wanglab/gogpt-training-data huggingface dataset:
Protein: Small COPII coat GTPase SAR1B (EC 3.6.5.2) (GTP-binding protein B) (GTBPB) (Secretion-associated Ras-related GTPase 1B) (Q9Y6B6)
Organism: Homo sapiens (Human)
Function: GTP-binding protein involved in transport from the endoplasmic reticulum to the Golgi apparatus (By similarity). Activated by the guanine nucleotide exchange factor PREB (By similarity). Involved in the selection of the protein cargo and the assembly of the COPII coat complex (By similarity). Synergizes with the cargo receptor SURF4 to mediate the export of lipoproteins from the endoplasmic reticulum, thereby regulating lipoprotein delivery and the maintenance of lipid homeostasis.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:33186557}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9QVY3}. Golgi apparatus, Golgi stack membrane {ECO:0000250|UniProtKB:Q9QVY3}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9QVY3}. Cytoplasm, cytosol {ECO:0000269|PubMed:34290409}. Lysosome membrane {ECO:0000269|PubMed:34290409}. Note=Active at endoplasmic reticulum exit sites (ERES) where it inserts into the membrane and recruits the remainder of the coat protein complex II/COPII (PubMed:23433038). Upon leucine deprivation, associates with lysosomal membranes to repress TORC1 signaling (PubMed:34290409). {ECO:0000269|PubMed:23433038, ECO:0000269|PubMed:34290409}.
Interaction partners:
- Guanine nucleotide-exchange factor SEC12
- Protein SEC13 homolog
- Protein transport protein Sec31A
- Protein transport protein Sec24A
- Protein transport protein Sec24B
- Protein transport protein Sec31B
- Small COPII coat GTPase SAR1A
- Protein transport protein Sec23A
- Protein transport protein Sec23B
- Protein transport protein Sec24D
Sequence:
MSFIFDWIYSGFSSVLQFLGLYKKTGKLVFLGLDNAGKTTLLHMLKDDRLGQHVPTLHPTSEELTIAGMTFTTFDLGGHVQARRVWKNYLPAINGIVFLVDCADHERLLESKEELDSLMTDETIANVPILILGNKIDRPEAISEERLREMFGLYGQTTGKGSISLKELNARPLEVFMCSVLKRQGYGEGFRWMAQYID
Protein: Caveolae-associated protein 1 (Cavin-1) (Polymerase I and transcript release factor) (Q6NZI2)
Organism: Homo sapiens (Human)
Function: Plays an important role in caveolae formation and organization. Essential for the formation of caveolae in all tissues. Core component of the CAVIN complex which is essential for recruitment of the complex to the caveolae in presence of calveolin-1 (CAV1). Essential for normal oligomerization of CAV1. Promotes ribosomal transcriptional activity in response to metabolic challenges in the adipocytes and plays an important role in the formation of the ribosomal transcriptional loop. Dissociates transcription complexes paused by DNA-bound TTF1, thereby releasing both RNA polymerase I and pre-RNA from the template (By similarity). The caveolae biogenesis pathway is required for the secretion of proteins such as GASK1A (By similarity).
Subcellular location: Membrane, caveola {ECO:0000269|PubMed:15242332, ECO:0000269|PubMed:18056712, ECO:0000269|PubMed:19525939}. Cell membrane {ECO:0000269|PubMed:15242332, ECO:0000269|PubMed:17026959, ECO:0000269|PubMed:18056712}. Microsome {ECO:0000269|PubMed:15242332, ECO:0000269|PubMed:17026959}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P85125}. Cytoplasm, cytosol {ECO:0000269|PubMed:15242332}. Mitochondrion {ECO:0000269|PubMed:15242332, ECO:0000269|PubMed:17026959}. Nucleus {ECO:0000269|PubMed:15242332, ECO:0000269|PubMed:17026959}. Note=Translocates to the cytoplasm from the caveolae upon insulin stimulation (PubMed:17026959). Colocalizes with CAV1 in lipid rafts in adipocytes. Localizes in the caveolae in a caveolin-dependent manner (By similarity). {ECO:0000250|UniProtKB:O54724, ECO:0000269|PubMed:17026959}.
