wanglab/gogpt-training-data huggingface dataset:
Protein: Integrator complex subunit 11 (Int11) (EC 3.1.27.-) (Cleavage and polyadenylation-specific factor 3-like protein) (CPSF3-like protein) (Protein related to CPSF subunits of 68 kDa) (RC-68) (Q5TA45)
Organism: Homo sapiens (Human)
Function: Catalytic component of the Integrator (INT) complex, a complex involved in the small nuclear RNAs (snRNA) U1 and U2 transcription and in their 3'-box-dependent processing. The Integrator complex is associated with the C-terminal domain (CTD) of RNA polymerase II largest subunit (POLR2A) and is recruited to the U1 and U2 snRNAs genes. Mediates the snRNAs 3' cleavage. Mediates recruitment of cytoplasmic dynein to the nuclear envelope, probably as component of the INT complex.
Subcellular location: Nucleus {ECO:0000269|PubMed:15684398, ECO:0000269|PubMed:23904267, ECO:0000269|PubMed:29471365, ECO:0000269|PubMed:36454007, ECO:0000269|PubMed:39032489, ECO:0000269|PubMed:39032490}. Cytoplasm {ECO:0000269|PubMed:15684398, ECO:0000269|PubMed:23904267, ECO:0000269|PubMed:29471365, ECO:0000269|PubMed:36454007, ECO:0000269|PubMed:39032489}.
Interaction partners:
- Integrator complex subunit 5
- Integrator complex subunit 1
- Integrator complex subunit 4
- Integrator complex subunit 9
- Integrator complex subunit 6
- Integrator complex subunit 3
- Integrator complex subunit 7
- Integrator complex subunit 2
- Integrator complex subunit 10
- Integrator complex subunit 8
Sequence:
MPEIRVTPLGAGQDVGRSCILVSIAGKNVMLDCGMHMGFNDDRRFPDFSYITQNGRLTDFLDCVIISHFHLDHCGALPYFSEMVGYDGPIYMTHPTQAICPILLEDYRKIAVDKKGEANFFTSQMIKDCMKKVVAVHLHQTVQVDDELEIKAYYAGHVLGAAMFQIKVGSESVVYTGDYNMTPDRHLGAAWIDKCRPNLLITESTYATTIRDSKRCRERDFLKKVHETVERGGKVLIPVFALGRAQELCILLETFWERMNLKVPIYFSTGLTEKANHYYKLFIPWTNQKIRKTFVQRNMFEFKHIKAFDRAFADNPGPMVVFATPGMLHAGQSLQIFRKWAGNEKNMVIMPGYCVQGTVGHKILSGQRKLEMEGRQVLEVKMQVEYMSFSAHADAKGIMQLVGQAEPESVLLVHGEAKKMEFLKQKIEQELRVNCYMPANGETVTLPTSPSIPVGISLGLLKREMAQGLLPEAKKPRLLHGTLIMKDSNFRLVSSEQALKELGLAEHQLRFTCRVHLHDTRKEQETALRVYSHLKSVLKDHCVQHLPDGSVTVESVLLQAAAPSEDPGTKVLLVSWTYQDEELGSFLTSLLKKGLPQAPS
Protein: Katanin p60 ATPase-containing subunit A1 (Katanin p60 subunit A1) (EC 5.6.1.1) (p60 katanin) (Q8SZ40)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm, cytoskeleton, spindle {ECO:0000256|ARBA:ARBA00004186, ECO:0000256|HAMAP-Rule:MF_03023}. Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03023}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000256|HAMAP-Rule:MF_03023}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000256|HAMAP-Rule:MF_03023}. Note=Predominantly cytoplasmic. Also localized to the interphase centrosome and the mitotic spindle poles. Enhanced recruitment to the mitotic spindle poles requires microtubules and interaction with KATNB1. {ECO:0000256|HAMAP-Rule:MF_03023}.
