wanglab/gogpt-training-data huggingface dataset:
Protein: Serine repeat antigen 3 (EC 3.4.22.-) (O96165)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- Uncharacterized protein
- Ribosome-interacting GTPase 1, putative
- DNA polymerase II subunit 2
- Uncharacterized protein
- non-specific serine/threonine protein kinase
- ADP/ATP translocase
- Raf kinase inhibitor
- Citrate synthase
- Citrate synthase-like protein, putative
- Syntaxin, Qa-SNARE family
Sequence:
MKFSISLFLILCVLFCKNDIKCTTVDESTKEGSQNPKNSSSTTPASGSQKGSSSESPGSSVEKQSQESNKESTNGGNVVSQGTPANTFGQNSNNPSDSPQGTSTLPSPPKSIDVKSAFLKHYKGVKVTGSCNANFQLFLVPHIFINVETKENNIQLDVKFLKLTKRIDFAKDKSMLKNKCESGKNQTFKFVLYFKDDILTIKWKVYEEKSATPQKSEENTVDIKLYKLPKLDQTITSIQVHTLSIEGTSYLMESKDYSLGNNLPEKCDAIASDCFLSGNINVEKCLKCTLKVKKVEASDECYKYVSKDKPKETKLAVSGSEVKEVKAASVDHSNDKEYELSQSINNILNKMYKKESNDEKNNKKELIKLEDADDSLQKELNKYCNSLKEVDLNGVLSKNEVGNEKDVFNNLTTLLKEHMLESHHVVFEKLKNSALCLKNIDDWLKNKNGLIVPPSKYKLKDTNEKKELNNNVEVIEDMFKANEHGIVDLTKFPIDTNYSSYKHIDHTYCNNDYCNWSKDKNSCISKINVEDQKNCALSWAFASKYHLETIKCMKGYEHIPISSLYIANCSKNEKKDVCTEGSNPLKVLQMIVEKGFLPTEGDYSYEQSKVGETCPEVQNGWVNLWANAKLLEQNNDEHNSLSTKGYTAYESEAFQKDMHSFVKLIKDEIMNKGSVIAYVKADKIMAYEFNGKKVQNLCGDKTPDHAVNIIGYGNYINDEHQKKSYWIVRNSWGKHWGDKGHFKVDMYGPSDCEDNFIHSVVIFNVDLPINQESVKKEPKIYNYYLKASPDFYHNLYYKNFDSQKGKADQAENKKSYLYGQEESTSEQLPSSLSSPQNNKQSERSKEKVDIFHVLKHIKDSKIKMGIVKYDHSDALGEDNVCSRSYSSNPEKQEGCVKFCNENWGKCKDAASPGFCLSELEKTNDCFFCYI
Protein: Protein LYRIC (Lysine-rich CEACAM1 co-isolated protein) (Metadherin) (Metastasis adhesion protein) (Q9Z1W6)
Organism: Rattus norvegicus (Rat)
Function: Down-regulates SLC1A2/EAAT2 promoter activity when expressed ectopically. Activates the nuclear factor kappa-B (NF-kappa-B) transcription factor. Promotes anchorage-independent growth of immortalized melanocytes and astrocytes which is a key component in tumor cell expansion. Promotes lung metastasis and also has an effect on bone and brain metastasis, possibly by enhancing the seeding of tumor cells to the target organ endothelium. Induces chemoresistance (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Nucleus membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Cell junction, tight junction {ECO:0000250}. Nucleus, nucleolus {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Note=In epithelial cells, recruited to tight junctions (TJ) during the maturation of the TJ complexes. A nucleolar staining may be due to nuclear targeting of an isoform lacking the transmembrane domain. TNF-alpha causes translocation from the cytoplasm to the nucleus (By similarity). {ECO:0000250}.
Interaction partners:
- Staphylococcal nuclease domain-containing protein 1
Sequence:
MAARSWQDELAQQAEEGSARLRELLSVGLGFLRTELGLDLGLEPKRYPSWVILVGTGALGLLLLFLLGYGWAAACAGARKKRRSPPRKREEVTPPTPAPEDPAQLKNLRSEEQKKKNRKKLPEKPKPNGRTVEIPEDEVVRTPRSITAKQPPETDKKNEKSKKNKKKSKSDAKAVQNSSRHDGKEVDEGAWETKISHREKRQQRKRDKVLTDSGSLDSTIPGIENTITVTTEQLTTASFPVGSKKNKGDSHLNVQVSNFKSGKGDSTLQVSSGLNENITVNGGGWSEKSVKLSSQLSAGEEKWNSVPPASAGKRKTEQSAWTQDPGDTNANGKDWGRNWSDRSIFSGIGSTAEPVSQSTTSDYQWDGSRNQPHIDDEWSGLNGLSSADPSSDWNAPAEEWGNWVDEDRASLLKSQEPISNDQKDSDDDKEKGEGALPTGKSKKKKKKKKKQGEDNSITQDTEDLEKDTREELPVNTSKARPKQEKACSLKTMSTSDPVEVLIKNSQPIKTLPPAISAEPSVTLSKGDSDKSSSQVPPMLQDTDKPKSNAKQNSVPPSQTKSETNWESPKQIKKKKKARRET
Protein: Transcription factor AP-2-alpha (AP-2 transcription factor) (Activating enhancer-binding protein 2-alpha) (Activator protein 2) (A0A2R8QRQ5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Forkhead box protein D3
- Transcription factor SOX-10
- BTB/POZ domain-containing protein KCTD1 isoform X2
- Potassium channel tetramerization domain containing 15.
