wanglab/gogpt-training-data huggingface dataset:
Protein: Caspase-1 (EC 3.4.22.-) [Cleaved into: Caspase-1 subunit p22; Caspase-1 subunit p13] (O02002)
Organism: Drosophila melanogaster (Fruit fly)
Function: Involved in the activation cascade of caspases responsible for apoptosis execution (By similarity). Proteolytically cleaves poly(ADP-ribose) polymerase (PARP). Loss of zygotic DCP-1 function causes larval lethality and melanotic tumors.
Interaction partners:
- Death-associated inhibitor of apoptosis 1
- Caspase Dronc
- Apoptosome protein Dark
- LD20892p
- Leucine-rich repeat, isoform F
- Caspase drICE
- Cytochrome c-1
- Cytochrome c-2
- BG1
- Autophagy protein 5
Sequence:
MTDECVTRNYGVGIRSPNGSENRGSFIMADNTDAKGCTPESLVVGGATAASPLPANKFVARMPVERYASEYNMSHKHRGVALIFNHEFFDIPSLKSRTGTNVDAQELKKAFENLGFAVSVHKDCKLRDILKHVGKAAELDHTDNDCLAVAILSHGEHGYLYAKDTQYKLDNIWHYFTATFCPSLAGKPKLFFIQACQGDRLDGGITLEKGVTETDGESSTSYKIPIHADFLFSYSTIPGYFSWRNINNGSWYMQSLIRELNANGKKYDLLTLLTFVNQRVALDFESNVPATPMMDRQKQIPCLTSMLTRILRFGDKPNGNKAG
Protein: Nuclear transcription factor Y subunit B-8 (OsNF-YB8) (Transcriptional activator HAP3I) (OsHAP3I) (Q75IZ7)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Component of the NF-Y/HAP transcription factor complex.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:26542958}.
Interaction partners:
- Nuclear transcription factor Y subunit C-4
- Nuclear transcription factor Y subunit C-6
- Nuclear transcription factor Y subunit C-2
- Nuclear transcription factor Y subunit
- Nuclear transcription factor Y subunit
- HAP5 subunit of HAP complex
- Nuclear transcription factor Y subunit
- HAP5 subunit of HAP complex
- Os08g0206500 protein
- Nuclear transcription factor Y subunit
Sequence:
MPDSDNDSGGPSNYAGGELSSPREQDRFLPIANVSRIMKKALPANAKISKDAKETVQECVSEFISFITGEASDKCQREKRKTINGDDLLWAMTTLGFEDYVDPLKHYLHKFREIEGERAAASTTGAGTSAASTTPPQQQHTANAAGGYAGYAAPGAGPGGMMMMMGQPMYGSPPPPPQQQQQQHHHMAMGGRGGFGHHPGGGGGGSSSSSGHGRQNRGA
Protein: ATP-dependent DNA helicase RecG (EC 5.6.2.4) (Q9HTL3)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- OxyR
- Holliday junction branch migration complex subunit RuvB
- DNA helicase RecQ
- Single-stranded-DNA-specific exonuclease RecJ
- DNA replication and repair protein RecF
- RecBCD enzyme subunit RecD
- DNA repair protein RecO
- Holliday junction branch migration complex subunit RuvA
- DNA polymerase I
- DNA repair protein RecN
Sequence:
MTELSRVPVTALKGVGAALAEKLARVGLETLQDILFHLPLRYQDRTRVTAIGALRPGADAVVEGVVAGADVVMGRRRSLLVRLQDGSGTLSLRFYHFSQAQKDGLKRGTHLRCYGEVRPGASGLEIYHPEYRALNGDEPIPVEQTLTPIYPTTEGLTQQRLRQLSQQALAMLGPSSLPDWLPAELARDYQLGPLDQAIRYLHRPPPDADIEELAEGRHWAQLRLAFEELLTHQLSLQRLREAVRSQAAPRLPAASRLPKRFLANLGFQPTGAQRRVGAEIAYDLAQDEPMLRLVQGDVGAGKTVVAALAALQAIEAGYQVALMAPTEILAEQHFLNFSKWLQPLDIEVAWLAGKLKGKARAAALERIGDGAPMVVGTHALFQDEVKFKRLALAIIDEQHRFGVQQRLALRQKGVDGRLCPHQLIMTATPIPRTLAMSAYADLDTSILDELPPGRTPVNTVLVADSRRIEVIERVRAACREGRQAYWVCTLIEESEELTCQAAETTYEELSSALGELRVGLIHGRMKPADKAVVMEAFKEGMLQLLVATTVIEVGVDVPNASLMIIENPERLGLAQLHQLRGRVGRGSAASHCVLLYHPPLSQIGRERLGIMRETSDGFVIAEKDLELRGPGEMLGTRQTGLLQFKVADLMRDADLLPAVRDAAQSLLAHWPQHVSPLLERWLRHGQQYGQV