Interaction partners:
Sequence:
MSITLLRGGKQKTTTCVGMTVMAKTTFEEICENAKLARDMALTGNYDSACIYYEGLQGLLARQLKATADPLRKGKWSMINQQISQEHAKIKAIQRTLQDISLDLQSTKFAHKLRHQLSEESTTSKDPSAWFKPDPDIWTPPPKDPDVWGPPKPPPTTQAVGRRAAPNNRRTTPATQNSRPSSTIPQSTARNGPASTRNSRNSTSATAPSGGARTTNGRAGGRKLSTSNTNEARDDDSTAAGNNGGAAGDGENGDPQAAQEEERKFQTNNHIEAELVDILERDILQKDPKVRWSDIADLHDAKRLLEEAVVLPMLMPDYFKGIRRPWKGVLMVGPPGTGKTMLAKAVATECGTTFFNVSSATLTSKYRGESEKMVRLLFEMARFYAPSTIFIDEIDSLCSRRGSESEHEASRRVKSELLVQMDGVGGGEEQAKVVMVLAATNFPWDIDEALRRRLEKRIYIPLPSDEGREALLKINLREVKVDDSVDLTYVANELKGYSGADITNVCREASMMSMRRKIAGLTPEQIRQLATEEVDLPVSNKDFNEAMSRCNKSVSRADLDKYEKWMREFGSS
Protein: Serine/threonine-protein phosphatase 4 regulatory subunit ppfr-4 (Q9N4E9)
Organism: Caenorhabditis elegans
Function: Probable regulatory subunit of serine/threonine-protein phosphatase PP4 which may play a role in meiosis and embryonic mitosis. Probably in association with catalytic subunit pph-4.1, regulates microtubule severing during oocyte meiosis II by dephosphorylating and likely activating mei-1, a component of the katanin microtubule severing complex.
Interaction partners:
- Serine/threonine-protein phosphatase 2A catalytic subunit
- Serine/threonine-protein phosphatase 6 catalytic subunit
- Serine/threonine-protein phosphatase 4 catalytic subunit 1
- Serine/threonine-protein phosphatase 4 catalytic subunit 2
- TIP41-like protein
- Target of rapamycin homolog
- Target of rapamycin complex subunit lst8
- DAF-15
- Serine/threonine-protein phosphatase 2A activator
- Serine/threonine-protein phosphatase 4 regulatory subunit 1
Sequence:
MSELSDEEISLQALYDPSKKVIGDIEDGIFSTPELQPRIKTGIDNLQLVTKLVNQMRLFSSNEQIEDVPTNSLPYLLVPCFLGILHQNLMTEPGLKLDELRKSKIYMRNFLDRLRDLCLITTRLPWEDEDTEEQNLKEKPKLAVEEIRRLKLERHKKKQELKMAELRIQKQLEAVSIDEQNLRELYITQLLFWSERCYEELQAIDDELPLLKMMAERASHPHRHPAPPPATKTVPTLKPFIITRDAQQKQVFGLGYPGIPAMSVDEWYHQKFGHNPQNAPQSSAPAGAEAQESEEEVDDDEARAKAMRWDEYKDDHRRGWGNMHNKG
Protein: Chromatin accessibility complex (CHRAC) (Q9NG24)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00475}.
Interaction partners:
Sequence:
MPICKREGFDLNQKEGKNETFHDNDQVFCCYITKRIFRDYEHYFRHVMVINSTVWQCEATGKENLTYEEAVKSERAARKKMEQFKQSLRSPVLLVVEHAQQSAVNTLNMIVAKFLRKRYFIGEEVSVQAKKNATYTVLGVKLDKNMPEPLNGIYEDTDNLVYRLRPNKGDPSAELDLPFRQLRRSRMEFNLENLSMFIKSNVSRVDGLLRPKPEAYKQYVTDPGVNFSTIFIGKMPRYSPAKIKKPDGKKQSTLNKYIVAGEATAAKSKAKAKSDAKSLAEELERVKREKEAKLIELEKQKAEKKAQLIERVENECNLLLQKTDDLERTDQKVLPRYRQIVTLLPEHLLGDAFMMREFMHTYTGLLSGIEVFRQNLSFYEMTRALTAREIAGPLSDILLVLLGTVFDLQKEEEEECAVTYLDRAAQTQEPYWSMAQAAKSHLYAKRHFSFKVNELPLDALTLNEVLRLHLLGSGAFVNEKAERWRVMYRNGYSSKEDPGLELRLEHSHILRILKNHSVYQLKFKDIMLLIRCLMSQIMTYSGTINLIEERMEQTAKARQDLRALVVGENKRLAAVEINRKKLTQMHHLEVNGVEPEKREALVEKLKKSIAELHAQSDQQHRKHELQMLKLHSQLFNFLVYLGMDRCYRKYYVLESMPGIFVEHSPDSLDTCLEQPITNKSQIEIRQQSALPKNRKDLRVYLLKLYGDDEKKTKKKAKHSLENKENQEHRLNGSAEPMDVESDSPEAPTHFELLMCSGDKRSCIVHDSRNGQRQRWAYIYKAEEIDELIKALNPNGLREYELLQELSVLRSLIEQHAKTCPVDLLSLENETMRKKFMAAMESETNRKYGEANFGLPNGTDLNEVMRLHLVDRIIQFENDIYTGDLGRLKVKDMEKWRSDLLGGNYDAQCKLQWGPGGKLEDEAGSDNESHETHEEDDGALLGKYARKPYRDPGMYLAASADTKPLPDSDDEEDQHTNAVSIPIAVHNMASALLQVEQAIGKRFLKEPYGMKKWDPKQEALKLACDSRLHQWEVSLMESTSFAQVFLHLNILHDCIQWRRSTNKSLCKVCRRGSDPEKMLLCDECNAGTHMFCLKPKLRSVPPGNWYCNDCVKSLGLSNGQNEKDKKQATKKKRKFIVEEEDDEATDEEEEEKKDDDMTDEDAEHENEKHDEDVEDDESVTSTPSSSRVNGRILRRPRTRPTSRRLTSKEIEEHAQEDVDSGDVSDDASLTAGEDTIEDESDEEKVCQKCFYDGGEIKCVQCRLFFHLECVHLKRPPRTDFVCKTCKPMPQRPRRRHSNMNGDHDRDEEEPKAKRPRNSLRLCIDKTARPSNGNNNNNNNNSSVNNNNHRRSGRRTNEHMPLNSAALYDLLEQIMKHKAAWPFLRPVLTSEVPDYHQIIKTPMDLAKIKSKLNMGAYQLNEELLSDIQLVFRNCDLYNVEGNEIYDAGCQLERFVIDRCRDMQLPFRPSDMNGEVKAC
Protein: Mast cell carboxypeptidase A (MC-CPA) (EC 3.4.17.1) (Carboxypeptidase A3) (P15089)
Organism: Mus musculus (Mouse)
Subcellular location: Cytoplasmic vesicle, secretory vesicle. Note=Secretory granules.
Interaction partners:
- Chymase
- Mast cell protease 4
- Tryptase beta-2
- Carboxypeptidase A1
- Carboxypeptidase A2
- High affinity immunoglobulin epsilon receptor subunit alpha
- High affinity immunoglobulin epsilon receptor subunit beta
- Tryptase
- Histidine decarboxylase
- Cathepsin G
Sequence:
MRFFLLMAVIYTTLAIAPVHFDREKVFRVKLQNEKHASVLKNLTQSIELDFWYPDAIHDIAVNMTVDFRVSEKESQTIQSTLEQHKIHYEILIHDLQEEIEKQFDVKDEIAGRHSYAKYNDWDKIVSWTEKMLEKHPEMVSRIKIGSTVEDNPLYVLKIGKKDGERKAIFMDCGIHAREWISPAFCQWFVYQATKSYGKNKIMTKLLDRMNFYVLPVFNVDGYIWSWTQDRMWRKNRSRNQNSTCIGTDLNRNFDVSWDSSPNTNKPCLNVYRGPAPESEKETKAVTNFIRSHLNSIKAYITFHSYSQMLLIPYGYTFKLPPNHQDLLKVARIATDALSTRYETRYIYGPIASTIYKTSGSSLDWVYDLGIKHTFAFELRDKGKSGFLLPESRIKPTCKETMLSVKFIAKYILKNTS
Protein: Ret-TPC (Q15302)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MADSASESDTDGAGGNSSSSAAMQSSCSSTSGGGGGGGGGGGGGKSGGIVISPFRLEELTNRLASLQQENKVLKIELETYKLKCKALQEENRDLRKASVTIEDPKWEFPRKNLVLGKTLGEGELESGQGNGF
Protein: Probable NAD(P)H-dependent D-xylose reductase xyl1 (XR) (EC 1.1.1.307) (A2Q8B5)
Organism: Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513)
Function: Catalyzes the initial reaction in the xylose utilization pathway by reducing D-xylose into xylitol. Xylose is a major component of hemicelluloses such as xylan. Most fungi utilize D-xylose via three enzymatic reactions, xylose reductase (XR), xylitol dehydrogenase (XDH), and xylulokinase, to form xylulose 5-phosphate, which enters pentose phosphate pathway (By similarity).
