wanglab/gogpt-training-data huggingface dataset:
Protein: Dynein axonemal assembly factor 11 (DNAAF11) (Leucine-rich repeat-containing protein 6) (Leucine-rich testis-specific protein) (TbLRTP) (Phosphatase) (Protein tilB homolog) (Q9NJE9)
Organism: Trypanosoma brucei brucei
Function: Involved in the regulation of the cell cycle; is required for the basal body replication and new flagellum biogenesis.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:15831481}. Cytoplasm, cytoskeleton, flagellum basal body {ECO:0000269|PubMed:15831481}.
Interaction partners:
Sequence:
MGRITTDLLRRRAEHNEGCLSNLKEVALHQQDIERIELIGDACRELEILYLCNNYISRIEGLQHLKYLKYLNLAVNNITYIEGLEGCEALERLDLTLNFVADVTCVERLRANAFLDQLHLTGNPCTKVAGYRAYVVHALPQLRELDGEEVIKTERLEARQSKDDISVAVNEEALRLQKRSVSSQRWLHEALTAFPPRYNEKGERLYGHTPEERLQMLREKEEEERRKREEQRERERSSQFGAIREELERKPQRLTAEEEIAKHGRLLLRNEPKLPFTLDEEADDGEAVVLTVKVPRFLSTTLIDVQVEVNYIRVFVKEKLIQVPLSQEVAPSGVNVQRSSVNGELRIRIPYAPHVLQEVSEARRRRQRLLGLLSDDKNEDGTG
Protein: Homocysteine-responsive endoplasmic reticulum-resident ubiquitin-like domain member 1 protein (Q9JJK5)
Organism: Mus musculus (Mouse)
Function: Component of the endoplasmic reticulum quality control (ERQC) system also called ER-associated degradation (ERAD) involved in ubiquitin-dependent degradation of misfolded endoplasmic reticulum proteins. Binds to ubiquilins and this interaction is required for efficient degradation of CD3D via the ERAD pathway.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- E3 ubiquitin-protein ligase synoviolin
- DnaJ homolog subfamily B member 9
- X-box-binding protein 1
- ER degradation-enhancing alpha-mannosidase-like protein 1
- Transitional endoplasmic reticulum ATPase
- E3 ubiquitin-protein ligase AMFR
- Endoplasmic reticulum chaperone BiP
Sequence:
MEPEPQPEPVTLLVKSPNQRHRDLELSGDRSWSVSRLKAHLSRVYPERPRPEDQRLIYSGKLLLDHQCLQDLLPKQEKRHVLHLVCNVKNPSKMPETSTKGAESTEQPDNSNQTQHPGDSSSDGLRQREVLRNLSPSGWENISRPEAVQQTFQGLGPGFSGYTTYGWLQLSWFQQIYARQYYMQYLAATAASGTFVPTPSAQEIPVVSTPAPAPIHNQFPAENQPANQNAAAQAVVNPGANQNLRMNAQGGPLVEEDDEINRDWLDWTYSAATFSVFLSILYFYSSLSRFLMVMGATVVMYLHHVGWFPFRQRPVQNFPDDGGPRDAANQDPNNNLQGGMDPEMEDPNRLPPDREVLDPEHTSPSFMSTAWLVFKTFFASLLPEGPPALAN
Protein: PSI (Q7JPS0)
Organism: Drosophila sp. (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSDFQQQGINQSQALAQAIQRAKQIAAKIQPSQQGGGTAGPSPPSSGGGPGFKRINDDGDSGPESKRSLGSPEYANNSSNMSSGSGGGGGGGGGPGGASITQAIAQAAAVAARLAASAGTSCEEQIRLPESVAGAFMGRSSNDTITHIQAESGVKVQVMQDQDRVIMLRGQRDTVTKGREMIQNMANRAGGGQVEVLLTINMPPPGPSGYPPYQEIMIPGAKVGLVIGKGGDTIKQLQEKTGAKMIIIQDGPNQELIKPLRISGEAQKIEHAKQMVLDLIAQKDAQGQQQGGRGGGGGGGGPGMGFNNFNNGNGGESTEVFVPKIAVGVVIGKGGDMIRKIQTECGCKLQFIQGKNDEMGDRRCVIQGTRQQVDDAKRTIDGLIENVMQRNGMNRNGNGGGGGPGGDSGNSNYGYGYGVNHAQGGREEITFLVPASKCGIVIGRGGETIKLINQQSGAHTEMDRNASNPPNEKLFKSKGTTDQVEAARQMISEKINMELNVISRKPIGGGPGGGGGNSGGGQNNSHHNQQQGGYGGQNQMQGGDPNSGAGYQQQPWGGPYGQQGWDPSGQQQQMAMANQGGSAAGGASGGQDYSAQWIEYYKQMGCHREAEMIEQQMKAKQAGGSSGPVQQQQPQQQQQSQQQTGGAGAGGADYSAQWAEYYRSVGKIEEAEAIEKTLKNKQNGSGGQSSTPNPSQGGSGQQQPNPAAAAAAAAAAAAAAGGYGQSMTPTQYAQYSQYYAAAAAAGGQPQGAPQPGGGQSGGPPGNYPGNYPGAGYGGYPGAPGQQQQKSHKNDNH
Protein: Vacuolar morphogenesis protein 7 homolog (O74509)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Essential for proper morphogenesis of the vacuole. May exist as structural reinforcement on the surface of the vacuolar membrane and be required for maintenance against rupture by osmotic pressure (By similarity).