Protein: TRAP transporter small permease protein (Q5LVG5)
Organism: Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3) (Silicibacter pomeroyi)
Subcellular location: Cell inner membrane {ECO:0000256|RuleBase:RU369079}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU369079}. Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
- TRAP transporter large permease protein
- TRAP dicarboxylate transporter, DctP subunit
- TRAP dicarboxylate transporter, DctP subunit
Sequence:
MTSLIRLARHASFAPVLVACLALFILMVMTFCDVILRSVLNAPIEAATELTRILMAVLVFSVLPIISVNNGQIAVDLTDGLFHRLRLDRIRDGLIHLVSGIMLYWPMSRVWILAERSRDYGDVTEYLAIPTYIVGWFIAISVGISAVALVITGLLHLFAPRLLSEALK
Protein: Unk like zinc finger (E9PDK2)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MPSVSKAAAAALSGSPPQTEKPTHYRYLKEFRTEQCPLFSQHKCAQHRPFTCFHWHFLNQRRRRPLRRRDGTFNYSPDVYCSKYNEATGVCPDGDECPYLHRTTGDTERKYHLRYYKTGTCIHETDARGHCVKNGLHCAFAHGPLDLRPPVCDVRELQAQEALQNGQLGGGEGVPDLQPGVLASQAMIEKILSEDPRWQDANFVLGSYKTEQCPKPPRLCRQGYACPHYHNSRDRRRNPRRFQYRSTPCPSVKHGDEWGEPSRCDGGDGCQYCHSRTEQQFHPEIYKSTKCNDMRQTGYCPRGPFCAFAHVEKSLGMVNEWGCHDLHLTSPSSTGSGQPGNAKRRDSPAEGGPRGSEQDSKQNHLAVFAAVHPPAPSVSSSVASSLASSAGSGSSSPTALPAPPARALPLGPASSTVEAVLGSALDLHLSNVNIASLEKDLEEQDGHDLGAAGPRSLAGSAPVAIPGSLPRAPSLHSPSSASTSPLGSLSQPLPGPVGSSAMTPPQQPPPLRSEPGTLGSAASSYSPLGLNGVPGSIWDFVSGSFSPSPSPILSAGPPSSSSASPNGAELARVRRQLDEAKRKIRQWEESWQQVKQVCDAWQREAQEAKERARVADSDRQLALQKKEEVEAQVIFQLRAKQCVACRERAHGAVLRPCQHHILCEPCAATAPECPYCKGQPLQW
Protein: Probable thioredoxin-2 (Q17424)
Organism: Caenorhabditis elegans
Function: Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions.
Interaction partners:
- Probable glutathione reductase 2
- Probable peroxiredoxin prdx-3
- Putative thiosulfate sulfurtransferase mpst-4
- peptide-methionine
- Large ribosomal subunit protein uL11m
- Peroxiredoxin prdx-2
- Thioredoxin reductase 1
- DNA-directed RNA polymerase II subunit RPB2
- Mitogen-activated protein kinase kinase kinase nsy-1
- Thioredoxin domain-containing protein
Sequence:
MQKALKLGSFFARSAISVKPTLATSKMTQLRHFSHGASVFDIDSVEDFTEKVIQSSVPVIVDFHAEWCGPCQALGPRLEEKVNGRQGSVLLAKINVDHAGELAMDYGISAVPTVFAFKNGEKISGFSGVLDDEQLDDFIEDVLAA
Protein: Zinc finger protein-like 1 (E9PNY1)
Organism: Homo sapiens (Human)
Subcellular location: Golgi apparatus, cis-Golgi network membrane {ECO:0000256|ARBA:ARBA00004612, ECO:0000256|RuleBase:RU369078}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004612, ECO:0000256|RuleBase:RU369078}.
Interaction partners:
Sequence:
MGLCKCPKRKVTNLFCFEHRVNVCEHCLVANHAKCIVQSYLQWLQDSDYNPNCRLCNIPLASRETTRLVCYDLFHWACLNERAAQLPRNTAPAGYQCPSCNGPIFPPTNLAGPVASALREKLATVNWARAGLGLPLIDEVVSPEPEPLNTSDFSDWSSFNASSTPGPEEVDSASAAPAFYSQAPRPPASPGRPEQHTVIHMGNPEPL
Protein: Penicillin-sensitive carboxypeptidase A (EC 3.4.16.4) (Q86I79)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Carboxypeptidase.