Interaction partners:
Sequence:
MASPTVKLNSGYDMPLVGFGLWKVNNDTCADQIYHAIKEGYRLFDGACDYGNEVEAGQGIARAIKDGLVKREELFIVSKLWNSFHDGDRVEPICRKQLADWGIDYFDLYIVHFPISLKYVDPAVRYPPGWKSEKDELEFGNATIQETWTAMESLVDKKLARSIGISNFSAQLVMDLLRYARIRPATLQIEHHPYLTQTRLVEYAQKEGLTVTAYSSFGPLSFLELSVQNAVDSPPLFEHQLVKSIAEKHGRTPAQVLLRWATQRGIAVIPKSNNPQRLKQNLDVTGWNLEEEEIKAISGLDRGLRFNDPLGYGLYAPIF
Protein: Homeobox protein vab-7 (Q93899)
Organism: Caenorhabditis elegans
Function: Transcription factor. Involved in motor neuron fate determination and maintenance, acting as a transcriptional repressor to counteract gene activation by transcription factor unc-3 in a subset of motor neurons. Probably acts by binding to specific promoter elements. Required for posterior-specific pattern formation in the embryo and may have a role in regulating egl-5 expression.
Subcellular location: Nucleus.
Interaction partners:
- T-box transcription factor tbx-8
- C2H2-type domain-containing protein
- T-box transcription factor tbx-9
- Putative T-box protein 30/42
Sequence:
MQSFDIESLIGVNKVPSLVEMVAASRASSFSPPFEQQHHDPMGVVAAAAAAAAAGRHHPYDNRDDGQMRRYRTAFSREQIGRLEREFAKENYVSRKTRGELAAELNLPEGTIKVWFQNRRMKDKRQRVGGLAWPFPPQMAAYMLNPFAYEMWMKTAAASQFGATGPGNGAYGNNGSSTSPSAAGSLPFLPPLGFPSFLSQNSTKSPSSPHSDDSSKSKNTSSDDDESKPVNFSNSPSSSSPSPYSTD
Protein: Sporulation-specific protein 20 (Q04359)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required to maintain the prospore membrane to the nucleus during sporulation in order to capture the daughter nuclei and form the spores. Mediates the fusion of exocytic vesicles with the plasma membrane during sporulation through its interactions with the t-SNARE SSO1 and v-SNARE SNC2.
Subcellular location: Cell membrane. Prospore membrane. Note=Membrane-associated to the plasma during vegetative growth and prospore membrane associated during sporulation.
Interaction partners:
- Protein SSO1
- Synaptobrevin homolog 2
- Synaptobrevin homolog 1
- Vacuolar v-SNARE NYV1
- Alpha-soluble NSF attachment protein
- Protein SSO2
- Syntaxin VAM3
- Protein transport protein SEC22
- Integral membrane protein SED5
- Synaptobrevin homolog YKT6
Sequence:
MGFRKILASKSHHSRHHNQHHKNLKLQNHRYVLISNITGSHETKYLSPFRMDNCSGSRRRDRLHVKLKSLRNKIHKQLHPNCRFDDATKTSDDKCVSYEVPERDGLATISLEEVFPKSNRCQIPEENLGETDSVIHRDLGNFANENDYPQWRKVESQYNLENVQPEEDEIVDRLRSEIRSTKLKSVKTTSRTLEKAIEARCTGKRVLQQLSCQSNQLTKIESNCDMLKIQSNVADRKIDELAHENRSLLALKSPNPFRKKREREKRDQIYNLKLKHRHLQQETMKRAQDSDKNLAINLSSEYGRYGQGVERQRILRDAQKYQFEADEEDNQMEIDLYGNLEQIKAVSGDLKIMAHAFGREFEAQNTRMFDIENNVQQADNALQAKRYRLEKVIGKRW
Protein: Claudin-7 (CLDN-7) (O95471)
Organism: Homo sapiens (Human)
Function: Plays a major role in tight junction-specific obliteration of the intercellular space.
Subcellular location: Cell membrane {ECO:0000269|PubMed:12673207, ECO:0000269|PubMed:14502431, ECO:0000269|PubMed:20375010}; Multi-pass membrane protein {ECO:0000255}. Basolateral cell membrane {ECO:0000269|PubMed:16054130}. Cell junction, tight junction {ECO:0000269|PubMed:16054130}. Note=Co-localizes with EPCAM at the basolateral cell membrane and tight junction. {ECO:0000269|PubMed:16054130}.
