wanglab/gogpt-training-data huggingface dataset:
Protein: Seripauperin-5 (P43575)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Seripauperin-2
- Seripauperin-7
- Seripauperin-3
- Seripauperin-24
- Seripauperin-15
- Seripauperin-12
- Probable electron transfer flavoprotein subunit alpha, mitochondrial
- Probable electron transfer flavoprotein subunit beta
Sequence:
MVKLTSIAAGVAAIAAGASAAATTTLSQSDERVNLVELGVYVSDIRAHLAEYYSFQAAHPTETYPVEIAEAVFNYGDFTTMLTGIPADQVTRVITGVPWYSSRLKPAISSALSADGIYTIAN
Protein: C2 calcium-dependent domain-containing protein 4A (Zgc:162595 protein) (A3KNW2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MWVVEKIRVSVERTNLPLPITEYSFKLGDIMFGDKSSIDKAKKVLLCPNIITPDTIPEFCIPPKISSPMEGKNIELGRQTPCIRVSPCEKGSPKREIVSRELTNNPIIQVESVDDGPYDNGCSDEETTNADPQSQAALSLPHLAKAQTCYGFCTLLESPHTRRKESLFHNDPNSSGIPLVLPRSRSSTCSKSSLSASPLLPSSYSPSSFSLNSLTSRLSPKGFTLHRQGTLDSDTTSSAESSPFSSPLLNRCPQKSSLLKALNHENLLYRNLRKAAMSRNNSLSTDEGSSTDNSPNVMRRASEGLVEPLPCGFGLAPPAIFPMDLVLHRERVMKENLVPVGREGTLRLSAEYCPENQRLRVRLISAEGLYALSVDPKSINCSVSLSLMPGKIQKQRSTVIRKSRNPIFNEDFFFDGITEDDLCQRSLRFKVVNKMSTMKRDYILGSYDLPLTSIVTL
Protein: Zinc finger protein GLI2 (Tax helper protein) (Q0VGT2)
Organism: Mus musculus (Mouse)
Function: Functions as transcription regulator in the hedgehog (Hh) pathway. Functions as transcriptional activator. May also function as transcriptional repressor. Requires STK36 for full transcriptional activator activity. Binds to the DNA sequence 5'-GAACCACCCA-3' which is part of the TRE-2S regulatory element (By similarity). Is involved in the smoothened (SHH) signaling pathway. Required for normal skeleton development.
Subcellular location: Nucleus {ECO:0000269|PubMed:10806483}. Cytoplasm {ECO:0000269|PubMed:10806483}. Cell projection, cilium {ECO:0000269|PubMed:25644602}. Note=STK36 promotes translocation to the nucleus (PubMed:10806483). In keratinocytes, it is sequestered in the cytoplasm by SUFU. In the absence of SUFU, it translocates to the nucleus (PubMed:23034632). {ECO:0000269|PubMed:10806483, ECO:0000269|PubMed:23034632}.
Interaction partners:
- Suppressor of fused homolog
- Kinesin-like protein KIF7
- Zinc finger protein GLI1
- F-box/WD repeat-containing protein 1A
- cAMP-dependent protein kinase catalytic subunit beta
- cAMP-dependent protein kinase catalytic subunit alpha
- Kinesin-like protein KIF3A
- Protein smoothened
- Runt-related transcription factor 2
- Speckle-type POZ protein
Sequence:
METSAPAPALEKKEAKSGLLEDSSFPDPGKKACPLAVAAAVAAHGVPQQLLPAFHAPLPIDMRHQEGRYHYDPHSVHSVHGPPTLSGSPVISDISLIRLSPHPAGPGESPFSAHHPYVNPHMEHYLRSVHSSPTLSMISAARGLSPADVAHEHLKERGLFSLAAPGTNPSDYYHQMTLMASHPTPYGDLLMQSGGAASAPHLHDYLNPVDASRFSSPRVTPRLSRKRALSISPLSDASLDLQRMIRTSPNSLVAYINNSRSSSAASGSYGHLSAGALSPAFTFPHPINPVAYQQILSQQRGLGSAFGHTPPLIQPSPTFLAQQPMTLTSISTMPTQLSSSSSNCLNDANQNKQNSESAVSSTVNPITIHKRSKVKTEAEGLRPASPLGLTQEQLADLKEDLDRDDCKQEAEVVIYETNCHWADCTKEYDTQEQLVHHINNEHIHGEKKEFVCRWQACTREQKPFKAQYMLVVHMRRHTGEKPHKCTFEGCSKAYSRLENLKTHLRSHTGEKPYVCEHEGCNKAFSNASDRAKHQNRTHSNEKPYICKIPGCTKRYTDPSSLRKHVKTVHGPDAHVTKKQRNDVHVRAPLLKENGDNEASAEPGGRGPEESVEASSTSHTVEDCLHIKAIKTESSGLCQSSPGAQSSCSSEPSPLGSAPNNDSGMEMPGTGPGSLGDLTALADTCPGADTSALAAPSTGGLQLRKHMSTVHRFEQLKREKLKSLKDSCSWAGPAPHTRNTKLPPLPVNGSVLENFNNTGGGGPAGLLPSQRLPELTEVTMLSQLQERRDSSTSTMSSAYTVSRRSSGISPYFSSRRSSEASPLGGLRPHNASSADSYDPISTDASRRSSEASQCSGGGPGLLNLTPAQQYNLRAKYAAATGGPPPTPLPGLDRVSLRTRLALLDAPERALPGACPHPLGPRRGSDGPTYSHGHGHGYAGAAPAFPHEGPNSSTRRASDPVRRPDPLILPRVQRFHSTHNMNPGSLPPCADRRGLHVQSHPSVDSNLTRNAYSPRPPSINENVVMEAVAAGVDGPGLECDLGLVEDELVLPDDVVQYIKAHTGGTLDDGIRQGYPTEGTGFPENSKLPSPGLQGHRRLAAADSNMGPSAPGLGGCQLSYSPSSNLNKSNMPVQWNEVSSGTVDALPTQVKPPPFPHSNLAVVQQKPAFGQYPGYNPQSVQSSSGGLDSTQPHLQLRGAPSASRGSYTQQPRQPAAGSQCLGMSAAMSPQASYSQAHPQLSPNIVSGSLNQFSPSCSNMAAKPSHLGLPQQMEVVPNATIMNGHQREHGVPNSSLAAVSQPHPVLSYPQQDSYQQGSNLLSSHQPGFMESQQNAGFGLMQPRPPLEPNTASRHRGVRSGQQQLYARTTGQAMVTSANQETAEAMPKGPAGTMVSLAPQPSQDTGRAQDQNTLYYYGQIHMYEQNGGCPAVQPQPPQPQACSDSIQPEPLPSPGVNQVSSTVDSQLLEPPQIDFDAIMDDGDHSSLFSGALSPTLLHNLSQNSSRLTTPRNSLTLPSIPAGISNMAVGDMSSMLTSLAEESKFLNMMT
Protein: SAGA-associated factor 29 (rSGF29) (Coiled-coil domain-containing protein 101) (SAGA complex-associated factor 29) (P0C606)
Organism: Rattus norvegicus (Rat)
Function: Chromatin reader component of some histone acetyltransferase (HAT) SAGA-type complexes like the TFTC-HAT, ATAC or STAGA complexes (By similarity). SGF29 specifically recognizes and binds methylated 'Lys-4' of histone H3 (H3K4me), with a preference for trimethylated form (H3K4me3) (By similarity). In the SAGA-type complexes, SGF29 is required to recruit complexes to H3K4me (By similarity). Involved in the response to endoplasmic reticulum (ER) stress by recruiting the SAGA complex to H3K4me, thereby promoting histone H3 acetylation and cell survival (By similarity). Also binds non-histone proteins that are methylated on Lys residues: specifically recognizes and binds CGAS monomethylated on 'Lys-491' (By similarity). May be involved in MYC-mediated oncogenic transformation.
Subcellular location: Nucleus {ECO:0000269|PubMed:17334388}.
