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P53367 (ARFP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Arfaptin-1
Alternative name(s):
ADP-ribosylation factor-interacting protein 1
Gene names
Name:ARFIP1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length373 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Putative target protein of ADP-ribosylation factor.

Subunit structure

Interacts with non-myristoylated GTP-bound ARF3, but not to GDP-bound ARF3, and also to ARF1. Binds with lower affinity to ARF5 and with very little affinity to ARF6. Ref.6

Tissue specificity

Ubiquitously expressed. Higher levels in liver, pancreas, placenta, skeletal muscle and heart.

Sequence similarities

Contains 1 AH domain.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform B (identifier: P53367-1)

Also known as: 1b;

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 A (identifier: P53367-2)

Also known as: 1a;

The sequence of this isoform differs from the canonical sequence as follows:
     69-100: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.9
Chain2 – 373372Arfaptin-1
PRO_0000064665

Regions

Domain153 – 353201AH

Amino acid modifications

Modified residue21N-acetylalanine Ref.9 Ref.11 Ref.12
Modified residue51Phosphoserine Ref.9
Modified residue691Phosphoserine Ref.7 Ref.9
Modified residue791Phosphoserine Ref.9
Modified residue1321Phosphoserine Ref.7 Ref.11
Modified residue3611Phosphothreonine Ref.8

Natural variations

Alternative sequence69 – 10032Missing in isoform A.
VSP_004088

Sequences

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

Last modified May 27, 2002. Version 2.
Checksum: 7A315D0E67DECDBF

FASTA37341,738
        10         20         30         40         50         60 
MAQESPKNSA AEIPVTSNGE VDDSREHSFN RDLKHSLPSG LGLSETQITS HGFDNTKEGV 

        70         80         90        100        110        120 
IEAGAFQGSP APPLPSVMSP SRVAASRLAQ QGSDLIVPAG GQRTQTKSGP VILADEIKNP 

       130        140        150        160        170        180 
AMEKLELVRK WSLNTYKCTR QIISEKLGRG SRTVDLELEA QIDILRDNKK KYENILKLAQ 

       190        200        210        220        230        240 
TLSTQLFQMV HTQRQLGDAF ADLSLKSLEL HEEFGYNADT QKLLAKNGET LLGAINFFIA 

       250        260        270        280        290        300 
SVNTLVNKTI EDTLMTVKQY ESARIEYDAY RTDLEELNLG PRDANTLPKI EQSQHLFQAH 

       310        320        330        340        350        360 
KEKYDKMRND VSVKLKFLEE NKVKVLHNQL VLFHNAIAAY FAGNQKQLEQ TLKQFHIKLK 

       370 
TPGVDAPSWL EEQ 

« Hide

Isoform A (1a) [UniParc].

Checksum: 94675E3FF3FB9D08
Show »

FASTA34138,599

References

« Hide 'large scale' references
[1]"Arfaptin 1, a putative cytosolic target protein of ADP-ribosylation factor, is recruited to Golgi membranes."
Kanoh H., Williger B.-T., Exton J.H.
J. Biol. Chem. 272:5421-5429(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
[2]"Arfaptin-1b, a long splice variant of arfaptin-1."
Premont R.T., Lefkowitz R.J.
Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B).
Tissue: Liver.
[3]"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. expand/collapse author list , 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 A).
Tissue: Brain.
[4]Mural R.J., Istrail S., Sutton 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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] (ISOFORMS A AND B).
Tissue: Brain and Uterus.
[6]"Arfaptin 1 forms a complex with ADP-ribosylation factor and inhibits phospholipase D."
Williger B.-T., Provost J.J., Ho W.-T., Milstine J., Exton J.H.
FEBS Lett. 454:85-89(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ARF1; ARF3; ARF5 AND ARF6.
[7]"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-69 AND SER-132, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"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 THR-361, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[9]"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5; SER-69 AND SER-79, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"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].
[11]"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U52521 mRNA. Translation: AAA97923.1.
AF124489 mRNA. Translation: AAD29390.1.
AK290472 mRNA. Translation: BAF83161.1.
CH471056 Genomic DNA. Translation: EAX04968.1.
CH471056 Genomic DNA. Translation: EAX04969.1.
BC103759 mRNA. Translation: AAI03760.1.
BC105114 mRNA. Translation: AAI05115.1.
BC105116 mRNA. Translation: AAI05117.1.
BC143675 mRNA. Translation: AAI43676.1.
CCDSCCDS34080.1. [P53367-1]
CCDS3780.1. [P53367-2]
PIRG02515.
RefSeqNP_001020764.1. NM_001025593.2. [P53367-2]
NP_001020766.1. NM_001025595.2. [P53367-1]
NP_001274360.1. NM_001287431.1. [P53367-1]
NP_001274361.1. NM_001287432.1. [P53367-1]
NP_001274362.1. NM_001287433.1. [P53367-2]
NP_055262.1. NM_014447.3. [P53367-2]
UniGeneHs.416089.

3D structure databases

ProteinModelPortalP53367.
SMRP53367. Positions 151-351.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid118084. 19 interactions.
IntActP53367. 3 interactions.
MINTMINT-3019815.
STRING9606.ENSP00000296557.

PTM databases

PhosphoSiteP53367.

Polymorphism databases

DMDM21264399.

Proteomic databases

MaxQBP53367.
PaxDbP53367.
PRIDEP53367.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000353617; ENSP00000296557; ENSG00000164144. [P53367-1]
ENST00000356064; ENSP00000348360; ENSG00000164144. [P53367-2]
ENST00000405727; ENSP00000384189; ENSG00000164144. [P53367-2]
ENST00000451320; ENSP00000395083; ENSG00000164144. [P53367-1]
GeneID27236.
KEGGhsa:27236.
UCSCuc003imz.3. human. [P53367-1]
uc003ina.3. human. [P53367-2]

Organism-specific databases

CTD27236.
GeneCardsGC04P153701.
HGNCHGNC:21496. ARFIP1.
HPACAB005080.
HPA037375.
MIM605928. gene.
neXtProtNX_P53367.
PharmGKBPA134920621.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG302946.
HOGENOMHOG000236308.
HOVERGENHBG050564.
InParanoidP53367.
OMALLTVKQY.
OrthoDBEOG7VQJD9.
PhylomeDBP53367.
TreeFamTF314945.

Gene expression databases

ArrayExpressP53367.
BgeeP53367.
CleanExHS_ARFIP1.
GenevestigatorP53367.

Family and domain databases

Gene3D1.20.1270.60. 1 hit.
InterProIPR027267. AH/BAR-dom.
IPR010504. AH_dom.
[Graphical view]
PfamPF06456. Arfaptin. 1 hit.
[Graphical view]
SMARTSM01015. Arfaptin. 1 hit.
[Graphical view]
PROSITEPS50870. AH. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSARFIP1. human.
GeneWikiARFIP1.
GenomeRNAi27236.
NextBio50103.
PROP53367.
SOURCESearch...

Entry information

Entry nameARFP1_HUMAN
AccessionPrimary (citable) accession number: P53367
Secondary accession number(s): Q2M2X4, Q3SYL4, Q9Y2X6
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: May 27, 2002
Last modified: July 9, 2014
This is version 116 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 chromosome 4

Human chromosome 4: entries, gene names and cross-references to MIM