wanglab/gogpt-training-data huggingface dataset:
Protein: Brother of ihog, isoform G (A8JUV7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Protein hedgehog
- Protein patched
- Interference hedgehog
- Protein smoothened
- Dally-like, isoform A
- Transcriptional activator cubitus interruptus
Sequence:
MAEIRLVVVLLVLMTTCIYTLQASDSNSSVATTLGVLFERAPESAVAPKGDEVVFECELNLKPDRLEWRFRRGDSSEPYLYLRPSAGYNVTSGSDGLAWRLRIYVSAQTAGDYQCVAWYGPGALASTPARLALVSIALDVGQGSMGARSSIRWSVAPKNCLLIRCGSVISNPPAIWSFYRNGKKLPQSELLPGAAGALVLDTVTAKDAGNYSCVATNSITGDELRLPQTIELRVDYTDRTPPYFLQRPPIEYSARPGETVVLECPGVGSPRPRVIWSSPNVVEIYNNRSTILSYGLQITDVKPEDQGSYICMLDNGIAPPIDHTIKLSVLQRPTILRGPAATLTNESNPLLLDCSASGNPQPDIYWLINGEDATKDPEAVVDNRSLQLKRVQKRHAGVVQCFAKNILGETSEGNILRVNPLEITGEDDEPLGEVPVWPVHESNTGMGTSSTSGGSKNKSGRRKFKASMVPPSRPNVTRLSDESVMLRWSVPQNSGLQITFFKVQYRMLGDGKNRRKNWQTTSDNIPYGNAHGSGPGQGNSHWRARNRDREYEMGNPPKNFTSSVTGLTAGKYYRFRIVAVYSNNDNKEGNTSLKFFLQNGTSKSNLPVPELREVETLSESAVVLHWSLVSSTQNEDIDGYYAYYRPADSAAEYLKATVDGGMSRSFKIDLLRPGTPYEFKLQSFNSDAASEFSAIRQARTRKTHEQPASSSATPVPANKAVEQHQNSLYPLIAGAAGGGILLLIASLVVCLCLKRRENSQPEDENKPQLEHIQADFVTSAVLGVGGHHKSGDVRRLNGVIPRMNITPNPLAQETASDKNRNVMELRFLPPLANGNGNGNCMARDLALERSNAEEQQDEDGHEDEKGLPAVASSSCETLEACDAAIKLNLPQKHDQEQLDAPNAVLEAPSKPLPPLPKKPANGAGQNNSGLHQNGLHHAQPYHPPGTPTLMHKRLDYHQQPPPVPPHSAYYQQAPTHQPSPMMERSVRGHQQPGGFHMEEGTPTPTRIPSLRRQRRTSGNQQVHNSHSNLNIGLSHHNNNNNNLPPHHQHLHHHPGHPGGLVGIPIVPGSPRVQRSPMPSRAMIKRTRLGSHTDNISSGSLNSIEV
Protein: Helicase-like transcription factor (EC 2.3.2.27) (EC 3.6.4.-) (DNA-binding protein/plasminogen activator inhibitor 1 regulator) (HIP116) (RING finger protein 80) (RING-type E3 ubiquitin transferase HLTF) (SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 3) (Sucrose nonfermenting protein 2-like 3) (Q14527)
Organism: Homo sapiens (Human)
Function: Has both helicase and E3 ubiquitin ligase activities. Possesses intrinsic ATP-dependent nucleosome-remodeling activity; This activity may be required for transcriptional activation or repression of specific target promoters (By similarity). These may include the SERPINE1 and HIV-1 promoters and the SV40 enhancer, to which this protein can bind directly. Plays a role in error-free postreplication repair (PRR) of damaged DNA and maintains genomic stability through acting as a ubiquitin ligase for 'Lys-63'-linked polyubiquitination of chromatin-bound PCNA.
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000269|PubMed:8672239}. Nucleus, nucleolus {ECO:0000250}. Nucleus, nucleoplasm {ECO:0000250}. Note=Nuclear localization is stimulated by progesterone. {ECO:0000250}.
