wanglab/gogpt-training-data huggingface dataset:
Protein: Stromal membrane-associated protein 2 (Stromal membrane-associated protein 1-like) (Q7TN29)
Organism: Mus musculus (Mouse)
Function: GTPase activating protein that acts on ARF1. Can also activate ARF6 (in vitro). May play a role in clathrin-dependent retrograde transport from early endosomes to the trans-Golgi network.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16571680}. Note=Detected in multiple foci throughout the cytoplasm and in juxtanuclear structures.
Interaction partners:
- Syntaxin-2
Sequence:
MTGKSVKDVDRYQAVLANLLLEEDNKFCADCQSKGPRWASWNIGVFICIRCAGIHRNLGVHISRVKSVNLDQWTQEQIQCMQEMGNGKANRLYEAYLPETFRRPQIDPAVEGFIRDKYEKKKYMDRSLDINVLRKEKDDKWKRGNEPAPEKKMEPVVFEKVKMPQKKEDAQLPRKSSPKSAAPVMDLLGLDAPVACSIANSKTSNALEKDLDLLASVPSPSSVSRKAVGSMPTAGSAGSVPENLNLFPEPGSKSEETGKKQLSKDSILSLYGSQTPQMPAQAMFMAPAQMAYPTAYPSFPGVTPPNSIMGGMVPPPVGMVAQPGASGMLTPMAMPAGYMGGMQASMMGVPNGMMTTQQAGYMASMAAMPQTVYGVQPAQQLQWNLTQMTQQMAGMNFYGANGMMNYGQSMGGGNGQAANQTLSPQMWK
Protein: Tyrosine-protein kinase receptor (EC 2.7.10.1) (Q6B515)
Organism: Taeniopygia guttata (Zebra finch) (Poephila guttata)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
KCSCEIMWIKKFQETKFYTETQDLYCVDDNNKKTALLDMKVPNCDLPSANLSNYNITVVEGKSITLYCDTTGGPPPNVSWVVTNLVSNHESDTNKNPASLTIKNVSSMDSGLEISCVAENIVGEDQASAELTVFFAPNITFIESPTPDHHWCIPFTVKGNPKPTLQWFYEGAVLNESEYICTKIHVINQSEYHGCLQLDNPTHLNNGAYTLLAKNDYGEDEKRVDAHFMSVPGDGNGPILDPDVYEYETTPNDLGDATNNSNQITSTDVSNKENEDSITVYVVVGIAALVCTGLVITLIILKFGRHSKFGMKGPSSVISNDDDSASPLHHISNGSNTPSSSEGGPDAVIIGMTKIPVIENPQYFGITNSQLKPDTFVHHIKRHNIVLKRELGEGAFGKVFLAECYNLCPEQGKILVAVKTLKDASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYMKHGDLNKFLRAHGPDAGLMAEGNRPAELTQSQMLHIAQQIASGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMSRDVYSTDYYRVGGHTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTYGKQPWYQLSNNEVIECITQGRVLQRPRTCPKEVYDLMLGCWQREPHMRLNIKEIHSLLQNLAKASPVYLDILG
Protein: Spermatid nuclear transition protein 1 (STP-1) (TP-1) (P10856)
Organism: Mus musculus (Mouse)
Function: Plays a key role in the replacement of histones to protamine in the elongating spermatids of mammals. In condensing spermatids, loaded onto the nucleosomes, where it promotes the recruitment and processing of protamines, which are responsible for histone eviction. The histone H2AB1-H2BC1/TH2B dimer is required for loading of TNP1 onto chromatin.
Subcellular location: Nucleus {ECO:0000269|PubMed:15163613}. Chromosome {ECO:0000269|PubMed:28366643}. Note=Loaded onto the nucleosomes of condensing spermatids (PubMed:28366643). Inclusion of the H2AB1-H2BC1/TH2B dimer into chromatin opens the nucleosomes, releasing the nucleosomal DNA ends and allowing the invasion of nucleosomes by transition protein TNP1 (PubMed:28366643). {ECO:0000269|PubMed:28366643}.