- Paired box 3a
- Nucleophosmin
- Homeobox protein Dlx3b
- Protein DEK
- Odd-paired-like)
- BTB/POZ domain-containing protein kctd15-like
Sequence:
MHCVKLKRRRTALYPQPMKMLWKLTDNIKYEDFEDRHDGTSNGTARLPQLGSVGQSPYTSAPPLSHTPNSDFQPPYFPPPYQPIYPQSQDPYSHVNDPYSINSLHAQSQPQHPGWPGQRQSQESSLLHQHRGLPHQLCREYRREVLLPSGHGIDTGLTDSIPIHGIPHSLEDVQQVEDQGIHIPDQTVIKKGPVSISKNNSNISAIPINKDGLFGGVVNPNEVFCSVPGRLSLLSSTSKYKVTVAEVQRRLSPPECLNASLLGGVLRRAKSKNGGRSLREKLDKIGLNLPAGRRKAANVTLLTSLVEGEAVHLARDFGYVCETEFPAKAIAEYMNRQHSDPNEQVQRKNMLLATKQICKEFTDLLSQDRSPLGNSRPQPILEPGIQSCLTHFSLISHGFGTPAVCAALTALQNYLTEAIKAMDKMYLNNNPNSHSETGSKAGDKDEKHRK
Protein: Gamma-tubulin complex component 3 (AtGCP3) (GCP-3) (Spindle pole body component 98) (AtSPC98) (Q9FG37)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Gamma-tubulin complex is necessary for microtubule nucleation at the microtubule organizing centers (MTOCs). Required for the positioning of the gamma-tubulin-containing complex on pre-existing microtubules and for the proper organization of cortical arrays.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center {ECO:0000250|UniProtKB:Q9BSJ2}. Nucleus envelope. Cytoplasm. Cytoplasm, cell cortex. Cytoplasm, cytoskeleton, spindle. Note=Associated to motile complexes in the cytosol that transiently stabilized at fixed locations in the cell cortex (e.g. along the outer periclinal edge of newly formed crosswalls) from which microtubules grow away prior to microtubules nucleation. Colocalizes with gamma-tubulin at the nuclear surface where microtubules are nucleated. Localizes to both cortical cytoplasm and mitotic microtubule arrays of the nematode feeding giant cells.
Interaction partners:
- Gamma-tubulin complex component 2
- Mitotic-spindle organizing protein 1B
- Tubulin gamma-1 chain
- Gamma-tubulin complex component 4
- Tubulin gamma-2 chain
- Protein NEDD1
- Mitotic-spindle organizing protein 1A
- Gamma-tubulin complex component
- Gamma-tubulin complex component
- SUN domain-containing protein 1
Sequence:
MEDDDQQKAADLVQELVLRLVSQNPQTPNLDPNSPAFLKTLRYAFRILSSRLTPSVLPDATAIAESLKRRLATQGKSSDALAFADLYTKFASKTGPGSVNNKWALVYLLKIVSDDRKSAINGLDSSVLLPNLGIGDTGNGVLSRGEAKKKDWSNGVLLVSKDPENLRDIAFREYAILVKEENEVTEEVLVRDVLYASQGIDGKYVKFNSEIDGYAVQESVKVPRATRIMVRMLSELGWLFRKVKTFITESMDRFPAEDVGTVGQAFCAALQDELSDYYKLLAVLEAQAMNPIPLVSESASSNNYLSLRRLSVWFAEPMVKMRLMAVLVDKCKVLRGGAMAGAIHLHAQHGDPLVHDFMMSLLRCVCSPLFEMVRSWVLEGELEDTFGEFFVVGQPVKVDLLWREGYKLHPAMLPSFISPSLAQRILRTGKSINFLRVCCDDHGWADAASEAAAASGTTTRRGGLGYGETDALEHLVTEAAKRIDKHLLDVLYKRYKFKEHCLAIKRYLLLGQGDFVQYLMDIVGPKLSEPANNISSFELAGFLEAAIRASNAQYDDRDMLDRLRVKMMPHGSGDRGWDVFSLEYEARVPLDTVFTESVLSKYLRVFNFLWKLKRVEHALIGIWKTMKPNCITSNSFVKLQSSVKLQLLSALRRCQVLWNEMNHFVTNFQYYIMFEVLEVSWSNFSKEMEAAKDLDDLLAAHEKYLNAIVGKSLLGEQSQTIRESLFVLFELILRFRSHADRLYEGIHELQIRSKESGREKNKSQEPGSWISEGRKGLTQRAGEFLQSMSQDMDSIAKEYTSSLDGFLSLLPLQQSVDLKFLFFRLDFTEFYSRLHSKG