Interaction partners:
- Tight junction protein 1
- Occludin
- CD81 antigen
- Tight junction protein 2
- Epithelial cell adhesion molecule
- Tight junction protein ZO-3
- Junctional adhesion molecule A
- Tumor-associated calcium signal transducer 2
- MARVEL domain-containing protein 2
- Claudin-4
Sequence:
MANSGLQLLGFSMALLGWVGLVACTAIPQWQMSSYAGDNIITAQAMYKGLWMDCVTQSTGMMSCKMYDSVLALSAALQATRALMVVSLVLGFLAMFVATMGMKCTRCGGDDKVKKARIAMGGGIIFIVAGLAALVACSWYGHQIVTDFYNPLIPTNIKYEFGPAIFIGWAGSALVILGGALLSCSCPGNESKAGYRVPRSYPKSNSSKEYV
Protein: LD11531p (Q95RU5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MYGVDMHTVLGKDGCEYHLGLTPTGILVFERDQKIGLFFWPKISKLDFKKKKLTLIVIEDDDEGREQEHTFVFRLYNEKACKHLWKCAVEHHTFFRLRAPVKGPSARQNFFRMGSRFRYSGRTEFQTTQQSRARRTVQFERRPSQRFASRQSHLLRERQKASQEAAVSAVASVNARAAAAAAAAAASQSPAPATPLVSSQVSTPTPNNDNNNDAFDSLISTDQFITVTPSPSVLTVIQNSAIIEPDAACSGSISSSSQAAANFASLGRNSLKSNFSNEDPAYSKIGSIGKASGLTVKLDPDYTPPYSPNATKNFDETNPFRNATSSHHGSFGKASISSGQLSVKSGLSDKDRELDSLLKSIVKDPSPSVLANEAINDANSIRVTINKTFDMDHNTETLKRLSNANEKPNNQVKLANVNTTALPPGNIKCNILKARVEEELGAGGNAKLTNQMFVPAAHSSNMHTSNTNSSNNHAHSDGPDSLNATYISVGGDKLTLSIPEQKPSTGSSSSSSTSSTATTTTNGNGPYSNATFVSGFSAPLTPPSSLPANLNNTGSGCNTTLTSVTTISTPSSPTATVSTTASESVAPALSNASAAEILINEIFINNIINNNASGSITAETAAKPAGSSTPSAGTLLFSTLSEQERLESQKTNQQMNQSLNLNQNHSEVDAPPSEKKTPSNYPDSSRIPFPSSSNSKDMVSPWLVSSEVVSAPKGRESAIIRKSVITTQL
Protein: DEAD-box ATP-dependent RNA helicase 22 (EC 3.6.4.13) (Q944S1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Protein STABILIZED1
- Small nuclear ribonucleoprotein Sm D2
- Pre-mRNA-processing-splicing factor 8B
- Pre-mRNA-processing-splicing factor 8A
- 110 kDa U5 small nuclear ribonucleoprotein component CLO
- 109 kDa U5 small nuclear ribonucleoprotein component GFL
- Small nuclear ribonucleoprotein E
- U1 small nuclear ribonucleoprotein C
- Small nuclear ribonucleoprotein E
- Small nuclear ribonucleoprotein SmD3a
Sequence:
MILSRSVSVLHLCGVSSSAPSKLLSQRFKVSFALAYGSSVSFRLSSLNRSDRKWVRGFASATEAEVEKKGNDTFFADHTVSWKSLGLSDNVSIALRDSGFDRPSLTQAVCIPSILSGKDVIVAAETGSGKTHGYLAPIIDQLTNTALDSEVTNREERPFPLKNISLILCPNVMLCEQVVRMVNGLVDEDGNPLLRVEAVCGSQGWPDRLPDIIVSTPAALLNNIEPKRNRRLEFLRCVKYVVFDEADMLLCGSFQNQIIRLINMLRFDEKQVSRLAKSNLGRPMEIDASVPQIDLENEDDAEFDEGSISEEEDEEEEEEYLDDIAQMPSVEAEAGSDTKKGWRRVRKIYTRSKQYIFIAATLPVNGKKTAGGILKHMFQDAVWVSGNFLHRNSPRLKQKWVEVTVDSQVDALIEAVKNNNNTNTERTMVFANTVEAVEAVADILEKASIQCYRYHKNHKLDERANILADFRETGGVFVCTDAAARGVDVPNVSHVIQADFASSAVDFLHRIGRTARAGQYGTVTSLYTEANRDLVEAIREAVKMGQPVETAFSRKRGFRNKVKKRAFLKAEEAEEPQAVRY
Protein: Virion protein (Membrane) (Q77CC2)
Organism: Bovine herpesvirus 1.1 (strain Cooper) (BoHV-1) (Infectious bovine rhinotracheitis virus)
Subcellular location: Host Golgi apparatus membrane {ECO:0000256|ARBA:ARBA00004252}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004252}. Host nucleus membrane {ECO:0000256|ARBA:ARBA00004634}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004634}. Virion {ECO:0000256|ARBA:ARBA00004328}.
