wanglab/gogpt-training-data huggingface dataset:
Protein: DNA polymerase epsilon catalytic subunit (EC 2.7.7.7) (Q9GV40)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU365029}.
Interaction partners:
Sequence:
MSDSGKGKVLQNTGKFVSENRTEGDDFFNEAGYRQSRENDKIDSKYGFDRVKDSQERTGYLINMHSNEVLDEDRRLIAALDLFFIQMDGSRFKCTVAYQPYLLIRPEDNMHLEVARFLGRKYSGQISGLEHITKEDLDLPNHLSGLQQQYIKLSFLNQTAMTKVRRELMSAVKRNQERQKSNTYYMQMLATSLAQSSAGSEDATLGKRQQDYMDCIVDIREHDVPYHVRVSIDLRIFCGQWYNIRCRSGVELPTITCRPDILDRPEPVVLAFDIETTKLPLKFPDAQTDQVMMISYMIDGQGYLITNREIISSNVDDFEYTPKPEFEGNFIVFNEENEMQLLQRFFDHIMEVRPHIIVTYNGDFFDWPFVETRAAVYDLDMKQEIGFSKLRDGNYLSRPAIHMDCLCWVKRDSYLPVGSQGLKAVAKAKLRYDPVELDPEDMCRMAVEQPQVLANYSVSDAVATYYLYMKYVHPFIFALNTIIPMEPDEILRKGSGTLCETLLMVEAYHAQIVYPNKHQSELNKLSNEGHVLDSETYVGGHVEALESGVFRADIPCRFRLDPAMVKQLQEQVDAVLRHAIEVEEGIPLEKVLNLDEVRQEIVQGLQGLHDIPNRLEQPVIYHLDVGAMYPNIILTNRLQPSAMVSDLDCAACDFNKPGVRCKRSMDWLWRGEMLPASRNEFQRIQQQLETEKFPPLFPGGPQRAFHELSKEDQAAYEKKRLTDYCRKAYKKTKLTKLETRTSTICQKENSFYVDTVRAFRDRRYEYKGLTKVAKASVNAAVASGDAAEIKAAKGREVLYDSLQLAHKCILNSFYGYVMRRGARWHSMPMAGIVCLTGSNIITKAREIIERVGRPLELDTDGIWCILPGSFPQEFTIHTSHEKKKKINISYPNAVLNTMVKDHFTNDQYHELRKDKENNLPKYDIRDENSIFFEVDGPYLAMVLPAAKEEGKKLKKRYAVFNFDGTLAELKGFEVKRRGELQLIKNFQSSVFEAFLAGSTLEECYASVAKVADYWLDVLYSRGSNLPDSELFELISENKSMSKKLEEYGAQKSTSISTAKRLAEFLGEQMVKDAGLACKYIISKKPEGAPVTERAIPLAIFQSEPSVRRHHLRRWLKDNTMGDADIRDVLDWNYYIERLGGTIQKIITIPAALQGLANPVPRVQHPDWLHKKMLEKNDVLKQRRINEMFTSRPKPKPLATEEDKLADMEDLAGKDGGEGAAGCPIVTKRKRIQLEEHDEEEAQPQATTWRQALGAPPPIGETRKTIVEWVRFQKKKWKWQQDQRQRNRQASKRTRGEDPRYTGRFLRRAQRTLLDQPWQIVQLVPVDDLGHFTVWALIGEELHKIKLTVPRIFYVNQRSAAPPEEGQLWRKVNRVLPRSRPVFNLYRYSVPEQLFRDNSLGMLADLATPDIEGIYETQMTLEFRALMDMGCICGVQREEARRLAQLATKDLETFSIEQLEQGPRLRSNIWLAPTIDCAKSTCISITHRRPRRRSVSLIPMPSKKAFVFALDTVRANQMPNMRQLYTAERLALLKNLTAEEQDKIPVEDYTFEVLIEVDVKQIYRHIQRALTTYKQEHQGPPTILCLQTALSARKLSLAMPILLEFPQAQIHISDDASLLSGLDWQRQGSRAVIRHFLNLNNVLDLMLDQCRYFHVPIGNMPPDTVLFGADLFFARLLQRHNFVLWWSASTRPDLGGREADDSRLLAEFEESISVVQNKAGFYPDVCVELALDSLAVSALLQSTRIQEMEGASSAITFDVMPQVSLEEMIGTVPAATLPSYDETALCSAAFRVMRSMVNGWLREVSINRNIFSDFQIVHFYRWVRSSNALLYDPALRRSLNNLMRKMFLRIIAEFKRLGATIIYADFNRIILSSGKKTVSDALGYVDYIVQSLRNKEMFHSIQLSFEQCWNFMLWMDQANFSGIRGKLPKGIDETVSSIVSTTMIRDSERNQDDDEDEEEDSENRDPVESNEAEQDQEDELSLELNWTIGEHLPDENECREKFESLLTLFMQSLAEKKTTEQAIKDISHCAFDFILKLHKNYGKGKPSPGLELIRTLIKALSVDKTLAEQINELRRNMLRLVGIGEFSDLAEWEDPCDSHIINEVICKACNHCRDLDLCKDKHRAMKDGCYVAYDNEEIEMRMLDALQRKMMSYVLQDLRCSRCSEIKRENLAEFCTCAGNFVPLISGKDIQTLLGTFNKVAANHKMQLLQQTVHQALTTPR
Protein: Melanoma-associated antigen 4 (Cancer/testis antigen 1.4) (CT1.4) (MAGE-4 antigen) (MAGE-41 antigen) (MAGE-X2 antigen) (P43358)
Organism: Homo sapiens (Human)
Function: Regulates cell proliferation through the inhibition of cell cycle arrest at the G1 phase. Also negatively regulates p53-mediated apoptosis.