Protein: ABC transporter domain-containing protein (Q20306)
Organism: Caenorhabditis elegans
Interaction partners:
- TOG domain-containing protein
- ABC transporter, class E
- Mitochondrial Ribosomal Protein, Large
- Small ribosomal subunit protein uS13
- Large ribosomal subunit protein bL21m
- Large ribosomal subunit protein uL29
- Large ribosomal subunit protein uL6
- Large ribosomal subunit protein uL30
- Large ribosomal subunit protein uL18
- Small ribosomal subunit protein uS3
Sequence:
MANVEAIPGYLTATFPTLPIEIKDYVSAILKENSDEITSLDEVMDAVGEHLQASVENLCEVGAKNACQQLLKLLHGDNLPKAIKQQEATTKRLEQTVDMAAENQNFEALQSIWKVQTRDTPTTVDKKKLAKAEDRAAAKAEARADAPVERKKKKNEPSATASQAPIRDSGARGANSKDIKLESVDISIGTKQLLSCADVTMAFGRRYGLVGRNGIGKTTLLKMISSQQLKIPAGISMLSVEQEVEGDDTLVLDAVLMSDTKRQTLLDREKTLQSRINKDNINDAEKTKWNDELSKLYIEMEALQLDKAPARASSLLYGLGFTPDEQKRPTKEFSGGWRMRVALARALFVKPDLLLLDEPTNMLDMRAVYWLEGHLQGWEGTILTVSHDRKFLNEICTDIVHLHTRRLDHYKGNYDQFEKTMKEKLTQQQREYESQQQLRQHTQEFIDKFRYNAKRAPMVQSRIKMLEKLPVLLPVELESDIHFKFPECEVLSNPVLQLDEVSFRYNEDSPYLFRKLNLGTHANSRICIVGENGAGKTTLLKLLLDDLQPSVGLRNVNRRIRIAYFTQHHVDQLDMETSAIEVLMKNHPGKTQEDYRAALGRFGLAGDMALQSVETLSGGQKSRLAFANLALMQPNYLILDEPTNHLDVETVEALGKALNVFNGGVVLVSHDEQLIELVCKELWVVKDRMVTTLEGGLEEYRKQVYKQLQLTA
Protein: MSL complex subunit 1 (J3KSZ8)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MTMRSAVFKAAAAPAGGNPEQRLDYERAAALGGPEDEPGAAEAHFLPRHRKLKEPGPPLASSQGGSPAPSPAGCGGKGRGLLLPAGAAPGQQEESWGGSVPLPCPPPATKQAGIGGEPAAAGAGCSPRPKYQAVLPIQTGSLVAAAKEPTPWAGDKGGAASPAATASDPAGPPPLPLPGPPPLAPTATAGTLAASEGRWKSMRKSPLGGGGGSGASSQAACLKQILLLQLDLIEQQQQQLQAKEKEIEELKSERDTLLARIERMERRMQLVKKDNEKERHKLFQGYETEEREETELSEKIKLECQPELSETSQTLPPKPFSCGRSGKGHKRKSPFGSTERKTPVKKLAPEFSKVKTKTPKHSPIKEEPCGSLSETVCKRELRSQETPEKPRSSVDTPPRLSTPQKGPSTHPKEKAFSSEIEDLPYLSTTEMYLCRWHQPPPSPLPLRESSPKKEETVAIPSWRDHSVEPLRDPNPSDLLENLDDSVFSKRHAKLELDEKRRKRWDIQRIREQRILQRLQLRMYKKKGIQESEPEVTSFFPEPDDVESLMITPFLPVVAFGRPLPKLTPQNFELPWLDERSRCRLEIQKKQTPHRTCRK
Protein: Rod cGMP-specific 3',5'-cyclic phosphodiesterase subunit alpha (GMP-PDE alpha) (EC 3.1.4.35) (PDE V-B1) (P16499)
Organism: Homo sapiens (Human)
Function: Rod-specific cGMP phosphodiesterase that catalyzes the hydrolysis of 3',5'-cyclic GMP. This protein participates in processes of transmission and amplification of the visual signal.
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cell projection, cilium, photoreceptor outer segment {ECO:0000269|PubMed:20940301}.