Interaction partners:
Sequence:
MLGPESAALLRAPEPPLGGADAEEGAAGASPGDSGSDDEEDELLRCVALSAYGGDVDFLTRSPRLAPRADGRAAFSAYVVFGAASAFGLNPACCLLFLYYYRTFGDATFAVAGAAATLAYYARLAAAAGFLYAGVRADRLPFGRGPRALLAALVLARAAVFAAVALPAAFAGPALFLRLSAAVADGGARAAAAGLLLAGLAAYTADLVCDVIGFFAPRAWMRVCLGGHVAV
Protein: Mevalonyl-coenzyme A hydratase sidH (EC 4.2.1.-) (Siderophore biosynthesis protein H) (Q4WF54)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Function: Mevalonyl-coenzyme A hydratase; part of the siderophore biosynthetic pathway. Aspergillus fumigatus produces 4 types of siderophores, low-molecular-mass iron chelators, including excreted fusarinine C (FsC) and triacetylfusarinine C (TAFC) for iron uptake and intacellular ferricrocin (FC) for hyphal and hydroxyferricrocin (HFC) for conidial iron distribution and storage. TAFC consists of 3 N(2)-acetyl-N(5)-anhydromevalonyl-N(5)-hydroxyornithine residues cyclically linked by ester bonds; FC is a cyclic hexapeptide with the structure Gly-Ser-Gly-(N(5)-acetyl-N(5)-hydroxyornithine)x3. The biosynthesis of all four siderophores depends on the hydroxylation of ornithine, catalyzed by the monooxygenase sidA. Subsequently, the pathways for biosynthesis of extra- and intracellular siderophores split. For biosynthesis of extracellular siderophores, the transacylase sidF transfers anhydromevalonyl to N(5)-hydroxyornithine. The required anhydromevalonyl-CoA moiety is derived from mevalonate by CoA ligation and dehydration catalyzed by sidI and sidH respectively. The acetylation of N(5)-hydroxyornithine for FC biosynthesis involves the constitutively expressed sidL. FC is hydroxylated to HFC by an as yet uncharacterized enzyme during conidiation. Assembly of fusarinine C (FsC) and FC is catalyzed by two different nonribosomal peptide synthetases (NRPS), sidD and sidC respectively. Subsequently, sidG catalyzes N2-acetylation of FsC for forming TAFC. Both extra- and intracellular siderophores are crucial for growth during iron limitation and virulence.
Subcellular location: Peroxisome {ECO:0000269|PubMed:23617799}. Note=Targeted to peroxisomes via its PTS1-type peroxisomal targeting signal and the corresponding receptor pexE (PubMed:23617799). {ECO:0000269|PubMed:23617799}.