Interaction partners:
- Cancer/testis antigen 1
- Cancer/testis antigen 2
- E3 ubiquitin-protein ligase RAD18
- Melanoma-associated antigen 10
- HLA class I histocompatibility antigen, A alpha chain
- E3 ubiquitin-protein ligase TRIM69
- Melanoma antigen preferentially expressed in tumors
Sequence:
MSSEQKSQHCKPEEGVEAQEEALGLVGAQAPTTEEQEAAVSSSSPLVPGTLEEVPAAESAGPPQSPQGASALPTTISFTCWRQPNEGSSSQEEEGPSTSPDAESLFREALSNKVDELAHFLLRKYRAKELVTKAEMLERVIKNYKRCFPVIFGKASESLKMIFGIDVKEVDPASNTYTLVTCLGLSYDGLLGNNQIFPKTGLLIIVLGTIAMEGDSASEEEIWEELGVMGVYDGREHTVYGEPRKLLTQDWVQENYLEYRQVPGSNPARYEFLWGPRALAETSYVKVLEHVVRVNARVRIAYPSLREAALLEEEEGV
Protein: Anhydromuropeptide permease (AmpG permease) (Muropeptide:H(+) symporter) (P0AE16)
Organism: Escherichia coli (strain K12)
Function: Permease involved in cell wall peptidoglycan recycling. Transports, from the periplasm into the cytoplasm, the disaccharide N-acetylglucosaminyl-beta-1,4-anhydro-N-acetylmuramic acid (GlcNAc-anhMurNAc) and GlcNAc-anhMurNAc-peptides. Transport is dependent on the proton motive force. AmpG is also involved in beta-lactamase induction.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:15728916, ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000269|PubMed:15728916}.
Interaction partners:
- 1,6-anhydro-N-acetylmuramyl-L-alanine amidase AmpD
- Beta-hexosaminidase
- N-acetylmuramoyl-L-alanine amidase AmiD
- Soluble lytic murein transglycosylase
- Beta-lactamase
- Anhydro-N-acetylmuramic acid kinase
- D-alanyl-D-alanine carboxypeptidase DacB
- Membrane-bound lytic murein transglycosylase B
- Protein AmpE
- UDP-N-acetylmuramate--L-alanyl-gamma-D-glutamyl-meso-2,6-diaminoheptandioate ligase
Sequence:
MSSQYLRIFQQPRSAILLILGFASGLPLALTSGTLQAWMTVENIDLKTIGFFSLVGQAYVFKFLWSPLMDRYTPPFFGRRRGWLLATQILLLVAIAAMGFLEPGTQLRWMAALAVVIAFCSASQDIVFDAWKTDVLPAEERGAGAAISVLGYRLGMLVSGGLALWLADKWLGWQGMYWLMAALLIPCIIATLLAPEPTDTIPVPKTLEQAVVAPLRDFFGRNNAWLILLLIVLYKLGDAFAMSLTTTFLIRGVGFDAGEVGVVNKTLGLLATIVGALYGGILMQRLSLFRALLIFGILQGASNAGYWLLSITDKHLYSMGAAVFFENLCGGMGTSAFVALLMTLCNKSFSATQFALLSALSAVGRVYVGPVAGWFVEAHGWSTFYLFSVAAAVPGLILLLVCRQTLEYTRVNDNFISRTAYPAGYAFAMWTLAAGVSLLAVWLLLLTMDALDLTHFSFLPALLEVGVLVALSGVVLGGLLDYLALRKTHLT
Protein: Thermostable carboxypeptidase 1 (EC 3.4.17.19) (TthCP1) (Q5SLM3)
Organism: Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)
Function: Broad specificity carboxypetidase that releases amino acids sequentially from the C-terminus, including neutral, aromatic, polar and basic residues, but not Pro. Has lower activity with substrates ending with Gly or Glu.
