wanglab/gogpt-training-data huggingface dataset:
Protein: Protein GRIP (AtGRIP) (Q8S2T0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Golgi matrix protein playing a role in tethering of vesicles to Golgi membranes and in maintaining the overall structure of the Golgi apparatus.
Subcellular location: Golgi apparatus {ECO:0000269|PubMed:15605178, ECO:0000269|PubMed:16236155, ECO:0000269|PubMed:16830178}. Note=Locates to the trans-Golgi or to the trans-Golgi network (TGN).
Interaction partners:
- Golgin candidate 5
- Nuclear pore complex protein NUP155
- Nuclear pore complex protein NUP54
- Nuclear pore complex protein NUP107
- Nuclear pore complex protein NUP88
- Nuclear pore complex protein NUP205
- Nuclear pore complex protein NUP85
- ADP-ribosylation factor 3
- Nuclear pore complex protein NUP93A
- Nuclear pore complex protein NUP93B
Sequence:
MSEDKESDVVGEEEESHVIKEDKELNDASNETLTENGDQLLQMIAELRLENDFLRSQFEGLKDEVAQGRSLQKAEQVEADSAQLKQLQEQVASLSREIDVEKQTRVAAEQALEHLREAYSEADAKSQEYSSKFSQVEQKLDQEIKERDEKYADLDAKFTRLHKRAKQRIQEIQKEKDDLDARFREVNETAERASSQHSSMQQELERTRQQANEALKAMDAERQQLRSANNKLRDTIEELRGSLQPKENKIETLQQSLLDKDQILEDLKKQLQAVEERKQIAVTELSAKHQKNLEGLEAQVVDALSERDKAAETISSLQVLLAEKESKIAEMEAAATGEAARLRAAAETLKGELAHLKSENEKEKETWEASCDALKSKLEIAESNYLQAEIEVAKMRSQLGSEMSMQTQILSTKDAELKGAREEINRLQSEFSSYKIRAHALLQKKDMELAAAKDSEQIKSLEEALKEAEKEVYLVSAERDRAQQDLQSALASLEKELEERAGALKDASEQIKSLEVKLDSTVARNQAEKQAWEEDLRVLEETWRRRCEALTAQNEASPAEGIEKELENAKLRNKRMKEEHESVRELADRLIEEKDREISRLVDEMTNLRKSMESKPVWNKSPSQVHHYGNNNTESQQQDVSNLSTSAAEHQILILARQQAQREEELAQTQRHILALQEEIEELERENRLHSQQEAVLKTELREMERKQKREGVDMTYLKNVILKLLETGEVEALLPVVGMLLQFSPEEIQKCQQAYHSSTTAATTTEATPSPASEGSGLSVFSRFSFS
Protein: T. brucei spp.-specific protein (Q389V0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MQHPGRADFEQLSRCVFFSARVFTFGEPFDSPAPPFSSVLFPFGAPHVPSVSLLIGVLSGCVVVVRRCCPTVSFVPPRGGGCAFGPFGGGGGGERNAFACPTSGGGMAIFDSIIDIPSLQNPRLIWGWVETHGWRAPSGHGNQLSLAMSRTEPGCHP
Protein: Vanillin dehydrogenase (G2IMC6)
Organism: Sphingobium sp. (strain NBRC 103272 / SYK-6)
Interaction partners:
- Aromatic-ring-hydroxylating dioxygenase alpha subunit
- Aryl-alcohol dehydrogenase
- Aryl-alcohol dehydrogenase
- Benzoylformate decarboxylase
- acylphosphatase
- Putative hydrolase
- Aromatic-ring-hydroxylating dioxygenase beta subunit
- 4-oxalomesaconate tautomerase
- Putative hydrolase
- 2-pyrone-4,6-dicarboxylate hydrolase
Sequence:
MDSARIAPDQERDRMEFTRLNPMTGEVASSAPALKAGDIPAIARKAREGFTAWSVMGPNARRAVLMKAATALEARADAFVDAMMGEIGATKGWALFNLGLAASMVREAAALTTQINGEVIPSDKPGCLAMALREPVGVILGIAPWNAPIILGVRAIAVPLACGNSVILKASETCPRTHALIIEAFADAGFPEGVVNVVTNAPADAGEVVGALIDAPEVKRINFTGSTGVGKIIAKRAAEHLKPVLLELGGKAPLIVLEDADLDEAVKAAAFGAFMNQGQICMSTERIIVVDAVADEFAARFKAKVSAMPVGDPRQGSTPLGAVVDTKTVAHCLSLIEDALGKGAEQLTGGETTQNVLMPAHVIDRVTPDMKLFRDESFGPVVGIIRARDAEHAIELANDTEYGLSASVFTRDTAKGLSVARRIESGICHVNGPTVHDEAQMPFGGVKASGYGRFGGKAGIDSFTELRWITIETQPGHFPI
Protein: 26S proteasome regulatory subunit RPN14 (Proteasome non-ATPase subunit 14) (P53196)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Acts as a regulatory subunit of the 26 proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins. Is not a genuine component of the 26S proteasome, but an auxiliary factor that interacts with the proteasomal ATPase of 19S regulatory particle (RP). Acts as a chaperone which regulates the highly structured assembly of the 19S regulatory particle. Involved in the substrate specificity of the 26S proteasome and is especially involved in the degradation of ubiquitinated GCN4. May contribute to the stability of the 26S proteasome in some stress conditions.
