GGA3

GGA3
사용 가능한 구조
PDB	Ortholog 검색: PDBe RCSB
PDB ID 코드 목록
	1JPL, 1JUQ, 1LF8, 1P4U, 1WR6, 1YD8
식별자
에일리어스	GGA3, 골지 관련, 감마 어댑틴 귀 함유, ARF 결합 단백질 3
외부 ID	OMIM : 606006 MGI : 2384159 HomoloGene : 121703 GenCard : GGA3
유전자 위치(인간)
크르.	17번 염색체(인간)
끝.	75,262,363 bp
유전자 위치(마우스)
크르.	11번 염색체(쥐)
끝.	115,494,877 bp
RNA발현패턴
	상단 표시 위치:
	상부 신경; ; 유문; ; 위점막; ; 비장; ; 단구; ; 니플; ; 림프절; ; 좌폐 상엽; ; 안저; ; 횡결장;
	상단 표시 위치:
	이차 난모세포; ; 상전두회; ; 소뇌 피질; ; 노른자낭; ; 안면 운동핵; ; 흉선; ; 척수 전각; ; 원형 피질; ; 상경부신경절; ; 상콜리큘러스;
	추가 참조 표현식 데이터
	; ;
	추가 참조 표현식 데이터
유전자 존재론
분자 함수	GO:0001948, GO:0016582 단백질 결합; 유비퀴틴 결합;
셀룰러 컴포넌트	내염색체; 골기 횡단망; 엔도솜막; 세포내 해부학적 구조; 막; 클라트린 어댑터 복합체; 골지 장치; 초기 엔도솜막; 재활용 엔도솜막; 초기 엔도솜; 재활용 엔도솜;
생물학적 과정	단백질 수송; 세포내단백질; GO: 190364 단백질 이화과정 양성조절; 소포체 수송; 리소좀에 대한 단백질 국재화; 단백질 안정성 조절; 단백질 불안정화; 세포내 재활용; 세포표면단백질국재; 골지-플라즈마막 단백질 수송; 아밀로이드-아밀로이드 형성의 음성 조절;
	출처:아미고 / QuickGO
맞춤법
	23163
	260302
	ENSG00000125447
	ENSMUSG000020740
	Q9NZ52
	Q8BMI3
NM_001172703; NM_001172704; NM_001291641; NM_001291642; NM_014001;
	NM_138619
	NM_001252067; NM_173048
NP_001166174; NP_001166175; NP_001278570; NP_001278571; NP_054720;
	NP_619525
	NP_001238996; NP_766636
	위키데이터
인간 보기/편집	마우스 표시/편집

ADP-리보실화인자결합단백질 GGA3는 GGA3유전자에 ^[5]^[6]의해 인체 내에서 코드되는 단백질이다.

이 유전자는 골지 국소화 감마 어댑틴 귀를 포함한 ARF 결합(GGA) 계열의 구성원을 코드한다.이 과는 골기 통과 네트워크와 리소좀 사이의 단백질 이동을 조절하는 유비쿼터스 외피 단백질을 포함합니다.이러한 단백질은 아미노 말단 VHS 도메인을 공유하여 Golgi 네트워크에서 만노스 6-인산 수용체의 분류를 매개한다.그들은 또한 감마 아답틴의 귀 도메인과 상동성을 갖는 카르복시 말단 영역을 포함한다.이 유전자의 대체 스플라이싱은 두 가지 전사 ^[7]변형을 일으킨다.

상호 작용

GGA3는 ARF1^[5]^[8] 및 ARF3와 ^[6]^[9]상호작용하는 것으로 나타났습니다.