Interaction partners:
- E3 ubiquitin-protein ligase RAD18
- Ubiquitin-conjugating enzyme E2 N
- Ubiquitin-conjugating enzyme E2 variant 2
- Proliferating cell nuclear antigen
- Protein S100-A10
- DNA repair protein RAD51 homolog 1
- Fanconi anemia group M protein
- E3 ubiquitin-protein ligase HERC2
- Structure-specific endonuclease subunit MUS81
- Replication protein A 70 kDa DNA-binding subunit
Sequence:
MSWMFKRDPVWKYLQTVQYGVHGNFPRLSYPTFFPRFEFQDVIPPDDFLTSDEEVDSVLFGSLRGHVVGLRYYTGVVNNNEMVALQRDPNNPYDKNAIKVNNVNGNQVGHLKKELAGALAYIMDNKLAQIEGVVPFGANNAFTMPLHMTFWGKEENRKAVSDQLKKHGFKLGPAPKTLGFNLESGWGSGRAGPSYSMPVHAAVQMTTEQLKTEFDKLFEDLKEDDKTHEMEPAEAIETPLLPHQKQALAWMVSRENSKELPPFWEQRNDLYYNTITNFSEKDRPENVHGGILADDMGLGKTLTAIAVILTNFHDGRPLPIERVKKNLLKKEYNVNDDSMKLGGNNTSEKADGLSKDASRCSEQPSISDIKEKSKFRMSELSSSRPKRRKTAVQYIESSDSEEIETSELPQKMKGKLKNVQSETKGRAKAGSSKVIEDVAFACALTSSVPTTKKKMLKKGACAVEGSKKTDVEERPRTTLIICPLSVLSNWIDQFGQHIKSDVHLNFYVYYGPDRIREPALLSKQDIVLTTYNILTHDYGTKGDSPLHSIRWLRVILDEGHAIRNPNAQQTKAVLDLESERRWVLTGTPIQNSLKDLWSLLSFLKLKPFIDREWWHRTIQRPVTMGDEGGLRRLQSLIKNITLRRTKTSKIKGKPVLELPERKVFIQHITLSDEERKIYQSVKNEGRATIGRYFNEGTVLAHYADVLGLLLRLRQICCHTYLLTNAVSSNGPSGNDTPEELRKKLIRKMKLILSSGSDEECAICLDSLTVPVITHCAHVFCKPCICQVIQNEQPHAKCPLCRNDIHEDNLLECPPEELARDSEKKSDMEWTSSSKINALMHALTDLRKKNPNIKSLVVSQFTTFLSLIEIPLKASGFVFTRLDGSMAQKKRVESIQCFQNTEAGSPTIMLLSLKAGGVGLNLSAASRVFLMDPAWNPAAEDQCFDRCHRLGQKQEVIITKFIVKDSVEENMLKIQNKKRELAAGAFGTKKPNADEMKQAKINEIRTLIDL
Protein: Blr1131 protein (Q89VB6)
Organism: Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110)
Interaction partners:
- Thiol:disulfide interchange protein TlpA
- Cytochrome c oxidase subunit 2
- Cytochrome c oxidase assembly protein CtaG
- Heme A synthase
- Alternative cytochrome c oxidase subunit 2
- Bll4481 protein
- Ubiquinol oxidase subunit 2
- Ubiquinol oxidase polypeptide II
- Protoheme IX farnesyltransferase
- Bll4880 protein
Sequence:
MSSATRPLVIATAFAASLIVGLLIMFWAMGGVGKVAQPAAIGGPFQLTDQNGKAVTDKSLKGKPTLIFFGYTHCPDVCPTSLFEISEVLRAMGKDADKVNAIFISVDPERDTPATMKNYLSSFDPHLEGLSGDPAEIAKVITSYRVYAKKVPTKDGDYTMDHTALIYLMDRDGRFVSPFNLKRTPEEAAADLKRYL
Protein: Tubulin-specific chaperone E (Tubulin-folding cofactor E) (Q32KS0)
Organism: Bos taurus (Bovine)
Function: Tubulin-folding protein; involved in the second step of the tubulin folding pathway and in the regulation of tubulin heterodimer dissociation. Required for correct organization of microtubule cytoskeleton and mitotic splindle, and maintenance of the neuronal microtubule network.
Subcellular location: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}.