Interaction partners:
- Nuclear transition protein 2
- Protamine-2
- Spermatid maturation protein 1
- Sperm protamine P1
- Protamine-3
- Acrosin
- Outer dense fiber protein 1
- Doublesex- and mab-3-related transcription factor 1
- A-kinase anchor protein 4
- Testis-specific H1 histone
Sequence:
MSTSRKLKTHGMRRGKNRAPHKGVKRGGSKRKYRKSVLKSRKRGDDASRNYRSHL
Protein: RNA-binding NOB1-like protein (AtNob1) (EC 3.1.-.-) (Q9FLL1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Essential protein required during embryogenesis and pollen development. Endonuclease cleaving pre-rRNA at the 3' end of the mature 18S rRNA (D-site); cleaves 20S pre-rRNA in the cytoplasm. Required for processing of 20S pre-rRNA precursor and biogenesis of 40S ribosomal subunits.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9ULX3}. Nucleus, nucleoplasm {ECO:0000269|PubMed:23382868}. Cytoplasm {ECO:0000269|PubMed:23382868}.
Interaction partners:
- At3g13230
- Bystin
- Serine/threonine-protein kinase RIO2
- At3g49990
- 18S rRNA
- At1g42440/F7F22_7
- Probable cytokinin riboside 5'-monophosphate phosphoribohydrolase LOG6
- Serine/threonine-protein kinase RIO1
- Serine/threonine-protein kinase RIO1
- Protein NUCLEOLAR COMPLEX ASSOCIATED 4
Sequence:
MDPKPTSMWSSIVKKDPPSKPPVNDGAPAAILGMVGNCKSTKGISIAVVDANAIIEGRQSLTNFADKFVTVPEVLSEIRDPASRRRLAFIPFTIDTMEPSPESLSKVIKFARATGDLQSLSDVDLKLIALSYTLEAQVYGTKNLRDVPPPIQTVRVKRLPEKDLPGWGSNVANLEEWEALENETEEKSNANSKILPLKDLNMNIIASDNVSEVGSVVSHTENHEEDVQEGGKKHRRYPPKKTEIKLEGKMVVEGVDASQGQYDDDDDASDWRPAVSRSTHSKYLRRKARWEHYNALAEQEIQKDQEADKARHTKEANETHAKDSGKNGEDISSILKDMRLEEESLRALQEETEETNAEATLINGEDDIDHDIEVEAEGIDVANQALENLEIASEAEDTFEASSIGDDGSSEQSWSLRALSESSVACITGDYAMQNVILQMGLRLLAPGGMQIRQLHRWILKCHACYTVTPEIGRIFCPKCGNGGTLRKVAVTIGANGAIIAACKPRITLRGTQYSIPMPKGGREAITKNLILREDQLPQKLLHPRTKKKASKPGDEYFVSDDVFLNHHSDRKAPLQPPVRKAMSVFSQKRNPNDNHYSRSMH
Protein: Sterol 14-alpha demethylase (EC 1.14.14.154) (Cytochrome P450 monooxygenase 51B) (Ergosterol biosynthesis protein cyp51B) (B8NFL5)
Organism: Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC 167)
Function: Cytochrome P450 monooxygenase involved in the biosynthesis of ergosterol (By similarity). The existence of several duplicated sterol 14-alpha demethylase genes could be a good strategy to modulate the composition and fluidity of the cell membrane (By similarity). Catalyzes C14-demethylation of erburicol to produce 4,4,24-trimethyl cholesta-8,24(28)-dien-3-beta-ol (By similarity). Shows a slight substrate preference toward eburicol over obtusifoliol (By similarity). As a target of azole drugs, plays a crucial role in azole susceptibility.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Terpene cyclase/mutase family member
- Terpene cyclase/mutase family member
- Delta
- Delta
- Terpene cyclase/mutase family member
- Sterol 14-alpha demethylase
- Sterol 14-alpha demethylase
- Farnesyl-diphosphate farnesyltransferase, putative.
- Sterol 24-C-methyltransferase
- 3-ketosteroid reductase.