Interaction partners:
- NLP/P60 domain-containing protein
Sequence:
MKNYKIITLLLIISILFNIIRSNKISLKDSDSGSNGNQDIQILINDILNNCSSSESSSCFGTQWGVVADIYTPSNGEFTNIFSLNELQAFTPASNTKLFTTISIFYTFGEDFKVFTPFFTDKPFNSVSGGSSNSELDFICVKGMGDPSMSIDNLIEAAKFFSSNPTMKKVNKLLLDTSFYNIGNGVDGNIPSAWEWEDLTSTYGSIPTPLIINENTMDIYITPSNVIGGKPTASFKYSGEDKYLPVIILATTTTTSNSSTSTLNYSFKMSSQSIYITGNCDINGGIQIITVPILDPEQYFLTVFSALLEDGGVEISQTAIGSCNYTGMDYKSFEVISPELSEMLNYTLLTSNNLYAETFLRQMGTFNSAASESTPTYQAGLEYIQQTLSIPTSLYTQVDGSGLSRNNFITPKSLITVIENVYTNVGDPQHDYISYLPVASLSGTLSKRFINTPASGIVHAKTGSMTGVNSLTGVILPNGLSDDQQNSIFFSIIANNSPAQNTDIIDIIDQIVILLTKFILSS
Protein: Alginate biosynthesis protein AlgF (Q06062)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Together with AlgI and AlgJ, forms an inner membrane complex which probably interacts with the alginate polymerization-transport complex and adds acetyl groups at the O-2 and O-3 positions of mannuronate residues. Acetylation of alginate is important for the architecture of biofilms and increases resistance to opsonic killing in the host.
Subcellular location: Periplasm {ECO:0000269|PubMed:12003941}.
Interaction partners:
- Probable alginate O-acetylase AlgI
- Probable alginate O-acetylase AlgJ
- Alginate biosynthesis protein AlgX
- Alginate biosynthesis protein AlgA
- Mannuronan C5-epimerase
- Alginate production protein AlgE
- Mannuronan synthase
- Alginate lyase
- Alginate biosynthesis protein AlgK
- GDP-mannose 6-dehydrogenase
Sequence:
MNPMTRRHTWTRLACALSLGVAAFAAQADEGALYGPQAPKGSAFVRAYNAGNSELDVSVGSTSLNDVAPLGSSDFKFLPPGSYTAQVGQQSLPVKLDPDSYYTLVSQPGGKPQLVAEPPFKNKQKALVRVQNLSGSKLTLKTADGKTDVVKDVGPQSHGDREINPVKVNLALFDGSKKVSDLKPVTLARGEVVCLYVTGSGGKLAPVWVKRPVKAD
Protein: DNA-binding transcriptional activator HetR (EC 3.4.21.-) (Heterocyst differentiation control protein) (Master regulator of differentiation) (P27709)
Organism: Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)
Function: Controls heterocyst differentiation. Dimerization is required for DNA-binding. Has both a protease and a DNA-binding activity.
Interaction partners:
- Global nitrogen regulator
- Transcriptional regulator peptide PatS
- Ketoacyl reductase HetN
- Heterocyst differentiation protein
- Heterocyst differentiation protein
- Alr1010 protein
- Protein PatA
- Nitrogenase iron protein 1
- Heterocyst differentiation ATP-binding protein HepA
- Filament integrity protein FraC
Sequence:
MSNDIDLIKRLGPSAMDQIMLYLAFSAMRTSGHRHGAFLDAAATAAKCAIYMTYLEQGQNLRMTGHLHHLEPKRVKIIVEEVRQALMEGKLLKTLGSQEPRYLIQFPYVWMEQYPWIPGRSRIPGTSLTSEEKRQIEHKLPSNLPDAQLVTSFEFLELIEFLHKRSQEDLPPEHRMELSEALAEHIKRRLLYSGTVTRIDSPWGMPFYALTRPFYAPADDQERTYIMVEDTARYFRMMKDWAEKRPNAMRALEELDVPPERWDEAMQELDEIIRTWADKYHQVGGIPMILQMVFGRKED
Protein: Olfactory receptor 2W1 (Hs6M1-15) (Olfactory receptor OR6-13) (Q9Y3N9)
Organism: Homo sapiens (Human)
Function: Odorant receptor.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
Sequence:
MDQSNYSSLHGFILLGFSNHPKMEMILSGVVAIFYLITLVGNTAIILASLLDSQLHTPMYFFLRNLSFLDLCFTTSIIPQMLVNLWGPDKTISYVGCIIQLYVYMWLGSVECLLLAVMSYDRFTAICKPLHYFVVMNPHLCLKMIIMIWSISLANSVVLCTLTLNLPTCGNNILDHFLCELPALVKIACVDTTTVEMSVFALGIIIVLTPLILILISYGYIAKAVLRTKSKASQRKAMNTCGSHLTVVSMFYGTIIYMYLQPGNRASKDQGKFLTLFYTVITPSLNPLIYTLRNKDMKDALKKLMRFHHKSTKIKRNCKS
Protein: Merlin (Moesin-ezrin-radixin-like protein) (Neurofibromin-2) (Schwannomin) (Q63648)
Organism: Rattus norvegicus (Rat)
Function: Probable regulator of the Hippo/SWH (Sav/Wts/Hpo) signaling pathway, a signaling pathway that plays a pivotal role in tumor suppression by restricting proliferation and promoting apoptosis. Along with WWC1 can synergistically induce the phosphorylation of LATS1 and LATS2 and can probably function in the regulation of the Hippo/SWH (Sav/Wts/Hpo) signaling pathway. May act as a membrane stabilizing protein. May inhibit PI3 kinase by binding to AGAP2 and impairing its stimulating activity. Suppresses cell proliferation and tumorigenesis by inhibiting the CUL4A-RBX1-DDB1-VprBP/DCAF1 E3 ubiquitin-protein ligase complex Plays a role in lens development and is required for complete fiber cell terminal differentiation, maintenance of cell polarity and separation of the lens vesicle from the corneal epithelium.