Interaction partners:
- Tubulin-specific chaperone D
- Tubulin-folding cofactor B
- Tubulin-specific chaperone C
- Tubulin-specific chaperone A
- Tubulin-specific chaperone A
- ADP-ribosylation factor-like protein 2
Sequence:
MNSTSTSDVIGRRVEVNGEHATVRFSGLVPPVAGLWLGVEWDNPERGKHDGSHEGTVYFKCRHPTAGSFIRPHKVNFGVDFLTAIKNRYVLEDEPKEEETEQIVIIGNKPVETIGFDSVIKQQSQLSKLQDVSLRNCAVNGAGDKGEIAKACPNIRSIDLSKNLLSSWEEVIDIADQLKHLEVLNLSENKLTSPSSSPSPTGTFPTLKVLVLNRTGVTWAEVLRCASGWPVLEKLYLESNNIIISERPTDVLQTVKLLDLSSNQLIDENQLFLIAYLPRLEQLILSDIGISSIHFPDAGIGCKTSMFPSLQYLVLNDNQIAQWSFMNELDKLQSLHALSCTRNPLTEGSKDAQTTRQFIIARIGQLRTLNKCAIEPEERRGAELDYRKAFGNEWKKAGGHQDPEKNRPNEEFLAAHPRYQALCLKYGAPEDGELKTQQPFLLKNQLLTLKIKYPNQHDQKVIEKQLPDSMTVQKVKGLLSRLLKVPVSELLLSYESPKMPGKEVELENDLQPLRFYSVENGDCLLVRW
Protein: Somatostatin [Cleaved into: Antrin; Somatostatin-28; Somatostatin-14; Neuronostatin (NST)] (P60041)
Organism: Mus musculus (Mouse)
Function: Inhibits the secretion of pituitary hormones, including that of growth hormone/somatotropin (GH1), PRL, ACTH, luteinizing hormone (LH) and TSH. Also impairs ghrelin- and GnRH-stimulated secretion of GH1 and LH; the inhibition of ghrelin-stimulated secretion of GH1 can be further increased by neuronostatin.
Subcellular location: Secreted {ECO:0000250|UniProtKB:P60042}.
Interaction partners:
- Somatostatin receptor type 2
- Somatostatin receptor type 1
- Somatostatin receptor type 5
- Somatostatin receptor type 4
- Somatostatin receptor type 3
- Cortistatin
- Pancreatic polypeptide prohormone
- Pro-neuropeptide Y
- Parvalbumin alpha
- Pro-glucagon
Sequence:
MLSCRLQCALAALCIVLALGGVTGAPSDPRLRQFLQKSLAAATGKQELAKYFLAELLSEPNQTENDALEPEDLPQAAEQDEMRLELQRSANSNPAMAPRERKAGCKNFFWKTFTSC
Protein: RNA-binding protein, putative (Q388P1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MADRGDARVVHVFVDDLSAVLAEDVHEWLRIIGDIDELKMRYDASRQRSFYWVRFHQSSAARLAVDHLDGERLKNHAIEIHSNVFKKQTAAVATLEGAAGGVQEEKTKLEMNPNLPKNHLMPRDLQMDELLVRAIPEMLETSEQAAEGGELLQRLLELQESYCRAQESLERTTEGIRETDGELTALLRGETTAATDVSGPSSEGFVQGNTPLASARIRNAVPVPLSTCDPAGLLSKLTRHVGPVADYAFSFASNGGSFATVVELFHPDDADFALALLTGRRMVSKSTEKHADAEDALAALVGFGWEAEASVAPLTPPSVPQASFAAHNRVATILRSCRSVA
Protein: Probable plastid-lipid-associated protein 12, chloroplastic (Fibrillin-10) (Q8LAP6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Plastid, chloroplast thylakoid {ECO:0000269|PubMed:22274653}. Note=Located in thylakoid as a peripheral protein at the stromal side. {ECO:0000269|PubMed:22274653}.
Interaction partners:
- Threonylcarbamoyl-AMP synthase
- Nucleusenvelope protein
- At4g13500
- Fibrillin-5, chloroplastic
- Protein TIC 20-I, chloroplastic
- Probable inactive ATP-dependent zinc metalloprotease FTSHI 5, chloroplastic
- Dehydration-responsive element-binding protein 2F
- Anthranilate synthase alpha subunit 2, chloroplastic
- Protein TIC 56, chloroplastic
- Probable plastid-lipid-associated protein 1, chloroplastic
Sequence:
MVAVRFYAVEMSLPCLCPCPSSPISLSLCSPRFNLLNTTSRRLGLSRNCRTLRISCSSSSTVTDQTQQSSFNDAELKLIDALIGIQGRGKSASPKQLNDVESAVKVLEGLEGIQNPTDSDLIEGRWRLMFTTRPGTASPIQRTFTGVDVFTVFQDVYLKATNDPRVSNIVKFSDFIGELKVEAVASIKDGKRVLFRFDRAAFDLKFLPFKVPYPVPFRLLGDEAKGWLDTTYLSPSGNLRISRGNKGTTFVLQKETVPRQKLLATISQDKGVAEAIDEFLASNSNSAEDNYELLEGSWQMIWSSQMYTDSWIENAANGLMGRQIIEKDGRIKFEVNIIPAFRFSMKGKFIKSESSTYDLKMDDAAIIGGAFGYPVDITNNIELKILYTDEKMRISRGFDNIIFVHIREI
Protein: Phospholipase D delta (AtPLDdelta) (PLD delta) (EC 3.1.4.4) (Q9C5Y0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Hydrolyzes glycerol-phospholipids at the terminal phosphodiesteric bond to generate phosphatidic acids (PA). May be involved in PA accumulation in the dehydration stress response and in the transduction of hormonal and environmental signals to the microtubules cytoskeleton. Prefers phosphatidylethanolamine to phosphatidylcholine as substrate. Involved in H(2)O(2) and abscisic acid (ABA)-induced stomatal closure. Involved in nitric oxide (NO) signaling during stomatal closure. Plays a positive role in ABA-promoted senescence. Involved in basal defense and nonhost resistance.