레퍼런스

^ ^a ^b ^c GRCh38: 앙상블 릴리즈 89: ENSG00000125447 - 앙상블, 2017년 5월
^ ^a ^b ^c GRCm38: 앙상블 릴리즈 89: ENSMUSG000020740 - 앙상블, 2017년 5월
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ ^a ^b Dell'Angelica EC, Puertollano R, Mullins C, Aguilar RC, Vargas JD, Hartnell LM, Bonifacino JS (April 2000). "GGAs: a family of ADP ribosylation factor-binding proteins related to adaptors and associated with the Golgi complex". The Journal of Cell Biology. 149 (1): 81–94. doi:10.1083/jcb.149.1.81. PMC 2175099. PMID 10747089.
^ ^a ^b Boman AL, Zhang C, Zhu X, Kahn RA (April 2000). "A family of ADP-ribosylation factor effectors that can alter membrane transport through the trans-Golgi". Molecular Biology of the Cell. 11 (4): 1241–55. doi:10.1091/mbc.11.4.1241. PMC 14844. PMID 10749927.
^ "Entrez Gene: GGA3 golgi associated, gamma adaptin ear containing, ARF binding protein 3".
^ Puertollano R, Randazzo PA, Presley JF, Hartnell LM, Bonifacino JS (April 2001). "The GGAs promote ARF-dependent recruitment of clathrin to the TGN". Cell. 105 (1): 93–102. doi:10.1016/S0092-8674(01)00299-9. PMID 11301005. S2CID 1158816.
^ Boman AL, Salo PD, Hauglund MJ, Strand NL, Rensink SJ, Zhdankina O (September 2002). "ADP-ribosylation factor (ARF) interaction is not sufficient for yeast GGA protein function or localization". Molecular Biology of the Cell. 13 (9): 3078–95. doi:10.1091/mbc.E02-02-0078. PMC 124144. PMID 12221117.