Subcellular location: Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cell projection {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Nucleus {ECO:0000250}. Note=Colocalizes with MPP1 in non-myelin-forming Schwann cells. Binds with DCAF1 in the nucleus. The intramolecular association of the FERM domain with the C-terminal tail promotes nuclear accumulation. The unphosphorylated form accumulates predominantly in the nucleus while the phosphorylated form is largely confined to the non-nuclear fractions (By similarity). {ECO:0000250}.
Interaction partners:
- non-specific serine/threonine protein kinase
- Angiomotin
- Angiomotin-like protein 2
- non-specific serine/threonine protein kinase
- FERM domain-containing protein 6
- Protein salvador homolog 1
- CD44 antigen
- Hepatocyte growth factor-regulated tyrosine kinase substrate
- WW and C2 domain containing 1
- Ezrin
Sequence:
IASRMSFSSLKRKQPKTFTVRIVTMDAEMEFNCEMKWKGKDLFDLVCRTLGLRETWFFGLQYTIKDTVAWLKMDKKVLDHDVSKEEPVTFHFLAKFYPENAEEELVQEITQHLFFLQVKKQILDEKVYCPPEASVLLASYAVQAKYGDYDPSVHKRGFLAQEELLPKRVINLYQMTPEMWEERITAWYAEHRGRARDEAEMEYLKIAQDLEMYGVNYFTIRNKKGTELLLGVDALGLHIYDPENRLTPKISFPWNEIRNISYSDKEFTIKPLDKKIDVFKFNSSKLRVNKLILQLCIGNHDLFMRRRKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEAERSRDEPERRVLHMKEEATMANEALMRSEETADLLAEKAQITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRAKQKLLEIATKPTYPPMNPIPAPLPPDIPSFDIIGDSLSFDFKDTDMKRLSMEIEKEKVEYMEKSKHLQEQLNELKTEIEALKLKERETALDILHSEHSDSGTSSKHNTIKKPQAQGRRPICI
Protein: Grip71 (Q9VJ57)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Gamma-tubulin complex component 4 homolog
- Gamma-tubulin complex component
- GEO02508p1
- Gamma-tubulin complex component 3
- Grip163
- Gamma-tubulin complex component 2 homolog
- Tubulin gamma-1 chain
- Tubulin gamma-2 chain
- Testis-specific gamma-tubulin ring protein 91
- Centrosomin
Sequence:
MHVISTSKKTVLSDFADLETKSEYVHQNAEPTDFQFNGQRRVFVEVDKMAGLAVMRIKEKDGKTPEIQRVRKLTIDNAFCVACAKQSLEEIAVGQSGCVKLYNFRTAQLIHRFPADPQRSTVLYMDYNNTDEYIAAVRDGGDISILGTKTKQKTNTFTIDGDSTLVRFHPSKRFHLSIASYKGAVTVYDVQGMRKIFHASEAHSAPCRDISMCTSQPALLVSVGYDCKINIFDIRRNRAQASTDRLTYSHPLSTVALSECGTYLCAGNLKGELIAYDMRSTKAPLAVRSVHDAAVTRVAFVPVPSGDNQQNGSLNSSENATGLATEAPRVERAPSDELRKSIAANLLSTQNQLTSLGYGVSTPTIVRRDSFCEFLDAQGPRAVDRMSTRLGASYRDSFDWETLNRKPQPYETANRQSLCPPVASGPSSVDNSVNSSTTESLQQTLSGPLKDRSNISGDGKLMKIAETDELCEEQSANISVASSTGGGSDKENPPPVDAEMKRRLRLLSASRNSTPHHANITPQSSNPLLKPQQLLAKSSSGLSAQMDADWRKEFSELRDFVDQRCEKVERELEYVTFSNQRLLANKMTNYMDQQVENTREIRDALALLLQGDSFMREFSRLQNENEMLKAKLKFYQEQEQTESCGE
Protein: Glutamate metabotropic receptor 1 (H0ZKH5)
Organism: Taeniopygia guttata (Zebra finch) (Poephila guttata)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
- Homer scaffold protein 3
- Homer protein homolog 2
- Guanine nucleotide-binding protein subunit alpha
- Uncharacterized protein.