Subcellular location: Cell membrane {ECO:0000269|PubMed:11706190, ECO:0000269|PubMed:23979971}; Peripheral membrane protein. Note=Colocalization with cortical microtubules also occurs. {ECO:0000269|PubMed:11549769}.
Interaction partners:
- CDP-diacylglycerol--serine O-phosphatidyltransferase 1
- Non-specific phospholipase C4
- Non-specific phospholipase C1
- Non-specific phospholipase C5
- Non-specific phospholipase C6
- Non-specific phospholipase C2
- Phosphatidyl-N-methylethanolamine N-methyltransferase
- Phosphatidylserine decarboxylase proenzyme 3
- Phosphatidylserine decarboxylase proenzyme 2
- Phosphatidylserine decarboxylase proenzyme 1, mitochondrial
Sequence:
MAEKVSEDVMLLHGDLDLKIVKARRLPNMDMFSEHLRRLFTACNACARPTDTDDVDPRDKGEFGDKNIRSHRKVITSDPYVTVVVPQATLARTRVLKNSQEPLWDEKFNISIAHPFAYLEFQVKDDDVFGAQIIGTAKIPVRDIASGERISGWFPVLGASGKPPKAETAIFIDMKFTPFDQIHSYRCGIAGDPERRGVRRTYFPVRKGSQVRLYQDAHVMDGTLPAIGLDNGKVYEHGKCWEDICYAISEAHHMIYIVGWSIFHKIKLVRETKVPRDKDMTLGELLKYKSQEGVRVLLLVWDDKTSHDKFGIKTPGVMGTHDEETRKFFKHSSVICVLSPRYASSKLGLFKQQASPSSSIYIMTVVGTLFTHHQKCVLVDTQAVGNNRKVTAFIGGLDLCDGRYDTPEHRILHDLDTVFKDDFHNPTFPAGTKAPRQPWHDLHCRIDGPAAYDVLINFEQRWRKATRWKEFSLRLKGKTHWQDDALIRIGRISWILSPVFKFLKDGTSIIPEDDPCVWVSKEDDPENWHVQIFRSIDSGSVKGFPKYEDEAEAQHLECAKRLVVDKSIQTAYIQTIRSAQHFIYIENQYFLGSSYAWPSYRDAGADNLIPMELALKIVSKIRAKERFAVYVVIPLWPEGDPKSGPVQEILYWQSQTMQMMYDVIAKELKAVQSDAHPLDYLNFYCLGKREQLPDDMPATNGSVVSDSYNFQRFMIYVHAKGMIVDDEYVLMGSANINQRSMAGTKDTEIAMGAYQPNHTWAHKGRHPRGQVYGYRMSLWAEHLGKTGDEFVEPSDLECLKKVNTISEENWKRFIDPKFSELQGHLIKYPLQVDVDGKVSPLPDYETFPDVGGKIIGAHSMALPDTLTT
Protein: RICTOR_N domain-containing protein (G5EFK2)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MDTRRKVYHRGENNTQRIQEIRESIRVKTRAKKVSETSEKRRERFRAREDVQKLIRGADSYTKATYEEKCEFLNGISRTILETTVESLTDNEFFEDICQLVLKFLPDDHPCIRAMCFHMVRKCTINERNLVVILTTHVDIFIVRAIDLQMENQTERLEAFKLIIWMLKIYEKSNLKKLIDSSAAQKNGKKYAFPKSIMQPIISIALSAFEGQQTTGKDKLTLPCVGLFLEFSLTEPLLVLEMAGTDWLVKALTGVSCMSRRIVLLASHVLISWLDSPTIRIKAHLDLVMEQIFAPLVEFGLFQKRGSMLTNDNANEAFHMNDFLENFKCSFLRIIRSWPGLFACAAVGPNSNIRPSSPFRLLDYLGLGTVANDNLVRIRDTIVDLCCEFVDVPYANKTFESWEEALSFYKTMHLPDKFKSNLKNDFVIAQNDARLKNDTERRKPTIDLLAAFRVLSQFVLINAQLPLSLARLILAMPDSSSGLKATLLMADMLRQAPSHVPMGYRAPVLSMPTLVQSACESLSQSHAVAAINGTFDINTTEQYTFLHATNAELVLNRFDKLNQSWIRSASTSSTVLKESDLMLFSPHMSEPIPLASTMKKSKSDSSFRSGGSFFKRNTSPDVYEEESPGEFSETVLRGRYDKNALMLMDDADDYDYAAPNIRDTLDDEEENAKKFFVDSTGAFDWNYVEYYVENIEKDGYEKLLKEFTSNTIQVHISNMFQYISPSEQEKHKRCIDRQQVIVTKSLIKLLLRVFQKEAHISDAYQPIFLKYVESFKALLEKRSNPNAYFAARNLSYTNSMLHFAIIGTFTMTSKGLSILTNAGVLHMYVDILSSTSQLEYTKVIISSLDYTNEGMVRVIIGKALTSTSEASRKWTTRYLAVLASFDLPTFSDWGIQYMLRQLADESSKVVRHTIRILNRWLPEHPSRNLRKIDWSLFGEAGDLLRAHVFAMESECASDEDEVRDVVRFWMSDFNKKYLNIIDEEMKEMMFHVKRSIDGSFSRSSSDIPDTSLGVQAPLHLFAALGSHETGRHILIDENVAEDLLSICKTGKCFEEIKASLLAVSSIGSTDGGFEILPADAVPVVIKIAEEHPVLTVRGIAFWALCTFSQCIEGAKRLGSFGWESNRFRYAMDLAKSKVVADDEPGTPGGATPGSTCSSWRPARKITIQSHRNSSMVDSQNNVKQSRAKSESALVRRGHSKGRSRSQSTGDIHEVIAKRESRIDSFFNQRLWNSEKYLYKTSGTSDSSSIPYHKRTVTNSSSGYHIQDDTTAVTISPPNHLNMEENVCKSAATSRISTDRRRANTTNSLFDEEEAPKTRSSTVARCIRDGLKITTEQLEAEGVLADGIMELHFSCRLREKYHLTAFRVRACLQITRHVGDPVRYVFMTREEERHFADYRRQVLRDPWLYNELKKEDNTVKKTINVVPIQTVALPTEIEIMCGNIFPAKPKSDPIFSFHENDDSAGVEDRGARTGHARSGIHIQPHSAYRCFHCSSNEDSVRIYPHPDAPMLRKEVLGHVDMLEIKEYPAKRLIGLRQHHPWLFEWPCMYADVLELLDEYRFKPHSRAFLQQIFYDALQL
Protein: Zinc finger protein 212 (A0A090N8N3)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAESAPARHRRKRRSTPLTSSTLPSQATEKSSYFQTTEISLWTVVAAIQAVEKKMESQAARLQSLEGRTGTAEKKLADCEKMAVEFGNQLEGKWAVLGTLLQEYGLLQRRLENVENLLRNRNFWILRLPPGSKGEAPKVSRSLENDGVCFTEQEWENLEDWQKELYRNVMESNYETLVSLKVLGQTEGEAELGTEMLGDLEEEGPGGAHPAGGVMIKQELQYTQEGPADLPGEFSCIAEEQAFLSPEQTELWGGQGSSVLLETGPGDSTLEEPVGSRVPSSSRTVGCPKQKSHRQVQLDQECGQGLKLKKDTSRPYECSECEITFRYKQQLATHLRSHSGWGSCTPEEPEESLRPRPRLKPQTKKAKLHQCDVCLRSFSCKVSLVTHQRCHLQEGPSAGQHVQERFSPNSLVALPGHIPWRKSRSSLICGYCGKSFSHPSDLVRHQRIHTGERPYSCTECEKSFVQKQHLLQHQKIHQRERGGLALEPGRPNGLL
Protein: Protein disulfide-isomerase (PDI) (EC 5.3.4.1) (Cellular thyroid hormone-binding protein) (Prolyl 4-hydroxylase subunit beta) (P04785)
Organism: Rattus norvegicus (Rat)
Function: This multifunctional protein catalyzes the formation, breakage and rearrangement of disulfide bonds. At the cell surface, seems to act as a reductase that cleaves disulfide bonds of proteins attached to the cell. May therefore cause structural modifications of exofacial proteins. Inside the cell, seems to form/rearrange disulfide bonds of nascent proteins. At high concentrations and following phosphorylation by FAM20C, functions as a chaperone that inhibits aggregation of misfolded proteins. At low concentrations, facilitates aggregation (anti-chaperone activity). May be involved with other chaperones in the structural modification of the TG precursor in hormone biogenesis. Also acts as a structural subunit of various enzymes such as prolyl 4-hydroxylase and microsomal triacylglycerol transfer protein MTTP. Receptor for LGALS9; the interaction retains P4HB at the cell surface of Th2 T helper cells, increasing disulfide reductase activity at the plasma membrane, altering the plasma membrane redox state and enhancing cell migration.