Interaction partners:
Sequence:
MTPEAAYQNLLEFQRETAYLASLGALAAWDQRTMIPKKGHEHRARQMAALARLLHQRMTDPRIGEWLEKVEGSPLVQDPLSDAAVNVREWRQAYERARAIPERLAVELAQAESEAESFWEEARPRDDWRGFLPYLKRVYALTKEKAEVLFALPPAPGDPPYGELYDALLDGYEPGMRARELLPLFAELKEGLKGLLDRILGSGKRPDTSILHRPYPVEAQRRFALELLSACGYDLEAGRLDPTAHPFEIAIGPGDVRITTRYYEDFFNAGIFGTLHEMGHALYEQGLPKEHWGTPRGDAVSLGVHESQSRTWENLVGRSLGFWERFFPRAREVFASLGDVSLEDFHFAVNAVEPSLIRVEADEVTYNLHILVRLELELALFRGELSPEDLPEAWAEKYRDHLGVAPKDYKDGVMQDVHWAGGLFGYFPTYTLGNLYAAQFFQKAEAELGPLEPRFARGEFQPFLDWTRARIHAEGSRFRPRVLVERVTGEAPSARPFLAYLEKKYAALYG
Protein: Homeobox protein abdominal-B (Infraabdominal 7) (IAB-7) (P3) (PH189) (P09087)
Organism: Drosophila melanogaster (Fruit fly)
Function: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis.
Subcellular location: Nucleus.
Interaction partners:
- Homeobox protein extradenticle
- Homeobox protein homothorax
- Protein doublesex
- Homeobox protein abdominal-A
- Homeotic protein ultrabithorax
- Heme oxygenase
- Homeotic protein deformed
- CTCF
- Zinc finger protein su
- Homeotic protein antennapedia
Sequence:
MQQHHLQQQQQQQQQQEQQHLQEQQQHLQQLHHHAHHHLPQPLHTTSHHHSAHPHLQQQQQQQQHAVVASSPSSVLQQQQQQSTPTTHSTPTHAVMYEDPPPVPLVAVQQQHLPAPQQQQQLQQQQQQQQQQLATTPVAGALSPAQTPTGPSAQQQQHLTSPHHQQLPQQQTPNSVASGASSNLQQQQQQQNAAVAPGQTQIVAPTTASVSPSSVSSQKEDINMSIQLAPLHIPAIRAGPGFETDTSAAVKRHTAHWAYNDEGFNQHYGSGYYDRKHMFAYPYPETQFPVGQYWGPNYRPDQTTSAAAAAAYMNEAERHVSAAARQSVEGTSTSSYEPPTYSSPGGLRGYPSENYSSSGASGGLSVGAVGPCTPNPGLHEWTGQVSVRKKRKPYSKFQTLELEKEFLFNAYVSKQKRWELARNLQLTERQVKIWFQNRRMKNKKNSQRQANQQNNNNNSSSNHNHAQATQQHHSGHHLNLSLNMGHHAAKMHQ
Protein: Candida glabrata strain CBS138 chromosome F complete sequence (Q6FUQ9)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Subcellular location: Cell envelope {ECO:0000256|ARBA:ARBA00004196}.
Interaction partners:
Sequence:
MAYTKTALLVSALAAFAVAQDATQLAELNAILQDFSSHLSDYTGLLANPNSGITAADLPAGVLQLGLAIQTATDKSYTSLYPSVDFKGIEALLPKLPWYSSRLLPAINAALSSATPAPSSSSAAPSSSAAPSSSAAPSSSSAAPSSSAAPSSSARPSSSAAPSSSAKPSSSAAPSSAAPTTTKAISQIGDGQIQAHQTTNGAGKVAAGMGAGVLAAAAMLL
Protein: Fibroblast growth factor 1 (Acidic fibroblast growth factor) (Heparin-binding growth factor 1) (C9JDC5)
Organism: Homo sapiens (Human)
Subcellular location: Secreted {ECO:0000256|RuleBase:RU364136}. Cytoplasm {ECO:0000256|RuleBase:RU364136}. Cytoplasm, cell cortex {ECO:0000256|RuleBase:RU364136}. Cytoplasm, cytosol {ECO:0000256|RuleBase:RU364136}. Nucleus {ECO:0000256|RuleBase:RU364136}.
Interaction partners:
Sequence:
MAEGEITTFTALTEKFNLPPGNYKKPKLLYCSNGGHFLRILPDGTVDGTRDRSDQHIQ
Protein: Protein GRIM REAPER (Stigma-specific STIG1-like protein GRI) [Cleaved into: GRIp] (Q9LNN7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in the regulation of cell death induced by extracellular reactive oxygen species. Only the processed peptide, and not the full length GRI can bind in vivo to the extracellular domain of the receptor PRK5. The GRIp-induced cell death is superoxide and salicylic acid dependent.
Subcellular location: Secreted, extracellular space, apoplast {ECO:0000269|PubMed:19279211}.