- Homer protein homolog 1
- Metabotropic glutamate receptor 5
- Glutamate receptor
Sequence:
MCRQGEPMKFVTWVWMTSCNKMIGVLLVFFPALLLEMEVLPKSGGRKVLLSAASSQRSVARMDGDVIIGALFSVHHQPPAEKVPERKCGEIREQYGIQRVEAMFHTLDKINADPVLLPNITLGSEIRDSCWHSSVALEQSIEFIRDSLISIRDDRDGGTRCISDSQTQPQSRVKKPIAGVIGPGSSSVAIQVQNLLQLFDIPQIAYSATSIDLSDKTLYKYFLRVVPSDTLQARAMLDIVKRYNWTYVSAVHTEGNYGESGMEAFKELAAQEGLCIAHSDKIYSNAGEKSFDRLLRKLRERLPKARVVVCFCEGMTVRGILIAMRRLGVLGEFLLIGSDGWADRDEVIEGYEPEANGGITIKLQSPEVLAFDDYYLKLRLDTNTRNPWFPEFWQHRFQCRIPGHPLENPNFQKNCTGNESLEENYVQDSKMGFVINAIYAMAYGLQNMHHSLCPGHVGLCDAMKPIDGSKLLEFLLKSSFIGVSGEEVWFDEKGDAPGRYDIMNLQYIEPNRYDYVLVGTWHEGVLNIDDYRIQMNKSGMVRSVCSEPCLKGQIKVIRKGEVSCCWICTACKENEFVQDEFTCKACDLGWWPNADLTGCEPIPVKYLQWSNIESIVAVVFSCLGILVTMFVTLIFVLYRDTPVVKSSSRELCYIILAGIFLGYVCPFTLIAKPTTTSCYLQRLLVGLSSAMCYSALVTKTNRIARILAGSKKKICTRKPRFMSAWAQVVIASILISVQLTLVITLIILEPPMPILSYPSIKEVYLICNTSNLGVVAPVGYNGLLIMSCTYYAFKTRNVPANFNEAKYIAFTMYTTCIIWLAFVPIYFGSNYKIITTCFAVSLSVTVALGCMFTPKMYIIIAKPERNVRSAFTTSDVVRMHVGDGKAPCKSNTFLNIFRRKKPGSGNPNSNGKSVSWSEPGGRQDPKGEHTWHRLSVHVKNQETGCNQTAVIKPLTKDYHGQSLTFTDISTKTLYNVVEEDREPVHLNQSSSPSMVVHRRVATTPPLQATAEETQLFLPEQSPKTLPLQPQSLMDQLQGVVNKFAAGIPDFNSVLPAPGSGNGVRPPCPPPPPQQPPLQPLQVDAFSEEPLSPPAEEAESEKVKLIQGYVYEKSTEEEEDEELATSKLTLEDSPALTPPSPFRDSVASGSSVPSSPVSESVLCTPPDVTYASVILRDYKQSSSTL
Protein: Disintegrin and metalloproteinase domain-containing protein 2 (ADAM 2) (Fertilin subunit beta) (PH-30) (PH30) (PH30-beta) (Q60718)
Organism: Mus musculus (Mouse)
Function: Sperm surface membrane protein that may be involved in sperm-egg plasma membrane adhesion and fusion during fertilization. Could have a direct role in sperm-zona binding or migration of sperm from the uterus into the oviduct. Interactions with egg membrane could be mediated via binding between its disintegrin-like domain to one or more integrins receptors on the egg. This is a non catalytic metalloprotease-like protein (By similarity).
Subcellular location: Membrane; Single-pass type I membrane protein.
