wanglab/gogpt-training-data huggingface dataset:
Protein: Autophagy-related protein 5 (Q3V5I7)
Organism: Caenorhabditis elegans
Function: Involved in autophagic vesicle formation (By similarity). Conjugation with lgg-3/ATG12, through a ubiquitin-like conjugating system involving atg-7 as an E1-like activating enzyme and atg-10 as an E2-like conjugating enzyme, is essential for its function (By similarity). Most likely a component of an atg-5-lgg-3-atg-16 complex that promotes autophagosome formation by associating with lgg-2, but not lgg-1, at the preautophagosomal membrane. Probably, as part of an atg-5-lgg-3-atg-16 complex, required for lgg-1 lipidation; the complex acts as an E3-like enzyme promoting atg-3-mediated lgg-1 lipidation (Probable). Furthermore, association with atg-16.2 is required for the nucleation of lgg-1 positive autophagic vesicles.
Subcellular location: Preautophagosomal structure membrane {ECO:0000255|RuleBase:RU361202, ECO:0000269|PubMed:24185444}; Peripheral membrane protein {ECO:0000255|RuleBase:RU361202}.
Interaction partners:
- Ubiquitin-like protein atg-12
- Ubiquitin-like-conjugating enzyme ATG3
- Autophagic-related protein 16.1
- Ubiquitin-like modifier-activating enzyme ATG7
- Autophagic-related protein 16.2
- Phosphatidylinositol 3-kinase catalytic subunit type 3
- Autophagy-related protein 18
- Serine/threonine-protein kinase unc-51
- Ubiquitin-like-conjugating enzyme ATG10
- Autophagy-related protein 13 homolog
Sequence:
MDYEVCRKVWESHVPCQFTLQSSGGTHGEPLPFYTMLPRFSYLALAIQKVLSSFNRRDDGEKVHSDKMWLEHNGIPLKMYIPIGVIYDQANLSENDSILEIIVRTSQPPPQFQMVDRDMMEAMFMQNIKEADYLKTKAEITKNMMKDESAQLWRSVCNIPDNFDEFWTIVQKLMETSEGNEFAHIPLRVYVKNQAFKQALITAKHPDGSLRTIGEAVSDVLSSSSSSSTDSQSEHPPRLISHGIDIPHHTPLIFAAKNLSYPDNFIHVVLLLVVP
Protein: Protein-arginine deiminase type-2 (EC 3.5.3.15) (PAD-H19) (Peptidylarginine deiminase II) (Protein-arginine deiminase type II) (Q9Y2J8)
Organism: Homo sapiens (Human)
Function: Catalyzes the deimination of arginine residues of proteins.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12392711}.
Interaction partners:
- Histone H3.2
- Histone H3.1
- GDP-fucose protein O-fucosyltransferase 2
Sequence:
MLRERTVRLQYGSRVEAVYVLGTYLWTDVYSAAPAGAQTFSLKHSEHVWVEVVRDGEAEEVATNGKQRWLLSPSTTLRVTMSQASTEASSDKVTVNYYDEEGSIPIDQAGLFLTAIEISLDVDADRDGVVEKNNPKKASWTWGPEGQGAILLVNCDRETPWLPKEDCRDEKVYSKEDLKDMSQMILRTKGPDRLPAGYEIVLYISMSDSDKVGVFYVENPFFGQRYIHILGRRKLYHVVKYTGGSAELLFFVEGLCFPDEGFSGLVSIHVSLLEYMAQDIPLTPIFTDTVIFRIAPWIMTPNILPPVSVFVCCMKDNYLFLKEVKNLVEKTNCELKVCFQYLNRGDRWIQDEIEFGYIEAPHKGFPVVLDSPRDGNLKDFPVKELLGPDFGYVTREPLFESVTSLDSFGNLEVSPPVTVNGKTYPLGRILIGSSFPLSGGRRMTKVVRDFLKAQQVQAPVELYSDWLTVGHVDEFMSFVPIPGTKKFLLLMASTSACYKLFREKQKDGHGEAIMFKGLGGMSSKRITINKILSNESLVQENLYFQRCLDWNRDILKKELGLTEQDIIDLPALFKMDEDHRARAFFPNMVNMIVLDKDLGIPKPFGPQVEEECCLEMHVRGLLEPLGLECTFIDDISAYHKFLGEVHCGTNVRRKPFTFKWWHMVP