Subcellular location: Vacuole {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Syntaxin-like protein fsv1
- Synaptobrevin homolog ykt6
- Syntaxin pep12
- Vesicle transport v-SNARE protein vti1
Sequence:
MALKIKIPETSQSSDEYSRWTVYHIEVAFPNGGKHVVFRRFNEFVALDAQIRPNDYNSRLCKLPSKSWVSSTVTNEKLRESRRLALQAYVQCLSETPWIKMPVVKKFLNIKDESEDETQGQFLGPTDWIQVFQDCKRNLHMYRVDLMSGKSITIGVQTKNVYAIKSLMDNLSESLDKLELANALGPGEILRRKDMLEQLGSEFLSFKRLVKNANSPVAPPSASSQLNSSNPSSPFRPLSASTDKQSNTSLNRVLGKNRMPETQTTKKLDNVGLYNMQNQTMEDQDMQAESLLPIIQRQKELSKMINQEVVEQNSMLDELSNEAYANQKKLHRTRAGLRKLG
Protein: Putative uncharacterized membrane protein PB15E9.02c (Q8TFG8)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MTGMFFFASLFSSFESLFFRLFFVCSFFFPLLYSFIFATLHAFVFLFSHTLVSSQFRRLKLPYHHHHTFTIEAFFYWFFFFFFFFSHCRRFHIAIFIHPYDSNVVPFFCFFFYFSLFSFFSFLFTSLHFNFFFRLCRHKHLLDIPDQTTLSSLLHRHTRLPRDVRRKHTCFHTSVWCDMSSYCIAWRS
Protein: ORF K9 (P88946)
Organism: Human herpesvirus 8 type M
Interaction partners:
Sequence:
MDPGQRPNPFGAPGAIPKKPCLSQGSPGTSGSGAPCDEPSRSESPGEGPSGTGGSAAAGDITRQAVVAAITEWSRTRQLRISTGASEGKASIKDWIVCQVNSGKFPGVEWEDEERTRFRIPVTPLADPCFEWRRDGELGVVYIRERGNMPVDASFKGTRGRRRMLAALRRTRGLQEIGKGISQDGHHFLVFRVRKPEEEQCVECGVVAGAVHDFNNMARLLQEGFFSPGQCLPGEIVTPVPSCTTAEGQEAVIDWGRLFIRMYYNGEQVHELLTTSQSGCRISSALRRDPAVHYCAVGSPGQVWLPNVPNLACEIAKRELCDTLDACAKGILLTSSCNGIFCVCYHNGPVHFIGNTVPPDSGPLLLPQGKPTRIFNPNTFLVGLANSPLPAPSHVTCPLVKLWLGKPVAVGKLEPHAPSPRDFAARCSNFSDACVVLEIMPKPLWDAMQ
Protein: Uncharacterized cell wall protein SPI1 (Stationary phase-induced protein 1) (P40092)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Cell wall protein that plays a role in adaptation and resistance to cell wall stress.
Subcellular location: Secreted, cell wall. Membrane; Lipid-anchor, GPI-anchor. Note=Covalently-linked GPI-modified cell wall protein (GPI-CWP).
Interaction partners:
- Cell wall protein SED1
- Protein YGP1
- Restriction of telomere capping protein 3
- Heat shock protein 26
- 6-phosphogluconolactonase 4
Sequence:
MLSNAKLLLSLAMASTALGLVSNSSSSVIVVPSSDATIAGNDTATPAPEPSSAAPIFYNSTATATQYEVVSEFTTYCPEPTTFVTNGATFTVTAPTTLTITNCPCTIEKPTSETSVSSTHDVETNSNAANARAIPGALGLAGAVMMLL
Protein: EGF-like domain-containing protein (Q585S0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Protein DPCD
- Cilia- and flagella-associated protein 206
Sequence:
MLVGVLVLYILCAPLAAVGSIAKYSKTVVTKRRLRGDDDTWTRYKPTPPGAQRLFDSLDENTPLPKLPIKTPFFSYDSVEWYVSPYGFLTLTAVPMCNSFCREGLDSPLTGSYRFARRNISEGGDWPLIGLFVADLDVTNLAGDAGVYYYTLDGEENPTKVIVEYRDIPVLNCHADGNELLTAQVEISTDGVIVARYEKVPRCRGSVGIVLSKSQRDIVQFRQREMGLVAVQYTPVPDTCGERNEGSCSETCTWCAATSSCMSAPLAGEICPRVSSNSSLNHNHYYTVTAKTESGSTQGGQSGGEPLDTTGSSVKVPLRFEFPFFTKGVGKHKINSVYILSSGVVSLLSNKQDCGPLKNVCSNGNYSYAIMPFVTSQTWGNSNAVVLRRESESITIFITTRSFGELYHTYTYWLRLEKSGAITFHYLASTVAGSREALSGFFAFPPPMIGVARYGMGDNASMIVPSAVARPGTTVRFEPRNEHDDCGINGRYENGGCVCSEGFQGNFCDDCTSGHYGPRCTKCPNCQNGGVCDSGRGGSGRCKCASSFGGKNCEKNCGNKGCVNCNSVGGYCDCGVCRCHEDSGWSGPDCTTFEDPCLKFSLQGCDACMSQEEHGCAFCADGACYSTKLEGTSLSHACSYKAETRDAPICQKVLQIAQSGTDFGYIIFFVLCLSAISLAVIISLLSRYLMYARRVVNVHVAAAAGGAPDYVPVRREREVVQAGFVPVNLPKGKKYVLGVPLKQISLHKLYKEQQNEGFPNKE
Protein: Histone-lysine N-methyltransferase EZH2 (EC 2.1.1.356) (A0A090N8E9)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MGQTGKKSEKGPVCWRKRVKSEYMRLRQLKRFRRADEVKSMFSSNRQKILERTEILNQEWKQRRIQPVHILTSVSSLRGTRECSVTSDLDFPTQVIPLKTLNAVASVPIMYSWSPLQQNFMVEDETVLHNIPYMGDEVLDQDGTFIEELIKNYDGKVHGDRECGFINDEIFVELVNALGQYNDDDDDDDGDDPEEREEKQKDLEDHRDDKESRPPRKFPSDKIFEAISSMFPDKGTAEELKEKYKELTEQQLPGALPPECTPNIDGPNAKSVQREQSLHSFHTLFCRRCFKYDCFLHRKCNYSFHATPNTYKRKNTETALDNKPCGPQCYQHLEGAKEFAAALTAERIKTPPKRPGGRRRGRLPNNSSRPSTPTINVLESKDTDSDREAGTETGGENNDKEEEEKKDETSSSSEANSRCQTPIKMKPNIEPPENVEWSGAEASMFRVLIGTYYDNFCAIARLIGTKTCRQVYEFRVKESSIIAPAPAEDVDTPPRKKKRKHRLWAAHCRKIQLKKDGSSNHVYNYQPCDHPRQPCDSSCPCVIAQNFCEKFCQCSSECQNRFPGCRCKAQCNTKQCPCYLAVRECDPDLCLTCGAADHWDSKNVSCKNCSIQRGSKKHLLLAPSDVAGWGIFIKDPVQKNEFISEYCGEIISQDEADRRGKVYDKYMCSFLFNLNNDFVVDATRKGNKIRFANHSVNPNCYAKVMMVNGDHRIGIFAKRAIQTGEELFFDYRYSQADALKYVGIEREMEIP
Protein: Surfeit locus protein 6 (P70279)
Organism: Mus musculus (Mouse)
Function: Binds to both DNA and RNA in vitro, with a stronger binding capacity for RNA. May represent a nucleolar constitutive protein involved in ribosomal biosynthesis or assembly.
Subcellular location: Nucleus, nucleoplasm {ECO:0000269|PubMed:8639267, ECO:0000269|PubMed:9548374}. Note=Granular component of the nucleolus.