Interaction partners:
- Transcriptional adapter 3
- Transcription initiation factor TFIID subunit 12
- Transcription initiation factor TFIID subunit 10
- ZZ-type zinc finger-containing protein 3
- Transcription initiation factor TFIID subunit 9B
- Cysteine-rich protein 2-binding protein
- SPT3 homolog, SAGA and STAGA complex component
- Transcriptional adapter 2-alpha
- Transcription factor SPT20 homolog
- Histone acetyltransferase
Sequence:
MALVSADSRIAELLTELHQLIKQTQEERSRSEHNLVNIQKTHERMQTENKISPYYRTKLRGLYTTAKADAEAECNILRKALDKIAEIKSLLEERRIAAKIAGLYNDSEPPRKTMRRGVLMTLLQQSAMTLPLWIGKPGDKPPPLCGAIPASGDYVAKPGDKVAARVKAVEGDEQWILAEVVSYSHATNKYEVDDIDEEGKERHTLSRRRIIPLPQWKANPETDPEALFQKEQLVLALYPQTTCFYRALIHTPPQRPQDDYSVLFEDTSYADGYSPPLNVAQRYVVACKEPKKK
Protein: Galanin receptor type 3 (GAL3-R) (GALR-3) (O60755)
Organism: Homo sapiens (Human)
Function: Receptor for the hormone galanin. Receptor for the hormone spexin-1.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Galanin peptides
- Galanin receptor type 2
- Galanin receptor type 1
- 2-amino-3-ketobutyrate coenzyme A ligase, mitochondrial
- Spexin
- Galanin-like peptide
- Urotensin-2 receptor
- Somatostatin receptor type 3
- Melanin-concentrating hormone receptor 1
Sequence:
MADAQNISLDSPGSVGAVAVPVVFALIFLLGTVGNGLVLAVLLQPGPSAWQEPGSTTDLFILNLAVADLCFILCCVPFQATIYTLDAWLFGALVCKAVHLLIYLTMYASSFTLAAVSVDRYLAVRHPLRSRALRTPRNARAAVGLVWLLAALFSAPYLSYYGTVRYGALELCVPAWEDARRRALDVATFAAGYLLPVAVVSLAYGRTLRFLWAAVGPAGAAAAEARRRATGRAGRAMLAVAALYALCWGPHHALILCFWYGRFAFSPATYACRLASHCLAYANSCLNPLVYALASRHFRARFRRLWPCGRRRRHRARRALRRVRPASSGPPGCPGDARPSGRLLAGGGQGPEPREGPVHGGEAARGPE
Protein: Nicotinic acetylcholine receptor alpha7, isoform A (Nicotinic acetylcholine receptor alpha7, isoform D) (Nicotinic acetylcholine receptor alpha7, isoform F) (Q9VWI9)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Postsynaptic cell membrane {ECO:0000256|ARBA:ARBA00034104}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00034104}.
Interaction partners:
Sequence:
MKKPSRSRPDNPSCPGQDRTRSMSFPQPHSLPEATANGGRMLVYGLGLLIMIPACAAGPHEKRLLHALLDNYNSLERPVVNESDPLQLSFGLTLMQIIDVDEKNQLLITNIWLKLEWNDMNLRWNSSEFGGVRDLRIPPHRLWKPDVLMYNSADEGFDGTYATNVVVRNNGSCLYVPPGIFKSTCKIDITWFPFDDQRCEMKFGSWTYDGFQLDLQLQDEAGGDISSFITNGEWDLLGVPGKRNEIYYNCCPEPYIDITFAILIRRKTLYYFFNLIVPCVLIASMALLGFTLPPDSGEKLSLGVTILLSLTVFLNMVAETMPATSDAVPLLGTYFNCIMFMVASSVVSTILILNYHHRNPDTHEMSEWIRVIFLYWLPCILRMQRPGQVGYECPPPPSSSSSSASGEKKQQIQNVELKERSSKSLLANVLDIDDDFRCNHRCASATLPHQPTYYRTMYRQGDDGSVGPVGPAGPVVDGRLHEAISHTCLTSSAEYELALILKELRWITEQLKKEDETSDITRDWKFAAMVVDRLCLIIFTLFTIIATLAVLFSAPHFIFP
Protein: Presenilin hop-1 (O02100)
Organism: Caenorhabditis elegans
Function: Probable catalytic subunit of the gamma-secretase complex, an endoprotease complex that catalyzes the intramembrane cleavage of integral membrane proteins such as Notch receptors (lin-12 or glp-1). Probably works redundantly of lin-12, which provides more presenilin function.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Nicastrin
- Gamma-secretase subunit aph-1
- Gamma-secretase subunit pen-2
- Protein lin-12
- Beta-catenin-like protein hmp-2
- Beta-catenin/armadillo-related protein 1
- cAMP-dependent protein kinase catalytic subunit
- Presenilin spe-4
- Presenilin sel-12
- Armadillo repeat-containing protein wrm-1
Sequence:
MPRTKRVYSGKTITGVLYPVAICMLFVAINVKLSQPEQQEQSKVVYGLFHSYDTADSGTITLYLIGFLILTTSLGVFCYQMKFYKAIKVYVLANSIGILLVYSVFHFQRIAEAQSIPVSVPTFFFLILQFGGLGITCLHWKSHRRLHQFYLIMLAGLTAIFILNILPDWTVWMALTAISFWDIVAVLTPCGPLKMLVETANRRGDDKFPAILYNSSSYVNEVDSPDTTRSNSTPLTEFNNSSSSRLLESDSLLRPPVIPRQIREVREVEGTIRLGMGDFVFYSLMLGNTVQTCPLPTVVACFVSNLVGLTITLPIVTLSQTALPALPFPLAIAAIFYFSSHIALTPFTDLCTSQLILI
Protein: HR-like lesion-inducing protein-like protein (Q8GYI3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- HR-like lesion-inducing protein
- At3g23190
- At2g32380
- T12C22.21 protein
Sequence:
MKMSISKVKSMFCTTLTKSMPAIAFFGRMAFSFVFFITAIQDYADHYGGGAGGPLEKTMGPAVNMLSKYGSKALTFYFGMQVVAFDVRLIEFALISAKATAALWFIFGQSIPAYFLLATQIFSTVIPFPTNLNDFTQNLTLIGALLYYIGLKHTVDNLDDEEKNKQTEG
Protein: Zealexin A1 synthase (EC 1.14.14.160) (Cytochrome P450 71Z18) (B4FVP3)
Organism: Zea mays (Maize)
Function: Involved in production of the antifungal phytoalexin zealexin A1. The enzyme sequentially oxidizes(S)-beta-macrocarpene via alcohol and aldehyde intermediates to form zealexin A1, a maize phytoalexin that provides biochemical protection against fungal infection.