Interaction partners:
- Caveolin-1
- Caveolin-3
- Caveolin-2
- Caveolae-associated protein 3
- EH domain-containing protein 2
- Epidermal growth factor receptor
- Seipin
- 1-acyl-sn-glycerol-3-phosphate acyltransferase beta
- Tripartite motif-containing protein 72
- GH3 domain-containing protein
Sequence:
MEDPTLYIVERPLPGYPDAEAPEPSSAGAQAAEEPSGAGSEELIKSDQVNGVLVLSLLDKIIGAVDQIQLTQAQLEERQAEMEGAVQSIQGELSKLGKAHATTSNTVSKLLEKVRKVSVNVKTVRGSLERQAGQIKKLEVNEAELLRRRNFKVMIYQDEVKLPAKLSISKSLKESEALPEKEGEELGEGERPEEDAAALELSSDEAVEVEEVIEESRAERIKRSGLRRVDDFKKAFSKEKMEKTKVRTRENLEKTRLKTKENLEKTRHTLEKRMNKLGTRLVPAERREKLKTSRDKLRKSFTPDHVVYARSKTAVYKVPPFTFHVKKIREGQVEVLKATEMVEVGADDDEGGAERGEAGDLRRGSSPDVHALLEITEESDAVLVDKSDSD
Protein: Diphthamide biosynthesis protein 3 (Q21102)
Organism: Caenorhabditis elegans
Function: Required for the first step of diphthamide biosynthesis, a post-translational modification of histidine which occurs in elongation factor 2. Dph-1 and dph-2 transfer a 3-amino-3-carboxypropyl (ACP) group from S-adenosyl-L-methionine (SAM) to a histidine residue, the reaction is assisted by a reduction system comprising dph-3 and a NADH-dependent reductase. Acts as an electron donor to reduce the Fe-S cluster in dph1-dph2 keeping the [4Fe-4S] clusters in the active and reduced state. Restores iron to dph-1-dph-2 iron-sulfur clusters which have degraded from [4Fe-4S] to [3Fe-4S] by donating an iron atom to reform [4Fe-4S] clusters, in a manner dependent on the presence of elongation factor 2 and SAM. Associates with the elongator complex and is required for tRNA Wobble base modifications mediated by the elongator complex. The elongator complex is required for multiple tRNA modifications, including mcm5U (5-methoxycarbonylmethyl uridine), mcm5s 2U (5-methoxycarbonylmethyl-2-thiouridine), and ncm5U (5-carbamoylmethyl uridine).
Interaction partners:
- 2-
- 2-
- Elongation factor 2
- Elongator complex protein 3
- Elongator complex protein 1
- Small ribosomal subunit protein uS15
Sequence:
MSVFHDEVEIEDFEFDEEKDVYHYPCPCGDRFEIPREMLEMGEDVAQCPSCSLLIRVIYDPEDFVKLETISTSKPIAEPV
Protein: Ribonuclease I (RNase I) (EC 4.6.1.21) (Enterobacter ribonuclease) (P21338)
Organism: Escherichia coli (strain K12)
Function: One of the few RNases that cleaves the phosphodiester bond between any two nucleotide. Shows a preference for cytidylic or guanylic acid.
Subcellular location: Periplasm. Cytoplasm. Note=RNase I (periplasmic) and RNase I* (cytoplasmic) appear to be isoforms apparently encoded by the same gene. The cytoplasmic form is less active towards natural polymer RNA.
Interaction partners:
- Exoribonuclease 2
- Putative acyl-CoA thioester hydrolase YbhC
- Ribonuclease E
Sequence:
MKAFWRNAALLAVSLLPFSSANALALQAKQYGDFDRYVLALSWQTGFCQSQHDRNRNERDECRLQTETTNKADFLTVHGLWPGLPKSVAARGVDERRWMRFGCATRPIPNLPEARASRMCSSPETGLSLETAAKLSEVMPGAGGRSCLERYEYAKHGACFGFDPDAYFGTMVRLNQEIKESEAGKFLADNYGKTVSRRDFDAAFAKSWGKENVKAVKLTCQGNPAYLTEIQISIKADAINAPLSANSFLPQPHPGNCGKTFVIDKAGY
Protein: Moesin/ezrin/radixin homolog 1 (A0T1Z4)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell junction, adherens junction {ECO:0000256|ARBA:ARBA00004536}. Cell projection, rhabdomere {ECO:0000256|ARBA:ARBA00043944}.