추가 정보

Nagase T, Seki N, Tanaka A, Ishikawa K, Nomura N (August 1995). "Prediction of the coding sequences of unidentified human genes. IV. The coding sequences of 40 new genes (KIAA0121-KIAA0160) deduced by analysis of cDNA clones from human cell line KG-1". DNA Research. 2 (4): 167–74, 199–210. doi:10.1093/dnares/2.4.167. PMID 8590280.
Hirst J, Lui WW, Bright NA, Totty N, Seaman MN, Robinson MS (April 2000). "A family of proteins with gamma-adaptin and VHS domains that facilitate trafficking between the trans-Golgi network and the vacuole/lysosome". The Journal of Cell Biology. 149 (1): 67–80. doi:10.1083/jcb.149.1.67. PMC 2175106. PMID 10747088.
Takatsu H, Yoshino K, Nakayama K (May 2000). "Adaptor gamma ear homology domain conserved in gamma-adaptin and GGA proteins that interact with gamma-synergin". Biochemical and Biophysical Research Communications. 271 (3): 719–25. doi:10.1006/bbrc.2000.2700. PMID 10814529.
Puertollano R, Randazzo PA, Presley JF, Hartnell LM, Bonifacino JS (April 2001). "The GGAs promote ARF-dependent recruitment of clathrin to the TGN". Cell. 105 (1): 93–102. doi:10.1016/S0092-8674(01)00299-9. PMID 11301005. S2CID 1158816.
Puertollano R, Aguilar RC, Gorshkova I, Crouch RJ, Bonifacino JS (June 2001). "Sorting of mannose 6-phosphate receptors mediated by the GGAs". Science. 292 (5522): 1712–6. Bibcode:2001Sci...292.1712P. doi:10.1126/science.1060750. PMID 11387475. S2CID 30836125.
Misra S, Puertollano R, Kato Y, Bonifacino JS, Hurley JH (February 2002). "Structural basis for acidic-cluster-dileucine sorting-signal recognition by VHS domains". Nature. 415 (6874): 933–7. Bibcode:2002Natur.415..933M. doi:10.1038/415933a. PMID 11859375. S2CID 4430757.
Takatsu H, Yoshino K, Toda K, Nakayama K (July 2002). "GGA proteins associate with Golgi membranes through interaction between their GGAH domains and ADP-ribosylation factors". The Biochemical Journal. 365 (Pt 2): 369–78. doi:10.1042/BJ20020428. PMC 1222692. PMID 11950392.
Kato Y, Misra S, Puertollano R, Hurley JH, Bonifacino JS (July 2002). "Phosphoregulation of sorting signal-VHS domain interactions by a direct electrostatic mechanism". Nature Structural Biology. 9 (7): 532–6. doi:10.1038/nsb807. PMID 12032548. S2CID 23740463.
Doray B, Bruns K, Ghosh P, Kornfeld SA (June 2002). "Autoinhibition of the ligand-binding site of GGA1/3 VHS domains by an internal acidic cluster-dileucine motif". Proceedings of the National Academy of Sciences of the United States of America. 99 (12): 8072–7. Bibcode:2002PNAS...99.8072D. doi:10.1073/pnas.082235699. PMC 123022. PMID 12060753.
Wasiak S, Legendre-Guillemin V, Puertollano R, Blondeau F, Girard M, de Heuvel E, Boismenu D, Bell AW, Bonifacino JS, McPherson PS (September 2002). "Enthoprotin: a novel clathrin-associated protein identified through subcellular proteomics". The Journal of Cell Biology. 158 (5): 855–62. doi:10.1083/jcb.200205078. PMC 2173151. PMID 12213833.
Doray B, Ghosh P, Griffith J, Geuze HJ, Kornfeld S (September 2002). "Cooperation of GGAs and AP-1 in packaging MPRs at the trans-Golgi network". Science. 297 (5587): 1700–3. Bibcode:2002Sci...297.1700D. doi:10.1126/science.1075327. PMID 12215646. S2CID 8810528.
Boman AL, Salo PD, Hauglund MJ, Strand NL, Rensink SJ, Zhdankina O (September 2002). "ADP-ribosylation factor (ARF) interaction is not sufficient for yeast GGA protein function or localization". Molecular Biology of the Cell. 13 (9): 3078–95. doi:10.1091/mbc.E02-02-0078. PMC 124144. PMID 12221117.
Mattera R, Arighi CN, Lodge R, Zerial M, Bonifacino JS (January 2003). "Divalent interaction of the GGAs with the Rabaptin-5-Rabex-5 complex". The EMBO Journal. 22 (1): 78–88. doi:10.1093/emboj/cdg015. PMC 140067. PMID 12505986.
Wakasugi M, Waguri S, Kametaka S, Tomiyama Y, Kanamori S, Shiba Y, Nakayama K, Uchiyama Y (July 2003). "Predominant expression of the short form of GGA3 in human cell lines and tissues". Biochemical and Biophysical Research Communications. 306 (3): 687–92. doi:10.1016/S0006-291X(03)01032-5. PMID 12810073.
He X, Zhu G, Koelsch G, Rodgers KK, Zhang XC, Tang J (October 2003). "Biochemical and structural characterization of the interaction of memapsin 2 (beta-secretase) cytosolic domain with the VHS domain of GGA proteins". Biochemistry. 42 (42): 12174–80. doi:10.1021/bi035199h. PMID 14567678.
Ghosh P, Griffith J, Geuze HJ, Kornfeld S (November 2003). "Mammalian GGAs act together to sort mannose 6-phosphate receptors". The Journal of Cell Biology. 163 (4): 755–66. doi:10.1083/jcb.200308038. PMC 2173681. PMID 14638859.
Shiba Y, Katoh Y, Shiba T, Yoshino K, Takatsu H, Kobayashi H, Shin HW, Wakatsuki S, Nakayama K (February 2004). "GAT (GGA and Tom1) domain responsible for ubiquitin binding and ubiquitination". The Journal of Biological Chemistry. 279 (8): 7105–11. doi:10.1074/jbc.M311702200. PMID 14660606.