Subcellular location: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MEDKVLIAVGTVAVVAVLSKLKSAVTKPKLNLPPGPWTLPLIGSIHHIVSNPLPYRAMRELAHKHGPLMMLWLGEVPTLVVSSPEAAQAITKTHDVSFADRHINSTVDILTFNGMDMVFGSYGEQWRQLRKLSVLELLSAARVQSFQRIREEEVARFMRSLAASASAGATVDLSKMISSFINDTFVRESIGSRCKYQDEYLAALDTAIRVAAELSVGNIFPSSRVLQSLSTARRKAIASRDEMARILGQIIRETKESMDQGDKTSNESMISVLLRLQKDAGLPIELTDNVVMALMFDLFGAGSDTSSTTLTWCMTELVRYPATMAKAQAEVREAFKGKTTITEDDLSTANLRYLKLVVKEALRLHCPVPLLLPRKCREACQVMGYDIPKGTCVFVNVWAICRDPRYWEDAEEFKPERFENSNLDYKGTYYEYLPFGSGRRMCPGANLGVANLELALASLLYHFDWKLPSGQEPKDVDVWEAAGLVAKKNIGLVLHPVSHIAPVNA
Protein: MKIAA1697 protein (Q5DTV6)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
SDNLHERLKILLQQTLLTAYTNVSRGLFEQHKLIYSFMLCVDIMREHEQLTEAEWNFFLRGSAGMEKERPPKPEAPWLPIQMWFSCCDLEESFPIFEGLTKHILLRPISIKLGSFETYINPPVWEGYPKQRHEEEKDHVWGLDFSSFHKLILVKCCKEEKVVFALTDFVIENLGKQFIETPPVDLATLYQDMSNSTPLVFILSTGSDPMGAFQRFARESGYAERVQSISLGQGQGPIAEKMIKDAMKTGNWVFLQNCHLAVSWMLAMEELIKTFTDPNQTIKDTFRLFLSSMPCSTFPVTVLQNSVKVTNEPPKGLRANIRRAFTEMTPSFFEENILGMKWRKLIFGICFFHAIIQERKKFGPLGWNICYEFNDSDRECALLNLNLYCHEGKIPWDALIYITGEITYGGRVTDTWDQRCLRTVLKRFFSPETLDDDYTYSDSGIYFAPLADSLQDFKEYIEDLPLIDDPEIFGMHENANLVFQYKETNTLITTILEVQPRSSSGGQGKSNDEIVQELVASIQTRVPESLQMEGASESLFVKDPQGRLNSLTTVLGQEVDRFNNLLKLIHISLETLNKAIAGLVVMSEEMEKVYQSFLNNQVPSLWSNTAYPSLKPLGSWVKDLILRTAFVDLWLKRGQPKSFWISGFFFPQGFLTGTLQNHARKYNLPIDELSFKYNMIPVYRDQAAVIESAKDIQFGTELPMDKELPSPEDGVLVHGMFMDASRWDDKDMVIEDALPGQMNPMLPVVHFEPKQNYEPVHTLYHSPLYKTGARAGTLSTTGHSTNFVVTVLLPSKRISDYWISKGSALLCQLSE
Protein: Metalloreductase STEAP3 (EC 1.16.1.-) (Dudulin-2) (Protein nm1054) (Six-transmembrane epithelial antigen of prostate 3) (Tumor suppressor-activated pathway protein 6) (Q8CI59)
Organism: Mus musculus (Mouse)
Function: Endosomal ferrireductase required for efficient transferrin-dependent iron uptake in erythroid cells. Participates in erythroid iron homeostasis by reducing Fe(3+) to Fe(2+). Also mediates reduction of Cu(2+) to Cu(1+), suggesting that it participates in copper homeostasis. Uses NADP(+) as acceptor. May play a role downstream of p53/TP53 to interface apoptosis and cell cycle progression. Indirectly involved in exosome secretion by facilitating the secretion of proteins such as TCTP.
