAG RSGGSTRTRGGRRRRRGRS in isoform 6. 1 PublicationVSP_029781Add
BLAST
Alternative sequencei238 – 2458Missing in isoform 2 and isoform 5. 3 PublicationsVSP_029782
Alternative sequencei277 – 421145Missing in isoform 6. 1 PublicationVSP_029783Add
BLAST
Alternative sequencei317 – 36448Missing in isoform 5. 1 PublicationVSP_029784Add
BLAST
Alternative sequencei404 – 42118QATRG…AGLLP → VGVAPLPAIRPQLCL in isoform 4. 1 PublicationVSP_029785Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
EU624490 mRNA. Translation: ACF07995.1. Different initiation.
EU624491 mRNA. Translation: ACF07996.1.
AC026362 Genomic DNA. No translation available.
CH471054 Genomic DNA. Translation: EAW98376.1.
CH471054 Genomic DNA. Translation: EAW98374.1.
BC001958 mRNA. Translation: AAH01958.1. Different initiation.
BC015569 mRNA. Translation: AAH15569.1. Different initiation.
BC015909 mRNA. Translation: AAH15909.2. Different initiation.
BC094839 mRNA. Translation: AAH94839.1. Different initiation.
AF267748 mRNA. Translation: AAF76892.1. Sequence problems.
AB035384 mRNA. Translation: BAA94744.1. Different initiation.
DQ099385 mRNA. Translation: AAZ13761.1.
EF036485 mRNA. Translation: ABO65071.1.
CCDSiCCDS31923.2. [Q66PJ3-1]
CCDS41856.2. [Q66PJ3-4]
CCDS45004.2. [Q66PJ3-2]
CCDS53843.2. [Q66PJ3-3]
CCDS61273.1. [Q66PJ3-7]
PIRiJC7220.
RefSeqiNP_001002251.2. NM_001002251.2. [Q66PJ3-2]
NP_001002252.2. NM_001002252.2. [Q66PJ3-4]
NP_001265307.1. NM_001278378.1. [Q66PJ3-5]
NP_001265308.1. NM_001278379.1.
NP_001265309.1. NM_001278380.1. [Q66PJ3-7]
NP_057722.3. NM_016638.3. [Q66PJ3-3]
NP_061164.3. NM_018694.3. [Q66PJ3-1]
UniGeneiHs.103561.

Genome annotation databases

EnsembliENST00000315580; ENSP00000313422; ENSG00000182196. [Q66PJ3-1]
ENST00000357866; ENSP00000350532; ENSG00000182196.
ENST00000392435; ENSP00000376230; ENSG00000182196. [Q66PJ3-4]
ENST00000426960; ENSP00000406036; ENSG00000182196.
ENST00000453766; ENSP00000414847; ENSG00000182196. [Q66PJ3-2]
ENST00000454885; ENSP00000396723; ENSG00000182196. [Q66PJ3-7]
ENST00000543566; ENSP00000442718; ENSG00000182196. [Q66PJ3-3]
GeneIDi51329.
KEGGihsa:51329.
UCSCiuc001uec.3. human. [Q66PJ3-2]
uc001ued.3. human. [Q66PJ3-1]
uc001uef.3. human. [Q66PJ3-4]
uc001uei.3. human. [Q66PJ3-5]
uc009zxt.3. human.

Polymorphism databases

DMDMi74736329.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism, RNA editing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
EU624490 mRNA. Translation: ACF07995.1 . Different initiation.
EU624491 mRNA. Translation: ACF07996.1 .
AC026362 Genomic DNA. No translation available.
CH471054 Genomic DNA. Translation: EAW98376.1 .
CH471054 Genomic DNA. Translation: EAW98374.1 .
BC001958 mRNA. Translation: AAH01958.1 . Different initiation.
BC015569 mRNA. Translation: AAH15569.1 . Different initiation.
BC015909 mRNA. Translation: AAH15909.2 . Different initiation.
BC094839 mRNA. Translation: AAH94839.1 . Different initiation.
AF267748 mRNA. Translation: AAF76892.1 . Sequence problems.
AB035384 mRNA. Translation: BAA94744.1 . Different initiation.
DQ099385 mRNA. Translation: AAZ13761.1 .
EF036485 mRNA. Translation: ABO65071.1 .
CCDSi CCDS31923.2. [Q66PJ3-1 ]
CCDS41856.2. [Q66PJ3-4 ]
CCDS45004.2. [Q66PJ3-2 ]
CCDS53843.2. [Q66PJ3-3 ]
CCDS61273.1. [Q66PJ3-7 ]
PIRi JC7220.
RefSeqi NP_001002251.2. NM_001002251.2. [Q66PJ3-2 ]
NP_001002252.2. NM_001002252.2. [Q66PJ3-4 ]
NP_001265307.1. NM_001278378.1. [Q66PJ3-5 ]
NP_001265308.1. NM_001278379.1.
NP_001265309.1. NM_001278380.1. [Q66PJ3-7 ]
NP_057722.3. NM_016638.3. [Q66PJ3-3 ]
NP_061164.3. NM_018694.3. [Q66PJ3-1 ]
UniGenei Hs.103561.