Interaction partners:
- Retinal rod rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit gamma
- Rod cGMP-specific 3',5'-cyclic phosphodiesterase subunit beta
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Cyclic nucleotide-gated channel beta-1
- Cyclic nucleotide-gated channel alpha-1
- Guanylate kinase
- GMP reductase 1
Sequence:
MGEVTAEEVEKFLDSNIGFAKQYYNLHYRAKLISDLLGAKEAAVDFSNYHSPSSMEESEIIFDLLRDFQENLQTEKCIFNVMKKLCFLLQADRMSLFMYRTRNGIAELATRLFNVHKDAVLEDCLVMPDQEIVFPLDMGIVGHVAHSKKIANVPNTEEDEHFCDFVDILTEYKTKNILASPIMNGKDVVAIIMAVNKVDGSHFTKRDEEILLKYLNFANLIMKVYHLSYLHNCETRRGQILLWSGSKVFEELTDIERQFHKALYTVRAFLNCDRYSVGLLDMTKQKEFFDVWPVLMGEVPPYSGPRTPDGREINFYKVIDYILHGKEDIKVIPNPPPDHWALVSGLPAYVAQNGLICNIMNAPAEDFFAFQKEPLDESGWMIKNVLSMPIVNKKEEIVGVATFYNRKDGKPFDEMDETLMESLTQFLGWSVLNPDTYESMNKLENRKDIFQDIVKYHVKCDNEEIQKILKTREVYGKEPWECEEEELAEILQAELPDADKYEINKFHFSDLPLTELELVKCGIQMYYELKVVDKFHIPQEALVRFMYSLSKGYRKITYHNWRHGFNVGQTMFSLLVTGKLKRYFTDLEALAMVTAAFCHDIDHRGTNNLYQMKSQNPLAKLHGSSILERHHLEFGKTLLRDESLNIFQNLNRRQHEHAIHMMDIAIIATDLALYFKKRTMFQKIVDQSKTYESEQEWTQYMMLEQTRKEIVMAMMMTACDLSAITKPWEVQSQVALLVAAEFWEQGDLERTVLQQNPIPMMDRNKADELPKLQVGFIDFVCTFVYKEFSRFHEEITPMLDGITNNRKEWKALADEYDAKMKVQEEKKQKQQSAKSAAAGNQPGGNPSPGGATTSKSCCIQ
Protein: Ceruloplasmin (Q1L857)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MKILILGIFLFLCSTPAWAKEKHYYIGIIETTWDYASDHGEKKLISVDTEHSNIYLQNGPDRIGRLYKKALYLQYTDETFRTTIEKPVWLGFLGPIIKAETGDKVYVHLKNLASRPYTFHSHGITYYKEHEGAIYPDNTTDFQRADDKVYPGEQYTYMLLATEEQSPGEGDGNCVTRIYHSHIDAPKDIASGLIGPLIICKKDSLDKEKEKHIDREFVVMFSVVDENFSWYLEDNIKTYCSEPEKVDKDNEDFQESNRMYSVNGYTFGSLPGLSMCAEDRVKWYLFGMGNEVDVHAAFFHGQALTNKNYRIDTINLFPATLFDAYMVAQNPGEWMLSCQNLNHLKAGLQAFFQVQECNKSSSKDNIRGKHVRHYYIAAEEIIWNYAPSGIDIFTKENLTAPGSDSAVFFEQGTTRIGGSYKKLVYREYTDASFTNRKERGPEEEHLGILGPVIWAEVGDTIRVTFHNKGAYPLSIEPIGVRFNKNNEGTYYSPNYNPQSRSVPPSASHVAPTETFTYEWTVPKEVGPTNADPVCLAKMYYSAVDPTKDIFTGLIGPMKICKKGSLHANGRQKDVDKEFYLFPTVFDENESLLLEDNIRMFTTAPDQVDKEDEDFQESNKMHSMNGFMYGNQPGLTMCKGDSVVWYLFSAGNEADVHGIYFSGNTYLWRGERRDTANLFPQTSLTLHMWPDTEGTFNVECLTTDHYTGGMKQKYTVNQCRRQSEDSTFYLGERTYYIAAVEVEWDYSPQREWEKELHHLQEQNVSNAFLDKGEFYIGSKYKKVVYRQYTDSTFRVPVERKAEEEHLGILGPQLHADVGDKVKIIFKNMATRPYSIHAHGVQTESSTVTPTLPGETLTYVWKIPERSGAGTEDSACIPWAYYSTVDQVKDLYSGLIGPLIVCRRPYLKVFNPRRKLEFALLFLVFDENESWYLDDNIKTYSDHPEKVNKDDEEFIESNKMHAINGRMFGNLQGLTMHVGDEVNWYLMGMGNEIDLHTVHFHGHSFQYK
Protein: WW domain-containing transcription regulator protein 1 (Transcriptional coactivator with PDZ-binding motif) (Q9GZV5)
Organism: Homo sapiens (Human)
Function: Transcriptional coactivator which acts as a downstream regulatory target in the Hippo signaling pathway that plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. The core of this pathway is composed of a kinase cascade wherein STK3/MST2 and STK4/MST1, in complex with its regulatory protein SAV1, phosphorylates and activates LATS1/2 in complex with its regulatory protein MOB1, which in turn phosphorylates and inactivates YAP1 oncoprotein and WWTR1/TAZ. WWTR1 enhances PAX8 and NKX2-1/TTF1-dependent gene activation. In conjunction with YAP1, involved in the regulation of TGFB1-dependent SMAD2 and SMAD3 nuclear accumulation. Plays a key role in coupling SMADs to the transcriptional machinery such as the mediator complex. Regulates embryonic stem-cell self-renewal, promotes cell proliferation and epithelial-mesenchymal transition.