Interaction partners:
- Pollen receptor-like kinase 5
- CASP-like protein 2A2
- Metacaspase-9
- At3g53980
- GDSL esterase/lipase At1g58725
- Uncharacterized protein At5g65660
- Large ribosomal subunit protein eL21z/eL21y
Sequence:
MVIKIPNTFIKATSLLSLILYFLIIATSKSNSVLADEVVDQEDDPEYYILDETPSILSNVTISSKTRLLVSHYKKIKKGMRCHVESYNICNGVKANKGTSLLHCCKKHCRNVLGDRNNCGRCGHKCGFGQRCCGGVCTYVNFNPNHCGKCTRKCASGVKCEYGYCGYA
Protein: Forkhead box K, isoform O (M9PI07)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00089}.
Interaction partners:
Sequence:
MAATTTTTTTTLATTTGNSSSTNNSSSNNNNSIASSHNNNNNIVTVHTVLNNPPTNTAGGGVADAATVAIAKDMLQLHHGAAAAATAALNNYNNSSNNNNNSADQLTGNSNNSANHPPATSSTTNSSSSSTTSANTNNPSANAASTLTSSSPPYGELRFNQEVLPITDAVTVIGRNSSTSLVHFNVAENNLVSRKHFQVLYDVELRAFFVQCLSKNGIFVDDFLQRRNVDPLRLPQRCYFRFPSTEIRIEFESYVPATSSDAIDGHSPSLVVGGGGGVAGGGAHVIITPLPRDELHQQQLHHHQQQPHLQQQQHPHHPPAHHLPLQQQQQQQQPAHHPLPHTPHHPLHHTALHQQQQRSGSIVVAPPAGAAAHLIAGDGPGIYSPLKISIPKKEQKSPYLSPTGTISAANSCPASPRQGFIQNQPNNYNNYGNNNTDLFQTPSTASYNHNEKPPYSYAQLIVQAISAAPDKQLTLSGIYSFIVKHYPYYRKETNKGWQNSIRHNLSLNRYFIKVARSQDEPGKGSFWRIDPDSGAKLIDHSYKKRRQRSSQGFRPPYGMPRSAPVSPSHMDNSRESSPLQDIVLQSAPGSPGMSLEQRAADPEIIYNSQNAHQQQQQQQQQQQQQTLSNNSNQYSSGSPYYVTNQSSGVATPQTHVEGSAASGGGGGGGVGALLALKRNHVMGGGASQHTLHQQQAVAQQQHSEIIYEELPTDYSGHIEASEEECVTTATDATVAKRPKYVSEVL
Protein: Rhodanese domain-containing protein (Q586G5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- 30S Ribosomal protein S17, putative
- Uncharacterized protein
- Manganese/iron superoxide dismutase C-terminal domain-containing protein
- 30S ribosomal protein S8, putative
- Uncharacterized protein
- Ubiquitin-like domain-containing protein
- Uncharacterized protein
- Uncharacterized protein
- LysM domain-containing protein
- Uncharacterized protein
Sequence:
MLVSYLRLQADRRTRHHMMVDGQINPREWFNWHPKEYQPWYFDRHKFLYEQRQYAQFHHLLCHQVYLKDMLHLMRYPEPYTHIIDCRTSTQKMHRWVPHSLWLPRDEVEYALQLSADEFLDMYGFRKPDKSDDVILLSHNGIYSEQAGWEWKKQFFQHVYNYRGGTNELFGESYSDMNVSDVLSPWKGPFPQSGVFVDKWSKRKVLTRTGPFDRQYEMQDFALPDLELEKARHPEEGPRQNMPFGLQ
Protein: PTPRF interacting protein alpha 1 (A0A0G2K3L9)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MMCEVMPTISEAEGPPGGGGSHGSGSPSQPDADSHFEQLMVSMLEERDRLLDTLRETQETLALTQGKLHEVGHERDSLQRQMVLLMHERSLRMTVVKRQAQSPAGVSSEVEVLKALKSLFEHHKALDEKVRERLRVALERCSLLEEELGATHKELMILKEQNSQKKALTEGMLDGNHEQENAPSTNGKRSSDGSLSHEDLAKVLELQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSESNERLQLHLKERMAALEDKNSLLREVENAKKQLEETQHDKDQLVLNIEALKAELEQMRLRGSSLHHGRPHLGSVPDFRFSVADGHVDAYSTSAVLRRPQKGRLAALRDEPSKVQTLNEQDWERAQQASVLANVAQAFESDVDVSDGEDDRDTLLSSVDLLSPSGQADAQTLAMMLQEQLDAINKEIRLIQEEKENTEQRAEEIESRVGSGSLDNLGRFRSMSSIPPYPASSLAGSSPPGSGRSTPRRVPHSPAREVDRLGVMTLLPASREEVRDDKTTIKCETSPPSSPRPLRLDRLHKGALHTVSHEDIRDLRNSTGSQDGPVSNPSSSNSSQDSLHKAPKKKGIKSSIGRLFGKKEKGRPGPLGKESPGQAGVSETENSSQDALGLSKLGGQAEKNRKLQKKHELLEEARRQGLPFAQWDGPTVVVWLELWVGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEIMSLTSPSAPPTSRTTLAYGDMNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRGQLKMVDSFHRNSFQCGIMCLRRLNYDRKELERKREESQNETRDVLVWSNDRVIRWILSIGLKEFANNLIESGVHGALLALDETFDFSALALLLQIPTQNTQARAVLEREFNNLLVTGTDRRFDEDDDKSFRRAPSWRKKFRPKDIRGLASGSAETLPANFRVTSSMSSPSMQPKKVQMDENPHLIES