3D structure databases

ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 119477. 21 interactions.
IntActi Q66PJ3. 8 interactions.
MINTi MINT-5010073.
STRINGi 9606.ENSP00000313422.

PTM databases

PhosphoSitei Q66PJ3.

Polymorphism databases

DMDMi 74736329.

Proteomic databases

MaxQBi Q66PJ3.
PaxDbi Q66PJ3.
PRIDEi Q66PJ3.

Protocols and materials databases

DNASUi 51329.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000315580 ; ENSP00000313422 ; ENSG00000182196 . [Q66PJ3-1 ]
ENST00000357866 ; ENSP00000350532 ; ENSG00000182196 .
ENST00000392435 ; ENSP00000376230 ; ENSG00000182196 . [Q66PJ3-4 ]
ENST00000426960 ; ENSP00000406036 ; ENSG00000182196 .
ENST00000453766 ; ENSP00000414847 ; ENSG00000182196 . [Q66PJ3-2 ]
ENST00000454885 ; ENSP00000396723 ; ENSG00000182196 . [Q66PJ3-7 ]
ENST00000543566 ; ENSP00000442718 ; ENSG00000182196 . [Q66PJ3-3 ]
GeneIDi 51329.
KEGGi hsa:51329.
UCSCi uc001uec.3. human. [Q66PJ3-2 ]
uc001ued.3. human. [Q66PJ3-1 ]
uc001uef.3. human. [Q66PJ3-4 ]
uc001uei.3. human. [Q66PJ3-5 ]
uc009zxt.3. human.

Organism-specific databases

CTDi 51329.
GeneCardsi GC12P123464.
HGNCi HGNC:18076. ARL6IP4.
HPAi HPA052098.
MIMi 607668. gene.
neXtProti NX_Q66PJ3.
PharmGKBi PA134879338.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG83556.
GeneTreei ENSGT00390000009670.
HOVERGENi HBG102109.
InParanoidi Q66PJ3.
OMAi WHRSAEE.
TreeFami TF350468.

Miscellaneous databases

ChiTaRSi ARL6IP4. human.
GeneWikii ARL6IP4.
GenomeRNAii 51329.
NextBioi 35470743.
PROi Q66PJ3.
SOURCEi Search...

Gene expression databases

Bgeei Q66PJ3.
CleanExi HS_ARL6IP4.
ExpressionAtlasi Q66PJ3. baseline.
Genevestigatori Q66PJ3.

Family and domain databases

InterProi IPR019532. Nucl_RNA-splicing_assoc_SR-25.
[Graphical view ]
Pfami PF10500. SR-25. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "SRrp37, a novel splicing regulator located in the nuclear speckles and nucleoli, interacts with SC35 and modulates alternative pre-mRNA splicing in vivo."
    Ouyang P.
    J. Cell. Biochem. 108:304-314(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 7), FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SRSF2 AND ZCCHC17, ALTERNATIVE SPLICING, TISSUE SPECIFICITY.
  2. "The finished DNA sequence of human chromosome 12."
    Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
    , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
    Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. 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), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 42-421 (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 175-421 (ISOFORM 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 176-421 (ISOFORM 4).
    Tissue: Brain, Eye, Skin and Uterus.
  5. "An SR-protein induced by HSVI binding to cells functioning as a splicing inhibitor of viral pre-mRNA."
    Li Q., Zhao H., Jiang L., Che Y., Dong C., Wang L., Wang J., Liu L.
    J. Mol. Biol. 316:887-894(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 128-421 (ISOFORM 6), POSSIBLE FUNCTION, PHOSPHORYLATION, DEVELOPMENTAL STAGE, INDUCTION.
    Tissue: Lung.
  6. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 165-421 (ISOFORM 3).
  7. Zhou G., Nong W., Li H., Ke R., Shen C., Zhong G., Zheng Z., Liang M., Wen S., Lin L., Yang S.
    Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 185-421 (ISOFORM 5).
  8. "Searching for interaction partners of the transcription factor REST/NRSF by two-hybrid screening."
    Santana-Roman H., Curiel-Quesada E., Tapia-Ramirez J.
    Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 190-287 (ISOFORM 2).
  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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-332, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-332, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "Screening of human SNP database identifies recoding sites of A-to-I RNA editing."
    Gommans W.M., Tatalias N.E., Sie C.P., Dupuis D., Vendetti N., Smith L., Kaushal R., Maas S.
    RNA 14:2074-2085(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: RNA EDITING OF POSITION 225.
  12. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-332, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-332, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  15. "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-332, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-332, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiAR6P4_HUMAN
AccessioniPrimary (citable) accession number: Q66PJ3
Secondary accession number(s): A4UCR8
, B3V0L0, B3V0L1, Q4F966, Q504R8, Q96BI2, Q9NR05, Q9P2R9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 4, 2007
Last sequence update: July 9, 2014
Last modified: October 29, 2014
This is version 87 of the entry and version 2 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

Caution

It is uncertain whether Met-1 or Met-62 is the initiator.Curated

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: 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