Subcellular location: Endoplasmic reticulum {ECO:0000250|UniProtKB:P07237}. Endoplasmic reticulum lumen {ECO:0000250|UniProtKB:P07237}. Melanosome {ECO:0000250|UniProtKB:P07237}. Cell membrane {ECO:0000250|UniProtKB:P09103}; Peripheral membrane protein {ECO:0000305}. Note=Highly abundant. In some cell types, seems to be also secreted or associated with the plasma membrane, where it undergoes constant shedding and replacement from intracellular sources. Localizes near CD4-enriched regions on lymphoid cell surfaces. Colocalizes with MTTP in the endoplasmic reticulum. {ECO:0000250|UniProtKB:P07237}.
Interaction partners:
- Prolyl 4-hydroxylase subunit alpha 2
- Endoplasmic reticulum chaperone BiP
- Prolyl 4-hydroxylase subunit alpha-1
- Endoplasmin
- Microsomal triglyceride transfer protein large subunit
- Prolyl 4-hydroxylase subunit alpha-3
- ERO1-like protein alpha
- Calreticulin
- Peptidyl-prolyl cis-trans isomerase B
- Hypoxia up-regulated protein 1
Sequence:
MLSRALLCLALAWAARVGADALEEEDNVLVLKKSNFAEALAAHNYLLVEFYAPWCGHCKALAPEYAKAAAKLKAEGSEIRLAKVDATEESDLAQQYGVRGYPTIKFFKNGDTASPKEYTAGREADDIVNWLKKRTGPAATTLSDTAAAESLVDSSEVTVIGFFKDAGSDSAKQFLLAAEAVDDIPFGITSNSDVFSKYQLDKDGVVLFKKFDEGRNNFEGEITKEKLLDFIKHNQLPLVIEFTEQTAPKIFGGEIKTHILLFLPKSVSDYDGKLSNFKKAAEGFKGKILFIFIDSDHTDNQRILEFFGLKKEECPAVRLITLEEEMTKYKPESDELTAEKITQFCHHFLEGKIKPHLMSQELPEDWDKQPVKVLVGKNFEEVAFDEKKNVFVEFYAPWCGHCKQLAPIWDKLGETYKDHENIVIAKMDSTANEVEAVKVHSFPTLKFFPASADRTVIDYNGERTLDGFKKFLESGGQDGAGDNDDLDLEEALEPDMEEDDDQKAVKDEL
Protein: peptidylprolyl isomerase (EC 5.2.1.8) (Q9V3V2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSKSNLVISCLLLVAISNSLVRAQDLKVEVISTPEVCEQKSKNGDSLTMHYTGTLQADGKKFDSSFDRDQPFTFQLGAGQVIKGWDQGLLNMCVGEKRKLTIPPQLGYGDQGAGNVIPPKATLLFDVELINIGNAPPTTNVFKEIDDNADKQLSREEVSEYLKKQMTAVEGQDSEELKNMLAENDKLVEEIFQHEDKDKNGFISHDEFSGPKHDEL
Protein: ER membrane protein complex subunit 2 (Q57VI5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|RuleBase:RU367091}; Peripheral membrane protein {ECO:0000256|RuleBase:RU367091}; Cytoplasmic side {ECO:0000256|RuleBase:RU367091}.