Interaction partners:
- Probable rRNA-processing protein EBP2
- Suppressor of SWI4 1 homolog
- Protein MAK16 homolog
- GTP-binding protein 4
- Ribosome production factor 1
- MKI67 FHA domain-interacting nucleolar phosphoprotein
- RRP15-like protein
- Ribosome biogenesis protein BRX1 homolog
- Pescadillo homolog
- Nucleolar GTP-binding protein 2
Sequence:
MASLLAKDTYLQDLAKKICAQPGPERQRSTWGVRTKGSEAAGAPKKKRKKTQKKSPEQEQKAMDHKTKALGKKPPTSSRPKNPMVSKQEKGLSSLGSPKDSQGTARESVFALDFLRQRLHEKIQLARGQGSTKELSAATLEKRQRRKQERERKKRKRKERQAKQQVAEAEKKEEPVEVTPKMACKELQESGLIFNKVEVTEEEPASKAQRKKEKRQKVKGNLTPLTGRNYRQLLDRLQARQGRLDELRDQDAAKAQELEAKMKWTNLLYKAEGVKIRDDERLLQEALKRKEKRRAQRQRKWEKRSEHVVEKMQQRQDKRRQNLRKKKAARAERRLQKAHKKGRVLPQDLERAGLS
Protein: Jabba, isoform H (A0A0B4KFV2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MAQETKTVATAKDQNQRDHIDEEEVIELHESRSFYDRVREQAERFASTRVGQFVIERADKALAMIEDTAKWSLPQDKSSAPLERPLPWAPFLMLIVLLRLTRIWLSVGALMIGNGPISPTDMVYFIQTRRRKLRAIRVHGLKVMRRRQQEVSYGSGKGMTQKLNQWFSRAMCRPGVQQDSSSRRVFVRHSEQGLSNFVVKRPREEDCNADADLTIDQMLAKYANENSEDDSDFVPNEEEEEEESSSSSGESESESGSSEGISSGEVDEVVSQPKQKSAGAVVENGVHKAEEKENDKGKLNITTTSNGNNDKEQADVAAAQPDEEWKSSPGHMSAAVMNTRLYNNTAAAGSPTCFNTSLGTQALLKRASIQSVLGNPLHAHDGDEGSTH
Protein: T-complex protein 1 subunit epsilon (TCP-1-epsilon) (CCT-epsilon) (P40413)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin. In yeast may play a role in mitotic spindle formation.
Subcellular location: Cytoplasm.
Interaction partners:
- T-complex protein 1 subunit eta
- T-complex protein 1 subunit beta
- T-complex protein 1 subunit alpha
- T-complex protein 1 subunit delta
- T-complex protein 1 subunit zeta
- T-complex protein 1 subunit gamma
- T-complex protein 1 subunit theta
- Phosducin-like protein 2
- Prefoldin subunit 4
- Factor arrest protein 8
Sequence:
MAARPQQPPMEMPDLSNAIVAQDEMGRPFIIVKDQGNKKRQHGLEAKKSHILAARSVASIIKTSLGPRGLDKILISPDGEITITNDGATILSQMELDNEIAKLLVQLSKSQDDEIGDGTTGVVVLASALLDQALELIQKGIHPIKIANGFDEAAKLAISKLEETCDDISASNDELFRDFLLRAAKTSLGSKIVSKDHDRFAEMAVEAVINVMDKDRKDVDFDLIKMQGRVGGSISDSKLINGVILDKDFSHPQMPKCVLPKEGSDGVKLAILTCPFEPPKPKTKHKLDISSVEEYQKLQTYEQDKFKEMIDDVKKAGADVVICQWGFDDEANHLLLQNDLPAVRWVGGQELEHIAISTNGRIVPRFQDLSKDKLGTCSRIYEQEFGTTKDRMLIIEQSKETKTVTCFVRGSNKMIVDEAERALHDSLCVVRNLVKDSRVVYGGGAAEVTMSLAVSEEADKQRGIDQYAFRGFAQALDTIPMTLAENSGLDPIGTLSTLKSKQLKEKISNIGVDCLGYGSNDMKELFVVDPFIGKKQQILLATQLCRMILKIDNVIISGKDEY
Protein: Folate-biopterin transporter 1, chloroplastic (Q9SKZ5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Mediates folate monoglutamate transport involved in tetrahydrofolate biosynthesis. It also mediates transport of antifolates, such as methotrexate and aminopterin.
Subcellular location: Plastid, chloroplast membrane {ECO:0000269|PubMed:16162503}; Multi-pass membrane protein {ECO:0000269|PubMed:16162503}. Plastid membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Note=Expressed in green as well as in non-green plastids.