Protein: Uncharacterized transcriptional regulatory protein C530.11c (O59746)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Uncharacterized transcriptional regulatory protein C2H10.01
- Uncharacterized transcriptional regulatory protein C320.03
- Transcription factor fil1
- Transcription factor cbf12
Sequence:
MLENSTAVHGVRLSDSPEDPFLRKRLASNTQLNQKKIRFTENENDLSPERAQKEPVSIPHGRYTWSTSPDTDSSHLPSTPPTVDIPFHHPHTIHSPTFTLSVSPDSQSSSATHQNDYISSPHADFSFSPPASKIQSHEPLNDMAAVHPLRPSHVSGPLSPPEPKAASVDHSINPAYNASFRLPDGPLWTEGSENLPSLDIQLQLAHIYFIYAHGQPYVLFHRDSFMEALKSQRLPPVLVLAMCAVAIRFWQTDKYDKNELFEQWFNRASAIAMANFDKLDLVYVASFVMLSYVCAATSKYWMFAGMAIRMVVALHPNKTPNLPYYDRPDSPLPFEIRVQLTRRLFWDCFMLDRLNSLYCNTQFLNLEDIHVPLPMRETLFMYKAHAVTETLTGKPSSPDSFTNANPTTAPIVSRNAQDNMGMLAYMIRMVSIWGRVVRCLKSYSQKQSNPYPFWHAKSTFKQLDQELYEWEKNLPNRLRYSRQTLLSYHMMGQGGQFACLHLIFLQIHLYVHRYAASISSVPFSHVKSPPTVFENQSAVLASQCANAICRIIQDCTELSISLAAPFTASSAYLAGTVLLYHYITRGSEVQASKAAVHLPIAKRHLAQLSVYWPALGMYAKALDAIAFHQGALVTPSVPPVIATVSKTNTTNTGVQQRGNVGVTTTGSILTQSSPALPVQPVPLAYSKPAPTTKSSLTELAYNTNVSLPPRSPGTGSLAAGNLPNEKAPSLMTMVNGGPVPGDIGEASIPVVQNLQPSTAHVDPESDLGRVIKICDWYQSPSSDVLLSKPLQLNSSEEMEQQCIDLSRHNTLLNLSSYGI
Protein: cAMP-dependent protein kinase catalytic subunit, putative (EC 2.7.11.1) (E9QXD5)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Interaction partners:
- cAMP-dependent protein kinase regulatory subunit
- Adenylate cyclase
- Mitogen-activated protein kinase mpkA
- RAS small monomeric GTPase RasA
- Ras-like protein B
- cAMP-dependent protein kinase
- non-specific serine/threonine protein kinase
- Cell pattern formation-associated protein stuA
Sequence:
MATGKAEPSTHSEIPSSSPPSRGVDTPLEDVQKREKQMVASFRPPHQRSVNPFVIKDRLEERQLGISTRTLCVNDFTLIKTLGTGTFARVWLAKFKDETIRRDNVYALKVLRKADVIKLKQVEHVRNERKALAAVAGHPFITTLIASFSDEQSLYMLLDYCPGGEIFSYLRRARRFNETTSRFYAAEITLTIEYLHDVEGIVYRDLKPENILLDADGHIKLVDFGFAKQINDRETYTLCGTPEYLAPEVIHNSGHGLAVDWWALGILIYEFLVGQPPFWDQNPMRIYEQIVEGRLRFPPNMSPAAQNIISCLCKTNPSERLGHISGGSARVKAHPFFEDIDWDDLFHRRMKGPIIPRVDHPADTGNFEDYPDVDVKGQAIYTDDMKKKYEALFSDF
Protein: Protein patched homolog 2 (PTC2) (O35595)
Organism: Mus musculus (Mouse)
Function: Plays a role in the control of cellular growth (By similarity). May have a role in epidermal development. May act as a receptor for Sonic hedgehog (SHH).
Subcellular location: Membrane; Multi-pass membrane protein.