Sequence:
MGILAVILDSVCERCSGSSLWMLSTVALLSILVVSVVINVLRQLLFKNYKEPPLVFHWFPFIGSTISYGMDPYRFFFNCREKYGDIFTFVLLGKKTTVYLGTKGNDFILNGKLRDVCAEEVYSPLTTPVFGRHVVYDCPNAKLMEQKKGPNGVFDVCKTIAEITIYTASRSLQGKEVRSRFDSTFAELYHDLDMGFAPINFMLPWAPLPHNRKRDAAQKRMTETYMEIIKERRKAGSKKDSEDMVWNLMSCMYKDGTPVPDEEIAHMMIALLMAGQHSSSSTAAWIVLHLAASPEITEELYQEQLRILGHDMPPLTYENLQKLDLHAKVIKETLRIHAPIHSIIRAVKNPMPVEGTPYVIPTSHNVLSSPGVTARSEEHFPDPLEWKPHRWDEAIAVSSEDEEKVDYGYGLVTKGTNSPYLPFGAGRHRCIGEQFAYVQLGAITAALVRLFKFSNLPGVQTLPDTDYSSLFSKPLGNSKIQFEKREPVTKA
Protein: MCC regulator of WNT signaling pathway (A0A096LNU0)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MNSGVAMKYGNDSSAELSELHSAALASLKGDIVELNKRLQQTERERDLLEKKLAKAQCEQSHLMREHEDVQERTTLRYEERITELHSVIAELNKKIDRLQGTTIREEDEYSELRSELSQSQHEVNEDSRSMDQDQTSVSIPENQSTMVTADMDNCSDLNSELQRVLTGLENVVCGRKKSSCSLSVAEVDKHIEQLTTASEHCDLAIKTVEEIEGVLGRDLYPNLAEERSRWEKELAGLREENESLTAMLCSKEEELNRTKATMNAIREERDRLRRRVRELQTRLQSVQATGPSSPGRLTSTNRPINPSTGELSTSSSSNDIPIAKIAERVKLSKTRSESSSSDRPVLGSEISSIGVSSSVAEHLAHSLQDCSNIQEIFQTLYSHGSAISESKIREFEVETERLNSRIEHLKSQNDLLTITLEECKSNAERMSMLVGKYESNATALRLALQYSEQCIEAYELLLALAESEQSLILGQFRAAGVGSSPGDQSGDENITQMLKRAHDCRKTAENAAKALLMKLDGSCGGAFAVAGCSVQPWESLSSNSHTSTTSSTASSCDTEFTKEDEQRLKDYIQQLKNDRAAVKLTMLELESIHIDPLSYDVKPRGDSQRLDLENAVLMQELMAMKEEMAELKAQLYLLEKEKKALELKLSTREAQEQAYLVHIEHLKSEVEEQKEQRMRSLSSTSSGSKDKPGKVGPEWLGDTLRLSDCPVTAQ
Protein: Ponticulin-like protein B (Q54M25)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Binds F-actin and nucleates actin assembly.
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-anchor {ECO:0000305}.
Interaction partners:
- Ponticulin
Sequence:
MLFIKSLLLLLSLIFAVSNATGYVGFKVDGPGCNATKIITLENGACQTVCTNLYGKVTPTNDPSKFNLNPFIDVDCKTPLMAEQQVTCLPDNKPFKVSTLTVTCIPDTTSSSTSPSSTSPSSTSPASTLIGSIAFVTLAALFALI
Protein: Eukaryotic translation initiation factor 2 subunit beta (eIF2-beta) (P09064)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: eIF-2 functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA. This complex binds to a 40S ribosomal subunit, followed by mRNA binding to form a 43S preinitiation complex. Junction of the 60S ribosomal subunit to form the 80S initiation complex is preceded by hydrolysis of the GTP bound to eIF-2 and release of an eIF-2-GDP binary complex. In order for eIF-2 to recycle and catalyze another round of initiation, the GDP bound to eIF-2 must exchange with GTP by way of a reaction catalyzed by eIF-2B.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P56329}.
Interaction partners:
- Eukaryotic translation initiation factor 3 subunit I
- Eukaryotic translation initiation factor 1A
- Translation initiation factor eIF2B subunit alpha
- Translation initiation factor eIF2B subunit epsilon
- Eukaryotic translation initiation factor 3 subunit G
- Eukaryotic translation initiation factor 2 subunit alpha
- Eukaryotic translation initiation factor eIF-1
- Translation initiation factor eIF2B subunit beta
- Eukaryotic translation initiation factor 3 subunit B
- Eukaryotic translation initiation factor 3 subunit C
Sequence:
MSSDLAAELGFDPALKKKKKTKKVIPDDFDAAVNGKENGSGDDLFAGLKKKKKKSKSVSADAEAEKEPTDDIAEALGELSLKKKKKKTKDSSVDAFEKELAKAGLDNVDAESKEGTPSANSSIQQEVGLPYSELLSRFFNILRTNNPELAGDRSGPKFRIPPPVCLRDGKKTIFSNIQDIAEKLHRSPEHLIQYLFAELGTSGSVDGQKRLVIKGKFQSKQMENVLRRYILEYVTCKTCKSINTELKREQSNRLFFMVCKSCGSTRSVSSIKTGFQATVGKRRRM
Protein: OVARIAN TUMOR DOMAIN-containing deubiquitinating enzyme 5 (OTU domain-containing protein 5) (EC 3.4.19.12) (Deubiquitinating enzyme OTU5) (Q9LYC7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Hydrolase that can remove conjugated ubiquitin from proteins in vitro and may therefore play an important regulatory role at the level of protein turnover by preventing degradation (Probable). Inactive cysteine protease. Deubiquitinating enzyme which regulates gene expression by contributing to chromatin organization and DNA methylation patterns (e.g. H3K4me3 and H3K27me3). Involved in the interpretation of environmental information, probably by altering chromatin organization and maintaining redox homeostasis. Required for phosphate (Pi) homeostasis (e.g. responses upon Pi starvation including DNA methylation and histone methylation). Negative regulator of root hair morphogenesis.
