wanglab/gogpt-training-data huggingface dataset:
Protein: Small ribosomal subunit protein uS15y (40S ribosomal protein S13-2) (P59224)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Small ribosomal subunit protein eS24z
- Small ribosomal subunit protein uS14z/uS14y/uS14x
- Small ribosomal subunit protein eS19x
- Small ribosomal subunit protein uS17z
- Small ribosomal subunit protein eS30z/eS30y/eS30x
- Small ribosomal subunit protein eS6z
- Small ribosomal subunit protein eS28x
- Small ribosomal subunit protein eS6y
- Small ribosomal subunit protein uS10z/uS10x
- Small ribosomal subunit protein uS13z/uS13y/uS13x
Sequence:
MGRMHSRGKGISASALPYKRSSPSWLKTTSQDVDESICKFAKKGLTPSQIGVILRDSHGIPQVKSVTGSKILRILKAHGLAPEIPEDLYHLIKKAVAIRKHLERNRKDKDSKFRLILVESRIHRLARYYKKTKKLPPVWKYESTTASTLVA
Protein: Cytohesin-3 (ARF nucleotide-binding site opener 3) (Protein ARNO3) (General receptor of phosphoinositides 1) (Grp1) (PH, SEC7 and coiled-coil domain-containing protein 3) (O43739)
Organism: Homo sapiens (Human)
Function: Promotes guanine-nucleotide exchange on ARF1 and ARF6. Promotes the activation of ARF factors through replacement of GDP with GTP. Plays a role in the epithelial polarization (By similarity).
Subcellular location: Cytoplasm, cytosol. Cell membrane {ECO:0000250|UniProtKB:O08967}; Peripheral membrane protein {ECO:0000250|UniProtKB:O08967}. Cell junction, adherens junction {ECO:0000250|UniProtKB:O08967}. Cell junction, tight junction {ECO:0000250|UniProtKB:O08967}. Note=Translocates from the cytosol to membranes enriched in phosphatidylinositol 3,4,5-trisphosphate. {ECO:0000250|UniProtKB:O08967}.
Interaction partners:
- ADP-ribosylation factor 6
- ADP-ribosylation factor 1
- Cytohesin-interacting protein
- Protein TAMALIN
- FERM domain-containing protein 4B
- Pleckstrin-2
- Pleckstrin
- Connector enhancer of kinase suppressor of ras 1
- Interaction protein for cytohesin exchange factors 1
- Cytohesin-1
Sequence:
MDEDGGGEGGGVPEDLSLEEREELLDIRRRKKELIDDIERLKYEIAEVMTEIDNLTSVEESKTTQRNKQIAMGRKKFNMDPKKGIQFLIENDLLQSSPEDVAQFLYKGEGLNKTVIGDYLGERDEFNIKVLQAFVELHEFADLNLVQALRQFLWSFRLPGEAQKIDRMMEAFASRYCLCNPGVFQSTDTCYVLSFAIIMLNTSLHNHNVRDKPTAERFIAMNRGINEGGDLPEELLRNLYESIKNEPFKIPEDDGNDLTHTFFNPDREGWLLKLGGGRVKTWKRRWFILTDNCLYYFEYTTDKEPRGIIPLENLSIREVEDPRKPNCFELYNPSHKGQVIKACKTEADGRVVEGNHVVYRISAPSPEEKEEWMKSIKASISRDPFYDMLATRKRRIANKK
Protein: CDK2-associated and cullin domain-containing protein 1 (Cdk-associated cullin 1) (Q86Y37)
Organism: Homo sapiens (Human)
Function: Cell cycle associated protein capable of promoting cell proliferation through the activation of CDK2 at the G1/S phase transition.