Interaction partners:
- Desert hedgehog protein
- Indian hedgehog protein
- Sonic hedgehog protein
- Protein smoothened
- Brother of CDO
- Cell adhesion molecule-related/down-regulated by oncogenes
- Growth arrest-specific protein 1
- Protein patched homolog 1
- E3 ubiquitin-protein ligase SMURF1
- E3 ubiquitin-protein ligase SMURF2
Sequence:
MVRPLSLGELPPSYTPPARSSAPHILAGSLQAPLWLRAYFQGLLFSLGCRIQKHCGKVLFLGLVAFGALALGLRVAVIETDLEQLWVEVGSRVSQELHYTKEKLGEEAAYTSQMLIQTAHQEGGNVLTPEALDLHLQAALTASKVQVSLYGKSWDLNKICYKSGVPLIENGMIERMIEKLFPCVILTPLDCFWEGAKLQGGSAYLPGRPDIQWTNLDPQQLLEELGPFASLEGFRELLDKAQVGQAYVGRPCLDPDDPHCPPSAPNRHSRQAPNVAQELSGGCHGFSHKFMHWQEELLLGGTARDLQGQLLRAEALQSTFLLMSPRQLYEHFRGDYQTHDIGWSEEQASMVLQAWQRRFVQLAQEALPANASQQIHAFSSTTLDDILRAFSEVSTTRVVGGYLLMLAYACVTMLRWDCAQSQGAVGLAGVLLVALAVASGLGLCALLGITFNAATTQVLPFLALGIGVDDIFLLAHAFTKAPPDTPLPERMGECLRSTGTSVALTSVNNMVAFFMAALVPIPALRAFSLQAAIVVGCNFAAVMLVFPAILSLDLRRRHRQRLDVLCCFSSPCSAQVIQMLPQELGDRAVPVGIAHLTATVQAFTHCEASSQHVVTILPPQAHLLSPASDPLGSELYSPGGSTRDLLSQEEGTGPQAACRPLLCAHWTLAHFARYQFAPLLLQTRAKALVLLFFGALLGLSLYGATLVQDGLALTDVVPRGTKEHAFLSAQLRYFSLYEVALVTQGGFDYAHSQRALFDLHQRFSSLKAVLPPPATQAPRTWLHYYRSWLQGIQAAFDQDWASGRITCHSYRNGSEDGALAYKLLIQTGNAQEPLDFSQLTTRKLVDKEGLIPPELFYMGLTVWVSSDPLGLAASQANFYPPPPEWLHDKYDTTGENLRIPAAQPLEFAQFPFLLHGLQKTADFVEAIEGARAACTEAGQAGVHAYPSGSPFLFWEQYLGLRRCFLLAVCILLVCTFLVCALLLLSPWTAGLIVLVLAMMTVELFGIMGFLGIKLSAIPVVILVASIGIGVEFTVHVALGFLTSHGSRNLRAASALEQTFAPVTDGAVSTLLGLLMLAGSNFDFIIRYFFVVLTVLTLLGLLHGLLLLPVLLSILGPPPQVVQVYKESPQTLNSAAPQRGGLRWDRPPTLPQSFARVTTSMTVALHPPPLPGAYVHPASEEPT
Protein: Phosphatidylinositol 3,4,5-trisphosphate-dependent Rac exchanger 2 protein (P-Rex2) (PtdIns(3,4,5)-dependent Rac exchanger 2) (DEP domain-containing protein 2) (Q70Z35)
Organism: Homo sapiens (Human)
Function: Functions as a RAC1 guanine nucleotide exchange factor (GEF), activating Rac proteins by exchanging bound GDP for free GTP. Its activity is synergistically activated by phosphatidylinositol 3,4,5-trisphosphate and the beta gamma subunits of heterotrimeric G protein. Mediates the activation of RAC1 in a PI3K-dependent manner. May be an important mediator of Rac signaling, acting directly downstream of both G protein-coupled receptors and phosphoinositide 3-kinase.