Interaction partners:
- OVARIAN TUMOR DOMAIN-containing deubiquitinating enzyme 9
- OVARIAN TUMOR DOMAIN-containing deubiquitinating enzyme 11
- OVARIAN TUMOR DOMAIN-containing deubiquitinating enzyme 10
- OVARIAN TUMOR DOMAIN-containing deubiquitinating enzyme 3
- At2g28120/F24D13.9
- Putative OVARIAN TUMOR DOMAIN-containing deubiquitinating enzyme 8
- OVARIAN TUMOR DOMAIN-containing deubiquitinating enzyme 2
- Ubiquitin carboxyl-terminal hydrolase 27
- Ubiquitin carboxyl-terminal hydrolase 14
- Mov34/MPN/PAD-1 family protein
Sequence:
MADNKTSEGIVSEETPMDASQEQQHETVEEMLARHRQEIKQLQNKETEMKKAAAKGSKAEQKAKKKQVEDDISKLSTKLKDKQLKELASQGFSSSSSNNIAKDETTEKKGDIDTLVRAIAGVSVTAQQEHSKPSKSVKRREKRAKEEADREQRIKEEQSHVKSDRMVENAKLEKKLKPLGLTVSEIKPDGHCLYRAVENQLANRSGGASPYTYQNLREMAASYMREHKTDFLPFFLSETEGDSNSGSAEERFEKYCREVESTAAWGSQLELGALTHCLRKHIKVYSGSFPDVEMGKEYRSGDDSSLMLSYHRHAFGLGEHYNSVVLVNNITG
Protein: Uncharacterized protein orf490 (Q2F997)
Organism: Oryza sativa subsp. indica (Rice)
Interaction partners:
Sequence:
MDEEYGALMRNNTWHLVPATQGRNLIDCKWVYKIKRKADGTIDRYKARLVAKGFKQRYGIDYEETFSPVVKAATIRLILSLAVSNGWSLRQLDVQNAFLHGVLEEDVYMRQPPGYEDKSKLDYVCKLDKALYGLKQAPRAWFSRLSMKLQNLGFQPSKADASLFFYKKGTISIFVLIYVDDIIVASSCEKATSALLQDLKEEFALKDLGALHYFLGIEVNKVHDGIILTQEKYATDLLKRVGMHGCKEINTPLSTTDKLLAKEGEPLGAEDSTRYRSIVGALQYLTLTRPDIAFPVNKVCQYLHAPTSLHWTAVKRILRYLKGSLGLGLRICKSDSTLVSAFSDADWAGCPDDRKSTGGFAVFLGANLISWNAWKQATVSRSSTEAEYKALANATAEIISVQTLLKERGIAQPRAACLWCDNIGATSLSANPVFHARTKHIEVDYHFVRERVSQGLLDIRFVPSGDQVADGFTCNRPRRQYIQGGLHCGG
Protein: Elongation of fatty acids protein (EC 2.3.1.-) (Q59PF0)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Acyl-CoA desaturase
- Acyl-CoA desaturase
- very-long-chain enoyl-CoA reductase
- Very-long-chain 3-oxoacyl-CoA reductase
- Elongation of fatty acids protein
- Very-long-chain
- Very-long-chain
- 3-oxoacyl-[acyl-carrier-protein] synthase
- Fad2p
Sequence:
MSSLSSSFPIPTWDTPFGIQLWPIFDKVISQATNNKFIPSQFQFISGHLPLSTLPEALMAITIYYIVIFGGDYIFKKFNIKPFVLNGLFQIHNLFLTTLSFTLLILMCEQIIPMIYHHGLFYTICDIKAWTQPLITLYYLNYITKFIEFIDTVFLVVKQKKLTFLHTYHHGATALLCYTQLVGTTSISWVPISLNLAVHVLMYWYYFLAARGIRVWWKEWVTRFQIIQFIIDLVFVYFGTYQKVVITHFSKVLPYCGDCAGTMIAAYSGCAILSSYLVLFIAFYIDVYRRKDSTKSKIVKSVKGGVAAQVNEYVHASGVQIPSNTNSTAKTVRSRKA
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (Q8T9I6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MDLDRAWDIYYHVFQKISRQLPQLTSLELPYVSPKLMTCKDLELAVPGSYNPGQELIRISIIKTNLQVITSKQRPRKLCIRGSNGKDYMYLLKGHEDLRQDERVMQLFSLVNTLLLDDPDTFRRNLAIQRYAVIPLSTNSGLIGWVPHCDTLHTLIRDYRDKKKVPLNQEHRTMLNFAPDYDHLTLMQKVEVFEHALGQTQGDDLAKLLWLKSPSSELWFERRNNYTRSLAVMSMVGYILGLGDRHPSNLMLDRMSGKILHIDFGDCFEVAMTREKFPEKIPFRLTRMLIKAMEVTGIEGTYRRTCESVMLVLRRNKDSLMAVLEAFVYDPLLNWRLLDVDKKGNDAVAGAGAPGGRGGSGMQDSLSNSVEDSLPMAKSKPYDPTLQQGGLHNNVADETNSKASQVIKRVKCKLTGTDFQTEKSVNEQSQVELLIQQATNNENLCQCYIGWCPFW
Protein: Beta-1,3-glucan-binding protein (BGBP) (Beta-1,3-glucan recognition protein) (BetaGRP) (Q76DI2)
Organism: Tenebrio molitor (Yellow mealworm beetle)
Function: Involved in the recognition of invading microorganisms. Binds specifically to beta-1,3-glucan and activates the phenoloxidase cascade.
Subcellular location: Secreted {ECO:0000269|PubMed:12923175}.
Interaction partners:
Sequence:
MKVLVVFIFCLVRSTFGQFEVPDALVEVFRPRGLRVSIPDQEGIKLFAFHGKINEEMNGREGGTFSRDILKAKNGRWTFYDANARLKEGDILYYWTYVDYFDGKNKLGYPNDDQKFVVKQLLDKDGAAPSVTPPTVTKAPPQEHTTLESGCKASVTTKVNERVCAGEQIFHEDFTTFETNIWRPEVKFADKPDYEFVFYRAGPPNLQVKHHRLTIRPVPSDAVFGEGFVSRREKVNLAPACTGVHGSIECVQTPGAFLILPPVTSAQISTKGKWSFKYGKVEIRAKLPKGDWIYPELYLNPVNEEYGPGYASGQIRIAFSGGNEDLCRDLRGGCILGSRPAARNYAVKNIVKNSGSWSDDFHKFIVIWKPDQITMMVDDQVYGNIYPPEGGFVSEAYNLDLVNVERWRGGTSFAPFDKEMYLVLGVGVGGHCFEDRSDATKPWTNNDPKSQKKFYQAAAQWGATWSNASRLEVDYVKVSAL
Protein: Ribosomal protein eL42-like (60S ribosomal protein L36a-like) (Large ribosomal subunit protein eL42-like) (Q969Q0)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Large ribosomal subunit protein uL23
- Large ribosomal subunit protein eL30
- Large ribosomal subunit protein eL19
- Large ribosomal subunit protein eL8
- Ubiquitin-like protein FUBI
- Large ribosomal subunit protein eL21
- Small ribosomal subunit protein uS17
- Large ribosomal subunit protein eL33
- Small ribosomal subunit protein eS25
- Small ribosomal subunit protein eS6
Sequence:
MVNVPKTRRTFCKKCGKHQPHKVTQYKKGKDSLYAQGRRRYDRKQSGYGGQTKPIFRKKAKTTKKIVLRLECVEPNCRSKRMLAIKRCKHFELGGDKKRKGQVIQF
Protein: Serine/threonine-protein kinase PknF (EC 2.7.11.1) (P9WI75)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Phosphorylates the FHA domains of the ABC transporter Rv1747, the heat-shock protein GroEL 1, and Rv0020c. May play a role in the regulation of glucose transport, cell growth and septum formation.
Subcellular location: Cell membrane {ECO:0000269|PubMed:11496007}; Single-pass membrane protein {ECO:0000269|PubMed:11496007}.
Interaction partners:
- Serine/threonine-protein kinase PknG
- ABC transporter ATP-binding/permease protein Rv1747
- Serine/threonine protein phosphatase PstP
- Glycogen accumulation regulator GarA
- FHA domain-containing protein FhaA
- Isopentenyl-diphosphate Delta-isomerase
- FHA domain-containing protein FhaB
Sequence:
MPLAEGSTFAGFTIVRQLGSGGMGEVYLARHPRLPRQDALKVLRADVSADGEYRARFNREADAAASLWHPHIVAVHDRGEFDGQLWIDMDFVDGTDTVSLLRDRYPNGMPGPEVTEIITAVAEALDYAHERRLLHRDVKPANILIANPDSPDRRIMLADFGIAGWVDDPSGLTATNMTVGTVSYAAPEQLMGNELDGRADQYALAATAFHLLTGSPPFQHANPAVVISQHLSASPPAIGDRVPELTPLDPVFAKALAKQPKDRYQRCVDFARALGHRLGGAGDPDDTRVSQPVAVAAPAKRSLLRTAVIVPAVLAMLLVMAVAVAVREFQRADDERAAQPARTRTTTSAGTTTSVAPASTTRPAPTTPTTTGAADTATASPTAAVVAIGALCFPLGSTGTTKTGATAYCSTLQGTNTTIWSLTEDTVASPTVTATADPTEAPLPIEQESPIRVCMQQTGQTRRECREEIRRSNGWP
Protein: Carboxy-terminal domain RNA polymerase II polypeptide A small phosphatase 1 (EC 3.1.3.16) (Golli-interacting protein) (GIP) (Nuclear LIM interactor-interacting factor 3) (NLI-interacting factor 3) (Small C-terminal domain phosphatase 1) (SCP1) (Small CTD phosphatase 1) (P58466)
Organism: Mus musculus (Mouse)
Function: Preferentially catalyzes the dephosphorylation of 'Ser-5' within the tandem 7 residue repeats in the C-terminal domain (CTD) of the largest RNA polymerase II subunit POLR2A. Negatively regulates RNA polymerase II transcription, possibly by controlling the transition from initiation/capping to processive transcript elongation (By similarity). Recruited by REST to neuronal genes that contain RE-1 elements, leading to neuronal gene silencing in non-neuronal cells.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- RE1-silencing transcription factor
Sequence:
MDSSAVITQISKEEARGPLRGKGDQKSAVSQKPRSRGILHSLFCCVCRDDGEPLPAHSGAPLLVEENGAIPKHTPVQYLLPEAKAQDSDKICVVIDLDETLVHSSFKPVNNADFIIPVEIDGVVHQVYVLKRPHVDEFLQRMGELFECVLFTASLAKYADPVADLLDKWGAFRARLFRESCVFHRGNYVKDLSRLGRDLRRVLILDNSPASYVFHPDNAVPVASWFDNMSDTELHDLLPFFEQLSRVDDVYSVLRQPRPGS
Protein: RNA polymerase II-associated protein 3 (Q9V3E9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- PIH1 domain containing 1, isoform D
- RuvB-like helicase 2
- IP21091p
- RuvB-like helicase 1
- Probable prefoldin subunit 6
- GEO12025p1
- Heat shock protein 83
- Probable prefoldin subunit 2
- DNA-directed RNA polymerases I, II, and III subunit RPABC1
- IP05962p
Sequence:
MSAQEKAFELQRQVRQNAREYENSVKDLYSWEQDIKNKEKELQKSPLSAANKDLPVRSHVQTDKSRKESPSSSAASSPTEKQDLPVDPVAQQYKKANDIKDRGNTYVKQGEYEKAIVAYSTAIAVYPHDPIYHINRALCYLKQESFDQCVEDCEAAIALDKLCVKAYYRRMQANESLGNNMEALKDCTTVLAIEPKNIEAKRSLARINDRLRKIATKSGPNFTPDRPGMIEILPIEKPAYKRSKKAMRSVPVVDVVSPRATIDDSNQLRISDEDIDKIFNSNCGIIEEVKKTNPKPTPMPDTSGPPKAETIAKTSKEVKPTKQTAVKVAPAVETPKETETRKDTKIVPESDNEAKPSAPKKTAVEVPKVQTQVSPPKTTIERSPEVNTVQTEKIEQASSNNAMSPSPIERFLPPAPTSTAQFHVTWKELSGPQKYQYLKSIEVPNLCKILGAGFDSDTFADLLRTIHDFFVPNKEPNTAAVLLEISKNDEFTILAMLMSAEEKKMVSSILNAIKNWPSKNPAVLDNLFKEYGVA
Protein: Acid sphingomyelinase-like phosphodiesterase 3b (ASM-like phosphodiesterase 3b) (EC 3.1.4.-) (P58242)
Organism: Mus musculus (Mouse)
Function: Lipid-modulating phosphodiesterase. Active on the surface of macrophages and dendritic cells and strongly influences macrophage lipid composition and membrane fluidity. Acts as a negative regulator of Toll-like receptor signaling. Has in vitro phosphodiesterase activity, but the physiological substrate is unknown. Lacks activity with phosphocholine-containing lipids, but can cleave CDP-choline, and can release phosphate from ATP and ADP (in vitro).
Subcellular location: Secreted {ECO:0000250}. Cell membrane; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:26095358}.
Interaction partners:
Sequence:
MTLLGWLIFLAPWGVAGAQLGRFWHISDLHLDPNYTVSKDPLQVCPSAGSQPVLNAGPWGDYLCDSPWALINSSLYAMKEIEPKPDFILWTGDDTPHVPNESLGEAAVLAIVERLTNLIKEVFPDTKVYAALGNHDFHPKNQFPAQSNRIYNQVAELWRPWLSNESYALFKRGAFYSEKLPGPSRAGRVVVLNTNLYYSNNEQTAGMADPGEQFRWLGDVLSNASRDGEMVYVIGHVPPGFFEKTQNKAWFRESFNEEYLKVIQKHHRVIAGQFFGHHHTDSFRMFYDNTGAPINVMFLTPGVTPWKTTLPGVVDGANNPGIRIFEYDRATLNLKDLVTYFLNLRQANVQETPRWEQEYRLTEAYQVPDASVSSMHTALTRIASEPHILQRYYVYNSVSYNHLTCEDSCRIEHVCAIQHVAFNTYATCLHGLGAKLVPGFLLILTLLPSLHVLEVL
Protein: Protein ARV 1 (AtArv1p) (Q5MK24)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Mediator of sterol homeostasis involved in sterol uptake, trafficking and distribution into membranes. Regulates also the sphingolipid metabolism.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16725371}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- NAC domain-containing protein 1
- Testis-expressed sequence 2-like protein
Sequence:
MAASEHRCVGCGFRVKSLFIQYSPGNIRLMKCGNCKEVADEYIECERMIIFIDLILHRPKVYRHVLYNAINPATVNIQHLLWKLVFAYLLLDCYRSLLLRKSDEESSFSDSPVLLSIKVLIGVLSANAAFIISFAIATKGLLNEVSRRREIMLGIFISSYFKIFLLAMLVWEFPMSVIFFVDILLLTSNSMALKVMTESTMTRCIAVCLIAHLIRFLVGQIFEPTIFLIQIGSLLQYMSYFFRIV
Protein: Uncharacterized lipoprotein Rv2585c (P9WL77)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}.
Interaction partners:
- Oligopeptide transport system permease protein OppB
- Oligopeptide transport system permease protein OppC
- Probable dipeptide-transport ATP-binding protein ABC transporter DppD
- Oligopeptide transport ATP-binding protein OppD
- Oligopeptide-binding protein OppA
- Protein translocase subunit SecF
- Protein translocase subunit SecD
- Uncharacterized protein Rv0010c
- Endonuclease
- Sec translocon accessory complex subunit YajC
Sequence:
MAPRRRRHTRIAGLRVVGTATLVAATTLTACSGSAAAQIDYVVDGALVTYNTNTVIGAASAGAQAFARTLTGFGYHGPDGQVVADRDFGTVSVVEGSPLILDYQISDDAVYSDGRPVTCDDLVLAWAAQSGRFPGFDAATQAGYVDIANIECTAGQKKARVSFIPDRSVVDHSQLFTATSLMPSHVIADQLHIDVTAALLSNNVSAVEQIARLWNSTWDLKPGRSHDEVRSRFPSSGPYKIESVLDDGAVVLVANDRWWGTKAITKRITVWPQGADIQDRVNNRSVDVVDVAAGSSGSLVTPDSYQRTDYPSAGIEQLIFAPQGSLAQSRTRRALALCVPRDAIARDAGVPIANSRLSPATDDALTDADGAAEARQFGRVDPAAARDALGGTPLTVRIGYGRPNARLAATIGTIADACAPAGITVSDVTVDTPGPQALRDGKIDVLLASTGGATGSGSSGSCAMDAYDLHSGNGNNLSGYANAQIDGIISALAVSADPAERARLLAEAAPVLWDEMPTLPLYRQQRTLLMSTKMYAVSRNPTRWGAGWNMDRWALAR
Protein: Uncharacterized protein At5g65300 (Q9FKQ7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- At1g56300
- Adenine nucleotide alpha hydrolases-like superfamily protein