Interaction partners:
- Acyl-CoA ligase sidI
- propanoyl-CoA C-acyltransferase
- 3-hydroxybutyryl-CoA dehydrogenase, putative
- N
- Nonribosomal peptide synthetase sidD
- Acyltransferase sidL
Sequence:
MSTEAHPTVQGCLVSFPTPHILLLTLNRPEKRNCISLATSAEIQRLWTWFDTQPALYVAIITGTGESFCAGADLKEWNDLNARGITNEMTAPGLAGLPRRRGSKPIIAAVNGYCLGGGFEMVANCDIVVASENATFGLPEVQRGIAAVAGSLPRLVRVLGKQRAAEIALSGLSFSASQLERWGLVNRVVEHDQLLATAVEIATAISRNSPDSVRVTMEGLHYGWEMASVEEASSALVDQWYAKLMAGENFHEGVRAFVEKRKPQWRPSKL
Protein: Solute carrier family 2 member 3a (Solute carrier family 2, facilitated glucose transporter member 3a) (Zgc:92476) (Q6DFZ5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MEGEKKQVTCYLLFSLSTAVIGSLQFGYNTGVINAPEQKLRAFFNATWMERYGEPISPGVCTIVWSFAVAIFSVGGMAGSFSVGVVANKFGRRKSMILVNVLALIGGGLMGLCTLCSSFEMIIAGRLMIGLFCGLFTGLTPMYVGEVSPTPLRGAFGTLHQLGVVVGILIAQIFGLESLLGSDKLWPILLALTILPAILQCFLLPFCPESPRYLLINLNEEEQARKALVRLRGYEDVGKDMQEMKEESAKMAMEKKVTIPELFRSAAYRQPLFIAIMLQLSQQLSGINAVFYYSTGIFKSAGVTQPIYATIGAGVVNTVFTVVSLFLVERAGRRTLHLIGLGGMAISALAMTIALLLKDIEALQYLSIAAIFAFVAMFEMGPGPIPWFIVAELFSQGPRPAAMAVAGCSNWTANFIVGITFPKLEELCGPYVFIIFMIFLIIFFIFTYFKVPETKGRTFDEIARGFSGAPPPSATSVEEPGRVALPASPVKEKVPLVEAPKSSSEQGPSSSEQPAKVEEKSSSVTQPLVDSSKEEKSNSTM
Protein: Protein PYRICULARIA ORYZAE RESISTANCE 21 (Pi21) (A2XT03)
Organism: Oryza sativa subsp. indica (Rice)
Function: Involved in defense responses. Contributes to slowing defense responses toward Magnaporthe oryzae.
Interaction partners:
Sequence:
MGILVISVDLQCCRCDAKIRKVLGCLEEEYCIEKVEYDVKNNRVIVRGKFDPEKLCKKIWCKAGKIIKEILIVDVWPPPLPPPCKPPPCEKPPEDCKPKPCHCCSCEKPKPKPKPCHCEKPKPCHCEKPKPCEKPPPCKPEEPPKPPPEKPPPKPECKLVPYPYPVPYPYAGQWCCPKPEPPKPPPEPPKEPEPPKPCGCSHAFVCVCKPAPPPPPPCGCSGGHGNCGCGIRPWPPQVWPPPPVCPPPPWCYTEDNANACSIM
Protein: Putative uncharacterized protein YCL046W (P25575)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Interaction partners:
- Putative uncharacterized protein YOR055W
- Putative uncharacterized protein YLR232W
- Putative regulator of rDNA transcription protein 16
- Putative increased recombination centers protein 14
- 5'-AMP-activated protein kinase subunit gamma
Sequence:
MVKGKTFLKRICPEETLNEETKQEVSVGFDKMRTLLRSRESGMTFSQGPKLASCQSVINASSEKTAWTQLVFRKSKMKTYTKSVHVIFIAMGEGEDESVDMNVGISY
Protein: RING-type E3 ubiquitin transferase (EC 2.3.2.27) (Q8LRC7)
Organism: Oryza sativa subsp. japonica (Rice)
Interaction partners:
Sequence:
MAGNPAAAAPSSSGSSSVFLPPPSPSDGELLRPLHRLARDLSAVDTPAPFLRAAFASISRRSKLLAAAFDDLLLCGAAGELPRSASLCLREVLLVLQRFKAIVADCSARSRMRLLLESDEMEAELRELNHDLATLLDLLPVVELGLADDVLDVLALASRQCRRCSPAPESEEALKASVLSLIQEIEREIVPERERLEEILVEVGINDPASCSEEIESLEQEIGDRASEKWTASMIALVGLLRYAKCVLFSATPRPSDSNSKADVEAEDGEPPVPPSDFRCPISLDLMRDPVVVASGQTYDRESIDRWFSSGKSTCPKTGQVLANLELVSNKALKNLISKWCRENGVAMEACEASKSEQAQAVAANKAALEAARMTASFLVKKLSVSFSPDAANRVVHEIRLLSKSGSENRAFVGEAGAVPLLVPLLYSEDAGLQLNAVTALLNLSILEANKKRIMHADGAVEAVAHIMSSGATWRAKENAAAAVLSLASVHSYRRRLGRNQSVVEKLVHLVRTGPTSTKKDALAALLTLAGERENVGKLVDAGVAEVALSAISKEETAAAVLAALAKRGGAEAIVNIDGAVARLVAEMRRGTDWARENATAALVLLCRRLGAPAVTQVMAVPGVEWAIWELMSIGTERARRKAASLGRICRRWAAASAADGERGGGCPVATVVPPAMMAS
Protein: Monocyte differentiation antigen CD14 (My23 antigen) (Myeloid cell-specific leucine-rich glycoprotein) (CD antigen CD14) [Cleaved into: Monocyte differentiation antigen CD14, urinary form; Monocyte differentiation antigen CD14, membrane-bound form] (P08571)
Organism: Homo sapiens (Human)
Function: Coreceptor for bacterial lipopolysaccharide. In concert with LBP, binds to monomeric lipopolysaccharide and delivers it to the LY96/TLR4 complex, thereby mediating the innate immune response to bacterial lipopolysaccharide (LPS). Acts via MyD88, TIRAP and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response. Acts as a coreceptor for TLR2:TLR6 heterodimer in response to diacylated lipopeptides and for TLR2:TLR1 heterodimer in response to triacylated lipopeptides, these clusters trigger signaling from the cell surface and subsequently are targeted to the Golgi in a lipid-raft dependent pathway. Binds electronegative LDL (LDL(-)) and mediates the cytokine release induced by LDL(-).