Subcellular location: Nucleus {ECO:0000269|PubMed:11118213, ECO:0000269|PubMed:18568018, ECO:0000269|PubMed:19010321, ECO:0000269|PubMed:21145499, ECO:0000269|PubMed:23911299, ECO:0000269|PubMed:25849865, ECO:0000269|PubMed:29695716}. Cytoplasm {ECO:0000269|PubMed:18568018, ECO:0000269|PubMed:23911299, ECO:0000269|PubMed:25849865, ECO:0000269|PubMed:29695716}. Cell membrane {ECO:0000269|PubMed:11118213}. Cell junction, tight junction {ECO:0000250|UniProtKB:A0A8I3PQN6}. Note=Concentrates along specific portions of the plasma membrane, and accumulates in punctate nuclear bodies (By similarity). When phosphorylated, is retained in the cytoplasm by YWHAZ (By similarity). Can be retained in the nucleus by MED15 (PubMed:18568018). Localized in the cytoplasm in areas of epithelial cell high density (PubMed:21145499). At blastocyst stage expressed in the nucleus in trophectodermal cells, however expressed in the cytoplasm in the inner cell mass (By similarity). In the nucleus, phosphorylation by PRP4K induces nuclear exclusion (PubMed:29695716). Interaction with AMOTL2 results in localization to the cytoplasm and tight junctions (PubMed:23911299). {ECO:0000250|UniProtKB:Q9EPK5, ECO:0000269|PubMed:18568018, ECO:0000269|PubMed:21145499, ECO:0000269|PubMed:23911299, ECO:0000269|PubMed:29695716}.
Interaction partners:
- Transcriptional enhancer factor TEF-1
- Transcriptional enhancer factor TEF-3
- Serine/threonine-protein kinase LATS1
- Angiomotin
- Transcriptional enhancer factor TEF-4
- Transcriptional enhancer factor TEF-5
- Serine/threonine-protein kinase LATS2
- F-box/WD repeat-containing protein 1A
- 14-3-3 protein epsilon
- Tight junction protein 1
Sequence:
MNPASAPPPLPPPGQQVIHVTQDLDTDLEALFNSVMNPKPSSWRKKILPESFFKEPDSGSHSRQSSTDSSGGHPGPRLAGGAQHVRSHSSPASLQLGTGAGAAGSPAQQHAHLRQQSYDVTDELPLPPGWEMTFTATGQRYFLNHIEKITTWQDPRKAMNQPLNHMNLHPAVSSTPVPQRSMAVSQPNLVMNHQHQQQMAPSTLSQQNHPTQNPPAGLMSMPNALTTQQQQQQKLRLQRIQMERERIRMRQEELMRQEAALCRQLPMEAETLAPVQAAVNPPTMTPDMRSITNNSSDPFLNGGPYHSREQSTDSGLGLGCYSVPTTPEDFLSNVDEMDTGENAGQTPMNINPQQTRFPDFLDCLPGTNVDLGTLESEDLIPLFNDVESALNKSEPFLTWL
Protein: Pyroglutamyl-peptidase I (PGP), putative (D6XFK3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Golgi pH regulator conserved domain-containing protein
- Prolyl endopeptidase
Sequence:
MKPTKPLLYITGYGPFLEVTENPSATIAQSVAEQVRQSGEADVHHETLDVNLEAVSKYFNRLNESVTAHLEATHPENRVLLVNVGLHSREKEKVLRLEVRAFNELEGNPIDDELPLSTCKDSAFVKGCKLETTTALIEELNAIERNGSDHHEKPRWIISYDAGRYYCNYALYRGVKMQEALNSRVFAVFLHIVASTVVCMEEQVAQVRMLVSHLLKHMEAVE
Protein: Lung adenoma susceptibility protein 2 (Q8IYD9)
Organism: Homo sapiens (Human)
Function: Might play a role in cell proliferation.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
Sequence:
MAKSKTKHRLCSQESSVSALLASCTLSGSNSSNSDGSFHYKDKLYRSASQALQAYIDDFDLGQIYPGASTGKINIDEDFTNMSQFCNYIYKPNNAFENLDHKKHSNFISCRRHTVNDIDSMSLTTDDLLRLPADGSFSYTYVGPSHRTSKKNKKCRGRLGSLDIEKNPHFQGPYTSMGKDNFVTPVIRSNINGKQCGDKIELLILKAKRNLEQCTEELPKSMKKDDSPCSLDKLEADRSWENIPVTFKSPVPVNSDDSPQQTSRAKSAKGVLEDFLNNDNQSCTLSGGKHHGPVEALKQMLFNLQAVQERFNQNKTTDPKEEIKQVSEDDFSKLQLKESMIPITRSLQKALHHLSRLRDLVDDTNGERSPKM