Interaction partners:
- Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN
- Cell division control protein 42 homolog
- Transforming protein RhoA
- Ras-related C3 botulinum toxin substrate 1
Sequence:
MSEDSRGDSRAESAKDLEKQLRLRVCVLSELQKTERDYVGTLEFLVSAFLHRMNQCAASKVDKNVTEETVKMLFSNIEDILAVHKEFLKVVEECLHPEPNAQQEVGTCFLHFKDKFRIYDEYCSNHEKAQKLLLELNKIRTIRTFLLNCMLLGGRKNTDVPLEGYLVTPIQRICKYPLILKELLKRTPRKHSDYAAVMEALQAMKAVCSNINEAKRQMEKLEVLEEWQSHIEGWEGSNITDTCTEMLMCGVLLKISSGNIQERVFFLFDNLLVYCKRKHRRLKNSKASTDGHRYLFRGRINTEVMEVENVDDGTADFHSSGHIVVNGWKIHNTAKNKWFVCMAKTPEEKHEWFEAILKERERRKGLKLGMEQDTWVMISEQGEKLYKMMCRQGNLIKDRKRKLTTFPKCFLGSEFVSWLLEIGEIHRPEEGVHLGQALLENGIIHHVTDKHQFKPEQMLYRFRYDDGTFYPRNEMQDVISKGVRLYCRLHSLFTPVIRDKDYHLRTYKSVVMANKLIDWLIAQGDCRTREEAMIFGVGLCDNGFMHHVLEKSEFKDEPLLFRFFSDEEMEGSNMKHRLMKHDLKVVENVIAKSLLIKSNEGSYGFGLEDKNKVPIIKLVEKGSNAEMAGMEVGKKIFAINGDLVFMRPFNEVDCFLKSCLNSRKPLRVLVSTKPRETVKIPDSADGLGFQIRGFGPSVVHAVGRGTVAAAAGLHPGQCIIKVNGINVSKETHASVIAHVTACRKYRRPTKQDSIQWVYNSIESAQEDLQKSHSKPPGDEAGDAFDCKVEEVIDKFNTMAIIDGKKEHVSLTVDNVHLEYGVVYEYDSTAGIKCNVVEKMIEPKGFFSLTAKILEALAKSDEHFVQNCTSLNSLNEVIPTDLQSKFSALCSERIEHLCQRISSYKKFSRVLKNRAWPTFKQAKSKISPLHSSDFCPTNCHVNVMEVSYPKTSTSLGSAFGVQLDSRKHNSHDKENKSSEQGKLSPMVYIQHTITTMAAPSGLSLGQQDGHGLRYLLKEEDLETQDIYQKLLGKLQTALKEVEMCVCQIDDLLSSITYSPKLERKTSEGIIPTDSDNEKGERNSKRVCFNVAGDEQEDSGHDTISNRDSYSDCNSNRNSIASFTSICSSQCSSYFHSDEMDSGDELPLSVRISHDKQDKIHSCLEHLFSQVDSITNLLKGQAVVRAFDQTKYLTPGRGLQEFQQEMEPKLSCPKRLRLHIKQDPWNLPSSVRTLAQNIRKFVEEVKCRLLLALLEYSDSETQLRRDMVFCQTLVATVCAFSEQLMAALNQMFDNSKENEMETWEASRRWLDQIANAGVLFHFQSLLSPNLTDEQAMLEDTLVALFDLEKVSFYFKPSEEEPLVANVPLTYQAEGSRQALKVYFYIDSYHFEQLPQRLKNGGGFKIHPVLFAQALESMEGYYYRDNVSVEEFQAQINAASLEKVKQYNQKLRAFYLDKSNSPPNSTSKAAYVDKLMRPLNALDELYRLVASFIRSKRTAACANTACSASGVGLLSVSSELCNRLGACHIIMCSSGVHRCTLSVTLEQAIILARSHGLPPRYIMQATDVMRKQGARVQNTAKNLGVRDRTPQSAPRLYKLCEPPPPAGEE
Protein: RNA helicase (EC 3.6.4.13) (Q9VRI0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- LD47540p
- Ribosome production factor 2 homolog
- Nucleolar complex protein 1
- Protein Peter pan
- LD27920p
- Probable rRNA-processing protein EBP2 homolog
- Nucleolar protein 58
- ATP-dependent RNA helicase
- Pescadillo homolog
- Nucleolar GTP-binding protein 1
Sequence:
MSQMTQKTVQFHELELDQRILKAVAQLGWQQPTLIQSTAIPLLLEGKDVVVRARTGSGKTATYALPLIQKILNSKLNASEQYVSAVVLAPTKELCRQSRKVIEQLVESCGKVVRVADIADSSNDTVTQRHALSESPDIVVATPANLLAYAEAGSVVDLKHVETLVVDEADLVFAYGYEKDFKRLIKHLPPIYQAVLVSATLTDDVVRMKGLCLNNPVTLKLEEPELVPQDQLSHQRILAEENDKPAILYALLKLRLIRGKSIIFVNSIDRCYKVRLFLEQFGIRACVLNSELPANIRIHTISQFNKGTYDIIIASDEHHMEKPGGKSATNRKSPRSGDMESSASRGIDFQCVNNVINFDFPRDVTSYIHRAGRTARGNNKGSVLSFVSMKESKVNDSVEKKLCDSFAAQEGEQIIKNYQFKMEEVESFRYRAQDCWRAATRVAVHDTRIREIKIEILNCEKLKAFFEENKRDLQALRHDKPLRAIKVQSHLSDMPEYIVPKALKRVVGTSSSPVGASEAKQPRQSAAKAAFERQVNDPLMASQVDFGKRRPAHRRKKKAL
