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Q8N6H7

- ARFG2_HUMAN

UniProt

Q8N6H7 - ARFG2_HUMAN

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Protein

ADP-ribosylation factor GTPase-activating protein 2

Gene

ARFGAP2

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

Functioni

GTPase-activating protein (GAP) for ADP ribosylation factor 1 (ARF1). Implicated in coatomer-mediated protein transport between the Golgi complex and the endoplasmic reticulum. Hydrolysis of ARF1-bound GTP may lead to dissociation of coatomer from Golgi-derived membranes to allow fusion with target membranes.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri26 – 4924C4-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. ARF GTPase activator activity Source: InterPro
  2. zinc ion binding Source: InterPro

GO - Biological processi

  1. protein transport Source: UniProtKB-KW
  2. regulation of ARF GTPase activity Source: InterPro
  3. vesicle-mediated transport Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

GTPase activation

Keywords - Biological processi

ER-Golgi transport, Protein transport, Transport

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
ADP-ribosylation factor GTPase-activating protein 2
Short name:
ARF GAP 2
Alternative name(s):
GTPase-activating protein ZNF289
Zinc finger protein 289
Gene namesi
Name:ARFGAP2
Synonyms:ZNF289
ORF Names:Nbla10535
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:13504. ARFGAP2.

Subcellular locationi

Cytoplasm 1 Publication. Golgi apparatus membrane 1 Publication; Peripheral membrane protein 1 Publication; Cytoplasmic side 1 Publication
Note: Also found on peripheral punctate structures likely to be endoplasmic reticulum-Golgi intermediate compartment.

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. Golgi apparatus Source: HPA
  3. nucleolus Source: HPA
  4. plasma membrane Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Golgi apparatus, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162376868.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 521520ADP-ribosylation factor GTPase-activating protein 2PRO_0000278468Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei146 – 1461Phosphoserine4 Publications
Modified residuei240 – 2401PhosphoserineBy similarity
Modified residuei368 – 3681Phosphoserine4 Publications
Modified residuei432 – 4321Phosphoserine3 Publications
Modified residuei433 – 4331Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ8N6H7.
PaxDbiQ8N6H7.
PeptideAtlasiQ8N6H7.
PRIDEiQ8N6H7.

PTM databases

PhosphoSiteiQ8N6H7.

Expressioni

Gene expression databases

BgeeiQ8N6H7.
CleanExiHS_ARFGAP2.
ExpressionAtlasiQ8N6H7. baseline and differential.
GenevestigatoriQ8N6H7.

Organism-specific databases

HPAiHPA016649.
HPA018152.

Interactioni

Subunit structurei

Interacts with the coatomer complex. Interacts with the C-terminal appendage domain of COPG1.2 Publications

Protein-protein interaction databases

BioGridi124065. 3 interactions.
STRINGi9606.ENSP00000327309.

Structurei

Secondary structure

1
521
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi7 – 1913
Helixi21 – 244
Turni27 – 293
Beta strandi36 – 383
Turni39 – 424
Beta strandi43 – 453
Helixi47 – 5610
Turni58 – 603
Beta strandi63 – 686
Helixi74 – 829
Helixi85 – 9410
Helixi102 – 1065
Helixi109 – 12416

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2P57X-ray1.80A3-130[»]
ProteinModelPortaliQ8N6H7.
SMRiQ8N6H7. Positions 4-127.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8N6H7.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini11 – 127117Arf-GAPPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni97 – 521425Required for interaction with coatomerAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili242 – 30867Sequence AnalysisAdd
BLAST

Sequence similaritiesi

Contains 1 Arf-GAP domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri26 – 4924C4-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Coiled coil, Zinc-finger

Phylogenomic databases

eggNOGiCOG5347.
GeneTreeiENSGT00390000005436.
HOGENOMiHOG000162970.
HOVERGENiHBG050563.
InParanoidiQ8N6H7.
KOiK12493.
OMAiDTDATWG.
OrthoDBiEOG7B8S42.
PhylomeDBiQ8N6H7.
TreeFamiTF313985.