Interaction partners:
Sequence:
MLRFLSRRKVRNNYVDNSREGGGATSSAVGVAGGGGAITSGGSSQIKPQRIVVNKNKIDCRVILLDNTDLSIELSKKALGSFLYEQVFYALDIIEKDYFGLQFMDANHVKHWLDPTKPIKKQVKIGPPYTFRLKVKFYSSEPNTLREELTRYLFFLQLKQDLLEGRLDCPEDKATELCALALQSELGDYDNQEHSAATVSEFRFVPEQTEDLEIAILDEYKTCRGLTPAQAETAFLNKAKWLDMYGVDMHTVLGKDGCEYHLGLTPTGILVFERDQKIGLFFWPKISKLDFKKKKLTLIVIEDDDEGREQEHTFVFRLYNEKACKHLWKCAVEHHTFFRLRAPVKGPSARQNFFRMGSRFRYSGRTEFQTTQQSRARRTVQFERRPSQRFASRQSHLLRERQKASQEAAVSAVASVNARAAAAAAAAAASQSPAPATPLVSSQVSTPTPNNDNNNDAFDSLISTDQFITVTPSPSVLTVIQNSAIIEPDAACSGSISSSSQAAANFASLGRNSLKSNFSNEDPAYSKIGSIGKASGLTVKLDPDYTPPYSPNATKNFDETNPFRNATSSHHGSFGKASISSGQLRVTINKTFDMDHNTETLKRLSNANEKPNNQVKLANVNTTALPPGNIKCNILKARVEEELGAGGNAKLTNQMFVPAAHSSNMHTSNTNSSNNHAHSDGPDSLNATYISVGGDKLTLSIPEQKPSTGSSSSSSTSSTATTTTNGNGPYSNATFVSGFSAPLTPPSSLPANLNNTGSGCNTTLTSVTTISTPSSPTATVSTTASESVAPALSNASAAEILINEIFINNIINNNASGSITAETAAKPAGSSTPSAGTLLFSTLSEQERLESQKTNQQMNQSLNLNQNHSEVDAPPSEKKTPSNYPDSSRIPFPSSSNSKDMVSPWLVSSEVVSAPKGRESAIIRKSVITTQL
Protein: Tetraspanin-16 (Tspan-16) (Tetraspanin TM4-B) (Transmembrane 4 superfamily member 16) (Q9UKR8)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Tropomyosin alpha-3 chain
- Short transient receptor potential channel 4
- Sodium-dependent serotonin transporter
Sequence:
MAEIHTPYSSLKKLLSLLNGFVAVSGIILVGLGIGGKCGGASLTNVLGLSSAYLLHVGNLCLVMGCITVLLGCAGWYGATKESRGTLLFCILSMVIVLIMEVTAATVVLLFFPIVGDVALEHTFVTLRKNYRGYNEPDDYSTQWNLVMEKLKCCGVNNYTDFSGSSFEMTTGHTYPRSCCKSIGSVSCDGRDVSPNVIHQKGCFHKLLKITKTQSFTLSGSSLGAAVIQRWGSRYVAQAGLELLA
Protein: Uncharacterized protein (Q57TU0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSSVTTGSSSYAAVLLVLLLTVTQCGNSKFPNLGCQKLWTTRSAQNDPLTCIKDKTRILSHWEDILLPVLAGLLLALIVVIFPLTFFSTCLCSSCCKPSSKDRGRKQRCCLWMWIAFAFIWAFGVAVFVLFGAQQLKITLDDLLSHRVNRPLNSLRCTADKILGLAYDWRTGEPLREGIGRETIDSTVDMARSYITMAKGYYDQYVHWVPTVSFCIGAFAVLVMVPMFMFAYFRCCSKWLPRLLSCVYWLFAILFTALGLVILLLAYAFGLVCGEITLHYDRSPGLIQWYALPMCEEKFNFANLNKMILDAQKDVSQKACEEILKYCDNDTSQLGDQTGTGGLAALLGRNLPPGLDPKALPPGVKPEDFEDEKGLDSLLESHIPGVNDKEKIPRRYEGSVPPDGSLPGNMRDVIGAKATQFPQLPFGPSNKMLTCGQGVGSKEECSTFGFTAAVISGTKVKGGYMVCPDGGRPCSLQVCADKCKVPDAQNIAKTLVGAAQLAVNVSIGLSIGRPLLECNFIFDTVLTALPNCDGLYWGTMMLGLGFFLGGMMFALSIYILLRGSCVWSDLKRWDEDEEKDSENKRESDKSPARK
Protein: Large ribosomal subunit protein bL35m (54S ribosomal protein MRP35) (P53921)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:17054397}. Note=Mitoribosomes are tethered to the mitochondrial inner membrane and spatially aligned with the membrane insertion machinery through two distinct membrane contact sites, formed by the 21S rRNA expansion segment 96-ES1 and the inner membrane protein MBA1. {ECO:0000269|PubMed:25609543}.