Protein: H2HPP isomerase (EC 5.3.3.19) (3-((4R)-4-hydroxycyclohexa-1,5-dien-1-yl)-2-oxopropanoate isomerase) (Bacilysin biosynthesis protein BacB) (Bi-cupin protein) (P39639)
Organism: Bacillus subtilis (strain 168)
Function: Part of the bacABCDEF operon responsible for the biosynthesis of the nonribosomally synthesized dipeptide antibiotic bacilysin, composed of L-alanine and L-anticapsin. Bacilysin is an irreversible inactivator of the glutaminase domain of glucosamine synthetase. BacB catalyzes the allylic isomerization of the endocyclic-delta(4),delta(8)-7R-dihydro-hydroxyphenylpyruvate (en-H2HPP) to generate a mixture of 3E,7R- and 3Z, 7R-olefins (E/Z ration of 3/1) of the exocyclic-delta(3),delta(5)-dihydro-hydroxyphenylpyruvate (ex-H2HPP).
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Dihydroanticapsin 7-dehydrogenase
- Prephenate decarboxylase
- Alanine--anticapsin ligase
- Putative bacilysin exporter BacE
- Transaminase BacF
- NADPH-dependent reductase BacG
- Uncharacterized MFS-type transporter YwfA
- Quercetin 2,3-dioxygenase
- Uncharacterized protein YlbA
- Oxalate decarboxylase OxdC
Sequence:
MKTKEDMQELYFPTPKLIEWENGVRQYSTVRGDTEVLMSYVPPHTNVEPHQHKEVQIGMVVSGELMMTVGDVTRKMTALESAYIAPPHVPHGARNDTDQEVIAIDIKRLKADETYTSPEDYFLDIFKTRDLLPGMEVTFFVEDWVEIMLAKIPGNGGEMPFHKHRNEQIGICIGGGYDMTVEGCTVEMKFGTAYFCEPREDHGAINRSEKESKSINIFFPPRYNRAKAKKMKADE
Protein: Paralithocin 1 (P23) (A0A2I8B346)
Organism: Paralithodes camtschaticus (Red king crab) (Maja camtschatica)
Function: Has weak antibacterial activity, mainly against marine Gram-positive bacteria like C.maltaromaticum (MIC=200 uM), C.mobile (MIC=100 uM), C.divergens (MIC=200 uM) and C.funditum (MIC=200 uM) but also against C.glutamicum (MIC=50 uM). Has very little or no activity against Gram-negative bacteria.
Interaction partners:
Sequence:
MGPMKVLLVLLVVMVAAPHIADAWQQPSCSSICDYSCGKSACISYSGRCGCCASCRRGPIYG
Protein: FI21342p1 (Q9VJZ1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MWITGQFVFLLLVALVAAKSKTSAVQDDIAEYKDFKKLLRTKNNVLALYVTSAKSAAAELKIFREAAEAIRGTGTMLLLDCGQQDRKKLCKKLKVSPDPYAIKHYKDGDFHKDYDRQLSVSSMITFMRDPSGDLPWEEDPAGKDVLHFSDAASFTKHLRKDIRPMLVMFYVPWCGFCKKMKPEYGKASTELKTKGGYILAAMNVERQENAPIRKMFNITGFPTLIYFENGKLRFTYEGENNKEALVSFMLNPNAKPTPKPKEPEWSADTNSEIVHLTSQGFEPALKDEKSALVMFYAPWCGHCKRMKPEYEKAALEMKQKKIPGLLAALDATKEPSIAEKYKVKGYPTVKFFSNGVFKFEVNVREASKIVEFMRDPKEPPPPPPPEKSWEEEEDSKEVLFLDDDNFSSTLKRKKHALVMFYAPWCGHCKHTKPEFTAAATALQDDPRIAFVAIDCTKLAALCAKYNVRGYPTILYFSYLKTKLDYNGGRTSKDFIAYMNNPPTSADRTEL
Protein: Probable target of rapamycin complex 2 subunit BIT2 (TORC2 subunit BIT2) (Binding partner of TOR2 protein 2) (P38346)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Interaction partners:
- Target of rapamycin complex 2 subunit TSC11
- Target of rapamycin complex 2 subunit AVO1
- Target of rapamycin complex 2 subunit AVO2
- Serine/threonine-protein kinase TOR2