Subcellular location: Cytoplasm. Nucleus.
Interaction partners:
- Probable 26S proteasome regulatory subunit p28
- 26S proteasome regulatory subunit 8 homolog
- 26S proteasome regulatory subunit 6B homolog
- 26S proteasome regulatory subunit 7 homolog
- DNA mismatch repair protein HSM3
- 26S proteasome regulatory subunit 6A
- 26S proteasome regulatory subunit 4 homolog
- 26S proteasome regulatory subunit RPN5
- 26S proteasome subunit RPT4
- 26S proteasome regulatory subunit RPN8
Sequence:
MTKTITVAHIQYDFKAVLEENDENDDEFYINVDKNLNEIKEHKIVVLGNSRGVDAGKGNTFEKVGSHLYKARLDGHDFLFNTIIRDGSKMLKRADYTAVDTAKLQMRRFILGTTEGDIKVLDSNFNLQREIDQAHVSEITKLKFFPSGEALISSSQDMQLKIWSVKDGSNPRTLIGHRATVTDIAIIDRGRNVLSASLDGTIRLWECGTGTTIHTFNRKENPHDGVNSIALFVGTDRQLHEISTSKKNNLEFGTYGKYVIAGHVSGVITVHNVFSKEQTIQLPSKFTCSCNSLTVDGNNANYIYAGYENGMLAQWDLRSPECPVGEFLINEGTPINNVYFAAGALFVSSGFDTSIKLDIISDPESERPAIEFETPTFLVSNDDEVSQFCYVSDDESNGEVLEVGKNNFCALYNLSNP
Protein: F-BAR domain only protein 2 (D3ZYR1)
Organism: Rattus norvegicus (Rat)
Function: Functions in an early step of clathrin-mediated endocytosis. Has both a membrane binding/bending activity and the ability to recruit proteins essential to the formation of functional clathrin-coated pits. Has a lipid-binding activity with a preference for membranes enriched in phosphatidylserine and phosphoinositides (Pi(4,5) biphosphate) like the plasma membrane. Its membrane-bending activity might be important for the subsequent action of clathrin and adaptors in the formation of clathrin-coated vesicles. Involved in adaptor protein complex AP-2-dependent endocytosis of the transferrin receptor, it also functions in the AP-2-independent endocytosis of the LDL receptor (By similarity).
Subcellular location: Membrane, clathrin-coated pit {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Associated with forming but not mature clathrin-coated vesicles. The recruitment to coated-pits precede the one of clathrin and the adaptor protein complex AP-2 (By similarity). {ECO:0000250}.
Interaction partners:
- AP-2 complex subunit mu
- AP-2 complex subunit sigma
- AP-2 complex subunit beta
- AP-2 complex subunit alpha-2
- Intersectin 2
- Epidermal growth factor receptor pathway substrate 15
- Intersectin-1
- Disabled homolog 2
- Formin-binding protein 1
- Clathrin coat assembly protein AP180
Sequence:
MVMAHFVENFWGEKNNGFDVLYHNMKHGQISTKELADFVRERATIEEAYSRSMTKLAKSASNYSQLGTFAPVWDVFKTSTEKLANCHLDLVRKLQELIKEVQKYGEEQVKSHKKTKEEVAGTLEAVQAIQNITQALQKSKENYNAKCVEQERLKKEGATPREIEKAAVKSKKATDTYKLYVEKYALTKADFEQKMTETAQKFQDIEETHLIHIKEIIGSLSNAIKEIHLQIGQVHEEFINNMANTTIESLIQKFAESKGTGKERPGLIEFEECDPASAVEGIKPRKRKTFALPGIIKKEKDAESVECPDADSLNIPDVDEEGFSIKPEANQNDTKENHFYSSSDSDSEDEEPKRYRIEIKPVHPNNVHHTMASLDELKVSIGNITLSPAVSRHSPVQMNRNSSNEELTKSKPSSLPTEKGTNDLLAWDPLFGSSLESSSAPLTSSSSARPTTPLSLGTIVPPPRPASRPKLTSGKLSGINEIPRPFSPPITSNTSPPPTAPLARAESSSSISSSASLSAANTPTVGVSRGPSPVSLGNQDTLPVAIALTESVNAYFKGADPTKCIVKITGDVTISFPSGIIKVFTSNPSPAVLCFRVKNISRLEQILPNSQLVFSDPSQCDSNTKDFWMNMQAVTVYLKKLSEQNPAASYYNVDVLKYQVSSNGIQSTPLNLATYWKCSASTTDLRVDYKYNPEAMVAPSVLSNIQVVVPVDGGVTNMQSLPPAIWNAEQMKAFWKLSGISEKSDSGGSGSLRAKFDLSEGPSKPATLAVQFLSEGNTLSGVDIELVGTGYRLSLVKKRFATGRYLADC
Protein: Toxin To5 (PT-Arthr*-beta* NaTx2.7) (Toxin Tc66) (Toxin To66) (P84693)
Organism: Tityus obscurus (Amazonian scorpion) (Tityus cambridgei)
Function: Beta toxins bind voltage-independently at site-4 of sodium channels (Nav) and shift the voltage of activation toward more negative potentials thereby affecting sodium channel activation and promoting spontaneous and repetitive firing.
Subcellular location: Secreted {ECO:0000269|PubMed:15025998, ECO:0000269|PubMed:22355312}.
Interaction partners:
Sequence:
MKAIIFFIGCLMLIDLVAGSRSGYPVTQKGCVYSCFWGSNWWCNAECTALGGSSGYCAWPSCWCYSLPDNRNIWGSYPNNCGKK
Protein: Xylosyl- and glucuronyltransferase LARGE2 (EC 2.4.-.-) (Glycosyltransferase-like 1B) (LARGE xylosyl- and glucuronyltransferase 2) [Includes: Alpha-1,3-xylosyltransferase LARGE2 (EC 2.4.2.-); Beta-1,3-glucuronyltransferase LARGE2 (EC 2.4.1.-)] (Q5XPT3)
Organism: Mus musculus (Mouse)
Function: Bifunctional glycosyltransferase with both alpha-1,3-xylosyltransferase and beta-1,3-glucuronyltransferase activities involved in the maturation of alpha-dystroglycan (DAG1) by glycosylation leading to DAG1 binding to laminin G-like domain-containing extracellular proteins with high affinity and in a phosphorylated-O-mannosyl trisaccharide dependent manner. Elongates the glucuronyl-beta-1,4-xylose-beta disaccharide primer structure by adding repeating units [-3-Xylose-alpha-1,3-GlcA-beta-1-] to produce a heteropolysaccharide. Supports the maturation of DAG1 more effectively than LARGE1 (By similarity). In addition, can modify both heparan sulfate (HS)- and chondroitin/dermatan sulfate (CS/DS)-proteoglycans (PGs), namely GPC4, with a glycosaminoglycan (GAG)-like polysaccharide composed of xylose and glucuronic acid to confer laminin binding.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:15958417}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
- Beta-1,4-glucuronyltransferase 1
- Xylosyl- and glucuronyltransferase LARGE1
- Ribitol-5-phosphate transferase FKTN
- Ribitol-5-phosphate xylosyltransferase 1
- Protein O-mannosyl-transferase 2
- Protein O-linked-mannose beta-1,2-N-acetylglucosaminyltransferase 1
- Protein O-mannosyl-transferase 1
- Ribitol 5-phosphate transferase FKRP
- Dystroglycan 1
Sequence:
MLPRGRPRAMGAAVLLLLLLLVVGFFLFGRDPDYGLGTTATLDEDPYRSRNLSASSPQLLLPPKCEMLHVAIVCAGYNSSREIITLTKSLLFYRKNPLHLHLITDAVARNILETLFRTWMVPAVVVSFYDAEELKPLVSWIPNKHYSGLYGLMKLVLPSILPPSLARVIVLDTDVTFSSDIVELWALFDHFSDKQVVGLVENQSDWYLGNLWKNHRPWPALGRGFNTGVILLWLDRLQQTGWEQMWKVTAKRELLTLMATSLADQDIFNAVIKEHPHLVHPLPCVWNVQLSDHTRAERCYLEAADLKVIHWNSPKKLRVKNKHAEFFRNLHLTFLGYDGKLLRRELFGCPNQFPPGAEQLQQALTQLDEEEPCFEFRQQQLTVHRVHITFLPHQPPPPQPHDVTLVAQLSMDRLQMLEALCRHWPGPMSLALYLTDEEAQQFLHFVETSPVLSMRKDVAYHVVYRDGPLYPVNQLRNVALAQALTPYVFLSDIDFLPAYSLYDYLRASIEQLELDSRRKTALVVPAFETLHYRFSFPNSKAELLTLLDAGSLHTFRYHEWPQGHSSTDYSRWREAQAPYSVQWSADYEPYVVVPRDCPRYDPRFVGFGWNKVAHIIELDAQEYEFLVLPEAFSIHLPHAPSLDISRFRSSPTYRNCLQALKEEFHQDLSRRYGSAALKYLTALQQARSRA
Protein: Beta-actin-like protein 2 (Kappa-actin) (Q8BFZ3)
Organism: Mus musculus (Mouse)
Function: Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250}.
Interaction partners:
- RuvB-like 1
- RuvB-like 2
Sequence:
MVDDELTALVVDNGSGMCKAGFGGDDAPRAVFPSMVGRPRHQGVMVGMGQKDCYVGDEAQSKRGILTLKYPIEHGVVTNWDDMEKIWYHTFYNELRVAPDEHPILLTEAPLNPKINREKMTQIMFEAFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVTHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYNFTTTAEREIVRDVKEKLCYVALDFEQEMVTAAASSSLERSYELPDGQVITIGNERFRCPEAIFQPSFLGIESRGIHETTFNSIMKCDVDIRKDLFANTVLSGGSTMYPGIADRMQKEIVTLAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDEAGPPIVHRKCF
Protein: Nuclear pore complex protein Nup133 (133 kDa nucleoporin) (Nucleoporin Nup133) (Q8WUM0)
Organism: Homo sapiens (Human)
Function: Involved in poly(A)+ RNA transport. Involved in nephrogenesis.
Subcellular location: Nucleus, nuclear pore complex {ECO:0000269|PubMed:11564755, ECO:0000269|PubMed:11684705}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:11564755}. Note=Located on both the cytoplasmic and nuclear sides of the nuclear pore (PubMed:11564755). During mitosis, localizes to the kinetochores (PubMed:11564755). {ECO:0000269|PubMed:11564755, ECO:0000269|PubMed:11684705}.
Interaction partners:
- Nucleoporin Nup37
- Nuclear pore complex protein Nup107
- Nuclear pore complex protein Nup160
- Protein SEC13 homolog
- Nuclear pore complex protein Nup85
- Nucleoporin Nup43
- Nuclear pore complex protein Nup98-Nup96
- Protein ELYS
- Nuclear pore complex protein Nup214
- Nucleoporin SEH1
Sequence:
MFPAAPSPRTPGTGSRRGPLAGLGPGSTPRTASRKGLPLGSAVSSPVLFSPVGRRSSLSSRGTPTRMFPHHSITESVNYDVKTFGSSLPVKVMEALTLAEVDDQLTINIDEGGWACLVCKEKLIIWKIALSPITKLSVCKELQLPPSDFHWSADLVALSYSSPSGEAHSTQAVAVMVATREGSIRYWPSLAGEDTYTEAFVDSGGDKTYSFLTAVQGGSFILSSSGSQLIRLIPESSGKIHQHILPQGQGMLSGIGRKVSSLFGILSPSSDLTLSSVLWDRERSSFYSLTSSNISKWELDDSSEKHAYSWDINRALKENITDAIWGSESNYEAIKEGVNIRYLDLKQNCDGLVILAAAWHSADNPCLIYYSLITIEDNGCQMSDAVTVEVTQYNPPFQSEDLILCQLTVPNFSNQTAYLYNESAVYVCSTGTGKFSLPQEKIVFNAQGDSVLGAGACGGVPIIFSRNSGLVSITSRENVSILAEDLEGSLASSVAGPNSESMIFETTTKNETIAQEDKIKLLKAAFLQYCRKDLGHAQMVVDELFSSHSDLDSDSELDRAVTQISVDLMDDYPASDPRWAESVPEEAPGFSNTSLIILHQLEDKMKAHSFLMDFIHQVGLFGRLGSFPVRGTPMATRLLLCEHAEKLSAAIVLKNHHSRLSDLVNTAILIALNKREYEIPSNLTPADVFFREVSQVDTICECLLEHEEQVLRDAPMDSIEWAEVVINVNNILKDMLQAASHYRQNRNSLYRREESLEKEPEYVPWTATSGPGGIRTVIIRQHEIVLKVAYPQADSNLRNIVTEQLVALIDCFLDGYVSQLKSVDKSSNRERYDNLEMEYLQKRSDLLSPLLSLGQYLWAASLAEKYCDFDILVQMCEQTDNQSRLQRYMTQFADQNFSDFLFRWYLEKGKRGKLLSQPISQHGQLANFLQAHEHLSWLHEINSQELEKAHATLLGLANMETRYFAKKKTLLGLSKLAALASDFSEDMLQEKIEEMAEQERFLLHQETLPEQLLAEKQLNLSAMPVLTAPQLIGLYICEENRRANEYDFKKALDLLEYIDEEEDININDLKLEILCKALQRDNWSSSDGKDDPIEVSKDSIFVKILQKLLKDGIQLSEYLPEVKDLLQADQLGSLKSNPYFEFVLKANYEYYVQGQI
Protein: PopD (YopD protein) (G3XCM5)
Organism: Pseudomonas aeruginosa
Interaction partners:
Sequence:
MIDTQYSLAATQAAIPSEPIAPGAAGRSVGTPQAAADLPQVPAARADRVELNAPRQVLDPVRMEAAGSELDSSVELLLILFRIAQKARELGVLQRDNENQSIIHAQKAQVDEMRSGATLMIAMAVIAGVGALASAVVGSLGALKNGKAISQEKTLQKNIDGRNELIDAKMQALGKTSDEDRKIVGKVWAADQVQDSVALRAAGRAFESRNGALQVANTVIQSFVQMANASVQVRQGESQASAREGEVNATIGQSQKQKVEDQMSFDAGFMKDVLQLIQQYTQSHNQAWRAAAGVV
Protein: 2-oxoisovalerate dehydrogenase subunit alpha 2, mitochondrial (EC 1.2.4.4) (Branched-chain alpha-keto acid dehydrogenase E1 component alpha chain) (BCKDE1A) (BCKDH E1-alpha) (Q84JL2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3) (By similarity).
Subcellular location: Mitochondrion matrix {ECO:0000269|PubMed:14671022, ECO:0000269|PubMed:14764908}.
Interaction partners:
- 2-oxoisovalerate dehydrogenase subunit beta 1, mitochondrial
- 2-oxoisovalerate dehydrogenase subunit beta 2, mitochondrial
- Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial
- Pyruvate dehydrogenase E1 component subunit beta-3, chloroplastic
- Pyruvate dehydrogenase E1 component subunit beta-2, chloroplastic
- Pyruvate dehydrogenase E1 component subunit beta-1, mitochondrial
- Dihydrolipoyl dehydrogenase 1, chloroplastic
- Dihydrolipoyl dehydrogenase 2, chloroplastic
- Dihydrolipoyl dehydrogenase 1, mitochondrial
- Dihydrolipoyl dehydrogenase 2, mitochondrial
Sequence:
MALHLRSSFSSKSTLLNILRHNLGFGSRSHVTRHIRQILPHDPPLRGSQNPISRLCNTMAEPETLSSFVQHEYANNHQVMDFPGGKVAFTPEIQFISESDKERVPCYRVLDDNGQLITNSQFVQVSEEVAVKIYSDMVTLQIMDNIFYEAQRQGRLSFYATAIGEEAINIASAAALTPQDVIFPQYREPGVLLWRGFTLQEFANQCFGNKSDYGKGRQMPVHYGSNKLNYFTVSATIATQLPNAVGAAYSLKMDKKDACAVTYFGDGGTSEGDFHAALNIAAVMEAPVLFICRNNGWAISTPTSDQFRSDGVVVKGRAYGIRSIRVDGNDALAMYSAVHTAREMAIREQRPILIEALTYRVGHHSTSDDSTRYRSAGEIEWWNKARNPLSRFRTWIESNGWWSDKTESDLRSRIKKEMLEALRVAEKTEKPNLQNMFSDVYDVPPSNLREQELLVRQTINSHPQDYPSDVPL
Protein: Translocase of chloroplast 132, chloroplastic (AtToc132) (EC 3.6.5.-) (132 kDa chloroplast outer envelope protein) (Q9SLF3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: GTPase involved in protein precursor import into chloroplasts. Seems to recognize chloroplast-destined precursor proteins and regulate their presentation to the translocation channel through GTP hydrolysis. Probably specialized in the import of nuclear encoded non-photosynthetic preproteins from the cytoplasm to the chloroplast.
Subcellular location: Plastid, chloroplast outer membrane {ECO:0000250|UniProtKB:O23680}; Single-pass membrane protein {ECO:0000250|UniProtKB:O23680}. Cytoplasm {ECO:0000250}. Note=Cycles between the cytoplasm and chloroplast, probably as a soluble preprotein receptor. The anchoring to the chloroplast outer membrane required the GTPase activity and GDP. May contain beta barrel transmembrane regions (By similarity). {ECO:0000250}.
Interaction partners:
- Protein TOC75-3, chloroplastic
- Protein TOC75-4, chloroplastic
- Protein TIC 56, chloroplastic
- Protein TIC110, chloroplastic
- E3 ubiquitin-protein ligase SP1
- Translocase of chloroplast 34, chloroplastic
- Outer envelope protein 80, chloroplastic
- Chaperone protein dnaJ 15
- Protein TIC 40, chloroplastic
- Solute carrier family 40 member 3, chloroplastic
Sequence:
MGDGTEFVVRSDREDKKLAEDRISDEQVVKNELVRSDEVRDDNEDEVFEEAIGSENDEQEEEEDPKRELFESDDLPLVETLKSSMVEHEVEDFEEAVGDLDETSSNEGGVKDFTAVGESHGAGEAEFDVLATKMNGDKGEGGGGGSYDKVESSLDVVDTTENATSTNTNGSNLAAEHVGIENGKTHSFLGNGIASPKNKEVVAEVIPKDDGIEEPWNDGIEVDNWEERVDGIQTEQEVEEGEGTTENQFEKRTEEEVVEGEGTSKNLFEKQTEQDVVEGEGTSKDLFENGSVCMDSESEAERNGETGAAYTSNIVTNASGDNEVSSAVTSSPLEESSSGEKGETEGDSTCLKPEQHLASSPHSYPESTEVHSNSGSPGVTSREHKPVQSANGGHDVQSPQPNKELEKQQSSRVHVDPEITENSHVETEPEVVSSVSPTESRSNPAALPPARPAGLGRASPLLEPASRAPQQSRVNGNGSHNQFQQAEDSTTTEADEHDETREKLQLIRVKFLRLAHRLGQTPHNVVVAQVLYRLGLAEQLRGRNGSRVGAFSFDRASAMAEQLEAAGQDPLDFSCTIMVLGKSGVGKSATINSIFDEVKFCTDAFQMGTKRVQDVEGLVQGIKVRVIDTPGLLPSWSDQAKNEKILNSVKAFIKKNPPDIVLYLDRLDMQSRDSGDMPLLRTISDVFGPSIWFNAIVGLTHAASVPPDGPNGTASSYDMFVTQRSHVIQQAIRQAAGDMRLMNPVSLVENHSACRTNRAGQRVLPNGQVWKPHLLLLSFASKILAEANALLKLQDNIPGRPFAARSKAPPLPFLLSSLLQSRPQPKLPEQQYGDEEDEDDLEESSDSDEESEYDQLPPFKSLTKAQMATLSKSQKKQYLDEMEYREKLLMKKQMKEERKRRKMFKKFAAEIKDLPDGYSENVEEESGGPASVPVPMPDLSLPASFDSDNPTHRYRYLDSSNQWLVRPVLETHGWDHDIGYEGVNAERLFVVKEKIPISVSGQVTKDKKDANVQLEMASSVKHGEGKSTSLGFDMQTVGKELAYTLRSETRFNNFRRNKAAAGLSVTHLGDSVSAGLKVEDKFIASKWFRIVMSGGAMTSRGDFAYGGTLEAQLRDKDYPLGRFLTTLGLSVMDWHGDLAIGGNIQSQVPIGRSSNLIARANLNNRGAGQVSVRVNSSEQLQLAMVAIVPLFKKLLSYYYPQTQYGQ
Protein: Apoptosome protein Dark (Death-associated APAF1-related killer) (Drosophila Apaf-1 related killer) (Homolog of Apaf-1 and ced-4) (Q7KLI1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Caspase Dronc
- Cytochrome c-2
- Cytochrome c-1
- BG1
- Caspase-8
- Death-associated inhibitor of apoptosis 1
- AT03047p
- Caspase drICE
- Cell death protein rpr
- AT16536p
Sequence:
MDFETGEHQYQYKDILSVFEDAFVDNFDCKDVQDMPKSILSKEEIDHIIMSKDAVSGTLRLFWTLLSKQEEMVQKFVEEVLRINYKFLMSPIKTEQRQPSMMTRMYIEQRDRLYNDNQVFAKYNVSRLQPYLKLRQALLELRPAKNVLIDGVLGSGKTWVALDVCLSYKVQCKMDFKIFWLNLKNCNSPETVLEMLQKLLYQIDPNWTSRSDHSSNIKLRIHSIQAELRRLLKSKPYENCLLVLLNVQNAKAWNAFNLSCKILLTTRFKQVTDFLSAATTTHISLDHHSMTLTPDEVKSLLLKYLDCRPQDLPREVLTTNPRRLSIIAESIRDGLATWDNWKHVNCDKLTTIIESSLNVLEPAEYRKMFDRLSVFPPSAHIPTILLSLIWFDVIKSDVMVVVNKLHKYSLVEKQPKESTISIPSIYLELKVKLENEYALHRSIVDHYNIPKTFDSDDLIPPYLDQYFYSHIGHHLKNIEHPERMTLFRMVFLDFRFLEQKIRHDSTAWNASGSILNTLQQLKFYKPYICDNDPKYERLVNAILDFLPKIEENLICSKYTDLLRIALMAEDEAIFEEAHKQVQRFDDRVWFTNHGRFHQHRQIINLGDNEGRHAVYLHNDFCLIALASGQILLTDVSLEGEDTYLLRDESDSSDILRMAVFNQQKHLITLHCNGSVKLWSLWPDCPGRRHSGGSKQQLVNSVVKRFIGSYANLKIVAFYLNEDAGLPEANIQLHVAFINGDVSILNWDEQDQEFKLSHVPVLKTMQSGIRCFVQVLKRYYVVCTSNCTLTVWDLTNGSSNTLELHVFNVENDTPLALDVFDERSKTATVLLIFKYSVWRLNFLPGLSVSLQSEAVQLPEGSFITCGKRSTDGRYLLLGTSEGLIVYDLKISDPVLRSNVSEHIECVDIYELFDPVYKYIVLCGAKGKQVVHVHTLRSVSGSNSHQNREIAWVHSADEISVMTKACLEPNVYLRSLMDMTRERTQLLAVDSKERIHLIKPAISRISEWSTITPTHAASNCKINAISAFNDEQIFVGYVDGVIIDVIHDTALPQQFIEEPIDYLKQVSPNILVASAHSAQKTVIFQLEKIDPLQPNDQWPLMMDVSTKYASLQEGQYIILFSDHGVCHLDIANPSAFVKPKDSEEYIVGFDLKNSLLFLAYENNIIDVFRLIFSCNQLRYEQICEEEIAQKAKISYLVATDDGTMLAMGFENGTLELFAVENRKVQLIYSIEEVHEHCIRQLLFSPCKLLLISCAEQLCFWNVTHMRNNQLEREQKRRRSRRHKQHSVTQEDAVDAAPIAADIDVDVTFVADEFHPVNRGTAELWRNKRGNAIRPELLACVKFVGNEARQFFTDAHFSHFYAIDDEGVYYHLQLLELSRLQPPPDPVTLDIANQYEDLKNLRILDSPLMQDSDSEGADVVGNLVLEKNGGVARATPILEEASS
Protein: Purine nucleoside phosphorylase YfiH (EC 2.4.2.1) (Adenosine deaminase YfiH) (EC 3.5.4.4) (Polyphenol oxidase YfiH) (EC 1.10.3.-) (S-methyl-5'-thioadenosine phosphorylase YfiH) (EC 2.4.2.28) (P33644)
Organism: Escherichia coli (strain K12)
Function: Purine nucleoside enzyme that catalyzes the phosphorolysis of adenosine and inosine nucleosides, yielding D-ribose 1-phosphate and the respective free bases, adenine and hypoxanthine. Also catalyzes the phosphorolysis of S-methyl-5'-thioadenosine into adenine and S-methyl-5-thio-alpha-D-ribose 1-phosphate. Also has adenosine deaminase activity. May also act as a polyphenol oxidase: able to oxidize syringaldazine and 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) (ABTS) in vitro.
Interaction partners:
- Ribosomal large subunit pseudouridine synthase D synthase)
- Pyridoxal phosphate homeostasis protein
Sequence:
MSKLIVPQWPQPKGVAACSSTRIGGVSLPPYDSLNLGAHCGDNPDHVEENRKRLFAAGNLPSKPVWLEQVHGKDVLKLTGEPYASKRADASYSNTPGTVCAVMTADCLPVLFCNRAGTEVAAAHAGWRGLCAGVLEETVSCFADNPENILAWLGPAIGPRAFEVGGEVREAFMAVDAKASAAFIQHGDKYLADIYQLARQRLANVGVEQIFGGDRCTYTENETFFSYRRDKTTGRMASFIWLI
Protein: Integrin alpha-1 (CD49 antigen-like family member A) (Laminin and collagen receptor) (VLA-1) (CD antigen CD49a) (Q3V3R4)
Organism: Mus musculus (Mouse)
Function: Integrin alpha-1/beta-1 is a receptor for laminin and collagen. It recognizes the proline-hydroxylated sequence G-F-P-G-E-R in collagen. Involved in anchorage-dependent, negative regulation of EGF-stimulated cell growth.