Interaction partners:
- NADPH-dependent pterin aldehyde reductase
- Protein ZINC INDUCED FACILITATOR-LIKE 1
- 10-formyltetrahydrofolate synthetase
- 10-formyltetrahydrofolate synthetase
Sequence:
MASRSLFSISISPSQFTVLPSINNERRRLAIAARSHRLSRRKIRKRPPDRDMSSIVSIPELPRRRDSEESLLLDSRISVAEGDTSNTDVEGDRDTTSSIRTQPPPRKGRNLSSSRIKFYGVELSPDNVAVAMVYFVQGVLGLARLAVSFYLKDDLHLDPAETAVITGLSSLPWLVKPLYGFISDSVPLFGYRRRSYLVLSGLLGAFSWSLMAGFVDSKYSAAFCILLGSLSVAFSDVVVDSMVVERARGESQSVSGSLQSLCWGSSAFGGIVSSYFSGSLVESYGVRFVFGVTALLPLITSAVAVLVNEQRVVRPASGQKENITLLSPGFLQTSKQNMIQLWGAIKQPNVFLPTLFIFLWQATPHSDSAMFYFTTNKLGFTPEFLGRVKLVTSIASLLGVGLYNGFLKTVPLRKIFLVTTIFGTGLGMTQVILVSGFNRQLGISDEWFAIGDSLILTVLAQASFMPVLVLAARLCPEGMEATLFATLMSISNGGSVLGGLMGAGLTQAFGITRDSFGNLSTLIILCNLSSLLPLPLLGLLPRDSPDTLTKDDADVEMKSN
Protein: Stringent starvation protein A (P0ACA3)
Organism: Escherichia coli (strain K12)
Function: Forms an equimolar complex with the RNA polymerase holoenzyme (RNAP) but not with the core enzyme. It is synthesized predominantly when cells are exposed to amino acid starvation, at which time it accounts for over 50% of the total protein synthesized. It is involved in the transition from P1 early to P1 late gene expression. Rnk and SspA can functionally replace P.aeruginosa alginate regulatory gene algR2.
Interaction partners:
- Stringent starvation protein B
- DNA-directed RNA polymerase subunit beta'
- RNA polymerase sigma factor RpoD
- DNA-directed RNA polymerase subunit omega
- DNA-directed RNA polymerase subunit alpha
- DNA-directed RNA polymerase subunit beta
- Lysine--tRNA ligase, heat inducible
Sequence:
MAVAANKRSVMTLFSGPTDIYSHQVRIVLAEKGVSFEIEHVEKDNPPQDLIDLNPNQSVPTLVDRELTLWESRIIMEYLDERFPHPPLMPVYPVARGESRLYMHRIEKDWYTLMNTIINGSASEADAARKQLREELLAIAPVFGQKPYFLSDEFSLVDCYLAPLLWRLPQLGIEFSGPGAKELKGYMTRVFERDSFLASLTEAEREMRLGRS
Protein: Gamma-secretase subunit APH-1B (APH-1b) (Aph-1beta) (Q8C7N7)
Organism: Mus musculus (Mouse)
Function: Probable subunit of the gamma-secretase complex, an endoprotease complex that catalyzes the intramembrane cleavage of integral proteins such as Notch receptors and APP (amyloid-beta precursor protein). It probably represents a stabilizing cofactor for the presenilin homodimer that promotes the formation of a stable complex. Probably present in a minority of gamma-secretase complexes compared to APH1A (By similarity).
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Gamma-secretase subunit PEN-2
- Presenilin-1
- Presenilin-2
- Nicastrin
- Transmembrane emp24 domain-containing protein 10
- Putative gamma-secretase subunit APH-1C
- Gamma-secretase subunit APH-1A
- Neurogenic locus notch homolog protein 1
- Amyloid-beta precursor protein
- Neurogenic locus notch homolog protein 3
Sequence:
MTAAVFFGCAFIAFGPALALYVFTIATDPLRVIFLIAGAFFWLVSLLLSSVFWFLVRVITDNRDGPVQNYLLIFGVLLSVCIQELFRLAYYKLLKKASEGLKSINPEETAPSMRLLAYVSGLGFGIMSGVFSFVNTLSNSLGPGTVGIHGDSPQFFLNSAFMTLVVIMLHVFWGVVFFDGCEKNKWYTLLTVLLTHLVVSTQTFLSPYYEVNLVTAYIIMVLMGIWAFYVAGGSCRSLKLCLLCQDKDFLLYNQRSR
Protein: Alr2887 protein (Q8YT39)
Organism: Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)
Subcellular location: Cell outer membrane {ECO:0000256|ARBA:ARBA00004442}.