Subcellular location: Cell membrane {ECO:0000269|PubMed:1698311, ECO:0000269|PubMed:2462937, ECO:0000269|PubMed:3385210}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:1698311, ECO:0000269|PubMed:2462937, ECO:0000269|PubMed:3385210}. Secreted {ECO:0000269|PubMed:25497142, ECO:0000269|PubMed:2779588}. Membrane raft {ECO:0000269|PubMed:16880211}. Golgi apparatus {ECO:0000269|PubMed:16880211}. Note=Secreted forms may arise by cleavage of the GPI anchor. {ECO:0000269|PubMed:2462937, ECO:0000269|PubMed:2779588, ECO:0000269|PubMed:3385210}.
Interaction partners:
- Toll-like receptor 4
- Toll-like receptor 2
- Lipopolysaccharide-binding protein
- Lymphocyte antigen 96
- Transcription factor PU.1
- TLR4 interactor with leucine rich repeats
- TYRO protein tyrosine kinase-binding protein
- Integrin beta-2
- Macrophage colony-stimulating factor 1 receptor
- Protein S100-A9
Sequence:
MERASCLLLLLLPLVHVSATTPEPCELDDEDFRCVCNFSEPQPDWSEAFQCVSAVEVEIHAGGLNLEPFLKRVDADADPRQYADTVKALRVRRLTVGAAQVPAQLLVGALRVLAYSRLKELTLEDLKITGTMPPLPLEATGLALSSLRLRNVSWATGRSWLAELQQWLKPGLKVLSIAQAHSPAFSCEQVRAFPALTSLDLSDNPGLGERGLMAALCPHKFPAIQNLALRNTGMETPTGVCAALAAAGVQPHSLDLSHNSLRATVNPSAPRCMWSSALNSLNLSFAGLEQVPKGLPAKLRVLDLSCNRLNRAPQPDELPEVDNLTLDGNPFLVPGTALPHEGSMNSGVVPACARSTLSVGVSGTLVLLQGARGFA
Protein: Ephrin A2 (F1MA19)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004609}; Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609}.
Interaction partners:
- receptor protein-tyrosine kinase
- Ephrin type-A receptor 2
- Ephrin type-A receptor 1
- Ephrin type-A receptor 5
- Ephrin type-A receptor 3
- Ephrin type-A receptor 8
- Ephrin type-A receptor 7
- Ephrin type-A receptor 10
- Ephrin type-A receptor 6
- Tyrosine-protein kinase Fyn
Sequence:
MAPAQRPLLPLLLLLLPLRARNEDPARANADRYAVYWNRSNPRFQVSAVGDGGGYTVEVSINDYLDIYCPHYGAPLPPAERMERYILYMVNGEGHASCDHRQRGFKRWECNRPAAPGGPLKFSEKFQLFTPFSLGFEFRPGHEYYYISATPPNLVDRPCLRLKVYVRPTNETLYEAPEPIFTSNSSCSGLGGCHLFLTTVPVLWSLLGS
Protein: Thymosin beta (Q9W7M8)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Plays an important role in the organization of the cytoskeleton. Binds to and sequesters actin monomers (G actin) and therefore inhibits actin polymerization (By similarity).
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250}.
Interaction partners:
- Actin, cytoplasmic 1
- Actin, cytoplasmic 2
- Thymosin beta
- Thymosin beta
Sequence:
MADKPNMTEITSFDKTKLRKTETQEKNPLPTKETIEQERQGESTP