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Q66PJ3 (AR6P4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 84. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:ARL6IP4
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length421 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.5

Subunit structure

Interacts with ARL6 By similarity. Interacts with ZCCHC17. Interacts with SRSF2. Ref.1

Subcellular location

Nucleusnucleolus. Nucleus speckle Ref.1.

Tissue specificity

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

Developmental stage

Expressed only in G1/S phase. Ref.5

Induction

In case of Herpes simplex virus (HSVI)-binding to cells. Ref.5

Sequence similarities

Belongs to the ARL6IP4 family.

Caution

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

RNA editing

Edited at position 286.
Partially edited. In the brain, edited at about 68%. Ref.11

Sequence caution

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.

Isoform 6: The sequence AAF76892.1 differs from that shown. Reason: Frameshift at position 276.

Ontologies

Keywords
   Biological processmRNA processing
mRNA splicing
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Polymorphism
RNA editing
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processRNA splicing

Traceable author statement Ref.6. Source: ProtInc

mRNA processing

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentnuclear speck

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleolus

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Traceable author statement Ref.6. Source: ProtInc

   Molecular_functionpoly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 20098747. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

IKBKGQ9Y6K92EBI-2683099,EBI-81279

Alternative products

This entry describes 7 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q66PJ3-1)

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.
Isoform 2 (identifier: Q66PJ3-2)

The sequence of this isoform differs from the canonical sequence as follows:
     238-245: Missing.
Isoform 3 (identifier: Q66PJ3-3)

The sequence of this isoform differs from the canonical sequence as follows:
     227-245: Missing.
Isoform 4 (identifier: Q66PJ3-4)

The sequence of this isoform differs from the canonical sequence as follows:
     227-245: Missing.
     404-421: QATRGDCLAFQMRAGLLP → VGVAPLPAIRPQLCL
Isoform 5 (identifier: Q66PJ3-5)

The sequence of this isoform differs from the canonical sequence as follows:
     238-245: Missing.
     317-364: Missing.
Isoform 6 (identifier: Q66PJ3-6)

The sequence of this isoform differs from the canonical sequence as follows:
     238-276: ASPSPCITER...SSSSSSSSSS → VLLAPLLPPR...GGRRRRRGRS
     277-421: Missing.
Isoform 7 (identifier: Q66PJ3-7)

Also known as: SRrp37-2;

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 421421ADP-ribosylation factor-like protein 6-interacting protein 4
PRO_0000312270

Regions

Compositional bias190 – 28293Ser-rich
Compositional bias286 – 31227Lys-rich

Amino acid modifications

Modified residue3321Phosphoserine Ref.9 Ref.10 Ref.13 Ref.14 Ref.15 Ref.17

Natural variations

Alternative sequence1 – 184184Missing in isoform 7.
VSP_054581
Alternative sequence227 – 24519Missing in isoform 3 and isoform 4.
VSP_029780
Alternative sequence227 – 23711Missing in isoform 7.
VSP_054582
Alternative sequence238 – 27639ASPSP…SSSSS → VLLAPLLPPRPPPLPPVMAG RSGGSTRTRGGRRRRRGRS in isoform 6.
VSP_029781
Alternative sequence238 – 2458Missing in isoform 2 and isoform 5.
VSP_029782
Alternative sequence277 – 421145Missing in isoform 6.
VSP_029783
Alternative sequence317 – 36448Missing in isoform 5.
VSP_029784
Alternative sequence404 – 42118QATRG…AGLLP → VGVAPLPAIRPQLCL in isoform 4.
VSP_029785
Natural variant1491P → A.
Corresponds to variant rs12825243 [ dbSNP | Ensembl ].
VAR_059583
Natural variant2861K → R in RNA edited version.
Corresponds to variant rs3178165 [ dbSNP | Ensembl ].
VAR_058333

Experimental info

Sequence conflict1601S → P in AAH94839. Ref.4
Sequence conflict2331A → V in AAF76892. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 9, 2014. Version 2.
Checksum: 46C75D66A5181DAC

FASTA42144,915
        10         20         30         40         50         60 
MPRCTYQLEQ NPGFLPDGPG VHARAHCQDL SGPYGHEFAT SESLGGRVGK TRAPQSGARS 

        70         80         90        100        110        120 
RMERAGPAGE EGGAREGRLL PRAPGAWVLR ACAERAALEV GAASADTGVR GCGARGPAPL 

       130        140        150        160        170        180 
LASAGGGRAR DGTWGVRTKG SGAALPSRPA SRAAPRPEAS SPPLPLEKAR GGLSGPQGGR 

       190        200        210        220        230        240 
ARGAMAHVGS RKRSRSRSRS RGRGSEKRKK KSRKDTSRNC SASTSQGRKA STAPGAEASP 

       250        260        270        280        290        300 
SPCITERSKQ KARRRTRSSS SSSSSSSSSS SSSSSSSSSS SSDGRKKRGK YKDKRRKKKK 

       310        320        330        340        350        360 
KRKKLKKKGK EKAEAQQVEA LPGPSLDQWH RSAGEEEDGP VLTDEQKSRI QAMKPMTKEE 

       370        380        390        400        410        420 
WDARQSIIRK VVDPETGRTR LIKGDGEVLE EIVTKERHRE INKQATRGDC LAFQMRAGLL 


P 

« Hide

Isoform 2 [UniParc].