Subcellular location: Endosome membrane {ECO:0000269|PubMed:16227996, ECO:0000269|PubMed:18955558}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- BCL2/adenovirus E1B 19 kDa protein-interacting protein 3-like
- Natural resistance-associated macrophage protein 2
- Plasma membrane ascorbate-dependent reductase CYBRD1
- Transferrin receptor protein 1
- Ferroportin
Sequence:
MSGEMDKPLISRRLVDSDGSLAEVPKEAPKVGILGSGDFARSLATRLVGSGFSVVVGSRNPKRTAGLFPSLAQVTFQEEAVSSPEVIFVAVFREHYSSLCSLADQLAGKILVDVSNPTEKEHLQHRQSNAEYLASLFPACTVVKAFNVISAWALQAGPRDGNRQVLICSDQPEAKRTISEMARAMGFTPLDMGSLASAREVEAIPLRLLPSWKVPTLLALGLFVCFYTYNFIRDVLQPYIRKDENKFYKMPLSVVNTTLPCVAYVLLSLVYLPGVLAAALQLRRGTKYQRFPDWLDHWLQHRKQIGLLSFFFAMLHALYSFCLPLRRSHRYDLVNLAVKQVLANKSRLWVEEEVWRMEIYLSLGVLALGMLSLLAVTSLPSIANSLNWKEFSFVQSTLGFVALILSTMHTLTYGWTRAFEENHYKFYLPPTFTLTLLLPCVIILAKGLFLLPCLSRRLTKIRRGWEKDGAVKFMLPGDHTQGEKTSHV
Protein: Spleen focus forming virus (SFFV) proviral integration oncogene spi1 like (Q0P4E9)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MESCVISPLSEEIIPYEHEARPIYDFYPYLSTDPETHPESGCEYSSVYGHHSEFEPPPGSHFTELHTSTYRYGDMEAFHPGVDAAMGTILPVVPPQYTYITHPRYQRSPVPHCSTDEEEPGGRSPPFEVSEGEEDHDGHPSTSSTLSGNKRKVRLYQFLLDLLQDGDMRDCIWWVDRERGVFQFSSKHKETAVSSLTLRTQCILPIIAIFTDNLKRNLRDMTCMLFECFTMDNKVKHCIFVCFNWSG
Protein: 26S proteasome regulatory subunit (A6MUT2)
Organism: Gossypium hirsutum (Upland cotton) (Gossypium mexicanum)
Interaction partners:
Sequence:
TGLSEAIALLEPLTSDVVDFVRQGALIAMAMVMVQTNEASDSRVGTFRRQLEKIILDKHEDTMSKMGAILASGILDAGGRNVTIRLLSKTKHDKVTAVVGLAVFSQFWYWYPLIYFVSLSFSPTAFIGLNYDLKVPKFEFLSHAKPSPFEYPKPTTVPTTTSAVKLPTAVLSTSAKAKARAKKEAEQKANAEKSTGAESSAAANTGKGKSSSEKDGEAMQVDSPPEKKSEPEPSFEILTNPARVVPAQEKFIKFLEDSRYVPVKLAPSGFVLLRDLCPNEPEVLSLTDAPTSTASPAGGSTAAAGQQSSSAMAVDDEPQPP
Protein: Ferruginol synthase 1 (RoFS1) (EC 1.14.14.175) (11-oxomiltiradiene synthase) (EC 1.14.14.-) (Cytochrome P450 76AH22) (Ferruginol monooxygenase) (11-hydroxyferruginol synthase) (EC 1.14.14.60) (Miltiradiene oxidase) (A0A0C5Q4Y6)
Organism: Rosmarinus officinalis (Rosemary) (Salvia rosmarinus)
Function: Monooxygenase involved in the biosynthesis of labdane-related diterpenes natural products. Catalyzes the oxidation of abietatriene to produce ferruginol. Catalyzes the oxidation of ferruginol at C-12 to produce 11-hydroxyferruginol. Ferruginol and 11-hydroxyferruginol are intermediates in the biosynthesis of carnosate, a potent antioxidant. May also convert miltiradiene into 11-oxomiltiradiene (By similarity).