Family and domain databases

InterProiIPR001164. ArfGAP.
[Graphical view]
PfamiPF01412. ArfGap. 1 hit.
[Graphical view]
PRINTSiPR00405. REVINTRACTNG.
SMARTiSM00105. ArfGap. 1 hit.
[Graphical view]
PROSITEiPS50115. ARFGAP. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q8N6H7-1) [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
MAAEPNKTEI QTLFKRLRAV PTNKACFDCG AKNPSWASIT YGVFLCIDCS
60 70 80 90 100
GVHRSLGVHL SFIRSTELDS NWNWFQLRCM QVGGNANATA FFRQHGCTAN
110 120 130 140 150
DANTKYNSRA AQMYREKIRQ LGSAALARHG TDLWIDNMSS AVPNHSPEKK
160 170 180 190 200
DSDFFTEHTQ PPAWDAPATE PSGTQQPAPS TESSGLAQPE HGPNTDLLGT
210 220 230 240 250
SPKASLELKS SIIGKKKPAA AKKGLGAKKG LGAQKVSSQS FSEIERQAQV
260 270 280 290 300
AEKLREQQAA DAKKQAEESM VASMRLAYQE LQIDRKKEEK KLQNLEGKKR
310 320 330 340 350
EQAERLGMGL VSRSSVSHSV LSEMQVIEQE TPVSAKSSRS QLDLFDDVGT
360 370 380 390 400
FASGPPKYKD NPFSLGESFG SRWDTDAAWG MDRVEEKEPE VTISSIRPIS
410 420 430 440 450
ERATNRREVE SRSSGLESSE ARQKFAGAKA ISSDMFFGRE VDAEYEARSR
460 470 480 490 500
LQQLSGSSAI SSSDLFGDMD GAHGAGSVSL GNVLPTADIA QFKQGVKSVA
510 520
GKMAVLANGV MNSLQDRYGS Y
Length:521
Mass (Da):56,720
Last modified:October 1, 2002 - v1
Checksum:i16655EBA94D29E81
GO
Isoform 2 (identifier: Q8N6H7-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-79: Missing.
     133-160: Missing.

Note: No experimental confirmation available.

Show »
Length:414
Mass (Da):44,543
Checksum:iCB86DEEF636E8D91
GO
Isoform 3 (identifier: Q8N6H7-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-269: Missing.

Note: No experimental confirmation available.

Show »
Length:252
Mass (Da):27,535
Checksum:i8DFD0EE52D062600
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti40 – 401T → M in BAB55144. (PubMed:14702039)Curated
Sequence conflicti107 – 1071N → S in BAB55144. (PubMed:14702039)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti143 – 1431P → R.
Corresponds to variant rs11542793 [ dbSNP | Ensembl ].
VAR_048321
Natural varianti339 – 3391R → H.
Corresponds to variant rs34662994 [ dbSNP | Ensembl ].
VAR_048322
Natural varianti406 – 4061R → W.
Corresponds to variant rs35950498 [ dbSNP | Ensembl ].
VAR_048323
Natural varianti411 – 4111S → N.1 Publication
Corresponds to variant rs3740691 [ dbSNP | Ensembl ].
VAR_030780

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 269269Missing in isoform 3. 1 PublicationVSP_056054Add
BLAST
Alternative sequencei1 – 7979Missing in isoform 2. 1 PublicationVSP_056055Add
BLAST
Alternative sequencei133 – 16028Missing in isoform 2. 1 PublicationVSP_056056Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK027482 mRNA. Translation: BAB55144.1.
AK301785 mRNA. Translation: BAG63241.1.
AK315992 mRNA. Translation: BAH14363.1.
AC090589 Genomic DNA. No translation available.
CH471064 Genomic DNA. Translation: EAW67963.1.
CH471064 Genomic DNA. Translation: EAW67968.1.
BC030148 mRNA. Translation: AAH30148.1.
AL834337 mRNA. Translation: CAD39004.1.
AB073358 mRNA. Translation: BAE45716.1.
CCDSiCCDS7926.1. [Q8N6H7-1]
RefSeqiNP_001229761.1. NM_001242832.1.
NP_115765.2. NM_032389.4.
UniGeneiHs.436204.

Genome annotation databases

EnsembliENST00000524782; ENSP00000434442; ENSG00000149182. [Q8N6H7-1]
GeneIDi84364.
KEGGihsa:84364.
UCSCiuc001ndt.3. human. [Q8N6H7-1]

Polymorphism databases

DMDMi74729129.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK027482 mRNA. Translation: BAB55144.1 .
AK301785 mRNA. Translation: BAG63241.1 .
AK315992 mRNA. Translation: BAH14363.1 .
AC090589 Genomic DNA. No translation available.
CH471064 Genomic DNA. Translation: EAW67963.1 .
CH471064 Genomic DNA. Translation: EAW67968.1 .
BC030148 mRNA. Translation: AAH30148.1 .
AL834337 mRNA. Translation: CAD39004.1 .
AB073358 mRNA. Translation: BAE45716.1 .
CCDSi CCDS7926.1. [Q8N6H7-1 ]
RefSeqi NP_001229761.1. NM_001242832.1.
NP_115765.2. NM_032389.4.
UniGenei Hs.436204.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2P57 X-ray 1.80 A 3-130 [» ]
ProteinModelPortali Q8N6H7.
SMRi Q8N6H7. Positions 4-127.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 124065. 3 interactions.
STRINGi 9606.ENSP00000327309.