Interaction partners:
- ER membrane protein complex subunit 4
- ER membrane protein complex subunit 6
- ER membrane protein complex subunit 3
- ER membrane protein complex subunit 1
- MPN domain-containing protein
- ER membrane protein complex subunit 7 beta-sandwich domain-containing protein
Sequence:
MKGPTDNVAESNISLQSLTPLGVKQLSRKEKRELLQLHREKETRNSNVVLLLGTDLLAGGTSGIGSQELFCIYEQILIAALDCGRVDTSRQYLSLLQKQFGRQSVRVRRLEGLCLEAEGRAEEAEGHYRALLKDFPSDDFPVKRLSTMLKSEGKYHKAIEVLEKQLVYTDVNDEKHTFLELHGGNCLSVYRELSNLHYLCENYTKALHHANEAMLLSSSCYLSHTRLAELYYMAGDHRHSLVEYAQSLRLNDHPNNSRAAYGLWVVANEIIRQSKSSTASRVGDEQKEEAVSLRAWAEKKLVDMYKGSPMLSALEAMLHRDD
Protein: IKAROS family zinc finger 1 (A0A0A0MRA0)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MDADEGQDMSQVSGDKGLSDTPYDSSASYEKENEMMKSHVMDQAINNAINYLGAESLRPLVQTPPGGSEVVPVISPMYQLHKPLAEGTPRSNHSAQDSAVENLLLLSKAKLVPSEREASPSNSCQDSTDTESNNEEQRSGLIYLTNHIAPHARNGLSLKEEHRAYDLLRAASENSQDALRVVSTSGEQMKVYKCEHCRVLFLDHVMYTIHMGCHGFRDPFECNMCGYHSQDRYEFSSHITRGEHRFHMS
Protein: Photosystem I assembly protein Ycf3 (P0C517)
Organism: Oryza sativa subsp. indica (Rice)
Function: Essential for the assembly of the photosystem I (PSI) complex. May act as a chaperone-like factor to guide the assembly of the PSI subunits.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000255|HAMAP-Rule:MF_00439}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_00439}.
Interaction partners:
- Photosystem I iron-sulfur center
- Photosystem I P700 chlorophyll a apoprotein A2
- Photosystem I P700 chlorophyll a apoprotein A1
- Photosystem I reaction center subunit II
- NAD
- Photosystem I reaction center subunit III
- Uncharacterized protein
- Cytochrome b6-f complex subunit 4
- Photosystem II CP47 reaction center protein
- ATP synthase subunit b, chloroplastic
Sequence:
MPRSRINGNFIDKTFSIVANILLRIIPTTSGEKRAFTYYRDGMLAQSEGNYAEALQNYYEAMRLEIDPYDRSYILYNIGLIHTSNGEHTKALEYYFRALERNPFLPQAFNNMAVICHYRGEQAILQGDSEIAEAWFDQAAEYWKQAIALTPGNYIEAQNWLKITKRFEFE
Protein: Mitochondrial prohibitin complex protein 1 (Prohibitin-1) (Q9BKU4)
Organism: Caenorhabditis elegans
Function: PHB proteins are essential during embryonic development and are required for somatic and germline differentiation in the larval gonad. A deficiency in PHB proteins results in altered mitochondrial biogenesis in body wall muscle cells.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:12794069}.
Interaction partners:
- Mitochondrial prohibitin complex protein 2
- AFG3-like protein spg-7
- Probable voltage-dependent anion-selective channel
- AAA+ ATPase domain-containing protein
- Stomatin-like protein stl-1
- ATP-dependent zinc metalloprotease YME1 homolog
- Heat shock protein hsp-6
- Conserved regulator of innate immunity protein 3
- Mitochondrial-processing peptidase subunit alpha
- ATP synthase subunit beta, mitochondrial
Sequence:
MAASAQKLLGRLGTVGVGLSIAGGIAQTALYNVDGGQRAVIFDRFSGVKNEVVGEGTHFLIPWVQKPIIFDIRSTPRAVTTITGSKDLQNVNITLRILHRPSPDRLPNIYLNIGLDYAERVLPSITNEVLKAVVAQFDAHEMITQREVVSQRASVALRERAAQFGLLLDDIAITHLNFGREFTEAVEMKQVAQQEAEKARYLVEKAEQMKIAAVTTAEGDAQAAKLLAKAFASAGDGLVELRKIEAAEEIAERMAKNKNVTYLPGNQQTLLNLQS
Protein: RecQ-mediated genome instability protein 1 (BLM-associated protein of 75 kDa) (BLAP75) (FAAP75) (Q9H9A7)
Organism: Homo sapiens (Human)
Function: Essential component of the RMI complex, a complex that plays an important role in the processing of homologous recombination intermediates to limit DNA crossover formation in cells. Promotes TOP3A binding to double Holliday junctions (DHJ) and hence stimulates TOP3A-mediated dissolution. Required for BLM phosphorylation during mitosis. Within the BLM complex, required for BLM and TOP3A stability.