Protein: Nuclear pore complex interacting protein family member B5 (E9PKP1)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MVKLSIVLTPQFLSHDQGQLTKELQQHVKSVTCPCEYLRKVINTLADHHHRGTDFGGSPWLHVIIAFPTSYKVVITLWIVYLWVSLLKTIFWSRNGHDGSTDVQQRAWRSNRRRQEGLRSICMHTKKRVSSFRGNKIGLKDVITLRRHVETKVRAKIRKRKVTTKINHHDKINGKRKTARKQKMFQRAQELRRRAEDYHKCKIPPSARKALCNWVRMAAAEHRHSSGLPYWPYLTAETLKNRMGHQPPPPTQQHSITDNSLSLKTPPECLLTPLPPSADDNLKTPPECVLTPLPPSADDNLKTPPECVLTPLPPSADDNLKTPPECLLTPLPPSADDNLKTPPECLLTPLPPSALPSAPPSADDNLKTRAECLLHPLPPSADDNLKTPSERQLTPLPPSAPPSADDNIKTPAERLRGPLPPSADDNLKTPSERQLTPLPPSAPPSADDNIKTPAERLRGPLPPSADDNLKTPSERQLTPLPPSAPPSADDNIKTPAERLRGPLPPSADDNLKTPSERQLTALPPSADDNIKTPAERLRGPLPPSADDNLKTPSERQLTPLPPSAPPSADDNIKTPAFHPQRMISRHLPSVSSLPF
Protein: Probable oxidoreductase (Q9HTM8)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- Alanine racemase N-terminal domain-containing protein
- Probable cytochrome c
- Low specificity L-threonine aldolase
- Low specificity L-threonine aldolase
- Lipoprotein
Sequence:
MVGNPALAELLRAPRLIPWRNWSGAQSCLPLAREAPKDLDELVRIIRQASGRIRPVGSGHSFSALVPTDGTLLSLAYFSGLLSHDSVTLQAEFGGGTPMSQMGAPLKEIGQALVNMADIDYQTLAGAIATSTHGTGVGFGSYSAQVRGLQLVTASGEVLECDAKRNVEVFDAARVSLGALGVVTRVRLQNRAAYRLRERQWIARTEELLEDVEKNTRENQHWEMLVVTHSDYALSIALNETDEPKTPPLDPAKEGGNEFVGLIEGLDKYLSDFPETRRTLLNSLRHFARFDERVDDSYAVYANVRNVRFNEMEYSVPAEHGPACLREILALIRDKDLRTWFPIEYRYVKADDIPLSMFEGRDSCSISVHQHYSMDHHNFFAAVEPIFWKYAGRPHWGKLHGLNAHQLQGLYPRWKAFAEVRQALDPRGRFLNAHLSSILGVT
Protein: Delta-aminolevulinic acid dehydratase (ALAD) (ALADH) (EC 4.2.1.24) (Porphobilinogen synthase) (Q59643)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Catalyzes an early step in the biosynthesis of tetrapyrroles. Binds two molecules of 5-aminolevulinate per subunit, each at a distinct site, and catalyzes their condensation to form porphobilinogen (By similarity).
Interaction partners:
- Porphobilinogen deaminase
- Glutamate-1-semialdehyde 2,1-aminomutase
- Glutamyl-tRNA reductase
- Uroporphyrinogen-III synthase
- Probable aminotransferase
- Probable aminotransferase
- Siroheme synthase
- Ferrochelatase
- Oxygen-dependent coproporphyrinogen-III oxidase
- uroporphyrinogen-III C-methyltransferase
Sequence:
MSFTPANRAYPYTRLRRNRRDDFSRRLVRENVLTVDDLILPVFVLDGVNQRESIPSMPGVERLSIDQLLIEAEEWVALGIPALALFPVTPVEKKSLDAAEAYNPEGIAQRATRALRERFPELGIITDVALDPFTTHGQDGILDDDGYVLNDVSIDVLVRQALSHAEAGAQVVAPSDMMDGRIGAIREALESAGHTNVRIMAYSAKYASAYYGPFRDAVGSASNLGKGNKATYQMDPANSDEALHEVAADLAEGADMVMVKPGMPYLDIVRRVKDEFRAPTFVYQVSGEYAMHMGAIQNGWLAESVILESLTAFKRAGADGILTYFAKQAAEQLRRGR
Protein: Rap guanine nucleotide exchange factor 1 (CRK SH3-binding GNRP) (Guanine nucleotide-releasing factor 2) (Protein C3G) (Q13905)
Organism: Homo sapiens (Human)
Function: Guanine nucleotide-releasing protein that binds to SH3 domain of CRK and GRB2/ASH. Transduces signals from CRK to activate RAS. Involved in cell branching and adhesion mediated by BCAR1-CRK-RAPGEF1 signaling and activation of RAP1. Plays a role in the establishment of basal endothelial barrier function. Plays a role in nerve growth factor (NGF)-induced sustained activation of Rap1 and neurite outgrowth.