Interaction partners:
- Disintegrin and metalloproteinase domain-containing protein 21
- Disintegrin and metalloproteinase domain-containing protein 1b
- Disintegrin and metalloproteinase domain-containing protein 25
- A disintegrin and metallopeptidase domain 30
- Disintegrin and metalloproteinase domain-containing protein 1a
- Zonadhesin
- Zona pellucida sperm-binding protein 3
- Hyaluronidase PH-20
- Calmegin
Sequence:
MWLILLLLSGLSELGGLSQSQTEGTREKLHVQVTVPEKIRSVTSNGYETQVTYNLKIEGKTYTLDLMQKPFLPPNFRVYSYDNAGIMRSLEQKFQNICYFQGYIEGYPNSMVIVSTCTGLRGFLQFGNVSYGIEPLESSSGFEHVIYQVEPEKGGALLYAEKDIDLRDSQYKIRSIKPQRIVSHYLEIHIVVEKQMFEHIGADTAIVTQKIFQLIGLANAIFAPFNLTVILSSLEFWMDENKILTTGDANKLLYRFLKWKQSYLVLRPHDMAFLLVYRNTTDYVGATYQGKMCDKNYAGGVALHPKAVTLESLAIILVQLLSLSMGLAYDDVNKCQCGVPVCVMNPEAPHSSGVRAFSNCSMEDFSKFITSQSSHCLQNQPRLQPSYKMAVCGNGEVEEDEICDCGKKGCAEMPPPCCNPDTCKLSDGSECSSGICCNSCKLKRKGEVCRLAQDECDVTEYCNGTSEVCEDFFVQNGHPCDNRKWICINGTCQSGEQQCQDLFGIDAGFGSSECFWELNSKSDISGSCGISAGGYKECPPNDRMCGKIICKYQSENILKLRSATVIYANISGHVCVSLEYPQGHNESQKMWVRDGTVCGSNKVCQNQKCVADTFLGYDCNLEKCNHHGVCNNKKNCHCDPTYLPPDCKRMKDSYPGGSIDSGNKERAEPIPVRPYIASAYRSKSPRWPFFLIIPFYVVILVLIGMLVKVYSQRMKWRMDDFSSEEQFESESESKD
Protein: Aminotransferase PigE (EC 2.6.1.-) (Q5W267)
Organism: Serratia sp. (strain ATCC 39006) (Prodigiosinella confusarubida)
Function: Involved in the biosynthesis of 2-methyl-3-n-amyl-pyrrole (MAP), one of the terminal products involved in the biosynthesis of the red antibiotic prodigiosin (Pig). Catalyzes the transamination to the aldehyde group of 3-acetyloctanal, resulting in an aminoketone, which spontaneously cyclizes to yield the dihydro form of MAP (H2MAP).
Interaction partners:
- Thiamine diphosphate dependent-3-acetyloctanal synthase PigD
- Oxidoreductase PigB
- Rubrerythrin family protein
- N-acetyl-gamma-glutamyl-phosphate reductase
- N-acetyl-gamma-glutamyl-phosphate reductase
- Amino-acid acetyltransferase
- Probable NAD
- Beta-ketoacyl synthase PigJ
- S-adenosyl-L-methionine-dependent methyl transferase PigF
- 4-hydroxy-2,2'-bipyrrole-5-methanol synthase PigH
Sequence:
MKFGFIAHPTSVGLKRYVKMIDLLQRNSTELHSGYKRDLWRRENLVPFMNFAKITSATGATCEGVIKYMPLVADEMLADARGIANRVVSGIEELVEDGAELVGLGGFTSIVGRRGEATAEKSPVPVTSGNSLTTYAGYKALMQIQSWLDIQPEQEPVAIVGYPGSICLALSRLLLAQGFSLHLLHRAGHKDEDELLSHLPEQYRSRVTLTSDPEDLYPRCKLFVAATSAGGVIDPYKLQPGSVFIDVALPRDINSDTRPDRDDILIIDGGCVTATDAVKLGGESLNVTIKQQLNGCMAETIVLALENRRENFSLGRYLALDNVLEIGELAEKHGFLVYPLASYGERIDRQRVINLKRYYHHDIYSDEPDTEQPPASQLAFIDAIIAQDPAREDTLDRYHQFINPMMVEFLKLQHCDNVFRRASGTQLFTADGEAFLDMVAGYGCINLGHNPQPIIDALKAYLDAQGPNFIQYISIPEQAAKLAEVLCHFAPGNMGRVFFSNSGTEAVEAAMKLAKASTGKAGIAYLKNSYHGKTLGALSITGREKHRRHFKPLLASMIEVPFADIEALRQTLSRDDIGALMIEPIQGEGGVHVPPPGYLRTVQEICRQTDTLLMVDEVQTGLGRTGKLFACEWEGIEPDVLMLSKSLSGGVMPIGATLCRAIFGNGPYGTADRFLMHSSTFGGGNIAAVVALSALREILAQDLVGNAERLGTYFKQALTDVAARYPFVAEIAGRGLMLGIQFDQTFAGAVGASAREFATRLPGDWHTTWKFLPDPVQAHLKAAMERMEQSLGEMFCMKFVTKLCQDHNILTFITANSSTVIRIQPPLTISKAEIDRFVSAFATVCDELSTFLE
Protein: N-succinylglutamate 5-semialdehyde dehydrogenase (EC 1.2.1.71) (Succinylglutamic semialdehyde dehydrogenase) (SGSD) (P76217)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the NAD-dependent reduction of succinylglutamate semialdehyde into succinylglutamate (Probable). Also shows in vitro activity with decanal or succinic semialdehyde as the electron donor and NAD as the electron acceptor. No activity is detected with NADP as the electron acceptor. Therefore, is an aldehyde dehydrogenase with broad substrate specificity.