Interaction partners:
- Large ribosomal subunit protein bL19m
- Large ribosomal subunit protein bL34m
- Small ribosomal subunit protein uS8m
- Large ribosomal subunit protein bL36m
- Large ribosomal subunit protein uL14m
- Large ribosomal subunit protein uL16m
- Large ribosomal subunit protein bL33m
- Large ribosomal subunit protein mL59
- Large ribosomal subunit protein uL13m
- Large ribosomal subunit protein uL15m
Sequence:
MKISLHNKRQRGDQNQNMSVFNVLKPLLKGSNSFKVKLNGFLFNNVSTITIRTLMKTHKGTAKRWRRTGNTFKRGIAGRKHGNIGWSHRSLKALTGRKIAHPAYSKHLKRLLPYH
Protein: Large ribosomal subunit protein uL11 (60S ribosomal protein L12) (Q59FI9)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
SNCSRLSARRRPRCNFLRSSRIRVHPTPAASTMPPKFDPNEIKVVYLRCTGGEVGATSALAPKIGPLGLSPKKVGDDIAKATGDWKGLRITVKLTIQNRQAQIEVVPSASALIIKALKEPPRDRKKQKNIKHSGNITFDEIVNIVRQMRHRSLARELSGTIKEILGTAQSVGCNVDGRHPHDIIDDINSGAVECPAS
Protein: Exchange protein directly activated by cAMP, isoform E (A1Z6P8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Ras-related protein Rap1
- small monomeric GTPase
- cAMP-dependent protein kinase catalytic subunit 1
- cAMP-dependent protein kinase catalytic subunit 2
- Rab3 interacting molecule, isoform F
- Guanine nucleotide exchange factor MSS4 homolog
- G protein alpha s subunit subunit alpha)
Sequence:
MAMEWITAMDKRPCDRNLRDVELISCRLRRVEPLCRLPGSALQQLAMCGFYEDLEKGVTLFRAGEQGRFWYAVLGGSLEVRYHAHADADGKSAVTLCNLGVGATFGESVLHDLPRDSTVVTKTTCELLRVEQQDFRLIWEKNKELMNDIFTNCKLKNGFGPSVQATAAATSPTKRPLSPDHPNPALPITETPSPAMNRMGWALRTLLVADNSSCLKDRKVSGKLIRKCAPGTELVDWLVNLSPIVHTRAQAAGMWQALLEEGVLAHVNKEQPFKDKCFLYRFRIDEEGGTAAAGVPQAEDLGAANEHIREALSALFQRGPDATLRMILRKPSHERTSEELELVFEELVHIAALSHLSTSIKRELSSIFVFEAHAQAGTILFNQGDEGRSWYILLKGSVDVVIHGKGTVATLKTGDDFGKLALINDAPRAATIVLKENNCHLLRVDKEHFNRILRDVEANTLRLQEHGKDVLVLERVAKQRGQHSAFKYTVMSGTPAKMLEHLLETRLGQSVGGMDPFLDDFLLTHIVFMPVVQLVDELANYFHCDAHEDAQTPEDREYIINFKKRVIQFMQKWVMAVRHAAFEEPSVCDFIEDLAAEVEADPDLNEETSIVHNVLTQMARYQEDRNQNAGQKWKLPPNGQPICLFSGNATPSKTVIRPDDDIIFRVYCADHTYCTLRFPMHTTAELIKACAADKLQLNRGPEDLVLVEVKSNGERSVFKDNDVSIPTGLSLNGRLFVSVKDHLDALTQLQEQECPTEGVDIDLEILSTKELAYHITLFEWDLFWAVHEYELLYHTFGRHHFGKITANLDVFLRRFNEVQYWIVTELVSTPSLSKRVGLVRKFIKLAAYCKEYQNLNAFFAVVMGLSNMAVSRLQQTWEKIPSKFRKIFQEFEALIDPSRNHRAYRVFVGKLQPPLIPFMPLLLKDMTFAHEGNKTSLDGLVNFEKMHMMAQTMRTIRFCRSRSLGLEPPSPKSEGEVRSYISSFRVIDNQRVLTAMSQKVEPTRKL
Protein: DNA 3'-5' helicase (EC 5.6.2.4) (Q4JNX8)