Subcellular location: Membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
Interaction partners:
- Integrin beta-1
- Integrin beta-5
- Integrin beta-3
- Fibronectin
- Integrin beta-6
- Integrin beta-4
- Integrin alpha-6
- Integrin beta-8
- Collagen alpha-2
- Integrin alpha-3
Sequence:
MVPRRPASLEVTVACIWLLTVILGVCISFNVDVKNSMSFSGPVEDMFGYTVQQYENEEGKWVLIGSPLVGQPKARTGDVYKCPVGRERSMPCVKLDLPVNTSIPNVTEIKENMTFGSTLVTNPKGGFLACGPLYAYRCGHLHYTTGICSDVSPTFQVVNSFAPVQECSTQLDIVIVLDGSNSIYPWESVTAFLNDLLKRMDIGPKQTQVGIVQYGANVTHEFNLNKYSSTEEVLVAANKIGRRGGLQTMTALGIDTARKEAFTEARGARRGVKKVMVIVTDGESHDNYRLKQVIQDCEDENIQRFSIAILGHYNRGNLSTEKFVEEIKSIASEPTEKHFFNVSDELALVTIVKALGERIFALEATADQSAASFEMEMSQTGFSAHYSQDWVMLGAVGAYDWNGTVVMQKANQIVIPHNTTFQTEPTKMNEPLASYLGYTVNSATIPGDVLYIAGQPRYNHTGQVVIYKMEDGDVNILQTLSGEQIGSYFGSVLTTIDIDKDSYTDLLLVGAPMYMGTEKEEQGKVYVYAVNQTRFEYQMSLEPIKQTCCSSLKDNSCTKENKNEPCGARFGTAVAAVKDLNVDGFNDVVIGAPLEDDHAGAVYIYHGSGKTIRKEYAQRIPSGGDGKTLKFFGQSIHGEMDLNGDGLTDVTIGGLGGAALFWARDVAVVKVTMNFEPNKVNIQKKNCRVEGKETVCINATMCFHVKLKSKEDSVYEADLQYRVTLDSLRQISRSFFSGTQERRIQRNLTVRESECIRHSFYMLDKHDFQDSVRVTLDFNLTDPENGPVLDDALPNSVHGHIPFAKDCGNKERCVSDLTLDVSTTEKNLLIVRSQNDKFNVSLTVKNKGDSAYNTRTVVQYSPNLIFSGIEEIQKDSCESNQNITCRVGYPFLRTGDVVNFKIIFQFNTSHLSENAIIHLSATSDSEEPLESLYDNEVNISIPVKYEVGLQFYSSASEHHISVAANETVPELINSTKDIGDEINVFYTIRKRGHFPMPELRLAISFPNLTSDGYPVLYPTGWSSSDNVNCRPRSLEDPLGINSGKKMTISKSEVLKRGTIQDCSTCKIATITCHLLPSDVSQVNVSLILWKPTFIKAHFSSLNLTIRGELQSENSSLTLSSSNRKRELAIQISKDGLPGRVPLWVILLSAFAGLLLLMLLILALWKIGFFKRPLKKKMEK
Protein: Delta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrial (P5C dehydrogenase) (EC 1.2.1.88) (L-glutamate gamma-semialdehyde dehydrogenase) (P07275)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:11502169}.
Interaction partners:
- Proline dehydrogenase, mitochondrial
- Pyrroline-5-carboxylate reductase
- Proline utilization trans-activator
- Gamma-glutamyl phosphate reductase
- Glutamate 5-kinase
- Ornithine aminotransferase
- NAD-specific glutamate dehydrogenase
- Aspartate aminotransferase, cytoplasmic
- NADP-specific glutamate dehydrogenase 2
- Uncharacterized protein YHR033W
Sequence:
MLSARCLKSIYFKRSFSQLGHIKPPKHIRNEPVKPFRNIDLKDWDLLRASLMKFKSSSLEVPLVINGERIYDNNERALFPQTNPANHQQVLANVTQATEKDVMNAVKAAKDAKKDWYNLPFYDRSAIFLKAADLISTKYRYDMLAATMLGQGKNVYQAEIDCITELSDFFRYYVKYASDLYAQQPVESADGTWNKAEYRPLEGFVYAVSPFNFTAIAANLIGAPALMGNTVVWKPSQTAALSNYLLMTVLEEAGLPKGVINFIPGDPVQVTDQVLADKDFGALHFTGSTNVFKSLYGKIQSGVVEGKYRDYPRIIGETGGKNFHLVHPSANISHAVLSTIRGTFEFQGQKCSAASRLYLPESKSEEFLSDMFGILQSQNVVPMNTSASPISGGNLRGFMGPVIHEQSFDKLVKVIEDAKKDPELEILYGGQYDKSQGWFVGPTVIKAKRPDHPYMSTEFFGPILTVYEYPDTEFNEICDIIDNTSQYALTGAIFAKDRKAIEYADEKLKFSAGNFYINDKCTGAVVSQQWFGGARMSGTDDKAGGPNILSRFVSIRNTKENFYELTDFKYPSNYE