Interaction partners:
- Succinylornithine transaminase
- Arginine N-succinyltransferase
- N-succinylarginine dihydrolase
- Succinylglutamate desuccinylase
- Bifunctional aldehyde-alcohol dehydrogenase AdhE
- Probable alcohol dehydrogenase EutG
- Probable alcohol dehydrogenase
- Acetaldehyde dehydrogenase
- NADPH-dependent aldehyde reductase YqhD
- 4-aminobutyrate aminotransferase GabT
Sequence:
MTLWINGDWITGQGASRVKRNPVSGEVLWQGNDADAAQVEQACRAARAAFPRWARLSFAERHAVVERFAALLESNKAELTAIIARETGKPRWEAATEVTAMINKIAISIKAYHVRTGEQRSEMPDGAASLRHRPHGVLAVFGPYNFPGHLPNGHIVPALLAGNTIIFKPSELTPWSGEAVMRLWQQAGLPPGVLNLVQGGRETGQALSALEDLDGLLFTGSANTGYQLHRQLSGQPEKILALEMGGNNPLIIDEVADIDAAVHLTIQSAFVTAGQRCTCARRLLLKSGAQGDAFLARLVAVSQRLTPGNWDDEPQPFIGGLISEQAAQQVVTAWQQLEAMGGRPLLAPRLLQAGTSLLTPGIIEMTGVAGVPDEEVFGPLLRVWRYDTFDEAIRMANNTRFGLSCGLVSPEREKFDQLLLEARAGIVNWNKPLTGAASTAPFGGIGASGNHRPSAWYAADYCAWPMASLESDSLTLPATLNPGLDFSDEVVR
Protein: Triazine hydrolase (Q6SJY7)
Organism: Paenarthrobacter aurescens (Arthrobacter aurescens)
Interaction partners:
Sequence:
MSSCEVLTSLGERMILIRGLTRVITFDDQERELEDADILIDGPKIVAVGKDLSDRSVSRTIDGRGMIALPGLINSHQHLYEGAMRAIPQLERVTMASWLEGVLTRSAGWWRDGKFGPDVIREVARAVLLESLLGGITTVADQHLFFPGATADSYIDATIEAATDLGIRFHAARSSMTLGKSEGGFCDDLFVEPVDRVVQHCLGLIDQYHEPEPFGMVRIALGPCGVPYDKPELFEAFAQMAADYDVRLHTHFYEPLDAGMSDHLYGMTPWRFLEKHGWASDRVWLAHAVVPPREEIPEFADAGVAIAHLIAPDLRMGWGLAPIREYLDAGITVGFGTTGSASNDGGNLLGDLRLAALAHRPADPNEPEKWLSARELLRMATRGSAECLGRPDLGVLEEGRAADIACWRLDGVDRVGVHDPAIGLIMTGLSDRASLVVVNGQVLVENERPVLADLERIVANTTALIPKNL
Protein: 6-phosphogluconate dehydrogenase, decarboxylating (EC 1.1.1.44) (P00350)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the oxidative decarboxylation of 6-phosphogluconate to ribulose 5-phosphate and CO(2), with concomitant reduction of NADP to NADPH.