Subcellular location: Nucleus {ECO:0000269|PubMed:15775963}. Note=Forms foci in response to DNA damage.
Interaction partners:
- Fanconi anemia group M protein
- Replication protein A 70 kDa DNA-binding subunit
- RecQ-mediated genome instability protein 2
- RecQ-like DNA helicase BLM
- Replication protein A 32 kDa subunit
- DNA topoisomerase 3-alpha
- Fanconi anemia group F protein
- Replication protein A 14 kDa subunit
- Centromere protein S
- Fanconi anemia core complex-associated protein 100
Sequence:
MNVTSIALRAETWLLAAWHVKVPPMWLEACINWIQEENNNVNLSQAQMNKQVFEQWLLTDLRDLEHPLLPDGILEIPKGELNGFYALQINSLVDVSQPAYSQIQKLRGKNTTNDLVTAEAQVTPKPWEAKPSRMLMLQLTDGIVQIQGMEYQPIPILHSDLPPGTKILIYGNISFRLGVLLLKPENVKVLGGEVDALLEEYAQEKVLARLIGEPDLVVSVIPNNSNENIPRVTDVLDPALGPSDEELLASLDENDELTANNDTSSERCFTTGSSSNTIPTRQSSFEPEFVISPRPKEEPSNLSIHVMDGELDDFSLEEALLLEETVQKEQMETKELQPLTFNRNADRSIERFSHNPNTTNNFSLTCKNGNNNWSEKNVSEQMTNEDKSFGCPSVRDQNRSIFSVHCNVPLAHDFTNKEKNLETDNKIKQTSSSDSHSLNNKILNREVVNYVQKRNSQISNENDCNLQSCSLRSSENSINLSIAMDLYSPPFVYLSVLMASKPKEVTTVKVKAFIVTLTGNLSSSGGIWSITAKVSDGTAYLDVDFVDEILTSLIGFSVPEMKQSKKDPLQYQKFLEGLQKCQRDLIDLCCLMTISFNPSLSKAMVLALQDVNMEHLENLKKRLNK
Protein: AN1-type zinc finger protein 2B (Arsenite-inducible RNA-associated protein-like protein) (AIRAP-like protein) (Q8WV99)
Organism: Homo sapiens (Human)
Function: Plays a role in protein homeostasis by regulating both the translocation and the ubiquitin-mediated proteasomal degradation of nascent proteins at the endoplasmic reticulum. It is involved in the regulation of signal-mediated translocation of proteins into the endoplasmic reticulum. It also plays a role in the ubiquitin-mediated proteasomal degradation of proteins for which signal-mediated translocation to the endoplasmic reticulum has failed. May therefore function in the endoplasmic reticulum stress-induced pre-emptive quality control, a mechanism that selectively attenuates the translocation of newly synthesized proteins into the endoplasmic reticulum and reroutes them to the cytosol for proteasomal degradation (By similarity). By controlling the steady-state expression of the IGF1R receptor, indirectly regulates the insulin-like growth factor receptor signaling pathway.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q91X58}; Lipid-anchor {ECO:0000250|UniProtKB:Q91X58}.
Interaction partners:
- Polyubiquitin-C
- Polyubiquitin-B
- Ubiquitin-ribosomal protein eS31 fusion protein
- Ubiquitin-ribosomal protein eL40 fusion protein
- Proteasomal ATPase-associated factor 1
- 26S proteasome non-ATPase regulatory subunit 6
- Transitional endoplasmic reticulum ATPase
- 26S proteasome regulatory subunit 10B
- 26S proteasome regulatory subunit 8
Sequence:
MEFPDLGAHCSEPSCQRLDFLPLKCDACSGIFCADHVAYAQHHCGSAYQKDIQVPVCPLCNVPVPVARGEPPDRAVGEHIDRDCRSDPAQQKRKIFTNKCERAGCRQREMMKLTCERCSRNFCIKHRHPLDHDCSGEGHPTSRAGLAAISRAQAVASTSTVPSPSQTMPSCTSPSRATTRSPSWTAPPVIALQNGLSEDEALQRALEMSLAETKPQVPSCQEEEDLALAQALSASEAEYQRQQAQSRSSKPSNCSLC