Checksum: BC723AA29C3D5E59
Show »

FASTA41344,159
Isoform 3 [UniParc].

Checksum: 13B57EF2169FA844
Show »

FASTA40243,132
Isoform 4 [UniParc].

Checksum: 23D0D604986EE066
Show »

FASTA39942,731
Isoform 5 [UniParc].

Checksum: 7E2C81AE496AC2D2
Show »

FASTA36538,699
Isoform 6 [UniParc].

Checksum: 6F944F7B299C9953
Show »

FASTA27628,528
Isoform 7 (SRrp37-2) [UniParc].

Checksum: C41994822C524656
Show »

FASTA22625,349

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"Molecular cloning and expression analysis of a putative nuclear protein, SR-25."
Sasahara K., Yamaoka T., Moritani M., Tanaka M., Iwahana H., Yoshimoto K., Miyagawa J., Kuroda Y., Itakura M.
Biochem. Biophys. Res. Commun. 269:444-450(2000) [PubMed] [Europe PMC] [Abstract]
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRJC7220.
RefSeqNP_001002251.2. NM_001002251.2.
NP_001002252.2. NM_001002252.2.
NP_001265307.1. NM_001278378.1.
NP_001265308.1. NM_001278379.1.
NP_001265309.1. NM_001278380.1. [Q66PJ3-7]
NP_057722.3. NM_016638.3.
NP_061164.3. NM_018694.3.
UniGeneHs.103561.

3D structure databases

ProteinModelPortalQ66PJ3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid119477. 8 interactions.
IntActQ66PJ3. 7 interactions.
MINTMINT-5010073.
STRING9606.ENSP00000313422.

PTM databases

PhosphoSiteQ66PJ3.

Polymorphism databases

DMDM74736329.

Proteomic databases

MaxQBQ66PJ3.
PaxDbQ66PJ3.
PRIDEQ66PJ3.

Protocols and materials databases

DNASU51329.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000315580; ENSP00000313422; ENSG00000182196. [Q66PJ3-1]
ENST00000357866; ENSP00000350532; ENSG00000182196.
ENST00000392435; ENSP00000376230; ENSG00000182196. [Q66PJ3-4]
ENST00000426960; ENSP00000406036; ENSG00000182196.
ENST00000453766; ENSP00000414847; ENSG00000182196. [Q66PJ3-2]
ENST00000454885; ENSP00000396723; ENSG00000182196.
ENST00000539770; ENSP00000438969; ENSG00000182196. [Q66PJ3-6]
ENST00000543566; ENSP00000442718; ENSG00000182196. [Q66PJ3-3]
GeneID51329.
KEGGhsa:51329.
UCSCuc001uec.3. human. [Q66PJ3-2]
uc001ued.3. human. [Q66PJ3-1]
uc001uef.3. human. [Q66PJ3-4]
uc001uei.3. human. [Q66PJ3-5]

Organism-specific databases

CTD51329.
GeneCardsGC12P123464.
HGNCHGNC:18076. ARL6IP4.
HPAHPA052098.
MIM607668. gene.
neXtProtNX_Q66PJ3.
PharmGKBPA134879338.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG83556.
HOVERGENHBG102109.
OMAWHRSAEE.
PhylomeDBQ66PJ3.
TreeFamTF350468.

Gene expression databases

BgeeQ66PJ3.
CleanExHS_ARL6IP4.
GenevestigatorQ66PJ3.

Family and domain databases

InterProIPR019532. Nucl_RNA-splicing_assoc_SR-25.
[Graphical view]
PfamPF10500. SR-25. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSARL6IP4. human.
GeneWikiARL6IP4.
GenomeRNAi51329.
NextBio35470743.
PROQ66PJ3.
SOURCESearch...

Entry information

Entry nameAR6P4_HUMAN
AccessionPrimary (citable) accession number: Q66PJ3
Secondary accession number(s): A4UCR8 expand/collapse secondary AC list , B3V0L0, B3V0L1, Q4F966, Q504R8, Q96BI2, Q9NR05, Q9P2R9
Entry history
Integrated into UniProtKB/Swiss-Prot: December 4, 2007
Last sequence update: July 9, 2014
Last modified: July 9, 2014
This is version 84 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM