wanglab/gogpt-training-data huggingface dataset:
Protein: Small ribosomal subunit protein uS4 (30S ribosomal protein S4) (P9WH35)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the body of the 30S subunit.
Interaction partners:
- Small ribosomal subunit protein bS1
- Small ribosomal subunit protein uS13
- Large ribosomal subunit protein uL3
- Small ribosomal subunit protein bS16
- Large ribosomal subunit protein bL35
- Large ribosomal subunit protein uL14
- Large ribosomal subunit protein uL29
- Small ribosomal subunit protein uS5
- Large ribosomal subunit protein uL24
- Small ribosomal subunit protein uS17
Sequence:
MARYTGPVTRKSRRLRTDLVGGDQAFEKRPYPPGQHGRARIKESEYLLQLQEKQKARFTYGVMEKQFRRYYEEAVRQPGKTGEELLKILESRLDNVIYRAGLARTRRMARQLVSHGHFNVNGVHVNVPSYRVSQYDIVDVRDKSLNTVPFQIARETAGERPIPSWLQVVGERQRVLIHQLPERAQIDVPLTEQLIVEYYSK
Protein: Presequence protease 2, chloroplastic/mitochondrial (AtPreP2) (PreP 2) (EC 3.4.24.-) (Zinc metalloprotease 2) (AtZnMP2) (Q8VY06)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: ATP-independent protease that degrades both mitochondrial and chloroplastic transit peptides after their cleavage. Also degrades other unstructured peptides. Specific for peptides in the range of 10 to 65 residues. Shows a preference for cleavage after small polar residues and before basic residues, but without any positional preference.
Subcellular location: Plastid, chloroplast stroma {ECO:0000269|PubMed:15827031}. Mitochondrion matrix {ECO:0000269|PubMed:15827031}.
Interaction partners:
- Organellar oligopeptidase A, chloroplastic/mitochondrial
- Probable cytosolic oligopeptidase A
- Ornithine transcarbamylase, chloroplastic
- At5g55900
Sequence:
MLRSLTCSSTITSTSLFFRSFRQLPRSYLSPSSSTTVVGASGRNIRRLSTLEAAGRRLFLRRGLKLLSAASRGLNGQFSRLSIRAVATQSAPSSYPGQDEAEKLGFEKVSEEFISECKSKAVLFKHKKTGCEVMSVSNDDENKVFGIVFRTPPKDSTGIPHILEHSVLCGSRKYPMKEPFVELLKGSLHTFLNAFTYPDRTCYPVASTNKKDFYNLVDVYLDAVFFPKCVDDVHTFQQEGWHYELNDPSEDISYKGVVFNEMKGVYSQPDNILGRVTQQALCPENTYGVDSGGDPKDIPKLTFEKFKEFHRQYYHPSNARIWFYGDDDPVHRLRVLSEYLDMFDASPARDSSKVEPQKLFSRPRRIVEKYPAGEDGDLKKKHMVCLNWLLSDKPLDLQTQLALGFLDHLMLGTPASPLRKILLESGLGEALVNSGMEDELLQPQFSIGLKGVSDDNVQKVEELVMNTLRKLADEGFDTDAVEASMNTIEFSLRENNTGSSPRGLSLMLQSIAKWIYDMDPFEPLKYEEPLKSLKARIAEKGSKSVFSPLIEEYILNNPHCVTIEMQPDPEKASLEEAEEKSILEKVKASMTEEDLTELARATEELRLKQETPDPPDALKCVPSLNLSDIPKEPIYVPTEVGDINGVKVLRNDLFTNNILYTEVVFDMGSVKHELLQLIPLFCQSLLEMGTQDLTFVQLNQLIGRKTGGISVYPLTSSVYGRDDPCSKIIVRGKSMVGRAEDLFNLMNCVLQEVRFTDQQRFKQFVSQSRARMENRLRGSGQGIAAARMDAMLNVAGWMSEQMGGLSYLEFLHTLEQKVDQDWEGISSSLEEIRRSFLSRNGCIVNMTADGKSLTNTEKYVGKFLDLLPENPSGELVTWDARLPLRNEAIVIPTQVNYVGKAGNIYSSGYKLDGSSYVISKHISNTWLWDRVRVSGGAYGGSCDFDSHSGVFSFLSYRDPNLLKTLDIYDGTGDFLRGLDVDEDTLTKAIIGTIGDVDSYQLPDAKGYTSLLRHLLNVTDEERQIRREEILSTSLKDFKEFAEAIDSVSDKGVAVAVASQEDIDAANRERSNFFEVKKAAL
Protein: Interleukin-1 alpha (IL-1 alpha) (Hematopoietin-1) (P01583)
Organism: Homo sapiens (Human)
Function: Cytokine constitutively present intracellularly in nearly all resting non-hematopoietic cells that plays an important role in inflammation and bridges the innate and adaptive immune systems. After binding to its receptor IL1R1 together with its accessory protein IL1RAP, forms the high affinity interleukin-1 receptor complex. Signaling involves the recruitment of adapter molecules such as MYD88, IRAK1 or IRAK4. In turn, mediates the activation of NF-kappa-B and the three MAPK pathways p38, p42/p44 and JNK pathways. Within the cell, acts as an alarmin and cell death results in its liberation in the extracellular space after disruption of the cell membrane to induce inflammation and alert the host to injury or damage. In addition to its role as a danger signal, which occurs when the cytokine is passively released by cell necrosis, directly senses DNA damage and acts as signal for genotoxic stress without loss of cell integrity.
Subcellular location: Nucleus {ECO:0000269|PubMed:26439902}. Cytoplasm {ECO:0000269|PubMed:32272059}. Secreted {ECO:0000269|PubMed:26439902}. Note=The lack of a specific hydrophobic segment in the precursor sequence suggests that IL-1 is released by damaged cells or is secreted by a mechanism differing from that used for other secretory proteins. The secretion is dependent on protein unfolding and facilitated by the cargo receptor TMED10; it results in protein translocation from the cytoplasm into the ERGIC (endoplasmic reticulum-Golgi intermediate compartment) followed by vesicle entry and secretion (PubMed:32272059). Recruited to DNA damage sites and secreted after genotoxic stress. {ECO:0000269|PubMed:32272059}.
Interaction partners:
- Interleukin-1 receptor type 2
- Interleukin-1 beta
- Interleukin-1 receptor type 1
- Interleukin-1 receptor accessory protein
- Interleukin-18
- Interleukin-2
- Myeloid differentiation primary response protein MyD88
- Granulocyte-macrophage colony-stimulating factor
- Interleukin-4
- Tumor necrosis factor
Sequence:
MAKVPDMFEDLKNCYSENEEDSSSIDHLSLNQKSFYHVSYGPLHEGCMDQSVSLSISETSKTSKLTFKESMVVVATNGKVLKKRRLSLSQSITDDDLEAIANDSEEEIIKPRSAPFSFLSNVKYNFMRIIKYEFILNDALNQSIIRANDQYLTAAALHNLDEAVKFDMGAYKSSKDDAKITVILRISKTQLYVTAQDEDQPVLLKEMPEIPKTITGSETNLLFFWETHGTKNYFTSVAHPNLFIATKQDYWVCLAGGPPSITDFQILENQA
Protein: Glutaminyl-peptide cyclotransferase (EC 2.3.2.5) (Iso glutaminyl cyclase) (Q86PD7)
Organism: Drosophila melanogaster (Fruit fly)
Function: Acts as a glutaminyl-peptide cyclotransferase. Responsible for the biosynthesis of pyroglutamyl peptides (By similarity). Might be more efficient in the conversion of tri and tetrapeptides in vitro. Might have a relative preference for substrates containing hydrophobic amino acids in vitro.
Subcellular location: [Isoform A]: Secreted {ECO:0000269|PubMed:17722885}.; SUBCELLULAR LOCATION: [Isoform B]: Mitochondrion {ECO:0000269|PubMed:17722885}.
Interaction partners:
- Neuralized-like protein 2
Sequence:
MRLLLRNYSLMEAVKRLLPRPRKKIYNLGACFELVDIPKISYNPSELSEPRFLEYSNLSDKLHLREAIDKILIPRVVGTTNHSIVREYIVQSLRDLDWDVEVNSFHDHAPIKGKLHFHNIIATLNPNAERYLVLSCHYDSKYMPGVEFLGATDSAVPCAMLLNLAQVLQEQLKPLKKSKLSLMLLFFDGEEAFEEWGPKDSIYGARHLAKKWHHEGKLDRIDMLVLLDLLGAPDPAFYSFFENTESWYMRIQSVETRLAKLQLLERYASSGVAQRDPTRYFQSQAMRSSFIEDDHIPFLRRNVPILHLIPVPFPSVWHTPDDNASVIDYATTDNLALIIRLFALEYLLAGTEAK
Protein: Decorin (Bone proteoglycan II) (PG-S2) (PG40) (P28654)
Organism: Mus musculus (Mouse)
Function: May affect the rate of fibrils formation.
Subcellular location: Secreted, extracellular space, extracellular matrix. Secreted {ECO:0000250|UniProtKB:P07585}.
Interaction partners:
- Transforming growth factor beta-1 proprotein
- Epidermal growth factor receptor
- Fibronectin
- Elastin
- Y-box-binding protein 3
- Y-box-binding protein 1
- Insulin-like growth factor 1
- Biglycan
- Toll-like receptor 2
- Toll-like receptor 4
Sequence:
MKATLIFFLLAQVSWAGPFEQRGLFDFMLEDEASGIIPYDPDNPLISMCPYRCQCHLRVVQCSDLGLDKVPWDFPPDTTLLDLQNNKITEIKEGAFKNLKDLHTLILVNNKISKISPEAFKPLVKLERLYLSKNQLKELPEKMPRTLQELRVHENEITKLRKSDFNGLNNVLVIELGGNPLKNSGIENGAFQGLKSLSYIRISDTNITAIPQGLPTSLTEVHLDGNKITKVDAPSLKGLINLSKLGLSFNSITVMENGSLANVPHLRELHLDNNKLLRVPAGLAQHKYIQVVYLHNNNISAVGQNDFCRAGHPSRKASYSAVSLYGNPVRYWEIFPNTFRCVYVRSAIQLGNYK
Protein: ADP/ATP translocase (ADP/ATP carrier) (TtAac) (G2QNH0)
Organism: Thermothelomyces thermophilus (strain ATCC 42464 / BCRC 31852 / DSM 1799) (Sporotrichum thermophile)
Function: ADP:ATP antiporter that mediates import of ADP into the mitochondrial matrix for ATP synthesis, and export of ATP out to fuel the cell. Cycles between the cytoplasmic-open state (c-state) and the matrix-open state (m-state): operates by the alternating access mechanism with a single substrate-binding site intermittently exposed to either the cytosolic (c-state) or matrix (m-state) side of the inner mitochondrial membrane.
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P18239}; Multi-pass membrane protein {ECO:0000269|PubMed:30611538}.
Interaction partners:
- ATP synthase subunit beta
- mitochondrial processing peptidase
- ATP synthase subunit alpha
- Mitochondrial outer membrane protein porin
- Mitochondrial import inner membrane translocase subunit
- Mitochondrial import inner membrane translocase subunit TIM22
Sequence:
MSNKQETKILGMPPFVVDFLMGGVSAAVSKTAAAPIERIKLLVQNQDEMIKAGRLDRRYNGIIDCFRRTTADEGLMALWRGNTANVIRYFPTQALNFAFRDKFKAMFGYKKDKDGYAKWMAGNLASGGAAGATSLLFVYSLDYARTRLANDAKSAKGGGARQFNGLIDVYRKTLASDGIAGLYRGFGPSVAGIVVYRGLYFGMYDSIKPVVLVGPLANNFLASFLLGWCVTTGAGIASYPLDTVRRRMMMTSGEAVKYKSSIDAFRQIIAKEGVKSLFKGAGANILRGVAGAGVLSIYDQLQILLFGKAFKGGSG
Protein: Arginine/serine-rich protein PNISR (Q9U252)
Organism: Caenorhabditis elegans
Interaction partners:
- Pinin/SDK/MemA protein domain-containing protein
- Liprin-alpha
- LUC7 related splicing factor homolog
- Luc7-like protein 3
- Probable splicing factor, arginine/serine-rich 7
- Rho GTPase-activating protein syd-1
- ELKS/RAB6-interacting/CAST family member 2
- Suppressor of forked domain-containing protein
- Protein cmt-1
Sequence:
MEDWTNYHQAQPAESVDWAQLAQQWMAMRDTDDRRAGNSHDFAQNHQLPWHQPRHPGPPAHQDWGDWSANRDEQWRGPPGPSGPSGPPVYHNQGPPRGYPPPPPQGADTWRGAPPPAHHGHFGPPGHHFQGPPQHFPPGPPRPHFPGPPGPHRPPEHYPGPPRPQAPAAPPPKSLFPSAQKPKPLFAAASSAPSFFGAPQRPPPQLHFFQESPSVQHDFQQPDFQPDFQPENYQNSPEPPAQAGPKGVPPPAPLMASGPTNPYAMNKEARKKLPAWILEGLEKAEREKQKQWEKEEKLKKAEEEKARRRAEAGKSKFDSSSDEESPENEKFPVGNGKSEYQEDDNDSEDDLEERREQFIRCVKTLMMNVLLESSNDVIMRIIQEELREHEKLQFERKKLATAPKIIGNSSALAALAAFGDGEDSDNSSDDGVGDDMEPRQESSGSAELNGASGAAEAGTPEAGGGEFKAPVGIPRKFSVKTDDVKPSVNDDGEGVDDLHVPDSKNGDNKKSEKSSSEKKREREMRDDEKERKSSKKSKKRSKSREKEQSSSRHNHRSRSRSSERDRRRKRSRSSERRRDRGDRDRHSRR
Protein: Centromere protein F (A0A286Y8J7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MSWAVEEWKDGLPAKALQKIQEIEAQLDKLKKERQQKQFQMDSLEATLQKQKQKMDSEKSEASALKRENQSLVESCEHLEKARQKLTHDIQTKEQQVNYLEGQLNSFKKQTDRLEQEVKKYKHELERSQTSHASEIQQLSTPQKTFATPATPNHWQQDSKITDLQEKYNREVEERKKLEAEIKVMHVKLLNQSSVSHKDIARQQTGSSIFPWQQDQKSSHQSLPVMETPSRRRNGASGMPWSYDDTPIKPHQQFTSGAPSDTVGSQQMEQLKNINQDLRSKVSELELRLQAHEKDMKNQINKFSEIQSQLEMAKKDVAEKDKLLNKSRDELTKATGQYEQSVSKCSAFEIKLKQVTEEMNCQRHNAESMHRSLEQKIKDQERESQKELAQLQSSYQALDQQFTQVKNKTSMEIQQAKKDHNVLQSEMDKVTALKNRLEKELEELKQKLLRSEQALQASQVKEAETKKKFEEMQREKNTLNCQLDQGMKRVKQLEDEKQNTEQILAKNRMMVDDLKVKTQTQNEELTELRKKMDHQSVSSAQELENLKKTLIEAEAKNMKTQAELQKLVHDVELKENKICAVEKENEELKMTSNSCQKELAEMKKEYDALLQWKTEKEQLINNAESNRNELLAKVADLEKDKDNLSNAHGDLQKKMQDLENEKIGLSGQIDSLKGELLVKCVELEEKGRVYEELQQQFGETKIKHKKEMDNLNQQITLTQGKVSELEAKLLQETSKLEGMEQAHGQLLAEYESACILAMSKDSIIEMNKTEIVHLQESFTLRDQELEKFKVEKDILAKECEDRLAQNKELEQQKLNTETSLMEVLAKFTLLESDLRCQKDLNAEIQGKYDELSKIKEDLVEKVSSLEKREKDLINEVESLLQKNKSLCSLEEQFNCLVAEAEETRSSLEKVKELQVQTTTELENQKTIAENLAIDLEEEKKKALSIKQENTQLKVKQEEIENKANDLFEKYESLQKLHDAVCQENANHLKEISIVTEALAEKDAMAERIALIKTELETSNNLSATLKNSLENLQTQFDSSVELISSLEKKLHDMSDEKSLLEISIKELTERHNKESEVYVSELETHIKKHKSLEEHISVLETELQNKSLETKTASEKLEVTTQEMIKLKQDFSLSENKLSVVTDSNKKVAKELEDMKQNVFLQEQEMEGLRLALSDLKNQEAAKSCEIETLKEKLQKAQSEHAKTSETLNEKNINMSKIKVQLEMLQMDLEDNENCINAFDAQVEELQGNVSILEAKLSESEAQRSNLESKLESVKEDYVKSSLEVSQLSACLEESQKEQQSRSVLVAELESLRVIHEQLKVSLEQENCKQANLEAMYTNLMDQKLKLESEIQELKADTQGSQKQIDQLKQANDRLASQIAEQQIHIEQLQSEKNLADTLNKEQTSGGNDQDICEMPFANTSLLPFEEDTAILGMSSPKGKHDSQEEPKTPLSAEEDYKDFALQEQMQNKSSDIEDMSHVLKETVRTMEEQTAIQIEQLKLQHATELQSMEEQMLNIKNELEAKLKEEKQHTEILSSQLEATMQQLQELDIASSSLLAADTSQNMGKFASGAQDDLIHHTEQSNSTLGIITESEHSNLETETLKEVLRKREEELLHLQSQFEVLESEMENEKLNKHIGELKEEIDSLTLQLQTSNCQLTDVMEMMESLEMAKGEWNEKFFQIESELKRVRSEKANLEKHILSMEADIEEMQEQKQKQEAELETARRTNCSLEQQLNITMAEGGRLKEELILCTDERESETHSLMKLKEKADLLEKRETDTKELIKELEDDIRVGKKQNEVASDQISVLLKEKEQLIQQSQNLENKIVLLNEDNERLLSELNDIKHNDSFTSRETENMSSKIHSLEDENVRLSQSLEMSLLEKGEIASRLISTQEEVAQMRQGIEKLKVRIESDERKKNHMSQLLKAAQRKADVLQDNIEKLEREKELSEQNLEDAILQAETAKAELEEIQAETQDLTKKIEEMTSELKDLKEEKYKLEQELDQKNKLIEELQLSIQEASVKLKSAEEATLNQEQMIKDFQFKVGAMEEELRLFQTEVESKEVKALELASHLLSLESENKEFAQRVLEYERSQEELHSSNQSLLKDFESKQQELSEENTQLRSQIAELQALSLIREEQDEELQKDKVELQSTIAQLEEKTQMQSTKMEVMQNSISSLEINIQQLEGQLDAMKLMNVELTGKLNSLQESSLHLETQHKQELCEAKEIQNALEINQNLLTCQLQESQKQIEEYKFSLEALAAEKDGLQKSISVIQESHDVQLKENNMRHEENLKRTQQQLEVELNALKENILVAEKNAAQYQSDLESIKSQNAEKDSALKELQNKWENCQKEKAELDSKITRLSKEKDSAMSKINLWMKSCKQLENEKQTLQEELQQQGQEIETLKASKEQAEGSSSSGALQEELEELKEALEEKSREADDSMDRYCSLMVKVHKLEDSNESLKNQLKQLSTQTKTPKSRRSLRSETSDLENSNPEGVTSGKRQRAIDDTPNKAQEALHNITKRLKAAAATPKAKQDDEDFRPEGLPELVQKGFADIPVGEMSPFIVRRTTAQRCSPRLAARTTAVLQSSGSAEHPAQISMQTAEGRTPNTVQKPKATPSRNVPLLSTLTNSPLKNSCERLAPVIEQKISRRSRSFKNSPQTSEQVTASPKQNDNCQVQ
Protein: Agouti-related protein (O00253)
Organism: Homo sapiens (Human)
Function: Plays a role in weight homeostasis. Involved in the control of feeding behavior through the central melanocortin system. Acts as alpha melanocyte-stimulating hormone antagonist by inhibiting cAMP production mediated by stimulation of melanocortin receptors within the hypothalamus and adrenal gland. Has very low activity with MC5R (By similarity). Is an inverse agonist for MC3R and MC4R being able to suppress their constitutive activity. It promotes MC3R and MC4R endocytosis in an arrestin-dependent manner.
Subcellular location: Secreted {ECO:0000269|PubMed:15927146}. Golgi apparatus lumen {ECO:0000269|PubMed:15927146}.
Interaction partners:
- Melanocortin receptor 4
- Melanocortin receptor 3
- Appetite-regulating hormone
- Pro-opiomelanocortin
- Pro-neuropeptide Y
- Leptin
- Insulin
- Forkhead box protein O1
- Cocaine- and amphetamine-regulated transcript protein
- Leptin receptor
Sequence:
MLTAAVLSCALLLALPATRGAQMGLAPMEGIRRPDQALLPELPGLGLRAPLKKTTAEQAEEDLLQEAQALAEVLDLQDREPRSSRRCVRLHESCLGQQVPCCDPCATCYCRFFNAFCYCRKLGTAMNPCSRT
Protein: Kelch-like ECH-associated protein 1 (K7EJD8)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MQPDPRPSGAGACCRFLPLQSQCPEGAGDAVMYASTECKAEVTPSQHGNRTFSYTLEDHTKQAFGIMNELRLSQQLCDVTLQVKYQDAPAAQFMAHKVVLASSSPVFKAMFTNGLREQGMEVVSIEGIHPKVMERLIEFAYTASISMGEKCVLHVMNGAVMYQIDSVVRACSDFLVQQLDPSNAIGIANFAEQIGCVELHQRAREYIYMHFGE
Protein: Dolichyldiphosphatase 1 (EC 3.6.1.43) (Dolichyl pyrophosphate phosphatase 1) (Protein 2-23) (Q9JMF7)
Organism: Mus musculus (Mouse)
Function: Required for efficient N-glycosylation. Necessary for maintaining optimal levels of dolichol-linked oligosaccharides. Hydrolyzes dolichyl pyrophosphate at a very high rate and dolichyl monophosphate at a much lower rate. Does not act on phosphatidate.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:12198133}; Multi-pass membrane protein {ECO:0000269|PubMed:12198133}.
Interaction partners:
- Dolichol kinase
- Dolichyl-phosphate beta-glucosyltransferase
- Dolichol-phosphate mannosyltransferase subunit 1
- UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 2
- Dolichol-phosphate mannosyltransferase subunit 3
- Dolichol phosphate-mannose biosynthesis regulatory protein
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3A
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 48 kDa subunit
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3B
Sequence:
MAADGQCSLPASWRPVTLTHVEYPAGDLSGHLLAYLSLSPIFVVVGFLTLIIFKRELHTISFLGGLALNQGVNWLIKHVIQEPRPCGGPHTAVGTKYGMPSSHSQFMWFFSVYSFLFLYLRMHQTNNARFLDLLWRHVLSLGLLTAAFLVSYSRVYLLYHTWSQVFYGGVAGSLMAVAWFIITQEILTPLFPRIAAWPISEFFLIRDTSLIPNVLWFEYTVTRAEARNRQRKLGTKLQ
Protein: Dachshund a (F1R0U6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MAVSATPPVLSPTSTPGGASLFRPDSLYSSPAESPRLTSSMINSFITGGGSTNGNGPGGVHNNECKMVEVHGVKVASFTVDGQELICLPQVFDLFLKHLVGGLHTVYTKLKRLDICPVVCTVEQVRILRGLGAIQPGVNRCKLITRKDFETLYNDCTNASSRPGRPPKRSLGVAMQDSSRLLPHSVHGLLSPGLLSPTGLTAAAMAEAMKLQKMKLMAMNNIHGAGSQNGTESENEELNSSAGGSESSWDKEKLQSPPSSGAQHGLAHAALSAQHGLSGSHLSSLQQSHLLANRLDLPFMMMPHPLLPVSLPPASVAMAMNQMNHLNTIANMAAAAQMHSPLSRAGASVIKECVQDSPSPTPSLEEAPRPGSQPSSHPSSSVSSSPNPHTQSPERLVLNPTDGDLPERDTGINMKKMLKEKDEAQITLPMQKPGFEKLPLGTQTLPPGFPAPFLFADGLSSVETLLTNIQGLLKVAVDNARVQEKQVQQERKELKMELYREREMRESLERQLTSELHSRATIQKRLKKEKKAKRKLQEALEFESKRREQVEQALKQATSPESLRMSLNEAVIPEVKSEHNGNQQENSSVQENRPYSKPPIMY
Protein: Ribonuclease H2 subunit A (RNase H2 subunit A) (EC 3.1.26.4) (Aicardi-Goutieres syndrome 4 protein) (AGS4) (RNase H(35)) (Ribonuclease HI large subunit) (RNase HI large subunit) (Ribonuclease HI subunit A) (O75792)
Organism: Homo sapiens (Human)
Function: Catalytic subunit of RNase HII, an endonuclease that specifically degrades the RNA of RNA:DNA hybrids. Participates in DNA replication, possibly by mediating the removal of lagging-strand Okazaki fragment RNA primers during DNA replication. Mediates the excision of single ribonucleotides from DNA:RNA duplexes.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Ribonuclease H2 subunit C
- Ribonuclease H2 subunit B
- Deoxynucleoside triphosphate triphosphohydrolase SAMHD1
- Ribonuclease H1
- Proliferating cell nuclear antigen
- Flap endonuclease 1
- Three-prime repair exonuclease 1
- DNA replication licensing factor MCM7
- DNA polymerase epsilon catalytic subunit A
- DNA primase small subunit
Sequence:
MDLSELERDNTGRCRLSSPVPAVCRKEPCVLGVDEAGRGPVLGPMVYAICYCPLPRLADLEALKVADSKTLLESERERLFAKMEDTDFVGWALDVLSPNLISTSMLGRVKYNLNSLSHDTATGLIQYALDQGVNVTQVFVDTVGMPETYQARLQQSFPGIEVTVKAKADALYPVVSAASICAKVARDQAVKKWQFVEKLQDLDTDYGSGYPNDPKTKAWLKEHVEPVFGFPQFVRFSWRTAQTILEKEAEDVIWEDSASENQEGLRKITSYFLNEGSQARPRSSHRYFLERGLESATSL
Protein: Protein ecm33 (Q4WNS8)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Function: Involved in conidial and mycelial cell wall biogenesis.
Subcellular location: Cell membrane; Lipid-anchor, GPI-anchor.
Interaction partners:
- 1,3-beta-glucanosyltransferase gel1
- 1,3-beta-glucanosyltransferase gel4
- 1,3-beta-glucanosyltransferase gel2
Sequence:
MAFLKYALPALAAAQAVLAANCGKTDETITISSQSDADGYSSCSTIKGTIEIDEHLSGAITFNNVKQIDGTLSCTGGANISSIAAPMLNSIADTFKLDGLTTLTTLSFPSLTSVGSIQWTALPQLQSLDFTKGVNEAGDVTITNTGLANLNGISLNTVGKFDITENTQLKSININNLKNATGLINFAGNLNSLEVELPNLSSGTNMTFRNVSAVSVPSLHNLTGQLGFWGDTFKSFSAPNLTETGDLVFNSNSKLTNISMPALETVNGGFLITRNDELSSIDLPSLKVVTGAVDFSGKFDEVSMPKLENVKGQFNLQSTGNFSCDTFDKAHNDKVIRGTYKCKAAEPNPTTKDGSSGTTTSSGSSASASKSNAADLNAANLPALGFAAVFGALVQYVL
Protein: Transcriptional enhancer factor TEF-1 (NTEF-1) (Protein GT-IIC) (TEA domain family member 1) (TEAD-1) (Transcription factor 13) (TCF-13) (P28347)
Organism: Homo sapiens (Human)
Function: Transcription factor which plays a key role in the Hippo signaling pathway, a pathway involved in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. The core of this pathway is composed of a kinase cascade wherein MST1/MST2, in complex with its regulatory protein SAV1, phosphorylates and activates LATS1/2 in complex with its regulatory protein MOB1, which in turn phosphorylates and inactivates YAP1 oncoprotein and WWTR1/TAZ. Acts by mediating gene expression of YAP1 and WWTR1/TAZ, thereby regulating cell proliferation, migration and epithelial mesenchymal transition (EMT) induction. Binds specifically and cooperatively to the SPH and GT-IIC 'enhansons' (5'-GTGGAATGT-3') and activates transcription in vivo in a cell-specific manner. The activation function appears to be mediated by a limiting cell-specific transcriptional intermediary factor (TIF). Involved in cardiac development. Binds to the M-CAT motif.
Subcellular location: Nucleus {ECO:0000269|PubMed:38512451}.
Interaction partners:
- WW domain-containing transcription regulator protein 1
- Transcriptional coactivator YAP1
- Transcription cofactor vestigial-like protein 4
- Transcription cofactor vestigial-like protein 1
- Transcriptional enhancer factor TEF-4
- Transcriptional enhancer factor TEF-3
- Transcription cofactor vestigial-like protein 2
- Transcription cofactor vestigial-like protein 3
- Malonyl-CoA-acyl carrier protein transacylase, mitochondrial
- Transcription factor 7-like 2
Sequence:
MEPSSWSGSESPAENMERMSDSADKPIDNDAEGVWSPDIEQSFQEALAIYPPCGRRKIILSDEGKMYGRNELIARYIKLRTGKTRTRKQVSSHIQVLARRKSRDFHSKLKDQTAKDKALQHMAAMSSAQIVSATAIHNKLGLPGIPRPTFPGAPGFWPGMIQTGQPGSSQDVKPFVQQAYPIQPAVTAPIPGFEPASAPAPSVPAWQGRSIGTTKLRLVEFSAFLEQQRDPDSYNKHLFVHIGHANHSYSDPLLESVDIRQIYDKFPEKKGGLKELFGKGPQNAFFLVKFWADLNCNIQDDAGAFYGVTSQYESSENMTVTCSTKVCSFGKQVVEKVETEYARFENGRFVYRINRSPMCEYMINFIHKLKHLPEKYMMNSVLENFTILLVVTNRDTQETLLCMACVFEVSNSEHGAQHHIYRLVKD
Protein: Galactose specific C-type lectin (Q94881)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MLKLTVLLITLLVIAKTGWTREKFSIQVNEGNTFGALVKAEPFTKINDGYYFFGTESLNWYEAYEKCRELNSELVTFETDQEFDAVTVSNGSRLTYWTSGNDLAKTGSHRWFTNGQRISSLRWARNQPDNAGQKEHCIHLGYIYKDSRKFELNDRPCSQDPNSLFKYICEAPEMETISIVVWK
Protein: ATPase subunit 9 homolog (O43937)
Organism: Trypanosoma brucei brucei
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MMRRLALQSSLRRVTPAAVSVMTPAKVTSPIGHAIAIRQASTVAISVQGLHYVGTGLAAIALAGVGLGIGTIFGNLLVACARQPNLTKMLFNYAILGFALTEAIGLFALMLAFLMLFS
Protein: Initiation-specific alpha-1,6-mannosyltransferase, putative (EC 2.4.1.232) (B9WEI9)
Organism: Candida dubliniensis (strain CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 / NRRL Y-17841) (Yeast)
Interaction partners:
Sequence:
MLQLREPKMVHRHLKLAILGIIVIVTTFFLISSLSNPSLTHKTEYNSPKLQLAKELELNSNWKELGLNFQPNKKYSLPDESTLRQQLSYQFPYDETKSFPKNIWQTWKVGIDDKSFPKRYLKYQQTWADKNPDYKHYVVPDKQCDLLVEQLYSQVPDVAKAYKIMPKSILKADFFRYLILFARGGVYTDIDTVGLKPIDEWISNTEMILEKTNRSGLVVGIEADPDRPDWADWYARRIQFCQWTIQSKKGHPMLRELIAKITDITLTRHKKGQLKKILGKNEGGDIMNWTGPGIFTDTIFEYMNNILQSPEVFKNKKKWATIIDWELFTGMEQPIAIDDVLILPITSFSPDVNQMGAKDSHDPMAYAKHMFSGSWKDDGMPEMQ
Protein: Sperm acrosome-associated protein 9 (Q4V8P4)
Organism: Rattus norvegicus (Rat)
Function: Microtubule inner protein (MIP) part of the dynein-decorated doublet microtubules (DMTs) of multiciliated respiratory cells and the distal singlet microtubules of monoflagellated spermatozoa. May stabilize the protofilaments to which they are bound.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q7TPM5}. Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000250|UniProtKB:Q7TPM5}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q7TPM5}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000250|UniProtKB:Q7TPM5}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250|UniProtKB:Q96E40}. Nucleus {ECO:0000269|PubMed:18756329}. Note=In caudal sperms localizes onto sperm head. Is also present on midpiece and principle piece of sperm tails. Acrosome and sperm tail localization is regulated by Y-chromosome. {ECO:0000250|UniProtKB:Q7TPM5}.
Interaction partners:
- Family with sequence similarity 209
- Cilia and flagella associated protein 90
- Cilia and flagella associated protein 144
Sequence:
MNEVKESLRSIEQKYKLFQQQQFTFIAALEHCRENAHDKIRPISSIEQVQSYMEHYCNNSTDRRILLMFMDICSELNKLCQHFEALHSGTPVTNSLLEKCKTLVSQSNDLSILRAKYPHDVVNHLSCDEARNHYGGVVSLIPIVLDLMKEWIAHSEKLPRKVLQHGTT
Protein: Prolyl 3,4-dihydroxylase ofd1 (EC 1.14.11.-) (2-oxoglutarate and Fe(II) dioxygenase domain-containing protein 1) (PKHD-type hydroxylase ofd1) (uS12 prolyl 3,4-dihydroxylase) (Q11120)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Prolyl 3,4-dihydroxylase that catalyzes 3,4-dihydroxylation of 'Pro-62' of small ribosomal subunit uS12 (rps23 and rps2302), thereby regulating protein translation termination efficiency. Negative regulator of the stability of the N-terminal transcription factor domain (Sre1N) of sre1 which is released from the membrane and enters the nucleus to activate hypoxic gene expression.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Negative regulator of ofd1
- Elongation factor 3
- Sterol regulatory element-binding protein 1
- Probable oxygen-dependent coproporphyrinogen-III oxidase
- mRNA export factor elf1
- Elongation factor Tu
- Small ribosomal subunit protein uS12B
- Uncharacterized protein P8A3.02c
- C-4 methylsterol oxidase erg25
- Delta
Sequence:
MGDTQQPTVLDRFAPHALDTSEAERLSREYHKNGPYNHVVIRPLINDTLLRNVRKELMENIHFTEKVTDIYRVWQTGDLANLDGLDKKEQNMLKYLRQVRDALYSEEFRSHVQKITGCGPLSASKKDLSVNVYSKGCHLMNHDDVIGTRCISYILYLVEPDEGWKPEYGGALRLFPTLQPSFPAADFCHSIPPQWNQLSFFRVKPGHSFHDVEEVYVDKPRMAISGWFHYPQPGEPGYDANYCDNTVSTLQSLTMKQMDLELPRFSYYPVVKPEPLSKQDTDILSNYINPLYLTPDGIEKLSKRFFQDSVIVLVEFLNQEFANTLLKRIIDAERQPTPMHSSEVSFPWKTAIPPHKHRYLYLDHEEFGPDIILPMDLQRLPAFQRWIQLVSGLPLRSFHQVGRRFRPGSDFTLATTNDTALLEATLCLSPGTGIANTDNGAYDIYMIGDEDPDVDAAVYRGDQQDDSILLSLPAAWNVFSLVYRDEGVLQFVKYVSRQAESSRWDIYSQWNPVAE