Subcellular location: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MDSFPLLAALFFILAATWFISFRRPRNLPPGPFPYPIVGNMLQLGTQPHETFAKLSKKYGPLMSIHLGSLYTVIVSSPEMAKEIMHKYGQVFSGRTVAQAVHACGHDKISMGFLPVGGEWRDMRKICKEQMFSHQSMEDSQWLRKQKLQQLLEYAQKCSERGRAIDIREAAFITTLNLMSATLFSMQATEFDSKVTMEFKEIIEGVASIVGVPNFADYFPILRPFDPQGVKRRADVYFGRLLAIIEGFLNERVESRRTNPNAPKKDDFLETLVDTLQTNDNKLKTDHLTHLMLDLFVGGSETSTTEIEWIMWELLANPEKMAKMKAELKSVMGEEKVVDESQMPRLPYLQAVVKESMRLHPPGPLLLPRKAESDQVVNGYLIPKGAQVLINAWAIGRDHSIWKNPDSFEPERFLDQKIDFKGTDYELIPFGSGRRVCPGMPLANRILHTVTATLVHNFDWKLERPEASDAHRGVLFGFAVRRAVPLKIVPFKV
Protein: Proteasome subunit alpha (20S proteasome alpha subunit) (Proteasome core protein PsmA) (Q60177)
Organism: Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
Function: Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation. The M.jannaschii proteasome is able to cleave oligopeptides after Glu, Asp, Tyr, Phe, Trp, slightly after Arg, but not after Ala. Thus, displays caspase-like and chymotrypsin-like activities and low level of trypsin-like activity.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00289}.
Interaction partners:
- Proteasome subunit beta
- Proteasome-activating nucleotidase
- Large ribosomal subunit protein eL40
- Uncharacterized protein MJ0106
- Cell division cycle protein 48 homolog MJ1156
- Uncharacterized protein MJ0639
- Large ribosomal subunit protein eL15
- Ribosome maturation protein SDO1 homolog
- Uncharacterized protein MJ1210
- Ribose 1,5-bisphosphate isomerase
Sequence:
MQMVPPSAYDRAITVFSPEGRLYQVEYAREAVRRGTTAIGIACKDGVVLAVDRRITSKLVKIRSIEKIFQIDDHVAAATSGLVADARVLIDRARLEAQIYRLTYGEEISIEMLAKKICDIKQAYTQHGGVRPFGVSLLIAGIDKNEARLFETDPSGALIEYKATAIGSGRPVVMELLEKEYRDDITLDEGLELAITALTKANEDIKPENVDVCIITVKDAQFKKIPVEEIKKLIEKVKKKLNEENKKEEENREETKEKQEE
Protein: Transglutaminase 6 (Q8BM11)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MAGVRITKVDWQHSKNGAAHHTQDYPCSELVVRRGQLFSLTLDLSRVLDSEEALIFTVETGPHASEALHTKAVFQTAELEIGDTWTAAKEEQTENTITVSLSSPSNAVIGRYLLSVRPSSRRKHSDRKLGQFILLFNPWCPEDDVFLDSEEERQEYVLNDSGVIFRGVEKHIRAQGWNYGQFEEDILNICLSILDRSPSHQEDPATDVSHRHDPVYVTRIISAMVNSNNDRGVVQGQWQGKYGGGTNPLNWRGSVAILQKWFKGRYKPVKYGQCWVFAGVMCTVLRCLGIATRVVSNFNSAHDTDGNLSVDKYVDSYGRTLEDLTEDSMWNFHVWNESWFARQDLGPSYDGWQVLDATPQEESEGMFRCGPASVTAIREGDVHLAHDGPFVFAEVNADYITWLWHEDKRRERVYSDTKKIGRCISTKAVGSDSRVDITGLYKYPEGSRKERQVYSKAVKKLLSVEAWGRRRRIRRASVRGVWRDDLLEPVTKPSITGKFKVLEPPVLGQDLKLALCLTNLTARAQRVRVNVSGATILYTRKPVAEILRESHTVKLGPLEEKKIPVTISYSQYKGDLTEDKKILLAAMCLVSKGEKLLVEKDITLEDFITIKVLGPAVVGVTVTVEVLVINPLSESVKDCVLMVEGSGLLQGQLSIEVPSLQPQEKALIQFNITPSKSGPRQLQVDLVSSQFPDIKGFVIIHVATAK
Protein: Replication origin-binding protein (OBP) (OriBP) (P10193)
Organism: Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1)
Function: Functions as a docking protein to recruit essential components of the viral replication machinery to viral DNA origins. In the presence of the major DNA-binding protein, opens dsDNA leading to a conformational change in the origin that facilitates DNA unwinding and subsequent replication.
Subcellular location: Host nucleus {ECO:0000305}.