Organism: Xenopus laevis (African clawed frog)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MERYNEVKVLLKKWETAFLQEHKRKPNKTDVESASNETQELYKEFKSLKKEQLDISTDTVFTPKSGQVMETSPKPTHRADAAGDSEGSASWGIHLNRASVTPKLTSKERDSLKASAQFYGMKLKANLGGALREHPVSLKKSFTPRFRPLDSPDVKIKNNLASPKSLDTPSSPLALLQDPPSEPFDTLSHVSLKEPPHKPVMNPPTQGQPIKKQHQLQAMVGQRMASLNQEWLQRCELRNGVEAMEVTAAEQRTVNRQQCNTMREALGEGAIEENCKSVKGPPNNDELTHSTQHTVASPKQKVQAYTPVFSPHAAAPSLPLTFGRQDTRPENPKLKAEEISDFGRSSSVRSQGNDLVSPAIRREEIWDPEHQPLKRKSPLRKQICGESKMSSEAGQVAQLDSKGPMSEHSKRWQDTDESRAMKNRTGQMQESLQEVDMSQENIAAEQVSVILAKGKRKKRQRETSAEPDTVEVSPKVSKKRRKTNRSPDNSENSSSVRKRRKKGARCQMDDSDDPAMESPASEQVTKAVSEDLFGELEEEPVQRSSVKTVNTRMPQIKSENFVRINLKKKSHVKCVALNGHRLRKQMWKQKWQKKGEQFGGGGKHFNRSGDTCFRCGGMGHWASQCPGSVPVVRQEVAETEEEEEVSLPTLEDVARMTNTQLRPNTNEGLSGWCQDPVVTVNVVRAVYEPPTPPPPMQPLYELGPDGRVKETPSEVYDNLSELGYRSFRSGQEQAVMRILSGFSSLGILSTGMGKSLCYQLPAYMYAKRSRCISLVISPLVSLMDDQVSGLSPKLKAVCIHSNMTRTQREAAIEKVKQGKVHVLLLSPEALVGGGFSGSSCLPPADQLPPVAFACIDEAHCVSEWSHNFRPCYLRLCKVLRERLGVNCLLGLTATATRATAEDVAHHLGVSPEGGIPVRMASVPPNLHLSVSMDRNRDQALVTLLKGERFGCLDSVIVYCTRREETQRISALLRTSLQGVTVSANSHLNSQEQEDTTVSDRKKAQALKKIRRPLKWIAESYHAGMSAAERRRVQNNFMCGQLRLVVATVAFGMGLDKSDVRGIIHYNMPKNFESYVQEIGRAGRDGKDAQCHLFLDPEGQDMDELRRHIYTDSVDYIAVKKLVRKVFPKCKCRDLHREQQALINAGEVDDSELLQFLEQGEEQDSMCDTPSSGRDPVCDTPSMGAERLCHRHERAVPIEETVQSLDIREEAIETMLCYLELNPSHWLEQLHPTLSHCRVVCYSGPQQLRLLARSCPPVAVCLARERLAGVDHTHVSSTEFNVVELADSMGWEVVPVKRALRDLQWRRQPDKGFKGTGRSGVLVEFSKLSFHFRSYGDLTDQELDQVCDFLHHKVTSRERTSLNQLKSCFHAFQSVAYRTSSACAEKMSAERSAQLKALLLDYFEKRDTELEAKVEDPDEELQQIKVQEAKDQVRSDVRHFLSIHEEERFSGRALARIFHGIGSPCYPAQVYGRDRRFWRKYIHLDFNEIMNLSKEEIIRLK
Protein: NF-kappa-B essential modulator (IkB kinase-associated protein 1) (Inhibitor of nuclear factor kappa-B kinase subunit gamma) (NF-kappa-B essential modifier) (F1QHG7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MVQPQPSGGCTLQYELNGEETAGSEGQVSLMASSQGSLRVPADLAGNEIVQKLITDNHQLREALKRSNDALKERCEEMEGWQRRSREEREFLSCRFREARELVQRLAQENQSLLGQLNLSVSQAGSLGISKETGSQDQELKCTNAEKNVLIDSPEVLNAAVLTECAEGDTDRHTMPQSLPAVGSNDFLKLLKSHKEKLEEGMRALRRKNEELEKEKAENEKERENLLAALEQLRSKLSQNVGVTEESVPPTCAVTVPAESSHLANITEQLQATQGRYRELQEKLDCLQKNSFQRDRTEALLKQKEKEFVQVQKDSEALRSQVTSLLGELNERQNWLEKSEAEKRTLEDKLVTKSERLQTVEREMEQQKKQHSVTVDNLLLKTQNLEAALKNERLVIVEERRKLAQLQHAYTCLFQDYDNKLKSEKQANHRGGETDTLANRLGEAEKALALKQEHIDKLKEEMEQLRAKLETIPVLNHQAEIYKMDFLAEREAREKLNQKKEELQEDLNKALVEIERFKQERTSRARIEEMQQRHLEDYRPRPHPPPPAAPFPGPAMFNSAQPPSARRRDEDQEELPDYRCPKCMYKAPDMDTLQIHVMDCIQ
Protein: Nuclear pore glycoprotein p62 (62 kDa nucleoporin) (Nucleoporin Nup62) (Q63850)
Organism: Mus musculus (Mouse)
Function: Essential component of the nuclear pore complex. The N-terminal is probably involved in nucleocytoplasmic transport. The C-terminal is involved in protein-protein interaction probably via coiled-coil formation, promotes its association with centrosomes and may function in anchorage of p62 to the pore complex. Plays a role in mitotic cell cycle progression by regulating centrosome segregation, centriole maturation and spindle orientation. It might be involved in protein recruitment to the centrosome after nuclear breakdown.