PTM databases

PhosphoSitei Q8N6H7.

Polymorphism databases

DMDMi 74729129.

Proteomic databases

MaxQBi Q8N6H7.
PaxDbi Q8N6H7.
PeptideAtlasi Q8N6H7.
PRIDEi Q8N6H7.

Protocols and materials databases

DNASUi 84364.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000524782 ; ENSP00000434442 ; ENSG00000149182 . [Q8N6H7-1 ]
GeneIDi 84364.
KEGGi hsa:84364.
UCSCi uc001ndt.3. human. [Q8N6H7-1 ]

Organism-specific databases

CTDi 84364.
GeneCardsi GC11M047185.
HGNCi HGNC:13504. ARFGAP2.
HPAi HPA016649.
HPA018152.
MIMi 606908. gene.
neXtProti NX_Q8N6H7.
PharmGKBi PA162376868.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5347.
GeneTreei ENSGT00390000005436.
HOGENOMi HOG000162970.
HOVERGENi HBG050563.
InParanoidi Q8N6H7.
KOi K12493.
OMAi DTDATWG.
OrthoDBi EOG7B8S42.
PhylomeDBi Q8N6H7.
TreeFami TF313985.

Miscellaneous databases

EvolutionaryTracei Q8N6H7.
GenomeRNAii 84364.
NextBioi 35480760.
PROi Q8N6H7.
SOURCEi Search...

Gene expression databases

Bgeei Q8N6H7.
CleanExi HS_ARFGAP2.
ExpressionAtlasi Q8N6H7. baseline and differential.
Genevestigatori Q8N6H7.

Family and domain databases

InterProi IPR001164. ArfGAP.
[Graphical view ]
Pfami PF01412. ArfGap. 1 hit.
[Graphical view ]
PRINTSi PR00405. REVINTRACTNG.
SMARTi SM00105. ArfGap. 1 hit.
[Graphical view ]
PROSITEi PS50115. ARFGAP. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "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; 2 AND 3).
    Tissue: Brain, Teratocarcinoma and Testis.
  2. 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).
    Tissue: Eye.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4-521 (ISOFORM 1).
    Tissue: Amygdala.
  6. "Neuroblastoma oligo-capping cDNA project: toward the understanding of the genesis and biology of neuroblastoma."
    Ohira M., Morohashi A., Nakamura Y., Isogai E., Furuya K., Hamano S., Machida T., Aoyama M., Fukumura M., Miyazaki K., Suzuki Y., Sugano S., Hirato J., Nakagawara A.
    Cancer Lett. 197:63-68(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 41-521 (ISOFORM 1), VARIANT ASN-411.
    Tissue: Neuroblastoma.
  7. "Gamma-COP appendage domain -- structure and function."
    Watson P.J., Frigerio G., Collins B.M., Duden R., Owen D.J.
    Traffic 5:79-88(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH COPG1.
  8. "Two human ARFGAPs associated with COP-I-coated vesicles."
    Frigerio G., Grimsey N., Dale M., Majoul I., Duden R.
    Traffic 8:1644-1655(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH COATOMER.
  9. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-368, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-146; SER-368 AND SER-432, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "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-146 AND SER-368, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  12. "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-146; SER-368 AND SER-432, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "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-146; SER-432 AND SER-433, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  16. "Gap domain of ZNF289, an ID1-regulated zinc finger protein."
    Structural genomics consortium (SGC)
    Submitted (MAR-2007) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 2-130.

Entry informationi

Entry nameiARFG2_HUMAN
AccessioniPrimary (citable) accession number: Q8N6H7
Secondary accession number(s): B4DX29
, B7Z9M7, D3DQQ9, Q3LIF2, Q8N3I1, Q96SX7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 20, 2007
Last sequence update: October 1, 2002
Last modified: October 29, 2014
This is version 106 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

Miscellaneous

Vero cells overexpressing truncated ARFGAP2 show accumulation of cholera toxin A subunit in the Golgi complex rather than the endoplasmic reticulum.

Keywords - Technical termi

3D-structure, 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3