Interaction partners:
Sequence:
MPFVGGAESGDPLGAGRPIGDDECEQYTSSVSLARMLYGGDLAEWVPRVHPKTTIERQQHGPVTFPNASAPTARCVTVVRAPMGSGKTTALIRWLREAIHSPDTSVLVVSCRRSFTQTLATRFAESGLVDFVTYFSSTNYIMNDRPFHRLIVQVESLHRVGPNLLNNYDVLVLDEVMSTLGQLYSPTMQQLGRVDALMLRLLRICPRIIAMDATANAQLVDFLCGLRGEKNVHVVVGEYAMPGFSARRCLFLPRLGTELLQAALRPPGPPSGPSPDASPEARGATFFGELEARLGGGDNICIFSSTVSFAEIVARFCRQFTDRVLLLHSLTPLGDVTTWGQYRVVIYTTVVTVGLSFDPLHFDGMFAYVKPMNYGPDMVSVYQSLGRVRTLRKGELLIYMDGSGARSEPVFTPMLLNHVVSSCGQWPAQFSQVTNLLCRRFKGRCDASACDTSLGRGSRIYNKFRYKHYFERCTLACLSDSLNILHMLLTLNCIRVRFWGHDDTLTPKDFCLFLRGVHFDALRAQRDLRELRCRDPEASLPAQAAETEEVGLFVEKYLRSDVAPAEIVALMRNLNSLMGRTRFIYLALLEACLRVPMATRSSAIFRRIYDHYATGVIPTINVTGELELVALPPTLNVTPVWELLCLCSTMAARLHWDSAAGGSGRTFGPDDVLDLLTPHYDRYMQLVFELGHCNVTDGLLLSEEAVKRVADALSGCPPRGSVSETDHAVALFKIIWGELFGVQMAKSTQTFPGAGRVKNLTKQTIVGLLDAHHIDHSACRTHRQLYALLMAHKREFAGARFKLRVPAWGRCLRTHSSSANPNADIILEAALSELPTEAWPMMQGAVNFSTL
Protein: Prolyl hydroxylase EGLN3 (EC 1.14.11.-) (Egl nine homolog 3) (EC 1.14.11.29) (Hypoxia-inducible factor prolyl hydroxylase 3) (HIF-PH3) (HIF-prolyl hydroxylase 3) (HPH-3) (Prolyl hydroxylase domain-containing protein 3) (PHD3) (SM-20) (Q62630)
Organism: Rattus norvegicus (Rat)
Function: Prolyl hydroxylase that mediates hydroxylation of proline residues in target proteins, such as PKM, TELO2, ATF4 and HIF1A (By similarity). Target proteins are preferentially recognized via a LXXLAP motif (By similarity). Cellular oxygen sensor that catalyzes, under normoxic conditions, the post-translational formation of 4-hydroxyproline in hypoxia-inducible factor (HIF) alpha proteins. Hydroxylates a specific proline found in each of the oxygen-dependent degradation (ODD) domains (N-terminal, NODD, and C-terminal, CODD) of HIF1A (By similarity). Also hydroxylates HIF2A (By similarity). Has a preference for the CODD site for both HIF1A and HIF2A (By similarity). Hydroxylation on the NODD site by EGLN3 appears to require prior hydroxylation on the CODD site (By similarity). Hydroxylated HIFs are then targeted for proteasomal degradation via the von Hippel-Lindau ubiquitination complex (By similarity). Under hypoxic conditions, the hydroxylation reaction is attenuated allowing HIFs to escape degradation resulting in their translocation to the nucleus, heterodimerization with HIF1B, and increased expression of hypoxy-inducible genes (By similarity). ELGN3 is the most important isozyme in limiting physiological activation of HIFs (particularly HIF2A) in hypoxia (By similarity). Also hydroxylates PKM in hypoxia, limiting glycolysis (By similarity). Under normoxia, hydroxylates and regulates the stability of ADRB2 (By similarity). Regulator of cardiomyocyte and neuronal apoptosis (By similarity). In cardiomyocytes, inhibits the anti-apoptotic effect of BCL2 by disrupting the BAX-BCL2 complex. In neurons, has a NGF-induced proapoptotic effect, probably through regulating CASP3 activity. Also essential for hypoxic regulation of neutrophilic inflammation (By similarity). Plays a crucial role in DNA damage response (DDR) by hydroxylating TELO2, promoting its interaction with ATR which is required for activation of the ATR/CHK1/p53 pathway (By similarity). Also mediates hydroxylation of ATF4, leading to decreased protein stability of ATF4 (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9H6Z9}. Cytoplasm {ECO:0000269|PubMed:16407229}. Note=Colocalizes with WDR83 in the cytoplasm. {ECO:0000269|PubMed:16407229}.