Protein: RNA polymerase I-specific transcription initiation factor RRN7 (P40992)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of RNA polymerase I core factor complex (CF) that acts as a SUA7/TFIIB-like factor and plays a key role in multiple steps during transcription initiation such as pre-initiation complex (PIC) assembly and postpolymerase recruitment events in polymerase I (Pol I) transcription. Binds rDNA promoters and plays a role in Pol I recruitment. After binding of UAF (upstream activation factor) to an upstream element of the promoter, CF is recruited in a SPT15/TBP-dependent manner to form a pre-initiation complex.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- RNA polymerase I-specific transcription initiation factor RRN11
- RNA polymerase I-specific transcription initiation factor RRN6
- RNA polymerase I-specific transcription initiation factor RRN3
- TATA-box-binding protein
- RNA polymerase I-specific transcription initiation factor RRN9
- RNA polymerase I-specific transcription initiation factor RRN5
- RNA polymerase I-specific transcription initiation factor RRN10
- DNA-directed RNA polymerase I subunit RPA135
- DNA-directed RNA polymerases I, II, and III subunit RPABC4
- Upstream activation factor subunit UAF30
Sequence:
MSTFIRGPICGTDNCPSRLWRIIDGRRTCQYGHVMEGDVEFNDDEDDLNGLGAGVITRRLNLTTNATGSFQSSQLTNSQLLQQQQRQSHKKFKKLIGHEAKLLFLKSFQFILKRQIRWLITEMRFPKEFEHVAKIIWLKILKTINDQPQEELKLQLHMTSTISILYLASTHLSLPVYTCDYIKWICTAKMPYFQASEILPKSWRIQLPNYYVSILEGSISPFNGQLYNKIALTCGMIHFKEFFNSEISCQGLLLKLVMQCALPPEFYFYTKQVIEFEETDIRNLTLWERTDERHTGRVSNHAELRVLSYFMLTINWMLSFDRDRQYPLKWILSLTESLTQRTTTSESIGRNIVKVVYPDKPTSSDYFQWSEEETLEFLKWMEKQFLPTQTKSLHNENGSMEMTIDQKIARRKLYKIFPLDREANHDGEFNDSTHQLTFIEDLQERYAKQTPFFESNKIRDSLNYQEANPPARKEAIGRLLTHIASQLLVDFAISKEQLKDCISRIKNACLHRMN
Protein: Nucleoporin NUP157 (Nuclear pore protein NUP157) (P40064)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors.
Subcellular location: Nucleus, nuclear pore complex {ECO:0000269|PubMed:10684247}. Nucleus membrane; Peripheral membrane protein; Cytoplasmic side. Nucleus membrane; Peripheral membrane protein; Nucleoplasmic side. Note=Symmetric distribution.
Interaction partners:
- Nucleoporin NIC96
- Nucleoporin ASM4
- Nucleoporin NUP188
- Nucleoporin NUP57
- Nucleoporin NUP53
- Nucleoporin NUP192
- Nucleoporin NUP133
- Nucleoporin NUP170
- Nucleoporin POM152
- Nucleoporin NUP85
Sequence:
MYSTPLKKRIDYDRETFTASASLGGNRLRNRPRDDQNNGKPNLSSRSFLSERKTRKDVLNKYGEAGNTIESELRDVTTHVKISGLTSSEPLQLASEFVQDLSFRDRNTPILDNPDYYSKGLDYNFSDEVGGLGAFTPFQRQQVTNIPDEVLSQVSNTEIKSDMGIFLELNYCWITSDNKLILWNINNSSEYHCIDEIEHTILKVKLVKPSPNTFVSSVENLLIVATLFDIYILTISFNDRTHELNIFNTGLKVNVTGFNVSNIISYERTGQIFFTGATDGVNVWELQYNCSENLFNSKSNKICLTKSNLANLLPTKLIPSIPGGKLIQKVLEGDAGTEEETISQLEVDQSRGVLHTLSTKSIVRSYLITSNGLVGPVLIDAAHIRRGMNALGVKNSPLLSNRAFKIAKIVSISMCENNDLFLAVITTTGVRLYFKGSISRRSIGSLKLDSVKFPPTSISSSLEQNKSFIIGHHPLNTHDTGPLSTQKASSTYINTTCASTIISPGIYFTCVRKRANSGELSKGITNKALLENKEEHKLYVSAPDYGILKNYGKYVENTALLDTTDEIKEIVPLTRSFNYTSTPQGYANVFASQYSAEPLKVAVLTSNALEIYCYRTPDEVFESLIENPLPFIHSYGLSEACSTALYLACKFNKSEHIKSSALAFFSAGIPGVVEIKPKSSRESGSVPPISQNLFDKSGECDGIVLSPRFYGSALLITRLFSQIWEERVFVFKRASKTEKMDAFGISITRPQVEYYLSSISVLADFFNIHRPSFVSFVPPKGSNAITASDAESIAMNALILLINSIKDALSLINVFYEDIDAFKSLLNTLMGAGGVYDSKTREYFFDLKFHDLFTPNAKTKQLIKEILIEVVNANIASGTSADYIVNVLKERFGSFCHSADILCYRAGEHLEAAQKFEMIDSKISRNHLDTAIDLYERCAENIELCELRRVVDIMVKLNYQPKTVGFLLRFADKIDKGNQAQEYVSRGCNTADPRKVFYDKRINVYTLIFEIVKSVDDYTSIEQSPSIANISIFSPASSLKKRVYSVIMNSNNRFFHYCFYDWLVANKRQDYLLRLDSQFVLPYLKERAEKSLEISNLLWFYLFKEEHFLEAADVLYALASSDFDLKLSERIECLARANGLCDSSTSFDQKPALVQLSENIHELFDIASIQDDLLNLVRNETRIDEDYRKQLTLKLNGRVLPLSDLFNDCADPLDYYEIKLRIFKVSQFKDEKVIQGEWNRLLDSMKNAPSPDVGSVGQESFLSSISNTLIRIGKTTRDTDVVFPVHFLMNKILESFIDKSSAADGSVCSMFLLAGVSHLKLYYILSRIIENSEGNVELAKKEMVWLIKDWYQSDSDLRGSIAPEQIKKLEKYDPNTDPVQDYVKDRHHGLK
Protein: Lysocardiolipin acyltransferase 1 (EC 2.3.1.-) (1-acylglycerol-3-phosphate O-acyltransferase 8) (1-AGP acyltransferase 8) (1-AGPAT 8) (EC 2.3.1.51) (Acyl-CoA:lysocardiolipin acyltransferase 1) (Q3UN02)
Organism: Mus musculus (Mouse)
Function: Exhibits acyl-CoA:lysocardiolipin acyltransferase (ALCAT) activity; catalyzes the reacylation of lyso-cardiolipin to cardiolipin (CL), a key step in CL remodeling. Recognizes both monolysocardiolipin and dilysocardiolipin as substrates with a preference for linoleoyl-CoA and oleoyl-CoA as acyl donors. Also exhibits 1-acyl-sn-glycerol-3-phosphate acyltransferase activity (AGPAT) activity; converts 1-acyl-sn-glycerol-3- phosphate (lysophosphatidic acid or LPA) into 1,2-diacyl-sn-glycerol-3- phosphate (phosphatidic acid or PA) by incorporating an acyl moiety at the sn-2 position of the glycerol backbone (By similarity). Possesses lysophosphatidylinositol acyltransferase (LPIAT) activity. Possesses lysophosphatidylglycerol acyltransferase (LPGAT) activity (By similarity). Required for establishment of the hematopoietic and endothelial lineages.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:15152008}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Tafazzin family protein
- Cardiolipin synthase
- Lysophospholipid acyltransferase LPCAT4
- Membrane-bound glycerophospholipid O-acyltransferase 2
- Membrane-bound glycerophospholipid O-acyltransferase 1
- Lysophosphatidylcholine acyltransferase 1
- 1-acyl-sn-glycerol-3-phosphate acyltransferase alpha
- 1-acyl-sn-glycerol-3-phosphate acyltransferase beta
- Lysophosphatidylcholine acyltransferase 2
- Membrane-bound acylglycerophosphatidylinositol O-acyltransferase MBOAT7
Sequence:
MVSWKGIYFILFLFAGSFFGSIFMLGPILPLMFINLSWYRWISSRLVATWLTLPVALLETMFGVRVVITGDAFVPGERSVIIMNHRTRVDWMFLWNCLMRYSYLRVEKICLKSSLKSVPGFGWAMQVAAFIFIHRKWKDDKSHFEDMIDYFCAIHEPLQLLIFPEGTDLTENNKARSNDFAEKNGLQKYEYVLHPRTTGFTFVVDRLREGKNLDAVHDITVAYPYNIPQTEKHLLLGDFPKEIHFHVQRYPADSLPTSKEDLQLWCHRRWEEKEERLRSFYQGEKNFHFTGQSTVPPCKSELRVLVVKLLSIVYWALFCSAMCLLIYLYSPVRWYFIISIVFFVLQERIFGGLEIIELACYRFLHKHPHLNSKKNE
Protein: Ferredoxin-dependent glutamate synthase 2, chloroplastic (EC 1.4.7.1) (Fd-GOGAT 2) (Q9T0P4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May play a role in primary nitrogen assimilation in roots. Could supply a constitutive level of glutamate to maintain a basal level of protein synthesis.
Subcellular location: Plastid, chloroplast stroma {ECO:0000250}.