Subcellular location: Early endosome {ECO:0000269|PubMed:17724123}.
Interaction partners:
- Crk-like protein
- Adapter molecule crk
- E3 ubiquitin-protein ligase CBL
- Breast cancer anti-estrogen resistance protein 1
- Ras-related protein Rap-1A
- Rho-related GTP-binding protein RhoQ
- Growth factor receptor-bound protein 2
- Ras-related protein Rap-1b
- Cadherin-1
- E3 ubiquitin-protein ligase CBL-B
Sequence:
MDTDSQRSHLSSFTMKLMDKFHSPKIKRTPSKKGKPAEVSVKIPEKPVNKEATDRFLPEGYPLPLDLEQQAVEFMSTSAVASRSQRQKNLSWLEEKEKEVVSALRYFKTIVDKMAIDKKVLEMLPGSASKVLEAILPLVQNDPRIQHSSALSSCYSRVYQSLANLIRWSDQVMLEGVNSEDKEMVTTVKGVIKAVLDGVKELVRLTIEKQGRPSPTSPVKPSSPASKPDGPAELPLTDREVEILNKTTGMSQSTELLPDATDEEVAPPKPPLPGIRVVDNSPPPALPPKKRQSAPSPTRVAVVAPMSRATSGSSLPVGINRQDFDVDCYAQRRLSGGSHSYGGESPRLSPCSSIGKLSKSDEQLSSLDRDSGQCSRNTSCETLDHYDPDYEFLQQDLSNADQIPQQTAWNLSPLPESLGESGSPFLGPPFQLPLGGHPQPDGPLAPGQQTDTPPALPEKKRRSAASQTADGSGCRVSYERHPSQYDNISGEDLQSTAPIPSVPYAPFAAILPFQHGGSSAPVEFVGDFTAPESTGDPEKPPPLPEKKNKHMLAYMQLLEDYSEPQPSMFYQTPQNEHIYQQKNKLLMEVYGFSDSFSGVDSVQELAPPPALPPKQRQLEPPAGKDGHPRDPSAVSGVPGKDSRDGSERAPKSPDALESAQSEEEVDELSLIDHNEIMSRLTLKQEGDDGPDVRGGSGDILLVHATETDRKDLVLYCEAFLTTYRTFISPEELIKKLQYRYEKFSPFADTFKKRVSKNTFFVLVRVVDELCLVELTEEILKLLMELVFRLVCNGELSLARVLRKNILDKVDQKKLLRCATSSQPLAARGVAARPGTLHDFHSHEIAEQLTLLDAELFYKIEIPEVLLWAKEQNEEKSPNLTQFTEHFNNMSYWVRSIIMLQEKAQDRERLLLKFIKIMKHLRKLNNFNSYLAILSALDSAPIRRLEWQKQTSEGLAEYCTLIDSSSSFRAYRAALSEVEPPCIPYLGLILQDLTFVHLGNPDYIDGKVNFSKRWQQFNILDSMRCFQQAHYDMRRNDDIINFFNDFSDHLAEEALWELSLKIKPRNITRRKTDREEKT
Protein: Defective proboscis extension response 17, isoform B (Defective proboscis extension response 17, isoform C) (Defective proboscis extension response 17, isoform E) (Q9VGD2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MTTQNDLITTASNLATAKKPATAASEAVVDTAETAETAPPTEATSSWSSTAVARGMSSADGAGEAIATSQSAQIGLTTQATVRQTEAQTASTATQAAAATSAATSAAIASAAAATETAAEMLISTIYPASTETDLHNSIERVEGQRGKMANAFHPGVPDSLTKGFSIPTFLPPFPVFAAADLPAYRAAADAAEAAKLAAEAAAQAAAAKTSSEAVTMSPEEQRRQMFNEQHSYLAAHRDGGDGAGSAVRRNLTMPVLNITAQMGNHAYMPCQIHRLSDKPVSWVRMRDNHIISVDETTFIADERFQSIYQEDHDYTWSLQIKYVEPSDAGWYECQMATEPKLSAKVHLQIVKPKTELIGDQSRFVKAGSKVALHCIVRGTLDPPKYIIWFRGQKKISDSDERTGWYTQLDRNIFGTVGDNQNTIGSLIIPLVRKEDSGNYTCQPSNSVSVSVDLHVLSGEYSASAIMSTAARTTKGGRSTCHSTLGLLGILGLLWAMQGAMHTPPTQT
Protein: Uncharacterized N-acetyltransferase C18E5.08 (EC 2.3.1.-) (O94498)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Large ribosomal subunit protein uL29
- Large ribosomal subunit protein uL24
- Small ribosomal subunit protein uS3
Sequence:
MSKIILKTSRFLLKSPVEEDDFDQITKIKSDPLVSNTQLYGKVESRELCRFMFQHYITDARITKTRRKRWVFGIYPLEVSSTFPSICYIGNVGLSKKNVKSDTANLFFEIGPLYWGMGIATECVGRVIEFGSENNIQNFIIDPIIGNEASKKVALKLGFEDSGTFVTAYNGLQQHIYKLSKQIRTG
Protein: Lebocin-like anionic peptide 1 (P85211)
Organism: Galleria mellonella (Greater wax moth)
Function: Antimicrobial protein. Has antibacterial activity against the Gram-positive bacteria M.luteus (MIC=22.7 uM) and L.monocytogenes (MIC=90.9 uM). Lacks antibacterial activity against the Gram-positive bacteria B.circulans, S.aureus, and S.lutea, and the Gram-negative bacteria E.coli D31, E.coli ATCC 25922, and S.typhimurium. Has antifungal activity against A.niger (MIC=90.9 uM) and T.harzianum (MIC=90.9 uM), but lacks antifungal activity against S.cerevisiae, P.pastoris, Z.marxianus, C.albicans, C.fructus, and F.oxysporum.
Subcellular location: Secreted {ECO:0000269|PubMed:17194500}.
Interaction partners:
Sequence:
EADEPLWLYKGDNIERAPTTADHPILPSIIDDVKLDPNRRYA
Protein: Tetratricopeptide repeat domain 5 (Q587E6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- GMP synthase
- Large ribosomal subunit protein uL5
- 60S ribosomal protein L13a, putative
- 60S ribosomal protein L17, putative
- 60S ribosomal protein L5, putative
- 60S ribosomal protein L2, putative
- 60S ribosomal protein L4
- DNA-directed RNA polymerase subunit beta
- arginine--tRNA ligase
- Small ribosomal subunit protein uS2
Sequence:
MTSIEMQVDVAELERKYEALANVKVFDDNVRKGVDTILATMPNPDKQHSPEEKVRLYVLRCKALLLLPSYSKDSERCCSAALKLRNDRPDLWVLLSECFTQRGATKEACEALDNALRLDSRNEKALSQYSQVLRIRSADSKLPLQESRKYLSEAVLRAKEAVAVSPASASCWHLYGIALLSEALSNGMNVEGAQRSLKALEQASRIEPRDPDVCYNKGAVEGVLGYFGSASCDLLTALEEDPHRLKGARKQLEDYLSIIRRAISMTESMQRTGKKAFTSLVTKLAKHVDSMTLREALERETSSLCKVSVGVVDVLSETTMEPMVVLSVDRVGEFCLLLFHGIRRGTFKMRDAVVTLTVPKSNPVRVTHEVPAIPFLDTSAYSCSYVQVIVDVDSTIVNGAPISSQMRVPPQVSTRLFI
Protein: Chondroitin sulfate N-acetylgalactosaminyltransferase 2 (EC 2.4.1.174) (Chondroitin beta-1,4-N-acetylgalactosaminyltransferase 2) (Beta4GalNAcT-2) (GalNAcT-2) (Q8N6G5)
Organism: Homo sapiens (Human)
Function: Transfers 1,4-N-acetylgalactosamine (GalNAc) from UDP-GalNAc to the non-reducing end of glucuronic acid (GlcUA). Required for addition of the first GalNAc to the core tetrasaccharide linker and for elongation of chondroitin chains.