Interaction partners:
- Endothelial PAS domain-containing protein 1
- Hypoxia-inducible factor 1-alpha
- Hypoxia-inducible factor 3-alpha
- Protein kinase C beta type
- Protein kinase C gamma type
- von Hippel-Lindau disease tumor suppressor
- Aryl hydrocarbon receptor nuclear translocator
- Egl nine homolog 1
- WD repeat domain-containing protein 83
- Cullin 2
Sequence:
MPLGHIMRLDLEKIALEYIVPCLHEVGFCYLDNFLGEVVGDCVLERVKQLHYNGALRDGQLAGPRAGVSKRHLRGDQITWIGGNEEGCEAINFLLSLIDRLVLYCGSRLGKYYVKERSKAMVACYPGNGTGYVRHVDNPNGDGRCITCIYYLNKNWDAKLHGGVLRIFPEGKSFVADVEPIFDRLLFSWSDRRNPHEVQPSYATRYAMTVWYFDAEERAEAKKKFRNLTRKTESALAKD
Protein: Timeout (Q8INH7)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Protein TIPIN homolog
- Claspin
- Chromosome transmission fidelity 4
- DNA replication licensing factor Mcm2
- CDC45L
- DNA polymerase epsilon catalytic subunit 1
- Replication protein A 70 kDa DNA-binding subunit
- DNA replication licensing factor Mcm5
- DNA replication licensing factor Mcm7
- DNA replication licensing factor MCM4
Sequence:
MSILLADIDATCAALGYSDGQKYQAEPDAAEGLKHLIWILRRDLDNHEYRRHLGRSKVLQTDLVYMLPDYVHHEELSDLLIRLLVILTNPTLLLYREGAPKDNHGRKVFMELIDILQGYKAAFAKDKVWSALFEKLKQALEIAFAIRSEEQNLLIERILVLVRNVLQVPANPEAECRADNDASLHDQVIWALHQTGMLDLVLFVISSPDEEQFHLHGLEIVCLLFREQSAESLADASLQRSLSEKQRDQQELLAARRRERARRQARPPPGRHSRFGGTYVIRNMKSVSDRDVICHQALERVSSIDFDREKQQQKRSHRHIQEEAQVTRRSAFTVRLCLREYCIEVLRSAYNTLVRQVRRVLERNAGSSSHDDSYLLWAIRFFMEFNRLSGLQLQLVSESLSVQCFHWVLTRMQHDMDMIVSDKKQARLWAKRLHVALLTFRELLQSLLALQKLKDDNNARALFDMLLNNVCYVLEYRETVLHLLMNYNEAHSTKVFLRDVVETANVFIKMMERFCQDSVVVQDKKRGRGASRKKKQAATKSKPPAAPQPTEEELSSKWAELATEVCSLLSTELEMPEDEQPLPFDAASEKSIDDQREDCMIRINKLLRSEKLDQAIALLRAAREVWPENEVFGAISAAPEDELLLLREIFMSNITTVESEDKENEKDQKQDEYEDEDDDLDNEEYEEQDNGLTEKTFKFDDFARRLLNPKIVRACTLVLSDWADIPTRSLKAAVTILHRIAYGCKCAGMLFQAKLFRIFQQVFSVERDVHQEELRRLAIFVVRKFVEVAPTNPKIYAELLFYKGIREANELESGYCDAYEAGTKGAWTEEQESELRFLFEENQRNPETDKDVIDWILDNLVDKTRNRRTVLKKLKELGLLFKAPTKRSTKSAQSGKNVWQPEEDDELRSLYDQHRIEPDCLERLVNEFAERRSKQQIIKRMLQIHLIADKSEILPAKKGRGKDKPKKDVEMEGEGDEFDFAEEPMFEDQGYKKPKSKPKKVQKRQMVRTPLDVGTIRALIGQVDSEKYQSAIEWLQECLQDASEDTEEAVEDDDGVPLLPLMENQKNAMEDGDFQKVLVALGMQPPISGMEAYWRIPIYLNSADLILRSKILAGEEVDAEPEDEAADDEDGEEAEESDEEEDFLEKHSRQRKENIATQQQRKLDSLMFNQSDDETEQRAPPKAKDKPKASEKKAKRKVKGKAKESKDCNDDGTDKAELEKPNTDDLFNQLRAKRATKIKLSDMALNESTNAAQEADDDAFNFNSEDYRARLLELEDEEQNSKDADENGGDKENITNKSLQRARRVNVIDSDSDNDDDGALPADKTNKRPRSDDDGDSGHMDANAEEDSDEEANFLARKKPAKVDGEPAKRRRLAIIDDDDEDDF