Interaction partners:
- Glutamate dehydrogenase 1
- Glutamate dehydrogenase 2
- NADPH:adrenodoxin oxidoreductase, mitochondrial
- glutamate dehydrogenase
- Glutamine synthetase cytosolic isozyme 1-4
- Glutamine synthetase cytosolic isozyme 1-3
- Glutamine synthetase cytosolic isozyme 1-1
- Glutamine synthetase, chloroplastic/mitochondrial
- Probable glutamate dehydrogenase 3
- Glutamine synthetase cytosolic isozyme 1-2
Sequence:
MALQSPGATGASSSVSRLLSSAKLSSTKTIFSVDFVRSYCISKGTKRRNELSGFRGYSPLLKSSLRSPFSVKAILNSDRAAGDASSSFSDLKPQVAYLEDIISERGACGVGFIANLENKATHKIVNDALIALGCMEHRGGCGSDNTSGDGSGLMTSIPWDLFNEWAEKQGIASFDRTHTGVGMLFLPRDDNIRKEAKKVITSIFEKEGLEVLGWRDVPVEASIVGHNAKQTMPNTEQVFVRIVKDDKVDDVERELYICRKLIERAVASESWASELYFSSLSNQTIVYKGMLRSEVLGLFYPDLQNDLYKSPFAIYHRRFSTNTSPRWHLAQPMRFLGHNGEINTIQGNLNWMTSREASLRSPVWHGRENDIRPISNPKASDSANLDSAAELLIRSGRTPEESLMILVPEAYKNHPTLMIKYPEAVDFYDYYKGQMEPWDGPALVLFSDGKTVGACLDRNGLRPARYWRTSDNVVYVASEVGVLPMDESKVTMKGRLGPGMMISVDLENGQVYENTEVKKRVASYNPYGKWVSENLRNLKPSNYLSSAILETDETLRRQQAFGYSSEDVQMVIESMAAQGKEPTFCMGDDTPVAVLSQKPHMLYDYFKQRFAQVTNPAIDPLREGLVMSLEVNIGKRGNILEVGPQNVSQVVLSGPVLNERELEGLLGDPLLKSQILPTFFDIRRGIEGSLKKGLLKLCEAADEAVRNGSQVLVLSDRSDNPEPTRPAIPMLLAVGAVHQHLIQNGLRMSASIIADTAQCFSTHHFACLIGYGASAICPHLALETCRQWRLSNKTVNMMRNGKMPTVTMEQAQKNYRKAVNTGLLKVLSKMGISLFSSYCGAQIFEIYGLGNEVVEFSFRGSASQIGGLTLDELARETLTFWVRAFSEDTAKRLENFGFIQFRPGGEYHGNNPEMSKLLHKAVREKSETAYAVYQQHLANRPITVFRDLLEFKSDRNPIPVGKVEPASSIVERFCTGGMSLGAISRETHETIAIAMNRLGGKSNSGEGGEDPIRWKPLTDVVDGYSSTLPHLKGLRNGDTATSAIKQVASGRFGVTPTFLVNADQLEIKVAQGAKPGEGGQLPGKKVSAYIARLRNSKPGVPLISPPPHHDIYSIEDLAQLIFDLHQVNPKAKVSVKLVSETGIGTVASGVAKANADIIQISGYDGGTGASPISSIKHAGGPWELGLAETQKTLIGNGLRERVIIRVDGGFKSGVDVLIAAAMGADEYGFGTLAMIATGCIMARICHTNNCPVGVASQREELRARFPGLPGDLVNFFLYIAEEVRGILAQLGYEKLDDIIGRTDLLKARDISLVKTHLDLSYLLSSVGLPKRSSTSIRKQEVHSNGPVLDDTLLQDPEIMDAIENEKTVHKTMSIYNVDRSVCGRIAGVIAKKYGDTGFAGQLNLTFTGSAGQSFACFLTPGMNIRLVGEANDYVGKGMAGGEVVILPVESTGFRPEDATIVGNTCLYGATGGLLFVRGKAGERFAVRNSLAQAVVEGTGDHCCEYMTGGCVVILGKVGRNVAAGMTGGLAYILDEDNTLLPKMNKEIVKIQRVTSPVGQTQLKSLIQAHVEKTGSSKGAMIVEEWDKYLAMFWQLVPPSEEDTPEANSDHILKTTTGDEEQVSSTLAEK
Protein: Intracellular chorismate mutase (CM) (EC 5.4.99.5) (A0R3N5)
Organism: Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis)
Function: Catalyzes the Claisen rearrangement of chorismate to prephenate. Probably involved in the aromatic amino acid biosynthesis.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Phospho-2-dehydro-3-deoxyheptonate aldolase AroG
- Chorismate synthase
- Prephenate dehydrogenase
- Anthranilate synthase component 1
- Secreted chorismate mutase
- Prephenate dehydratase
- Anthranilate synthase component 2
- Cyclohexadienyl dehydratase
- isochorismate synthase
