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1.I.1.1.3
Nuclear Pore Complex, NPC, with 86 protein components.  NPCs mediate nucleocytoplasmic transport and gain transport selectivity through nucleoporin FG domains. Chug et al. 2015 reported a structural analysis of the frog FG Nup62•58•54 complex. It comprises a ≈13 nanometer-long trimerization interface with an unusual 2W3F coil, a canonical heterotrimeric coiled coil, and a kink that enforces a compact six-helix bundle. Nup54 also contains a ferredoxin-like domain. Chug et al. 2015 further identified a heterotrimeric Nup93-binding module for NPC anchorage. The quaternary structure alternations in the Nup62 complex, which were previously proposed to trigger a general gating of the NPC, are incompatible with the trimer structure. Chug et al. 2015 suggested that the highly elongated Nup62 complex projects barrier-forming FG repeats far into the central NPC channel, supporting a barrier that guards the entire cross section. The Sun1/UNC84A protein and Sun2/UNC84B may function redundantly in early HIV-1 infection steps and therefore influence HIV-1 replication and pathogenesis (Schaller et al. 2017).  The integral transmembrane nucleoporin Pom121 functionally links nuclear pore complex assembly to nuclear envelope formation (Antonin et al. 2005) and ensures efficient HIV-1 pre-integration complex nuclear import (Guo et al. 2018). Mechanosensing at the nuclear envelope by nuclear pore complex stretch activation involves cell membrane integrins (TC# 8.A.54) and SUN proteins, SUN1 and SUN2, in the nuclear membrane (Donnaloja et al. 2019). TMX2 is a thioredoxin-like protein that facilitates the transport of proteins across the nuclear membrane (Oguro and Imaoka 2019). Torsin ATPase deficiency leads to defects in nuclear pore biogenesis and sequestration of the myelokd leukemia factor 2, MLF2 (Rampello et al. 2020).    G4C2 repeat RNA initiates a POM121-mediated reduction in specific nucleoporins (Coyne et al. 2020) (Pom121: acc# A8CG34). Defects in nucleocytoplasmic transport and accumulation of specific nuclear-pore-complex-associated proteins play roles in multiple neurodegenerative diseases, including C9orf72 Amyotrophic Lateral Sclerosis and Frontotemporal Dementia (ALS/FTD). Using super-resolution structured illumination microscopy, Coyne et al. 2020 have explored the mechanism by which nucleoporins are altered in nuclei isolated from C9orf72 induced pluripotent stem-cell-derived neurons (iPSNs). Of the 23 nucleoporins evaluated, they observed a reduction in a subset of 8, including key components of the nuclear pore complex scaffold and the transmembrane nucleoporin POM121. Reduction in POM121 appeared to initiate a decrease in the expression of seven additional nucleoporins, ultimately affecting the localization of the Ran GTPase and subsequent cellular toxicity in C9orf72 iPSNs. Thus, the expression of expanded C9orf72 ALS/FTD repeat RNA affects nuclear POM121 expression in the initiation of a pathological cascade affecting nucleoporin levels within neuronal nuclei and ultimately downstream neuronal survival (Coyne et al. 2020).  

Accession Number:O60318
Protein Name:Germinal-center associated nuclear protein
Length:1980
Molecular Weight:218405.00
Species:Homo sapiens (Human) [9606]
Location1 / Topology2 / Orientation3: Cytoplasm1
Substrate proteins, RNA

Cross database links:

Structure:
4DHX     

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FASTA formatted sequence
1:	MNPTNPFSGQ QPSAFSASSS NVGTLPSKPP FRFGQPSLFG QNSTLSGKSS GFSQVSSFPA 
61:	SSGVSHSSSV QTLGFTQTSS VGPFSGLEHT STFVATSGPS SSSVLGNTGF SFKSPTSVGA 
121:	FPSTSAFGQE AGEIVNSGFG KTEFSFKPLE NAVFKPILGA ESEPEKTQSQ IASGFFTFSH 
181:	PISSAPGGLA PFSFPQVTSS SATTSNFTFS KPVSSNNSLS AFTPALSNQN VEEEKRGPKS 
241:	IFGSSNNSFS SFPVSSAVLG EPFQASKAGV RQGCEEAVSQ VEPLPSLMKG LKRKEDQDRS 
301:	PRRHGHEPAE DSDPLSRGDH PPDKRPVRLN RPRGGTLFGR TIQDVFKSNK EVGRLGNKEA 
361:	KKETGFVESA ESDHMAIPGG NQSVLAPSRI PGVNKEEETE SREKKEDSLR GTPARQSNRS 
421:	ESTDSLGGLS PSEVTAIQCK NIPDYLNDRT ILENHFGKIA KVQRIFTRRS KKLAVVHFFD 
481:	HASAALARKK GKSLHKDMAI FWHRKKISPN KKPFSLKEKK PGDGEVSPST EDAPFQHSPL 
541:	GKAAGRTGAS SLLNKSSPVK KPSLLKAHQF EGDSFDSASE GSEGLGPCVL SLSTLIGTVA 
601:	ETSKEKYRLL DQRDRIMRQA RVKRTDLDKA RTFVGTCLDM CPEKERYMRE TRSQLSVFEV 
661:	VPGTDQVDHA AAVKEYSRSS ADQEEPLPHE LRPLPVLSRT MDYLVTQIMD QKEGSLRDWY 
721:	DFVWNRTRGI RKDITQQHLC DPLTVSLIEK CTRFHIHCAH FMCEEPMSSF DAKINNENMT 
781:	KCLQSLKEMY QDLRNKGVFC ASEAEFQGYN VLLSLNKGDI LREVQQFHPA VRNSSEVKFA 
841:	VQAFAALNSN NFVRFFKLVQ SASYLNACLL HCYFSQIRKD ALRALNFAYT VSTQRSTIFP 
901:	LDGVVRMLLF RDCEEATDFL TCHGLTVSDG CVELNRSAFL EPEGLSKTRK SVFITRKLTV 
961:	SVGEIVNGGP LPPVPRHTPV CSFNSQNKYI GESLAAELPV STQRPGSDTV GGGRGEECGV 
1021:	EPDAPLSSLP QSLPAPAPSP VPLPPVLALT PSVAPSLFQL SVQPEPPPPE PVPMYSDEDL 
1081:	AQVVDELIQE ALQRDCEEVG SAGAAYAAAA LGVSNAAMED LLTAATTGIL RHIAAEEVSK 
1141:	ERERREQERQ RAEEERLKQE RELVLSELSQ GLAVELMERV MMEFVRETCS QELKNAVETD 
1201:	QRVRVARCCE DVCAHLVDLF LVEEIFQTAK ETLQELQCFC KYLQRWREAV TARKKLRRQM 
1261:	RAFPAAPCCV DVSDRLRALA PSAECPIAEE NLARGLLDLG HAGRLGISCT RLRRLRNKTA 
1321:	HQMKVQHFYQ QLLSDVAWAS LDLPSLVAEH LPGRQEHVFW KLVLVLPDVE EQSPESCGRI 
1381:	LANWLKVKFM GDEGSVDDTS SDAGGIQTLS LFNSLSSKGD QMISVNVCIK VAHGALSDGA 
1441:	IDAVETQKDL LGASGLMLLL PPKMKSEDMA EEDVYWLSAL LQLKQLLQAK PFQPALPLVV 
1501:	LVPSPGGDAV EKEVEDGLML QDLVSAKLIS DYTVTEIPDT INDLQGSTKV LQAVQWLVSH 
1561:	CPHSLDLCCQ TLIQYVEDGI GHEFSGRFFH DRRERRLGGL ASQEPGAIIE LFNSVLQFLA 
1621:	SVVSSEQLCD LSWPVTEFAE AGGSRLLPHL HWNAPEHLAW LKQAVLGFQL PQMDLPPLGA 
1681:	PWLPVCSMVV QYASQIPSSR QTQPVLQSQV ENLLHRTYCR WKSKSPSPVH GAGPSVMEIP 
1741:	WDDLIALCIN HKLRDWTPPR LPVTSEALSE DGQICVYFFK NDLKKYDVPL SWEQARLQTQ 
1801:	KELQLREGRL AIKPFHPSAN NFPIPLLHMH RNWKRSTECA QEGRIPSTED LMRGASAEEL 
1861:	LAQCLSSSLL LEKEENKRFE DQLQQWLSED SGAFTDLTSL PLYLPQTLVS LSHTIEPVMK 
1921:	TSVTTSPQSD MMREQLQLSE ATGTCLGERL KHLERLIRSS REEEVASELH LSALLDMVDI