- UDP-glycosyltransferase 89A2
- Cytochrome b561 and DOMON domain-containing protein At4g12980
Sequence:
MECRKHNHQGNRGVCPCCLRDKLSRLPNTTSYYIVHRSSSSSSTTVSSSPSSPAVKDHRRAGSMSMSFAVREALNGNLIEALGGGLMKSRSMAHVPKDYIVRDLTKKKTEKLKSTTVKKKTGFWTKLLHLKGKGGGADVGGFVTSRQRVY
Protein: Transcription factor BTF3 homolog (Inhibitor of cell death 1) (Nascent polypeptide-associated complex subunit beta) (NAC-beta) (Q18885)
Organism: Caenorhabditis elegans
Function: May be a general transcription factor that can form a stable complex with RNA polymerase II (By similarity). May prevent inappropriate targeting of non-secretory polypeptides to the endoplasmic reticulum (ER) (By similarity). In response to heat stress, plays a role in modulating the unfolded protein response by negatively regulating the accumulation of proteins such as the chaperone protein hsp-4 in the endoplasmic reticulum. Required to suppress apoptosis in neuronal and intestinal cells to promote development.
Subcellular location: Nucleus {ECO:0000305}. Cytoplasm {ECO:0000250|UniProtKB:P20290}. Mitochondrion {ECO:0000269|PubMed:12944970}.
Interaction partners:
- Nascent polypeptide-associated complex subunit alpha
- Large ribosomal subunit protein eL31
- Nsp1_C domain-containing protein
- Large ribosomal subunit protein uL23B
- Large ribosomal subunit protein eL6
- Large ribosomal subunit protein uL29
- Large ribosomal subunit protein uL16
- Large ribosomal subunit protein eL21
- Small ribosomal subunit protein eS19
- Large ribosomal subunit protein eL14
Sequence:
MDSKAIAERIKKLQAQQEHVRIGGKGTPRRKKKVIHKTAAADDKKLQSNLKKLSVTNIPGIEEVNMIKDDGTVIHFNNPKVQTSVPANTFSVTGSADNKQITEMLPGILNQLGPESLTHLKKLANNVTKLGPDGKGEDEDVPELVGDFDAASKNETKADEQ
Protein: 33 kDa inner dynein arm light chain, axonemal, putative (Q389G1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MGLLKVETHVINDDVQVDDVLQEQRLSESVPLSRRLEVRKHTSGQGAVECKEKAATSQMSSPSTQLVVAGETTPSTDIRRSLMAQRGSKLPSCTKECVSNTSVNKTPLSALKLSQNASSPAAKLAFLKRHNKAPSVSHPGGAILPALMTRVTDVETLLYTLLPPQRIVCEETGETIVKSVSLEQPSRVEVAKLHERTLQQLQQRRAREWGICPLRREIYTELFDELIREITLEEPARGVLLLRIRDEMNQTLAAHRALAERTLLFASKQRMEPPEDISALRQRIKELEEEREELLVKRRMATVREEQIQSALLDENTARVKLWQDETCYYRRANRQVSQRIKTETERANAHGVQVDRFVLEGGPPSSDLGVEL
Protein: Hkb protein (Q26364)
Organism: Drosophila sp. (Fruit fly)
Interaction partners:
Sequence:
MSTINLHPPQTYSRLFRPWDTQRQAATSAAPRTVKQEPEDYHQDGAGQQQFRPRLRRRLLLRILLCVKQQQQQQVLLRGGPEPQQLHPHFHPAAGRRPAPRLFTPAVVAVGHARRRHRILAPPNQHAPFLSAASDLYYAAAAAAAAAASTPTAVPGFGMDPFTMGLMEQEYARVMAEDAQLKALNSRKQRPKKFKCPNCDVAFSNNGQLKGHIRIHTGERPFKCDVNTCGKTFTRNEELTRHKRIHTGLRPYPCSACGKKFGRRDHLKKHMKTHMPQERQLGPSIFVPMYSYLYGY