Subcellular location: Golgi apparatus, Golgi stack membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
- Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 3
- Chondroitin sulfate synthase 2
- Chondroitin sulfate N-acetylgalactosaminyltransferase 1
- Chondroitin sulfate synthase 1
- Chondroitin sulfate glucuronyltransferase
- Chondroitin sulfate synthase 3
- Carbohydrate sulfotransferase 7
Sequence:
MPRRGLILHTRTHWLLLGLALLCSLVLFMYLLECAPQTDGNASLPGVVGENYGKEYYQALLQEQEEHYQTRATSLKRQIAQLKQELQEMSEKMRSLQERRNVGANGIGYQSNKEQAPSDLLEFLHSQIDKAEVSIGAKLPSEYGVIPFESFTLMKVFQLEMGLTRHPEEKPVRKDKRDELVEVIEAGLEVINNPDEDDEQEDEEGPLGEKLIFNENDFVEGYYRTERDKGTQYELFFKKADLTEYRHVTLFRPFGPLMKVKSEMIDITRSIINIIVPLAERTEAFVQFMQNFRDVCIHQDKKIHLTVVYFGKEGLSKVKSILESVTSESNFHNYTLVSLNEEFNRGRGLNVGARAWDKGEVLMFFCDVDIYFSAEFLNSCRLNAEPGKKVFYPVVFSLYNPAIVYANQEVPPPVEQQLVHKKDSGFWRDFGFGMTCQYRSDFLTIGGFDMEVKGWGGEDVHLYRKYLHGDLIVIRTPVPGLFHLWHEKRCADELTPEQYRMCIQSKAMNEASHSHLGMLVFREEIETHLHKQAYRTNSEAVG
Protein: Eukaryotic translation initiation factor 1 (eIF1) (A121) (Protein translation factor SUI1 homolog) (Sui1iso1) (P41567)
Organism: Homo sapiens (Human)
Function: Necessary for scanning and involved in initiation site selection. Promotes the assembly of 48S ribosomal complexes at the authentic initiation codon of a conventional capped mRNA.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Eukaryotic translation initiation factor 5
- Eukaryotic translation initiation factor 1A, X-chromosomal
- Eukaryotic translation initiation factor 3 subunit C
- Eukaryotic translation initiation factor 3 subunit B
- Eukaryotic initiation factor 4A-I
- Eukaryotic translation initiation factor 2 subunit 1
- Eukaryotic translation initiation factor 2 subunit 2
- Eukaryotic translation initiation factor 3 subunit G
- Eukaryotic translation initiation factor 3 subunit I
- Eukaryotic translation initiation factor 4 gamma 1
Sequence:
MSAIQNLHSFDPFADASKGDDLLPAGTEDYIHIRIQQRNGRKTLTTVQGIADDYDKKKLVKAFKKKFACNGTVIEHPEYGEVIQLQGDQRKNICQFLVEIGLAKDDQLKVHGF
Protein: Nephronectin (Preosteoblast EGF-like repeat protein with MAM domain) (Q91V88)
Organism: Mus musculus (Mouse)
Function: Functional ligand of integrin alpha-8/beta-1 in kidney development. Regulates the expression of GDNF with integrin alpha-8/beta-1 which is essential for kidney development. May also play a role in the development and function of various tissues, regulating cell adhesion, spreading and survival through the binding of several integrins.
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:11470831, ECO:0000269|PubMed:11546798}. Note=Trapped on the cell surface or in the extracellular matrix.
Interaction partners:
- Integrin alpha-8
Sequence:
MAVLLAAVLASSLYLQVAADFDGRWPRQIVSSIGLCRYGGRIDCCWGWARQSWGQCQPVCQPQCKHGECVGPNKCKCHPGFAGKTCNQDLNECGLKPRPCKHRCMNTFGSYKCYCLNGYMLLPDGSCSSALSCSMANCQYGCDVVKGQVRCQCPSPGLQLAPDGRTCVDIDECATGRVSCPRFRQCVNTFGSYICKCHTGFDLMYIGGKYQCHDIDECSLGQHQCSSYARCYNIHGSYKCQCRDGYEGDGLNCVYIPKVMIEPSGPIHMPERNGTISKGDGGHANRIPDAGSTRWPLKTPYIPPVITNRPTSKPTTRPTPNPTPQPTPPPPPPLPTEPRTTPLPPTPERPSTRPTTIAPATSTTTRVITVDNRIQTDPQKPRGDVFIPRQPTNDLFEIFEIERGVSADEEVKDDPGILIHSCNFDHGLCGWIREKDSDLHWETARDPAGGQYLTVSAAKAPGGKAARLVLRLGHLMHSGDLCLSFRHKVTGLHSGTLQVFVRKHGTHGAALWGRNGGHGWRQTQITLRGADVKSVIFKGEKRRGHTGEIGLDDVSLKRGRC