- Target of rapamycin complex subunit LST8
- Target of rapamycin complex 2 subunit BIT61
- Phosphatidylinositol 4,5-bisphosphate-binding protein SLM1
- Target of rapamycin complex 1 subunit TCO89
- Serine/threonine-protein kinase TOR1
- Target of rapamycin complex 1 subunit KOG1
Sequence:
MATDLNRKRSATSGSLSVTNPNIKATNRKPARVYSVSSDIVPQALTHPDEDVHLKTSKSPHDAAPRWSQVGFQSIFHDGSNARRSTDSIEEEYSQGTENNDGHSEIGSSSSNRMEGNTTSNDSLFSSNSRGNKRRLSIFTNSKDNMRNRSRSGSKNYGTVITGTSSNNISRSGSKLFHTKSNMSVNSLQSSLSTGHSHSNKGSNVFSKMAKKLLPYKPHNSIGKDDVEPVVPSPFSKFLHSSYGKHRSPVQFIHTSTGGLIDSGKSVYSFNPSINNNPNDTALSLIQDDAFDATNVSLLHDLLKNLPSLIANYKSFTVQELFVLEGNIWGIYCSIVVELFKNKRVWQLPAKIEDIDRLLEFYITLKTQTKAAVTHSRFLAEIEEFITTSLYILENQIVFNYANEDTVNTALKRVGIIWKVFYQQVYYDMMAVLLPFEKSFQKNSNYWLDGYLSEPSRYAPSIDVLLLKCFRDSIILPYYESFLHTNDGASKSFQRYIFSEEEQNGVTEEDKLTLLQCFGILNTIKGNSRNQRIIGELLEGIRMSI
Protein: Cytochrome c oxidase subunit 7A2-like, mitochondrial (Supercomplex assembly factor 1) (Q6FGA0)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004434}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004434}.
Interaction partners:
Sequence:
MYYKFSGFTQKLAGAWASEAYSPQGLKPVVSTEAPPIIFATPTKLTSDSTVYDYAGKNKVPELQKFFQKADGVPVYLKRGLPDQMLYRTTMALTVGGTIYCLIALYMASQPKNK
Protein: Zinc finger protein 330 homolog (Nucleolar autoantigen 36 homolog) (Q9VAU9)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000250}. Nucleus, nucleolus {ECO:0000250}. Note=Predominantly expressed in the nucleolus. {ECO:0000250}.
Interaction partners:
- Homeobox protein goosecoid
- LD24318p
- RE37218p2
Sequence:
MPKKKTGQRKKAEKQKLRLKEIRSREVPLADLPCNAPMECDKCEKKQKSRAFCYFCQSIQRLPICAQCGKIKCMLKTGDCVVKHPGVYTTGLGMVGAICDFCEAWVCHGRKCLQNHACTCPLQNATCLECERGVWEHGGRIFKCSFCNGFLCEDDQFEHQASCQVLESENYKCQSCNKLGQYSCLRCKTCYCEDHVRRKGFKYDKNKPIPCPKCNYDTSVTKDLSMSTRSHKFGRQQQGGNSDDEEGYGGYYGAGGSGYYGGAASGGYSYGGDDDEDESDGDYDDESDEDDDDDEEEDETTESEPEKETDKKATK
Protein: Defective proboscis extension response 8, isoform A (Defective proboscis extension response 8, isoform B) (GH05565p) (Q9VY33)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Dpr-interacting protein beta, isoform C
- Common Dpr-interacting protein
Sequence:
MSTHWIIFLGILCLLAGCTDGASKRFFTDFLQDLPTPGTGGPTFDTTIGTNITGLVGKTVKLTCRVKNLGNRTVSWVRHRDIHLLTVGRYTYTSDQRFEAMHSPHAEDWTLRIRYAQRKDSGIYECQISTTPPIGHSVYLNIVEPVTDIIGGPELHINRGSTINLTCIVKFAPEPPPTVIWSHNREIINFDSPRGGISLVTEKGVLTTSRLLVQKAITQDSGLYTCTPSNANPTSVRVHIVDGEHPAAMHTGNNGNSTASQPPVLLPLVLLTCSTLMLLQLVASCSTLVPATPPGCRTVQQASTFAEEKAMGQRSNRNCQDLQELEESQDLRRRGVERSAVPGT
Protein: Plexin-A4 (Q80UG2)
Organism: Mus musculus (Mouse)
Function: Coreceptor for SEMA3A. Necessary for signaling by class 3 semaphorins and subsequent remodeling of the cytoskeleton. Plays a role in axon guidance in the developing nervous system. Class 3 semaphorins bind to a complex composed of a neuropilin and a plexin. The plexin modulates the affinity of the complex for specific semaphorins, and its cytoplasmic domain is required for the activation of down-stream signaling events in the cytoplasm.