Interaction partners:
- Alr3647 protein
- Alr5293 protein
- Heterocyst specific ABC-transporter, membrane fusion protein
- Alr2269 protein
- All4388 protein
- RND multidrug efflux transporter
- All2652 protein
- All4499 protein
- Alr3648 protein
- Alr4281 protein
Sequence:
MKGQHLFYSFLPGVTAAVLTTQPAVAEAMKVSSVQLVPSSSVVATQNSQTLLVDKSQTQLPNATVQIFPDIIPTSGVTTPNLQFSSSHSHPIILTENTGIDREQKSRQDEVKNFPLKSKLTLSQRLKQRRFSSQQKQINSGITKPKLVTKVVSTTSSTLLAGQQTFSPSYLQNPAPQEKLKTQLPMLLQTKANHVGAAKLLNISSCSPQTCQLTKLTGQQIAQGNTTQDPASVPVPDESTLVDTQAPTDTPVPNESAPTDTPVSTESAPADTQSPRVAPVQTESAPVNTQAPAGAVEVPQNLIPNANPLQFPTKPEEVTLKENQPITLTQALELARRSNRDLQVSLLELQRTQALLKEAQAALLPNLSVSSDVTRSQSASGQLQDELISKQGGVGNNDEPGTAFNSQAQLSYDLYTSGRRKAAIQEAEEQVRFNELDVERQSEEIRLSVTRAYYDLQQADEQVRIARSAVENAQASLRDAEALERAGVGTRFDVLRSQVNLANNTQQLTNNLSRQQTTRRQLATLLSVPQAVNISAADPVQLAGLWNQSLEQSIILAYQNRPELHQQLAQRNISEQQRRQALATLGPQVSFVANYNLLDQFDDGVGLTDGYSVGVRATLNLYDGGAARARASQARANIAIAETRFASQRDQVRFQVEQAFTNQRSNLENVQTANVALEQAREALRLARLRFQAGVGTQTDVINSENDLTQAEGNRITAILDYNRALAELQRAVTSRALISSQ
Protein: Flavin-dependent halogenase ptaM (EC 1.14.14.-) (Pestheic acid biosynthesis cluster protein M) (A0A067XMV4)
Organism: Pestalotiopsis fici (strain W106-1 / CGMCC3.15140)
Function: Flavin-dependent halogenase; part of the gene cluster that mediates the biosynthesis of pestheic acid, a diphenyl ether which is a biosynthetic precursor of the unique chloropupukeananes. The biosynthesis initiates from condensation of acetate and malonate units catalyzed by the non-reducing PKS ptaA. As the ptaA protein is TE/CLC domain-deficient, hydrolysis and Claisen cyclization of the polyketide could be catalyzed by ptaB containing a beta-lactamase domain. The ptaB protein might hydrolyze the thioester bond between the ACP of ptaA and the intermediate to release atrochrysone carboxylic acid, which is spontaneously dehydrated to form endocrocin anthrone. Endocrocin anthrone is then converted to endocrocin, catalyzed by the anthrone oxygenase ptaC. Spontaneous decarboxylation of endocrocin occurs to generate emodin. An O-methyltransferase (ptaH or ptaI) could methylate emodin to form physcion. PtaJ could then catalyze the oxidative cleavage of physcion, and rotation of the intermediate could then afford desmethylisosulochrin. PtaF, a putative NADH-dependent oxidoreductase, might also participate in the oxidative cleavage step. Desmethylisosulochrin is then transformed by another O-methyltransferase (ptaH or ptaI) to form isosulochrin. Chlorination of isosulochrin by ptaM in the cyclohexadienone B ring then produces chloroisosulochrin. PtaE is responsible for the oxidative coupling reactions of both benzophenones isosulochrin and chloroisosulochrin to RES-1214-1 and pestheic acid respectively, regardless of chlorination.