- Anthranilate synthase component I
Sequence:
MRPDHRMGPPHDEEPHMPETIDAVPEIDDLRREIDELDATIIAAIQRRTEVSKTIGKARMASGGTRLVHSREMKVIERYIDALGPEGKDLAMLLLRLGRGRLGY
Protein: Neural friend of GATA-B (Zfpm2b protein) (Zinc finger protein ZFPM2b isoform X1) (Zinc finger protein, FOG family member 2b) (B2GM63)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSRRKQSNPKQFKRVFENGLEADSEETLCEKKEILKEEDQSVEDDPIYFSDPENGISKDGDHSRNGEMGGSVKVEQQDSDGQEERVQSSPVTAEEWDGPRELKIVCEGEERKICSCQALLLGTTWGPFPGKIEATTGGSDKVSLVLNGGPRWLMDIMWVSAEDGKSNCAVYSKGGHVWCSTTKNIMEGDELAACVVDLHSHLQTPGPNPYGQGMYPSRQLDAIQLLPQQAAMASILPGAIINSLKSDEVSTGSNLKCTICDYSAETLMVLQHHILSHLSQTGLRCGQCHFSFQTPREMAKHQELHGHNCTVTNKPIKEDKTDNAPNSITSNSQQVRAKTNINDLQESTAQCDVTQISDLQNTDSSQKSNKGEANSGNKANLSYSRVKSEPSSPRLASSPIQHHLPPAFPLPPFIPHVPFSQDITMGPQASEILAKMSELVHRRLRHGGNSYPPVMYSALVPKGATCFECNITFNNLDNYLVHKKHYCNSRWENTHKSHDFSGLLDKPAGTVSPKIGASLAVMLNAGHPSEVKGQEPKPCNPIAGGKVTDELTVQVKKASTPSGAQERPNGTQLDLQSQKMPPTETDPSHTTCEACKITFSRHETYMVHKQYYCATRHDPQIKRANNKGPANQKAVRPRKRRKAYELANSEQEQMPPMGMPSFLGMPTLGGPYMSKDTLDSFRDHQRYNMIQGLVPKYPEASLTVTKSALVSKCNIISKEETDAPIDLSKKCVPQFGNTPVSPKGLMDYHECVVCKISFNKVEDYLKHKQNFCPGTILQSASTENKSIKKEVPRNTNNLLENPLFEFPAPQIKTEHPNAVPTSDTQASSEEQLIPTKDDLRNMFQTSSTYPSPAKKMRPDEQIWPYYEIKPTDYATGMLVSQSERRQSPNEGSEGEKDQPMPDGSHLSTDDPENQSQSSSLKDNVEIEEKMEDAENKHESPTPESRLDDPINSKDVTTQMPSIKTEEVSTSLKKALTGSIANSSNVKYCRPCDIQFNNLSNFITHKKFYCSSQTAEHVK
Protein: Protein-lysine N-methyltransferase EFM1 (EC 2.1.1.-) (Elongation factor methyltransferase 1) (P38732)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: S-adenosyl-L-methionine-dependent protein-lysine N-methyltransferase that monomethylates elongation factor 1-alpha (TEF1/TEF2) at 'Lys-30'.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Protein-lysine N-methyltransferase EFM4
- Protein-lysine N-methyltransferase EFM5
- Protein-lysine N-methyltransferase EFM2
- Protein-lysine N-methyltransferase EFM6
- Protein N-terminal and lysine N-methyltransferase EFM7
- Cytochrome c lysine N-methyltransferase 1
- Protein-lysine N-methyltransferase EFM3
- Potential protein lysine methyltransferase SET6
Sequence:
MITQTELDNCLQWAQNNGAFIDPKISFRITEDAGVSAFVNEKFSPKPDQALIRVPETLLITSQQALSEFSQAANERSLLNSVTQLYLSKLKFGTDAVHLKSFYKPYLDVLPLHLPQPYFWSTDEVMNLHGTDVYLTMRDTLNKLVKEWRMLFQALSIEHSSQDKQFLSLFQENKDSAVVPLEQFCAHINGCKLEDSEWNSFVAYLWSYCIFNSRAFPRVILGRAGTDRTNLNEGFLYPIVDLLNHKNDVPVRWEMNEQNELCFMSQTTTFSAQDELFNNYGNISNEKCLLNYGFWDSSNKFDFSRLTLKLPSTLVSGLPVDFNKSGNFVTDDGETTILQFSLKISEPLPPVLLALFAYLSKLKSEETPTVRSVLEGIDQLTSVVSQRLLFYKNFKIKTSSTQKLRPHVIKLIKLYYQDNKKILNATTEKLSVLQKKIYSNNKEFSLSFKTIFKNDKIFANSLLLVFGAINYEDLITKDCLNDALLLWIVKLINDKSNNQGGFIKQTFKEVSDSIVIEKEDVMEFLPFYKKYFPNLSERIPEIYSVGDWGIRQFIVADTAIDRLVWIRKSNKEPIFLMKKAYDLQI