Interaction partners:
- Glucose-6-phosphate 1-dehydrogenase
- Thermoresistant gluconokinase
- Thermosensitive gluconokinase
- Ribulose-phosphate 3-epimerase
- Phosphogluconate dehydratase
- Ribose-5-phosphate isomerase A
- 6-phosphogluconolactonase
- Transketolase 1
- Ribose-5-phosphate isomerase B
- Transaldolase B
Sequence:
MSKQQIGVVGMAVMGRNLALNIESRGYTVSIFNRSREKTEEVIAENPGKKLVPYYTVKEFVESLETPRRILLMVKAGAGTDAAIDSLKPYLDKGDIIIDGGNTFFQDTIRRNRELSAEGFNFIGTGVSGGEEGALKGPSIMPGGQKEAYELVAPILTKIAAVAEDGEPCVTYIGADGAGHYVKMVHNGIEYGDMQLIAEAYSLLKGGLNLTNEELAQTFTEWNNGELSSYLIDITKDIFTKKDEDGNYLVDVILDEAANKGTGKWTSQSALDLGEPLSLITESVFARYISSLKDQRVAASKVLSGPQAQPAGDKAEFIEKVRRALYLGKIVSYAQGFSQLRAASEEYNWDLNYGEIAKIFRAGCIIRAQFLQKITDAYAENPQIANLLLAPYFKQIADDYQQALRDVVAYAVQNGIPVPTFSAAVAYYDSYRAAVLPANLIQAQRDYFGAHTYKRIDKEGVFHTEWLD
Protein: DDB1- and CUL4-associated factor 8 (WD repeat-containing protein 42A) (Q5TAQ9)
Organism: Homo sapiens (Human)
Function: May function as a substrate receptor for CUL4-DDB1 E3 ubiquitin-protein ligase complex.
Subcellular location: Nucleus {ECO:0000269|PubMed:22500989}. Cytoplasm {ECO:0000269|PubMed:22500989}. Note=It shuttles between the nucleus and the cytoplasm. Nuclear import is mediated by KPNA1 and KPNB1 under the regulation of nuclear GTPase RAN. Nuclear export to the cytoplasm is XPO1 dependent. {ECO:0000269|PubMed:22500989}.
Interaction partners:
- DNA damage-binding protein 1
- Cullin-4B
- Cullin-4A
- DET1- and DDB1-associated protein 1
- DDB1- and CUL4-associated factor 4
- DDB1- and CUL4-associated factor 15
- DDB1- and CUL4-associated factor 11
- E3 ubiquitin-protein ligase RBX1
- DDB1- and CUL4-associated factor 12
- Protein cereblon
Sequence:
MSSKGSSTDGRTDLANGSLSSSPEEMSGAEEGRETSSGIEVEASDLSLSLTGDDGGPNRTSTESRGTDTESSGEDKDSDSMEDTGHYSINDENRVHDRSEEEEEEEEEEEEEQPRRRVQRKRANRDQDSSDDERALEDWVSSETSALPRPRWQALPALRERELGSSARFVYEACGARVFVQRFRLQHGLEGHTGCVNTLHFNQRGTWLASGSDDLKVVVWDWVRRQPVLDFESGHKSNVFQAKFLPNSGDSTLAMCARDGQVRVAELSATQCCKNTKRVAQHKGASHKLALEPDSPCTFLSAGEDAVVFTIDLRQDRPASKLVVTKEKEKKVGLYTIYVNPANTHQFAVGGRDQFVRIYDQRKIDENENNGVLKKFCPHHLVNSESKANITCLVYSHDGTELLASYNDEDIYLFNSSHSDGAQYVKRYKGHRNNATVKGVNFYGPKSEFVVSGSDCGHIFLWEKSSCQIIQFMEGDKGGVVNCLEPHPHLPVLATSGLDHDVKIWAPTAEASTELTGLKDVIKKNKRERDEDSLHQTDLFDSHMLWFLMHHLRQRRHHRRWREPGVGATDADSDESPSSSDTSDEEEGPDRVQCMPS
Protein: PvdO (Q9I185)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- PvdN
- PvdP
- Probable dipeptidase
- Acyl-homoserine lactone acylase PvdQ
- L-2,4-diaminobutyrate:2-ketoglutarate 4-aminotransferase, PvdH
- L-ornithine N
- Pyoverdine export outer membrane protein OpmQ
- PvdG
- Pyoverdine export membrane fusion protein PvdR
- Pyoverdine biosynthesis protein PvdE
Sequence:
MHALSPLALAALIVATAPAFADEAKKPGTVFKDCKDCPEMVVLPAGSFTMGTPDDEVGRQPDEGPLHDVTFAKPFAISRYQVTAGELDAYLKATGVKLADGDTRPGRECIAGKPRYQQGPRQPAVCVDYNDVKNYAAWLSKKTGKRYRMLSEAEREYGARAGSAGPFPFPFDEGKEYSIAKHANTYGASDGYNFTSPVGSFPPNAFGVYDMHGNVYEWVADCWHDHYNGAPSDGSAWMEEKCELVQIRGNDWGEPPIFSRSGNRNNAAPSDRGDWIGFRVAREL
Protein: Protein FAM162A (F8W7Q4)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
Sequence:
MRSCFRLCERDVSSSLRLTRSSDLKRINGFCTKPQESPGAPSRTYNRVPLHKPTDWQKKILIWSGRFKKEDEIPETVSLEMLDAAKNKMRVKISYLMIALTVVGCIFMVIEGKKAAQRHETLTSLNLEKKARLKEEAAMKAKTE