Interaction partners:
Sequence:
MSVPAQTSVLIVGGGPAGSYAATVLAREGVDVVLLEAEKFPRYHIGESMLASIRFFLRFVELEEEFDRHGFEKKYGATFKITEKNPAYTDFAASLGEGGYSWNVVRSESDEIIFRYAGKCGAKTFDGTKVESLTFEPYPHEGFDESVHLANPGRPVSANWSRKDGSSGVIKFDYIIDGSGRNGLISTKYLKNRSFNQGLKNIANWTYWKGAKRFNVGEKNENSPLFEALKDGSGWVWAIPLHNDTISVGVVARQDAFFEKKKESGLSGEAFYKEYLKLAPQIKNELLRDATIVSDIKQATDWSYSASAYAGPNFRLIGDAGCFVDPYFSSGCHLAMTSALSASVSIQAVRRGQCDELTGAKWHTTKVAEGYTRFLLLVMTVQRQLRMKDKNIISTDEEEGFDMAFKKIQPVIQGVADTRTEDEQTQRRAAEAVDFSLESFEITPEKQAAVISKIERSQAEPELLEKLTPEEVHILGNIVNRTFEREKDELNLTHFTGDMIDGYSAKLEHGNIGLYKREKALLNGTASRAAAVLKSIHQVA
Protein: RNA-binding protein 3 (RNA-binding motif protein 3) (RNPL) (P98179)
Organism: Homo sapiens (Human)
Function: Cold-inducible mRNA binding protein that enhances global protein synthesis at both physiological and mild hypothermic temperatures. Reduces the relative abundance of microRNAs, when overexpressed. Enhances phosphorylation of translation initiation factors and active polysome formation (By similarity).
Subcellular location: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Cell projection, dendrite {ECO:0000250}. Note=Localizes in mRNA granules in dentrites. {ECO:0000250}.
Interaction partners:
- U1 small nuclear ribonucleoprotein A
- Heterogeneous nuclear ribonucleoprotein K
- ELAV-like protein 1
- RNA-binding motif protein, X chromosome
- Heterogeneous nuclear ribonucleoprotein A1
- Endoribonuclease Dicer
- KH domain-containing, RNA-binding, signal transduction-associated protein 2
- RNA-binding motif protein, Y chromosome, family 1 member A1
Sequence:
MSSEEGKLFVGGLNFNTDEQALEDHFSSFGPISEVVVVKDRETQRSRGFGFITFTNPEHASVAMRAMNGESLDGRQIRVDHAGKSARGTRGGGFGAHGRGRSYSRGGGDQGYGSGRYYDSRPGGYGYGYGRSRDYNGRNQGGYDRYSGGNYRDNYDN
Protein: Dihydropyrimidinase-related protein 2 (DRP-2) (Unc-33-like phosphoprotein 2) (ULIP-2) (O08553)
Organism: Mus musculus (Mouse)
Function: Plays a role in neuronal development and polarity, as well as in axon growth and guidance, neuronal growth cone collapse and cell migration. Necessary for signaling by class 3 semaphorins and subsequent remodeling of the cytoskeleton. May play a role in endocytosis.
Subcellular location: Cytoplasm, cytosol {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Membrane {ECO:0000250}. Note=Tightly but non-covalently associated with membranes. {ECO:0000250}.
Interaction partners:
- Dihydropyrimidinase-related protein 5
- Protein numb homolog
- Glycogen synthase kinase-3 beta
- Cyclin-dependent kinase 5
- Tyrosine-protein kinase Fes/Fps
- Dihydropyrimidinase-related protein 3
- Plexin-A1
- Plexin-A2
- Semaphorin-3A
- Sodium channel protein type 9 subunit alpha
Sequence:
MSYQGKKNIPRITSDRLLIKGGKIVNDDQSFYADIYMEDGLIKQIGENLIVPGGVKTIEAHSRMVIPGGIDVHTRFQMPDQGMTSADDFFQGTKAALAGGTTMIIDHVVPEPGTSLLAAFDQWREWADSKSCCDYSLHVDITEWHKGIQEEMEALVKDHGVNSFLVYMAFKDRFQLTDSQIYEVLSVIRDIGAIAQVHAENGDIIAEEQQRILDLGITGPEGHVLSRPEEVEAEAVNRSITIANQTNCPLYVTKVMSKSAAEVIAQARKKGTVVYGEPITASLGTDGSHYWSKNWAKAAAFVTSPPLSPDPTTPDFLNSLLSCGDLQVTGSAHCTFNTAQKAVGKDNFTLIPEGTNGTEERMSVIWDKAVVTGKMDENQFVAVTSTNAAKVFNLYPRKGRISVGSDADLVIWDPDSVKTISAKTHNSALEYNIFEGMECRGSPLVVISQGKIVLEDGTLHVTEGSGRYIPRKPFPDFVYKRIKARSRLAELRGVPRGLYDGPVCEVSVTPKTVTPASSAKTSPAKQQAPPVRNLHQSGFSLSGAQIDDNIPRRTTQRIVAPPGGRANITSLG
Protein: TLC domain-containing protein 2 (A6NGC4)
Organism: Homo sapiens (Human)
Function: Regulates the composition and fluidity of the plasma membrane. Inhibits the incorporation of membrane-fluidizing phospholipids containing omega-3 long-chain polyunsaturated fatty acids (LCPUFA) and thereby promotes membrane rigidity. Does not appear to have any effect on LCPUFA synthesis.