Subcellular location: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:P37198}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:P37198}. Nucleus envelope {ECO:0000250|UniProtKB:P37198}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:P37198}. Note=Central region of the nuclear pore, within the transporter. During mitotic cell division, it associates with the poles of the mitotic spindle. {ECO:0000250|UniProtKB:P37198}.
Interaction partners:
- Nuclear pore complex protein Nup54
- Nuclear pore complex protein Nup214
- Nucleoporin p58/p45
- Nuclear pore complex protein Nup93
- Nuclear pore complex protein Nup98-Nup96
- Nuclear pore complex protein Nup88
- E3 SUMO-protein ligase RanBP2
- Nuclear pore complex protein Nup107
- Nuclear pore complex protein Nup155
- Nucleoporin 205
Sequence:
MSGFNFGGTGAPAGGFTFGTAKTATTTPATGFSFSASGTGTGGFNFGTPSQPAATTPSTSLFSLTTQTPTTQTPGFNFGTTPASGGTGFSLGISTPKLSLSNAAATPATANTGSFGLGSSTLTNAISSGSTSNQGTAPTGFVFGSSTTSAPSTGSTGFSFTSGSASQPGASGFSLGSVGSSAQPTALSGSPFTPATLVTTTAGATQPAAAAPTAATTSAGSTLFASIAAAPASSSATGLSLPAPVTTAATPSAGTLGFSLKAPGAAPGASTTSTTTTTTTTTTTAAAAAASTTTTGFALSLKPLVSAGPSSVAATALPASSTAAGTATGPAMTYAQLESLINKWSLELEDQERHFLQQATQVNAWDRTLIENGEKITSLHREVEKVKLDQKRLDQELDFILSQQKELEDLLSPLEESVKEQSGTIYLQHADEEREKTYKLAENIDAQLKRMAQDLKDIIEHLNMAGGPADTSDPLQQICKILNAHMDSLQWVDQSSALLQRRVEEASRVCEGRRKEQERSLRIAFD
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (A0A1D8PKB4)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- non-specific serine/threonine protein kinase
- Alpha-factor pheromone receptor
- Ste3p
Sequence:
MTTNPALAAAQASHNNIPTKQMNHSTSSSNGNGSNNSSVVGLHYKIGKKIGEGSFGVIFEGTNIINGVPVAIKFEPRKTEAPQLRDEYRTYKHLQGCDGIPNAYYFGQEGLHNILVIDLLGPSLEDLFDWCGRRFSVKTVVQVAIQMLTLVEEVHRHDLIYRDIKPDNFLIGRRGATDENNVHLIDFGMAKQYRDPRTKQHIPYREKKSLSGTARYMSINTHLGREQSRRDDLEALGHVFFYFLRGQLPWQGLKAPTNKQKYEKIGDKKRTTPAVTLCDGLPQQFAEYLDSVRSLPFDAEPPYEEYRMLLLSVLDDLGQACDGDMDWMHLNGGRGWDATINKKPNLHGYGHPNPPNERERRHRDQRRTRQHQQSQQVQQQQLQAQAQAQQLQQLQQAQQAQQQQQSQQHQPLSAAQLHQQKLQHLVNRPLPPIKQESQSAIQSGNGHHELLNNNLGDQHGGKHEGYSSRPDQYQQQQMVAEEEENKGFWSKLCCH
Protein: Bromo domain-containing protein (Q4GYN3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MRHVDVLQSLMVRLVDPEEEEHDWLLISSLFYSLTKLMLPATRVKELYYHYLQVHGSRPAMEAACKDFSNKLSEKLRQRIESTTTTTTATTLAGIHRSSVSGTSAAVGVLDVTKVSAGAAGGEPGIPVGVLSGSPTVATSVWDESGFCGREAAFRKLTSEQKARWHNLRRELISPDILIDLVQQFTLVDGAAVFLAPVVPSTVMEFNGVRSGPYVTVIHQPLSLMCVKRRVLAARRDYELHKHQSGAYLPTGQNNVGVGSRKRERGNGGVTSRASAVSQPPHFSIATNSGEKGNVIRTLQELEQAVWHITANCVMFNAPESYYPYVARKFALACVAIIDDYCTQRIAGV
Protein: BRCT domain-containing protein (Q57XA8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Protein artemis
- Endo/exonuclease Mre11
- DNA repair protein RAD50
- non-specific serine/threonine protein kinase
- BRCT domain-containing protein
- FHA domain-containing protein
- Helicase-like protein
- Helicase, putative
- Exonuclease, putative
- Flap endonuclease 1
Sequence:
MTLGARGTTLSLRWSPMRVFTVDYNDGCMYEWMSRCGAVTVSDIALADYLVTPHLTITPAAVAVLCRFSSHIVTPEYFKVLQEGRESNPQKELQDPRAYFPSVDSSWSALLSSESSEIFVSDNRAPPAAGEISAGLKVVLSDSSLKERRQRLFAGTTFVVVQQFLYDEVRVFLPFTQGCAVLDLSLLDAVDSCGDEAAVRAFYAKHCNHIVLYSDREELPVLGPLRTLQYAMGMCCVEHTAFIRSVVWLKPLPTLSLSSNVSPSGESEQPAACSCKSVERGSAYANPKQKDHRCEKKMGRGYDETERFPSEQTGRSATEEGQEMREEQECGCRMQGEMEREDAEEDHDCESNMILTQVETGRPCVGMKRGRVGAAAVGRLTDPNPLFQELWSDEEVDGYDDDDATGHHEQNTRSVGAGGWICRKRQAAEVGMDFTVRDGLAISSHPCLKRYAASLISSGGGGGGKWFKKQQLIECREKVELDRTETAPGVGSLMRQLAIDDVDIIPDAVGKAIRMDIRQLGTRHTTRNLQPRQQRRPKKKAPAQYSVLDCDTLSEFPWPYAEGWPSKTTSLGEKQMAKRVDSLNDLLRGPQSRRAPLSVFDLEAFL
Protein: p-hydroxybenzoic acid--AMP ligase FadD22 (p-HB--AMP ligase FadD22) (EC 6.2.1.50) (p-hydroxybenzoic acid-AMP synthetase) (p-HB-AMP synthetase) (P9WQ61)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Catalyzes the adenylation of p-hydroxybenzoic acid (pHBA) to form p-hydroxybenzoic acid-AMP (pHBA-AMP), which is converted directly to p-hydroxybenzoyl-S-FadD22 (pHBA-S-FAdD22) thioester intermediate in a CoA-independent manner by attack of the phosphopantetheine thiol of FadD22. Usually, this intermediate primes the biosynthesis of the phenolphthiocerol (PPOL) by presenting the pHBA starter unit for elongation by Pks15/1, but M.tuberculosis lacks Pks15/1 due to a natural frameshift and thus is unable to produce PPOL.
Interaction partners:
- Chorismate pyruvate-lyase
- Putative inactive phenolphthiocerol synthesis polyketide synthase type I Pks15
- 4-hydroxyphenylalkanoate adenylyltransferase
- Putative inactive phenolphthiocerol synthesis polyketide synthase type I Pks1
- Probable multifunctional mycocerosic acid synthase membrane-associated Mas
- Phenolphthiocerol/phthiocerol polyketide synthase subunit B
- Phenolphthiocerol/phthiocerol polyketide synthase subunit C
- Large ribosomal subunit protein uL6
- Phenolphthiocerol/phthiocerol polyketide synthase subunit E
- Probable fatty-acid-CoA ligase FadD18
Sequence:
MRNGNLAGLLAEQASEAGWYDRPAFYAADVVTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDDHALAARNTEPALVVTSDALRDRFQPSRVAEAAELMSEAARVAPGGYEPMGGDALAYATYTSGTTGPPKAAIHRHADPLTFVDAMCRKALRLTPEDTGLCSARMYFAYGLGNSVWFPLATGGSAVINSAPVTPEAAAILSARFGPSVLYGVPNFFARVIDSCSPDSFRSLRCVVSAGEALELGLAERLMEFFGGIPILDGIGSTEVGQTFVSNRVDEWRLGTLGRVLPPYEIRVVAPDGTTAGPGVEGDLWVRGPAIAKGYWNRPDSPVANEGWLDTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFLVATSGATIDGSVMRDLHRGLLNRLSAFKVPHRFAVVDRLPRTPNGKLVRGALRKQSPTKPIWELSLTEPGSGVRAQRDDLSASNMTIAGGNDGGATLRERLVALRQERQRLVVDAVCAEAAKMLGEPDPWSVDQDLAFSELGFDSQMTVTLCKRLAAVTGLRLPETVGWDYGSISGLAQYLEAELAGGHGRLKSAGPVNSGATGLWAIEEQLNKVEELVAVIADGEKQRVADRLRALLGTIAGSEAGLGKLIQAASTPDEIFQLIDSELGK
Protein: Radixin (Q5WQV5)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004413}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004413}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004413}. Cell projection {ECO:0000256|ARBA:ARBA00004316}.