Subcellular location: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
Interaction partners:
- Semaphorin-6A
- Semaphorin-3A
- Neuropilin-1
- Plexin-A1
- Rho-related GTP-binding protein Rho6
- Rho-related GTP-binding protein RhoD
- Neuropilin-2
- Semaphorin-6D
- Tyrosine-protein kinase Fyn
- Ras-related C3 botulinum toxin substrate 2
Sequence:
MKAMPWNWTCLLSHLLVVGMGSSTLLPRQPPQLSQKPSFVTFRGEPAEGFNHLVVDERTGHIYLGAVNRIYKLSSDLKVLVTHQTGPDEDNPKCYPPRIVQTCNEPLASTNNVNKMLLIDYKENRLIACGSLYQGICKLLRLEDLFKLGEPFHKKEHYLSGVNESGSVFGVIVSYSNFDDKLFIATAVDGKPEYFPTISSRKLTKNSEADGMFAYVFHDEFVASMIKIPSDTFTVIPDFDIYYVYGFSSGNFVYFLTLQPEMVSPPGSTTKEQVYTSKLVRLCKEDTAFNSYVEVPIGCERNGVEYRLLQAAYLSKAGAVLGRTLGVRPDDDLLFTVFSKGQKRKMKSLDESALCIFILKQINDRIKDRLQSCYRGEGTLDLAWLKVKDIPCSSALLTIDDNFCGLDMNAPLGVSEMVRGIPVFTEDRDRMTSVIAYVYKNHSLAFVGTKSGKLKKIRVDGPKGNALQYETVQVVDSGPVLRDMAFSKDHEQLYIMSERQLTRVPVESCGQYRSCGECLGSGDPHCGWCVLHNTCTRKERCERSREPRRFASEMKQCVRLTVHPNNISVSQYNVLLVLETYNVPELSAGVNCTFEDLSEMDGLVIGNQIQCYSPAAKEVPRIITENGDHHVVQLQLKSKETGMTFASTSFVFYNCSVHNSCLSCVESPYRCHWCKYRHVCTHDPNTCSFQEGRVKLPEDCPQLLRVDKILVPVEVIKPITLKAKNLPQPQSGQRGYECILNIQGIEQRVPALRFNSSSVQCQNTSYSYEGMEINNLPVELTVVWNGHFNIDNPAQNKVYLYKCGAMRESCGLCLKADPDFECGWCQSPGQCTLRQHCPAHESRWLELSGANSKCTNPRITEIIPVTGPREGGTKVTIRGENLGLEFRDIASHVKVAGVECSPLVDGYIPAEQIVCEMGEAKPSQHAGFVEICVAVCRPEFMARSSQLYYFMTLTLADLKPNRGPMSGGTQVTITGTNLNAGSNVVVMFGSQPCLFHRRSPSYIICNTTSSEEVLDMKVTVQVDRARIRQDLVFQYVEDPTIVRIEPEWSIVSGNTPIAVWGTHLDLIQNPQIRAKHGGKEHINICEVLNATEMTCQAPALALGPDHQSDLTERPEEFGFILDNVQSLLILNKTNFTYYPNPVFEAFSPSGILELKPGTPIILKGKNLIPPVAGGNVKLNYTVLVGEKPCTVTVSDVQLLCESPNLIGRHKVMARVGGMEYSPGMVYIAPDSPLSLPAIVSIAVAGGLLIIFIVAVLIAYKRKSRESDLTLKRLQMQMDNLESRVALECKEAFAELQTDIHELTSDLDGAGIPFLDYRTYTMRVLFPGIEDHPVLRDLEVPGYRQERVEKGLKLFAQLINNKVFLLSFIRTLESQRSFSMRDRGNVASLIMTVLQSKLEYATDVLKQLLADLIDKNLESKNHPKLLLRRTESVAEKMLTNWFTFLLYKFLKECAGEPLFSLFCAIKQQMEKGPIDAITGEARYSLSEDKLIRQQIEYKTLVLSCVSPDNVNSPEVPVKILNCDTITQVKEKILDAIFKNVPCSHRPKAADMDLEWRQGSGARMILQDEDITTKIENDWKRLNTVAHYQVPDGSVVALVSKQVTAYNAVNNSTVSRTSASKYENMIRYTGSPDSLRSRTPMITPDLESGVKLWHLVKNHEHGDQKEGDRGSKMVSEIYLTRLLATKGTLQKFVDDLFETIFSTAHRGSALPLAIKYMFDFLDEQADKHGIHDPHVRHTWKSNCLPLRFWVNMIKNPQFVFDIHKNSITDACLSVVAQTFMDSCSTSEHRLGKDSPSNKLLYAKDIPSYKNWVERYYSDIGKMPAISDQDMNAYLAEQSRMHMNEFNTMSALSEIFSYVGKYSEEILGPLDHDDQCGKQKLAYKLEQVITLMSLDS