Subcellular location: Cell membrane {ECO:0000305|PubMed:30509349}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MAPTGLLVAGASFLAFRGLHWGLRRLPTPESAARDRWQWWNLCVSLAHSLLSGTGALLGLSLYPQMAADPIHGHPRWALVLVAVSVGYFLADGADLLWNQTLGKTWDLLCHHLVVVSCLSTAVLSGHYVGFSMVSLLLELNSACLHLRKLLLLSRQAPSLAFSVTSWASLATLALFRLVPLGWMSLWLFRQHHQVPLALVTLGGIGLVTVGIMSIILGIRILVNDVLQSRPHPPSPGHEKTRGTRTRRDNGPVTSNSSTLSLKD
Protein: UPF0524 protein C3orf70 homolog B (A3KNX6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Plays a role in neuronal and neurobehavioral development. Required for normal expression of the postmitotic and mature neuron markers elavl3 and eno2 and neurobehaviors related to circadian rhythm and altered light-dark conditions.
Interaction partners:
- Iroquois homeobox 3b.
Sequence:
MAYSGAQKALKSDKLDEAQALAKSCAGRPDFLPCDGLSICATHSHGKCFKLHWCCYLGWCHCKYVYQPMTNVAQLPSTPVPAAPSDCPDTIDLSISLTERFLRISPCFQAPPCPESPKYCNIAELFIDDYIVKRINGKMCYVQRPQAHVEPAQMNPIQKQHTEDKQIVEETVKGPKMGHCSSPSTSEDSGINALGGHFLESCEEESEEEDELSTDGHSSPGSLWDQDECTLLSPSKSMVEIIENIETTV
Protein: Farnesylcysteine lyase (EC 1.8.3.6) (P57681)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in the degradation of prenylcysteine. Cleaves specifically the thioether bond of S-farnesyl-L-cysteine and has no activity with S-geranylgeranyl-L-cysteine. Recognizes also N-acetyl-farnesylcysteine and may have a role in deprenylation of farnesylated proteins.
Subcellular location: Lysosome {ECO:0000250|UniProtKB:Q9UHG3}.
Interaction partners:
- NAD
- WPP domain-interacting protein 3
- O-fucosyltransferase 5
- O-fucosyltransferase 14
- CAAX prenyl protease 1 homolog
- CAAX prenyl protease 2
- O-fucosyltransferase 36
- At1g17100
Sequence:
MKDFPIAISLLFALLSPVLLPCSGDSTGGVEDDSPATVCIVGSGIGGSSVAHFLRNYSVSTGLNQAKILMFERHEIVGGRMRTVTVAGDTFEAGGSILHPKNYHVKDFVERFNLTVRLPTPIEESSAIGIWDGKRFVVKTFGSGTKFPFLDTIVSWVNDLYLFLRYGLSLLRMSSFIENTVDNFLKYYESLESRPIFDNVEGMLKWSGLYNLTKLTLQEKLSEAQLSPLLVNELVTVITRINYGQSVLISGLAGAVSLAGSGGGLWSVEGGNWQMAAKLINHSDVTLHLNEKIESISYLENHYELKSTKGNSYKCDVTVVATPLDEVDIQFSPTISIPKRELQHTHTTFVRGLLNPGYFGMKSLSDVPALVGTLEDPLIPFSCISILRKYSKTDMTYKIFTRQPASDSLLDELFSRRTETVRIDWGAYPKYHAPEVFAPFILDDHHLYYVNAFENAASTMETSAVAGENIARLIISRFMTKESLSSSDKRSCSSGLHSDS
Protein: Apolipoprotein L3 isoform X1 (Apolipoprotein L3-like) (F1SPU1)
Organism: Sus scrofa (Pig)
Interaction partners:
Sequence:
MSSDDPRDHSESESFLEEVTEYFRNTVSREELQLLLTEGKAWEKFVTEADLSREEADALREYLKELETDLALEDKDSLLQDQLERTRFLQEFPRVKLEIEAQIGKLHALAAKVDKVHRDCTISNVVATSTGAASGILTVLGLALAPVTAGFSLALSATGLGLGVAASVTGVSASIVDKVNSSLAEREASRLMSTSFNKAEVISESLGKSTPQIVSLTKNFIQGLPRIGKNIRAIKLAKANPRLAANAKRFMTAGQVSVRNRRLVKKTFEGTVLAMTKNARIIGMATAGVALLMDVGFLVKESIHLQQGAKAESAERLRQQAQELEKKLEELTRIYENLQ