Interaction partners:
Sequence:
MPKPINVRVTTMDAELEFAIQPNTTGKQLFDQVVKTVGLREVWFFGLQYVDSKGYSTWLKLNKKVTQQDVKKENPLQFKFRAKFFPEDVSEELIQEITQRLFFLQVKEAILNDEIYCPPETAVLLASYAVQAKYGDYNKEIHKPGYLANDRLLPQRVLEQHKLTKEQWEERIQNWHEEHRGMLREDSMMEYLKIAQDLEMYGVNYFEIKNKRGTELWLGVDALGLNIYEHDDKLTPKIGFPWSEIRNISFNDKKFVIKPIDKKAPDFVFYAPRLRINKRILALCMGNHELYMRRRKPDTIEVQQMKAQAREEKHQKQLERAQLENEKKKREIAEKEKERIEREKEELMERLRQIEEQTMKAQKELEEQTRKALELEQERQRAKEEAERLDRERRAAEEAKSAIAKQAADQMKNQEQLAAELAEFTAKIALLEEAKKKKEEEATEWQHKAFAAQEDLEKTKEELKTVMCAPPPPPPPAVVPPTENEHDEQDEHSAEASAELSSEGVTNHRSEEERVTETQKNERVKKQLQALSSELAQARDETKKTQNDVLHAENVKAGRDKYKTLRQIRQGNTKQRIDEFEAM
Protein: Inositol-tetrakisphosphate 1-kinase 2 (GmItpk2) (EC 2.7.1.134) (Inositol 1,3,4-trisphosphate 5/6-kinase 2) (Inositol-triphosphate 5/6-kinase 2) (Ins(1,3,4)P(3) 5/6-kinase 2) (EC 2.7.1.159) (Inositol-hexakisphosphate 5-kinase) (EC 2.7.4.21) (A7X665)
Organism: Glycine max (Soybean) (Glycine hispida)
Function: Kinase that can phosphorylate various inositol polyphosphate such as Ins(3,4,5,6)P4, Ins(3,4,6)P3 and Ins(1,3,4)P3. May participate in an inositol lipid-independent pathway of InsP6 synthesis. Barely able to add a beta-phosphate to InsP6 to yield 5-InsP7, thus exhibiting negligible InsP6 kinase activity. Has also Ins(1,3,4,5,6)P5 phosphatase activity. Probably involved in the regulation of drought and salinity tolerance by diverting the flux of inositol phosphate pool towards phytate biosynthesis.
Interaction partners:
- Inositol-pentakisphosphate 2-kinase
- Inositol-pentakisphosphate 2-kinase
- Inositol polyphosphate multikinase
- 3'
- Uncharacterized protein
- Inositol polyphosphate-related phosphatase domain-containing protein
- Inositol-pentakisphosphate 2-kinase
- Multiple inositol polyphosphate phosphatase 1
- Multiple inositol polyphosphate phosphatase 1
- histidinol-phosphatase
Sequence:
MSESEVAGQRYRVGYALQGKKVESFIQPSLLDHAKQHSIDLVQIDPTAPLQQQGPFHCIIHKLHTQHWKNLLQQFSSKHPNTVIIDPPELVDRLHNRVSMLDAVTHLQFSLENATIGVPKQVVVNEPKSFDLHKFEEEQGLRFPVIAKPLAADGGAGSHELCLVFDEEGLHALSVPMVLQEFVNHGGVVFKIYVAGQRVNCVKRKSLGDITEEKLKVLRGSLPFSRVSSLGVEDEGGGAVEDAEMPPQSLVGELARGLREALGLNLFNVDVIRDGKEPTRYLVIDINYFPGYAKLPSYEPFITDFLLDIVRSKTA