wanglab/gogpt-training-data huggingface dataset:
Protein: HSPA12B (Heat shock 70 kDa protein 12B) (Heat shock protein 12B) (Q0R4G9)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Heat shock cognate 71 kDa protein
- Heat shock protein 70 family, member 13.
- Heat shock protein 9
- Heat shock 70 kDa protein 4a
- Heat shock protein 105 kDa
- Heat shock 70 kDa protein 4L
- Immunoglobulin binding protein
- Heat shock cognate 71 kDa protein
- Heat shock protein 75 kDa, mitochondrial
- DnaJ heat shock protein family
Sequence:
MADVLQLSINSLQVPGEDKSDSTSPSGSPFPSRNECSITPLTPSPSPRTEVRPRLARPFYVVVAIDFGTTSSGYAFSFIEDPETIHMMRRWEGGDPGVANQKSPTCLLLTPDLRFHSFGFAARDSYHDLDPEEARHWLYFDKFKMKIHSTSDLTMETELESVSGRRVQAIEVFAHALRFFREHALKEVKDQSSSVLEGNEVRWVITVPAVWRQPAKQFMREAAYLAGLVPPDSPEQLLIALEPEAASIYCRKLRLHQVTDLSQRPVTNGFDIDGSRPFDSSFRQAREQLRRARHSRTFLVESGTGELWSEMQTGDRYIVADCGGGTVDLTVHQIEQPQGTLKELYKASGGPYGAVGVDLAFETMLCQIFGTDFIDSFKAKRPAAWVDLTIAFEARKRTAAPGRANTLNISLPFSFIDFYKQHRGQSVETALRKSNMNFIKWSSQGMLRLSTEATNELFQPTINNIIKHIENVMQKEEVKGVRFLFLVGGFAESPMLQRAIQNTLGRNCRIIIPHDVGLTILKGAVLFGLDPTVVRVRRCPLTYGVGVLNRFVEGRHPHDKLLIKDGREWCTDILDRFVSVDQSVALGEVVRRSYTPARMGQRKIIINIYCSDTDDITYITDPGVRKCGAITLDLLESGEASASTGDNDKGSAFERREIRTTMQFGDTEIKVTAVDVATGRLVRASIDFLSN
Protein: Envoplakin (210 kDa cornified envelope precursor protein) (p210) (Q9D952)
Organism: Mus musculus (Mouse)
Function: Component of the cornified envelope of keratinocytes. May link the cornified envelope to desmosomes and intermediate filaments.
Subcellular location: Cell junction, desmosome {ECO:0000250}. Cornified envelope {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Note=Colocalized with DSP at desmosomes and along intermediate filaments. {ECO:0000250}.
Interaction partners:
- Periplakin
- Protein-glutamine gamma-glutamyltransferase K
- Plakophilin-1
- Desmoglein-3
- Desmoglein-1-alpha
- Desmoglein-1-beta
- Desmoglein-1-gamma
- Loricrin
- Alpha-2-macroglobulin-like protein 1
- Desmoplakin
Sequence:
MFKGLSKGSQGKGSPKGSPAKGSPKGSPNKHNRAATQELALLISRMQANADQVERDILETQKKLQQDRQNGEQNQALQHQQETGRNLKEAEVLLKDLFLDVDKARRLKHPQAEEIEKDIKQLHERVTQECSEYRALYEKMVLPPDVGPRVDWARVLEQKQNLVREGHYGPGMAELEQQVAEHNILQREIEAYGQQLRTLVGPDANTIRNQYRELLKAASWRRQSLGSLYTHLQGCTKQLSALADQQGRILQQDWSDLMPDPAGVRREYEHFKQHELLAQERSINQLEDDADRMVELGHPAIGPIQVHQEALKMEWQNFLNLCICQESQLQRVEDYRRFQEEADSVSQTLAKLSSNLDTKYGFGTGDSSGSPTELLLQLEAEEKQLAIAERAVGDLQQRSQEVAPLPQRRNPSKQPLHVDSICDWDSGEVQLLRGERYTLKDNADPYTWLVQGPGGETKSAPAACLCIPAPDPEAVAKASRLATELQTLKQKLSTEKNRLKAAAVEHLQPGQQAPAGSAPADPQGQTLLSQMTQLDGDLGQIERQVLSWARSPLSQSSSLKDLEGRIHSCEGTAQRLQSLGAEKEAAQQECEAFLSTKPTGSAALQLPVVLNSVKNRYNDVQSLCHLYGEKAKAALGLEKQIQEADRVIQGFEAALALEGPVPEGSGALQERVSELQRQRKELLQQQACVLGLHRQLKATEHACSALQNNFQEFCQDLPRQQRQVRALTDRYHAVGDQLDLREKIVQDASLTYQQLRNSRDNLSSWLEQLPHHRVQPSDGPSQISYKLQAQKRLIQEILGREQDQATVSRLTRDLQEALQDYELQADTYRCSLEPALAVSAPKRLRVISLQESIQAQEKNLAKAYTEVAAAEQQQLRQLEFAKKMLRKKELDEDIQAIHSARQGSGSPAHARTAESEVLKTQLEEERKRVAEVQRDLEEQRQRLLQLRTQQPVARLEEKEVVEFYRDPQLESNLSQAASRVEEEGKRRARLQAELEAVAQKVVHLEGKRKTMQPHLLTKEVTQIERDPGLDSQVTQLHSEMQRLRGENGVLTARLEELKDELLALEQKEMNVKEKVVVKEVVKVEKDLEMVKAAQTLRLQIEEDAARRKGAKETVAKIQARIKDLEQAISSVEPKVIVKEVKKVEQDPGLLKEASRLRSLLEEEKNNNVALARELQELQEKYRVVEKQKPKVQLQERVSEIFQVLPETEQEIRRLRAQLQETGSKKSGVEQEVEKLLPELEVLRAQKPVVEYKEVTQEVVRHEKNPEVLREIDRLKAQLNELVNTNGRSQEQLIRLQGERDEWKRERSKVETKMVSKEVVRHEKDPVLEKEAERLRQEVREAVQRRRATEDAVYELQNKLLLLERRRPEEQIVVQEVVVTQKDPKLREEHSRLSRSLDEEVGRRRQLELEVRQLGARVEEEEARLSFEEDRSKKLAAERELRQLTLKIQELEKRPPALQEKIIMEEVVKLEKDPDLERSTEALRRELDQEKNRVTELHRECQGLQVQVDLLQKTKSQEKTIYKEVIRVEKDPVLEGERARVWEILNRERAARKGREEDVRSLQERIDRAEALRRSWSREEAELQRARDQASQDCGRLQRQLRELEQQKQQKARQLQEEGRLLSQKTESERQKAAQRSQAVTQLEAAILQEKDKIYEKERTLRDLHTKVSREELNQETQTRETNLSTKICILEPETGNDMSPYEAYKRGVIDRGQYLQLQELECDWEEVTTSSPCGEESVLLDRKSGKQYSIEAALRCRRISKEEYHRYKDGRLPISEFALLVAGETKPSSSLSIGSIISKSPVCSPGPQSTGFFSPGLSFGLTEDSFPIAGIYDTTTDNKCSIKAAVAKNMLDPITGQKLLEAQAATGGIVDLLSRERYSVHKAVERGLIENTSTQRLLNAQKAFTGIEDPVTRKRLSVGEAIQKGWMPQESVLPHLLVQHLTGGLIDPKRTGRIPVPQAVLCGMISEDLGQLLQDESGYEKDLTDPITKERLSYKEAMGRCRKDPLSGLLLLPAMLEGYRCYRAASPTLPRSCVR
Protein: Testicular tissue protein Li 213 (A0A140VJY6)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MGQKGHKDSLYPCGGTPESSLHEALDQCMTALDLFLTNQFSEALSYLKPRTKESMYHSLTYATILEMQAMMTFDPQDILLAGNMMKEAQMLCQRHRRKSSVTDSFSSLVNRPTLGQFTEEEIHAEVCYAECLLQRAALTFLQDENMVSFIKGGIKVRNSYQTYKELDSLVQSSQYCKGENHPHFEGGVKLGVGAFNLTLSMLPTRILRLLEFVGFSGNKDYGLLQLEEGASGHSFRSVLCVMLLLCYHTFLTFVLGTGNVNIEEAEKLLKPYLNRYPKGAIFLFFAGRIEVIKGNIDAAIRRFEECCEAQQHWKQFHHMCYWELMWCFTYKGQWKMSYFYADLLSKENCWSKATYIYMKAAYLSMFGKEDHKPFGDDEVELFRAVPGLKLKIAGKSLPTEKFAIRKSRRYFSSNPISLPVPALEMMYIWNGYAVIGKQPKLTDGILEIITKAEEMLEKGPENEYSVDDECLVKLLKGLCLKYLGRVQEAEENFRSISANEKKIKYDHYLIPNALLELALLLMEQDRNEEAIKLLESAKQNYKNYSMESRTHFRIQAATLQAKSSLENSSRSMVSSVSL
Protein: Stromelysin-2 (SL-2) (EC 3.4.24.22) (Matrix metalloproteinase-10) (MMP-10) (Transin-2) (O55123)
Organism: Mus musculus (Mouse)
Function: Can degrade fibronectin, gelatins of type I, III, IV, and V; weakly collagens III, IV, and V. Activates procollagenase.
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000305}.
Interaction partners:
- Stromelysin-1
- Metalloproteinase inhibitor 2
- Metalloproteinase inhibitor 1
- Fibronectin
- Metalloproteinase inhibitor 3
- Matrilysin
- Stromelysin-3
- Collagenase 3
Sequence:
MEPLAILALLSLPICSAYPLHGAVTQGHPSMDLAQQYLEKYYNFKKNEKQIFKRKDSSPVVKKIQEMQKFLGLEMTGKLDSNTMELMHKPRCGVPDVGGFSTFPGSPKWRKSHITYRIVNYTPDLPRQSVDSAIEKALKVWEEVTPLTFSRISEGEADIMISFAVGEHGDFYPFDGPGQSLAHAYPPGPGFYGDVHFDDDEKWTLAPSGTNLFLVAAHELGHSLGLFHSDKKESLMYPVYRFSTSPANFHLSQDDIEGIQSLYGAGPSSDATVVPVLSVSPRPETPDKCDPALSFDSVSTLRGEVLFFKDRYFWRRSHWNPEPEFHLISAFWPTLPSDLDAAYEAHNTDSVLIFKGSQFWAVRGNEVQAGYPKGIHTLGFPPTVKKIDAAVFEKEKKKTYFFVGDKYWRFDETRHVMDKGFPRQITDDFPGIEPQVDAVLHEFGFFYFFRGSSQFEFDPNARTVTHILKSNSWLLC
Protein: Transformer-2 protein homolog beta (TRA-2 beta) (TRA2-beta) (Silica-induced gene 41 protein) (SIG-41) (Splicing factor, arginine/serine-rich 10) (Transformer-2 protein homolog B) (P62996)
Organism: Mus musculus (Mouse)
Function: Sequence-specific RNA-binding protein which participates in the control of pre-mRNA splicing. Can either activate or suppress exon inclusion. Acts additively with RBMX to promote exon 7 inclusion of the survival motor neuron SMN2. Activates the splicing of MAPT/Tau exon 10. Alters pre-mRNA splicing patterns by antagonizing the effects of splicing regulators, like RBMX. Binds to the AG-rich SE2 domain in the SMN exon 7 RNA. Binds to pre-mRNA (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:28785060}.
Interaction partners:
- Serine/arginine-rich splicing factor 3
- Serine/arginine-rich splicing factor 7
- Serine/arginine-rich splicing factor 1
- Serine/arginine-rich splicing factor 9
- Serine/arginine-rich splicing factor 2
- Serine/arginine-rich splicing factor 10
- Heterogeneous nuclear ribonucleoproteins A2/B1
- Serine/arginine-rich splicing factor 6
- Heterogeneous nuclear ribonucleoproteins C1/C2
- Serine/arginine-rich splicing factor 5
Sequence:
MSDSGEQNYGERESRSASRSGSAHGSGKSARHTPARSRSKEDSRRSRSKSRSRSESRSRSRRSSRRHYTRSRSRSRSHRRSRSRSYSRDYRRRHSHSHSPMSTRRRHVGNRANPDPNCCLGVFGLSLYTTERDLREVFSKYGPIADVSIVYDQQSRRSRGFAFVYFENVDDAKEAKERANGMELDGRRIRVDFSITKRPHTPTPGIYMGRPTYGSSRRRDYYDRGYDRGYDDRDYYSRSYRGGGGGGGGWRAAQDRDQIYRRRSPSPYYSRGGYRSRSRSRSYSPRRY
Protein: Allergen Ara h 1, clone P41B (Allergen Ara h I) (allergen Ara h 1) (P43238)
Organism: Arachis hypogaea (Peanut)
Interaction partners:
Sequence:
MRGRVSPLMLLLGILVLASVSATHAKSSPYQKKTENPCAQRCLQSCQQEPDDLKQKACESRCTKLEYDPRCVYDPRGHTGTTNQRSPPGERTRGRQPGDYDDDRRQPRREEGGRWGPAGPREREREEDWRQPREDWRRPSHQQPRKIRPEGREGEQEWGTPGSHVREETSRNNPFYFPSRRFSTRYGNQNGRIRVLQRFDQRSRQFQNLQNHRIVQIEAKPNTLVLPKHADADNILVIQQGQATVTVANGNNRKSFNLDEGHALRIPSGFISYILNRHDNQNLRVAKISMPVNTPGQFEDFFPASSRDQSSYLQGFSRNTLEAAFNAEFNEIRRVLLEENAGGEQEERGQRRWSTRSSENNEGVIVKVSKEHVEELTKHAKSVSKKGSEEEGDITNPINLREGEPDLSNNFGKLFEVKPDKKNPQLQDLDMMLTCVEIKEGALMLPHFNSKAMVIVVVNKGTGNLELVAVRKEQQQRGRREEEEDEDEEEEGSNREVRRYTARLKEGDVFIMPAAHPVAINASSELHLLGFGINAENNHRIFLAGDKDNVIDQIEKQAKDLAFPGSGEQVEKLIKNQKESHFVSARPQSQSQSPSSPEKESPEKEDQEEENQGGKGPLLSILKAFN
Protein: N-alpha-acetyltransferase 35, NatC auxiliary subunit (Embryonic growth-associated protein) (zEGAP) (Protein MAK10 homolog) (Q7T322)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Auxillary component of the N-terminal acetyltransferase C (NatC) complex which catalyzes acetylation of N-terminal methionine residues. Regulates cell proliferation during embryonic development. May be involved in acetylating the N-terminus of mtor.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q5VZE5}.
Interaction partners:
- N-alpha-acetyltransferase 38, NatC auxiliary subunit
- N-alpha-acetyltransferase 30
- Small nuclear ribonucleoprotein E
- N-alpha-acetyltransferase 50
- N
- PHD finger protein 20, b
- Zinc finger protein 710
- N-terminal amino-acid N
- N-alpha-acetyltransferase 20
- DALR anticodon-binding domain-containing protein 3
Sequence:
MVMKSSVEEEEGGWGLGIPEKMRNNANWVDVTQEFKGACKELKLGELLHDKLFGLFEAMSAIEMMDPKMDAGMIGNQVNRKVLNFDQAVKDEAIRVKDLSIPELIGIMDTCFCCLITWLEGHSLAQTVFTCLYVHNPDLIQDPALKAFALGILKICDIAREKVNKAAVFEEEDFQAMTYGFKMANNVTDLRVTGMLKDVEDELQRKVKSTRSRQGEQRDPEVELDHQQCLALFSRVKFTRLLLSALISFTKKETSAVSEAQKLMSQAADLLPAVHATIQYGIQSQNDTTKGDHPIMMGFEPLVNQRLLPPTFPRYAKIIKREEMVNYFSKLIERIKSVCEVINITNLHSILDFFCEFSEQSPCVLSRSLLQTTFLIDNKKVFGTHLMQDMIKDALRCFVSPPVLSSKCSLNNNHQAKDYIDSFVTHCTRPFCSLIQIHGHNRARQRDKLGHILEEFATLQDEAEKVDAALHGLLMKLEPQRQHLACLGTWILYHNLRIMIQYLLSGFELELYSMHEYYYIYWYLSEFLYAWLMSTLSRADSSQMAEERILEEQLKVRSSKKSKKKKKARPLSKEITMSQAYQNMCAGMYKTMIALDMDRKVRKPQFELDSEQVRYEHRFAPFNSVVTPPPVHYIQFKEMSDLKKYNPPPRSADLYMAASKHFQQAKLLLENVTSPDAEVNRILKVAKPNIVVMKLLAGGHKKETKALPEFDFSAHKYFPIVKIL
Protein: GPN-loop GTPase 2 (EC 3.6.5.-) (ATP-binding domain 1 family member B homolog) (Q9UTL7)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Small GTPase required for proper nuclear import of RNA polymerase II and III (RNAPII and RNAPIII). May act at an RNAP assembly step prior to nuclear import.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- GPN-loop GTPase 1
- DNA-directed RNA polymerase II subunit RPB2
- RNA polymerase II nuclear localization protein iwr1
- DNA-directed RNA polymerase II subunit RPB3
- Probable aminomethyltransferase, mitochondrial
- DNA-directed RNA polymerases I, II, and III subunit RPABC5
- mRNA cleavage and polyadenylation factor clp1
- Probable Rho-type GTPase-activating protein 3
- Probable Rho-type GTPase-activating protein 4
- DNA-directed RNA polymerase II subunit RPB11
Sequence:
MPFCQVVVGPPGSGKSTYCFGMYQLLSAIGRSSIIVNLDPANDFIKYPCAIDIRKVLDVEMIQKDYDLGPNGALIYAMEAIEYHVEWLLKELKKHRDSYVIFDCPGQVELFTNHNSLQKIIKTLEKELDYRPVSVQLVDAYCCTNPSAYVSALLVCLKGMLQLDMPHVNILSKADLLCTYGTLPMKLDFFTEVQDLSYLAPLLDRDKRLQRYSDLNKAICELVEDFNLVSFEVVAVENKASMLRVLRKIDQAGGYAYGSTEIGGDAVWVNAVRQGGDPLQGISPQERWIDKKEEYDKYEWELEQKSTMDEDENEG
Protein: Acyl-CoA dehydrogenase FadE34 (ACAD) (EC 1.3.99.-) (3-oxochol-4-en-24-oyl-CoA dehydrogenase) (P96855)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Involved in the second cycle of side chain dehydrogenation in the beta-oxidation of cholesterol catabolism. It contributes partly to the virulence by increasing the efficiency of beta-oxidation. Catalyzes the dehydrogenation of the five-carbon steroid side chain of 3-oxo-chol-4-en-24-oyl-CoA (3-OCO-CoA) to yield 3-oxochol-4,22-dien-24-oyl-CoA. Can also use 3beta-hydroxy-chol-5-ene-24-oyl-CoA, and shows weak activity with cholyl-CoA and deoxycholyl-CoA.
Interaction partners:
- Steroid 3-ketoacyl-CoA thiolase
- 17-hydroxy-3-oxo-4-pregnene-20-carboxyl-CoA lyase
- 3-hydroxyisobutyryl-CoA hydrolase
- HTH-type transcriptional repressor KstR
- Possible lipid transfer protein or keto acyl-CoA thiolase Ltp4
- 3-oxo-4,17-pregnadiene-20-carboxyl-CoA hydratase beta subunit
- Probable lipid carrier protein or keto acyl-CoA thiolase Ltp3
- Medium/long-chain-fatty-acid--CoA/3-oxocholest-4-en-26-oate--CoA ligase
- Probable fatty-acid-CoA ligase FadD36
- (7aS)-7a-methyl-1,5-dioxo-2,3,5,6,7,7a-hexahydro-1H-indene-carboxyl-CoA hydrolase (HIEC-CoA hydrolase)
Sequence:
MVATVTDEQSAARELVRGWARTAASGAAATAAVRDMEYGFEEGNADAWRPVFAGLAGLGLFGVAVPEDCGGAGGSIEDLCAMVDEAARALVPGPVATTAVATLVVSDPKLRSALASGERFAGVAIDGGVQVDPKTSTASGTVGRVLGGAPGGVVLLPADGNWLLVDTACDEVVVEPLRATDFSLPLARMVLTSAPVTVLEVSGERVEDLAATVLAAEAAGVARWTLDTAVAYAKVREQFGKPIGSFQAVKHLCAQMLCRAEQADVAAADAARAAADSDGTQLSIAAAVAASIGIDAAKANAKDCIQVLGGIGCTWEHDAHLYLRRAHGIGGFLGGSGRWLRRVTALTQAGVRRRLGVDLAEVAGLRPEIAAAVAEVAALPEEKRQVALADTGLLAPHWPAPYGRGASPAEQLLIDQELAAAKVERPDLVIGWWAAPTILEHGTPEQIERFVPATMRGEFLWCQLFSEPGAGSDLASLRTKAVRADGGWLLTGQKVWTSAAHKARWGVCLARTDPDAPKHKGITYFLVDMTTPGIEIRPLREITGDSLFNEVFLDNVFVPDEMVVGAVNDGWRLARTTLANERVAMATGTALGNPMEELLKVLGDMELDVAQQDRLGRLILLAQAGALLDRRIAELAVGGQDPGAQSSVRKLIGVRYRQALAEYLMEVSDGGGLVENRAVYDFLNTRCLTIAGGTEQILLTVAAERLLGLPR
Protein: Cell division control protein 11 (P32458)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Septins are GTPases involved in cytokinesis that assemble early in the cell cycle as a patch at the incipient bud site and form a ring approximate 15 minutes before bud emergence, which transforms into an hour-glass shaped collar of cortical filaments that spans both sides of the mother-bud neck. This collar persists until just before cytokinesis, when it splits into two rings that occupy opposite sides of the neck. The septins at the bud neck serve as a structural scaffold that recruits different components involved in diverse processes at specific stages during the cell cycle. Many proteins bind asymmetrically to the septin collar. The septin assembly is regulated by protein kinases GIN4 and/or CLA4. May act by recruiting MYO1 and HOF1, a protein involved in septation, to the site of cleavage. Septins are also involved in cell morphogenesis, bud site selection, chitin deposition, cell cycle regulation, cell compartmentalization and spore wall formation.
Subcellular location: Membrane {ECO:0000269|PubMed:14562095}. Bud neck {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:25971666}. Note=Present at the bud neck during cell division. Interacts with phosphatidylinositol 4-phosphate and phosphatidylinositol 5-phosphate (PI(4)P and PI(5)P).
Interaction partners:
- Cell division control protein 12
- Seventh homolog of septin 1
- Cell division control protein 3
- Cell division control protein 10
- Probable serine/threonine-protein kinase KCC4
- Sporulation-regulated protein 28
- Serine/threonine-protein kinase GIN4
- Bud neck protein 5
- Probable serine/threonine-protein kinase HSL1
- Sporulation-regulated protein 3
Sequence:
MSGIIDASSALRKRKHLKRGITFTVMIVGQSGSGRSTFINTLCGQQVVDTSTTILLPTDTSTEIDLQLREETVELEDDEGVKIQLNIIDTPGFGDSLDNSPSFEIISDYIRHQYDEILLEESRVRRNPRFKDGRVHCCLYLINPTGHGLKEIDVEFIRQLGSLVNIIPVISKSDSLTRDELKLNKKLIMEDIDRWNLPIYNFPFDEDEISDEDYETNMYLRTLLPFAIIGSNEVYEMGGDVGTIRGRKYPWGILDVEDSSISDFVILRNALLISHLHDLKNYTHEILYERYRTEALSGESVAAESIRPNLTKLNGSSSSSTTTRRNTNPFKQSNNINNDVLNPASDMHGQSTGENNETYMTREEQIRLEEERLKAFEERVQQELLLKRQELLQREKELREIEARLEKEAKIKQEE
Protein: Bifunctional lipase/adenylate cyclase LipJ [Includes: Lipase (EC 3.1.1.-); Adenylate cyclase (EC 4.6.1.1) (Adenylyl cyclase)] (O07732)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Uncharacterized protein Rv1899c
- Alanine aminotransferase
Sequence:
MAQAPHIHRTRYAKCGDMDIAYQVLGDGPTDLLVLPGPFVPIDSIDDEPSLYRFHRRLASFSRVIRLDHRGVGLSSRLAAITTLGPKFWAQDAIAVMDAVGCEQATIFAPSFHAMNGLVLAADYPERVRSLIVVNGSARPLWAPDYPVGAQVRRADPFLTVALEPDAVERGFDVLSIVAPTVAGDDVFRAWWDLAGNRAGPPSIARAVSKVIAEADVRDVLGHIEAPTLILHRVGSTYIPVGHGRYLAEHIAGSRLVELPGTDTLYWVGDTGPMLDEIEEFITGVRGGADAERMLATIMFTDIVGSTQHAAALGDDRWRDLLDNHDTIVCHEIQRFGGREVNTAGDGFVATFTSPSAAIACADDIVDAVAALGIEVRIGIHAGEVEVRDASHGTDVAGVAVHIGARVCALAGPSEVLVSSTVRDIVAGSRHRFAERGEQELKGVPGRWRLCVLMRDDATRTR
Protein: Colipase (D5FQ08)
Organism: Meleagris gallopavo (Wild turkey)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
GLIFNLDTGELCVQSAQCKSGCCQRDSGLSLARCSLKAAETQDCSRKSLYGVYYKCPCESGLSCDADWSIVGSITNTDYGVCYDKRDPTSR
Protein: Alpha-2-antiplasmin (Alpha-2-AP) (Alpha-2-plasmin inhibitor) (Alpha-2-PI) (Serpin F2) (P83168)
Organism: Struthio camelus (Common ostrich)
Function: Serine protease inhibitor. The major targets of this inhibitor are plasmin and trypsin, but it also inactivates matriptase-3/TMPRSS7 and chymotrypsin.
Subcellular location: Secreted.
Interaction partners:
Sequence:
LQVDYLVLEVA
Protein: RE64043p (Q8SYF5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MVQNRMSTSVIVLYALMCIAFSTASLNDIPEITPAIDNNLSFQYDDTCWTPPRIKNAKASVKLRRNGEHVFLVTYYSCRVNYKLKRAKDNALYCSNGIWLGLKPNCIKIGKGNTHSMKQKKMRCRIDNGGCAHICNRSTHKCECYEGYTLNSTDLRSCNDIDECKESNGGCSQVCNNLPGEFICTCNSGFEIDESDEKTCLDIDECADPELSWDCTAGCKNLNGTYKCLPSLVGRVEPTDGDGFSPGEIVCKSGFKLSDDGSECQDINECDLADIDSDSWRMTYRYCEHKCENTVGSYICHCPQGYHLLDDQNSCILDGSKLPPSKDAPVSQEAPRKDICPLFKGPANGKASCDKYLQNGFNYTRCNITCNAGYIMQGSQFAVCGHTGLWSSPEAKCVESLALSCPVLTPPRNGRFYPASCNNEPSKSLAICELLCDRGYLPRMDTQLICAAPWGWIQRRWQDNVPQYVFQQSVKQDEGCVKIAPP
Protein: Mitochondrial import inner membrane translocase subunit TIM50 (Q9D880)
Organism: Mus musculus (Mouse)
Function: Essential component of the TIM23 complex, a complex that mediates the translocation of transit peptide-containing proteins across the mitochondrial inner membrane. Has some phosphatase activity in vitro; however such activity may not be relevant in vivo.
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q3ZCQ8}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q3ZCQ8}.
Interaction partners:
- Mitochondrial import inner membrane translocase subunit Tim23
- Mitochondrial import inner membrane translocase subunit Tim21
- Mitochondrial import inner membrane translocase subunit Tim17-B
- Mitochondrial import inner membrane translocase subunit Tim17-A
- Mitochondrial import inner membrane translocase subunit TIM16
- Mitochondrial import inner membrane translocase subunit TIM44
- Mitochondrial import receptor subunit TOM40 homolog
- Mitochondrial import inner membrane translocase subunit TIM14
- Mitochondrial import receptor subunit TOM22 homolog
- Mitochondrial import receptor subunit TOM70
Sequence:
MAASAALFSRLRSGLRVGARGLCTRLAPPPPRTPEQVTEIANRGGSKAQGPQHQPGSEGPSYAKKIALWIAGLLGAGGTVSIVYIFGNNPVDENGTKIPDEFDSDPILVQQLRRTYKYFKDYRQMIIEPTSPCLLPDPLREPYYQPPYTLVLELTGVLLHPEWSLATGWRFKKRPGIETLFQQLAPLYEIVIFTSETGMTAFPLIDSVDPHGFISYRLFRDATRYMEGHHVKDISCLNRDPARVVVVDCKKEAFRLQPFNGVALRPWDGNSDDRVLLDLSAFLKTIALNQVEDVRTVLEHYALEDDPLEAFKQRQSRLEQEEQQRLAELSKSNRQGLSFGSLASRLWPRSKQP
Protein: Pyocin-S2 immunity protein (Q06579)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- Pyocin-S2
Sequence:
MKSKISEYTEKEFLEFVKDIYTNNKKKFPTEESHIQAVLEFKKLTEHPSGSDLLYYPNENREDSPAGVVKEVKEWRASKGLPGFKAG
Protein: Kinesin-like protein KIF17 (KIF3-related motor protein) (Q9P2E2)
Organism: Homo sapiens (Human)
Function: Dendrite-specific motor protein which, in association with the Apba1-containing complex (LIN-10-LIN-2-LIN-7 complex), transports vesicles containing N-methyl-D-aspartate (NMDA) receptor subunit NR2B along microtubules.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000305}. Cell projection, cilium {ECO:0000250|UniProtKB:Q99PW8}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q99PW8}. Note=Localizes to dendrites of pyramidal neurons (By similarity). Does not localize to the axons or nuclei in cerebral cortex, hippocampus or olfactory bulb (By similarity). Co-localizes with NR2B-containing vesicles along microtubules (By similarity). {ECO:0000250|UniProtKB:Q99PW8}.
Interaction partners:
- Amyloid-beta A4 precursor protein-binding family A member 1
- Glutamate receptor ionotropic, NMDA 2B
- Transportin-1
- Protein lin-7 homolog A
- Peripheral plasma membrane protein CASK
- Kinesin-like protein KIF11
- Kinesin-associated protein 3
- Septin-9
- Disks large homolog 4
- Microtubule-associated protein RP/EB family member 1
Sequence:
MASEAVKVVVRCRPMNQRERELRCQPVVTVDCARAQCCIQNPGAADEPPKQFTFDGAYHVDHVTEQIYNEIAYPLVEGVTEGYNGTIFAYGQTGSGKSFTMQGLPDPPSQRGIIPRAFEHVFESVQCAENTKFLVRASYLEIYNEDVRDLLGADTKQKLELKEHPEKGVYVKGLSMHTVHSVAQCEHIMETGWKNRSVGYTLMNKDSSRSHSIFTISIEMSAVDERGKDHLRAGKLNLVDLAGSERQSKTGATGERLKEATKINLSLSALGNVISALVDGRCKHVPYRDSKLTRLLQDSLGGNTKTLMVACLSPADNNYDETLSTLRYANRAKNIRNKPRINEDPKDALLREYQEEIKKLKAILTQQMSPSSLSALLSRQVPPDPVQVEEKLLPQPVIQHDVEAEKQLIREEYEERLARLKADYKAEQESRARLEEDITAMRNSYDVRLSTLEENLRKETEAVLQVGVLYKAEVMSRAEFASSAEYPPAFQYETVVKPKVFSTTDTLPSDDVSKTQVSSRFAELPKVEPSKSEISLGSSESSSLEETSVSEAFPGPEEPSNVEVSMPTEESRSRYFLDECLGQEAAGHLLGEQNYLPQEEPQEVPLQGLLGLQDPFAEVEAKLARLSSTVARTDAPQADVPKVPVQVPAPTDLLEPSDARPEAEAADDFPPRPEVDLASEVALEVVRTAEPGVWLEAQAPVALVAQPEPLPATAGVKRESVGMEVAVLTDDPLPVVDQQQVLARLQLLEQQVVGGEQAKNKDLKEKHKRRKRYADERRKQLVAALQNSDEDSGDWVLLNVYDSIQEEVRAKSKLLEKMQRKLRAAEVEIKDLQSEFQLEKIDYLATIRRQERDSMLLQQLLEQVQPLIRRDCNYSNLEKILRESCWDEDNGFWKIPHPVITKTSLPVAVSTGPQNKPARKTSAADNGEPNMEDDRYRLMLSRSNSENIASNYFRSKRASQILSTDARKSLTHHNSPPGLSCPLSNNSAIPPTQAPEMPQPRPFRLESLDIPFTKAKRKKSKSNFGSEPL
Protein: Dihydrofolate synthase/folylpolyglutamate synthase (DHFS / FPGS) (EC 6.3.2.12) (EC 6.3.2.17) (Folylpoly-gamma-glutamate synthetase-dihydrofolate synthetase) (Folylpolyglutamate synthetase) (Tetrahydrofolylpolyglutamate synthase) (P08192)
Organism: Escherichia coli (strain K12)
Function: Functions in two distinct reactions of the de novo folate biosynthetic pathway. Catalyzes the addition of a glutamate residue to dihydropteroate (7,8-dihydropteroate or H2Pte) to form dihydrofolate (7,8-dihydrofolate monoglutamate or H2Pte-Glu). Also catalyzes successive additions of L-glutamate to tetrahydrofolate or 10-formyltetrahydrofolate or 5,10-methylenetetrahydrofolate, leading to folylpolyglutamate derivatives.
Interaction partners:
- Dihydropteroate synthase
- Dihydrofolate reductase
- 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase
- Cell division protein DedD
- Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta
- Thymidylate synthase
- Dihydromonapterin reductase
- GTP cyclohydrolase 1
- Dihydroneopterin aldolase
- Amidophosphoribosyltransferase
Sequence:
MIIKRTPQAASPLASWLSYLENLHSKTIDLGLERVSLVAARLGVLKPAPFVFTVAGTNGKGTTCRTLESILMAAGYKVGVYSSPHLVRYTERVRVQGQELPESAHTASFAEIESARGDISLTYFEYGTLSALWLFKQAQLDVVILEVGLGGRLDATNIVDADVAVVTSIALDHTDWLGPDRESIGREKAGIFRSEKPAIVGEPEMPSTIADVAQEKGALLQRRGVEWNYSVTDHDWAFSDAHGTLENLPLPLVPQPNAATALAALRASGLEVSENAIRDGIASAILPGRFQIVSESPRVIFDVAHNPHAAEYLTGRMKALPKNGRVLAVIGMLHDKDIAGTLAWLKSVVDDWYCAPLEGPRGATAEQLLEHLGNGKSFDSVAQAWDAAMADAKAEDTVLVCGSFHTVAHVMEVIDARRSGGK
Protein: tRNA pseudouridine synthase A-like protein (Q387U9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- 30S Ribosomal protein S17, putative
- Methyltransferase
- Uncharacterized protein
- Rhodanese domain-containing protein
- PROP1-like PPR domain-containing protein
- Uncharacterized protein
- Uncharacterized protein
- Uncharacterized protein
- Mitochondrial ribosomal protein S18
- Uncharacterized protein
Sequence:
MRRLSVSFLPFHLIVTTQRRQFGGNSKDGHKGEDKPIERVGGVPPTGPHPFNITSGAEGQISNQQRKAHDAITQLFRDDAQRKALYQKPGRTIGAQTTTAAISTPPNEDEFEGLQPISGDAEPSSITAVEAVEQELLDDAFLYFPPAQQSASGSVATTATNELYVPGQQIIPPGLTRYRVDVQYQGNDFDGWWKSTTRQLFRREVGLDGSITRVPVAEPGTIGNAAGVSRGETMGSRYHARTVLEEALAVALDVNTVRVVAGVIPEVGVSVRRLCCHVDVPSHIELQPRTVIQRATMWMEKRQQPLAILSYRRCKNQDFHARHSGLRRVYVYRILNRVAPPLFDAGLQWHVDRHLDVDRMKRFAKTLEGTKDFGYFADPKMANALRRAAMSPGGFSTGAVTEENFQPKATGESHRVTRGKAPKVTMEKGPSNLDRAAALPTFNEYGQRVVQPGAHGKEYYRVATNLPTVRTVDRLDVVRQDDEVLIWFVGRSFLRHQIRNMVSVLKAAGHGLWNDLELQQALQSGFEPSRHRFKRERFPTAPAYGLTLWDVEYPDQHRDDYVQFVDSGPYEQVNIARDI
Protein: TSC22D4 protein (Q8IV54)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSGGKKKSSFQITSVTTDYEGPGSPGASDPPTPQPPTGPPPRLPNGEPSPDPGGKGTPRNGSPPPGAPSSRFRVVKLPHGLGEPYRRGRWTCVDVYERDLEPHSFGGLLEGIRGASGGAGGRSLDSRLELASLGLGAPTPPSGLSQGPTSWLRPPPTSPGPQARSFTGGLGQLVVPSKAKAEKPPLSASSPQQRPPEPETGESAGTSRAATPLPSLRVEAEAGGSGARTPPLSRRKAVDMRLRMELGAPEEMGQVPPLDSRPSSPALYFTHDASLVHKSPDPFGAVAAQKFSLAHSMLAISGHLDSDDDR