Interaction partners:
Sequence:
MEESMEEEEGGSYEAMMDDQNHNNWEAAVDGFRQPLPPPPPPSSIPAPAREPPGGQLLAVPAVSVDRKGPKEGLPMGPQPPPEANGVIMMLKSCDAAAAVAKAAPAPTASSTININTSTSKFLMNVITIEDYKSTYWPKLDGAIDQLLTQSPGDYIPISYEQIYSCVYKCVCQQHSEQMYSDLIKKITNHLERVSKELQASPPDLYIERFNIALGQYMGALQSIVPLFIYMNKFYIETKLNRDLKDDLIKLFTEHVAEKHIYSLMPLLLEAQSTPFQVTPSTMANIVKGLYTLRPEWVQMAPTLFSKFIPNILPPAVESELSEYAAQDQKFQRELIQNGFTRGDQSRKRAGDELAYNSSSACASSRGYR
Protein: Tetratricopeptide repeat protein 1 (TPR repeat protein 1) (Q99614)
Organism: Homo sapiens (Human)
Interaction partners:
- Heat shock 70 kDa protein 4
- Heat shock cognate 71 kDa protein
- Heat shock protein HSP 90-alpha
- Vesicle-associated membrane protein-associated protein A
- E3 ubiquitin-protein ligase NRDP1
- Protein phosphatase 1 regulatory subunit 7
- Heat shock protein HSP 90-beta
- Neurofibromin
- DnaJ homolog subfamily C member 7
- Peroxisomal targeting signal 1 receptor
Sequence:
MGEKSENCGVPEDLLNGLKVTDTQEAECAGPPVPDPKNQHSQSKLLRDDEAHLQEDQGEEECFHDCSASFEEEPGADKVENKSNEDVNSSELDEEYLIELEKNMSDEEKQKRREESTRLKEEGNEQFKKGDYIEAESSYSRALEMCPSCFQKERSILFSNRAAARMKQDKKEMAINDCSKAIQLNPSYIRAILRRAELYEKTDKLDEALEDYKSILEKDPSIHQAREACMRLPKQIEERNERLKEEMLGKLKDLGNLVLRPFGLSTENFQIKQDSSTGSYSINFVQNPNNNR
Protein: Replication initiator 1 (E7EVL6)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MLERRCRGPLAMGLAQPRLLSGPSQESPQTLGKESRGLRQQGTSVAQSGAQAPGRAHRCAHCRRHFPGWVALWLHTRRCQARLPLPCPECGRRFRHAPFLALHRQVHAAATPDLGFACHLCGQSFRGWVALVLHLRAHSAAKRPIA
Protein: Adenylyl cyclase (At4g15640) (Q1JPP0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Uncharacterized protein
- Translation elongation factor EF1B/ribosomal protein S6 family protein
- Ribosomal protein L18e/L15 superfamily protein
- Ribosomal protein L31
- Small ribosomal subunit protein mS29
- Small ribosomal subunit protein mS47
- Large ribosomal subunit protein uL4m
- Large ribosomal subunit protein bL21m
- Large ribosomal subunit protein mL46
- Large ribosomal subunit protein mL101
Sequence:
MQFLQNSRRIATVLKPIVTTETNLRFFSSASQISRSFQWRSQASSSSSVLKGIDSSSHLSSMSLLIPRSSFTSEAEKLAGNPTVTVKDLHDKMLNSVNVKRSMPPNAWLWLLIENCQNQDDIHLLFDVLQNLRRFRLSNLRIHDNFNCNLCQQVAKTCVRVGAIDSGKKALWKHNVHGLTPSVASAHHLMSYALEHKNSELMEEVMQLLKTNDLPLQPGTADLVFRICHDTDKWDLLAKYSKKFSKAGVKLRKTTFDVWMEFAAKRGDTESLWKVDKQRSETYSQHTLSTAFSCAKGFLLESKPEEAAAVIQIICQAYPDEKKSAISTEFEKLVNEWPVDVIKHQTDEDKKALAASLKSVIPSMVNTLLSSGLKVSVDLDELNKNEALLS
Protein: Endoplasmic reticulum oxidoreductin-1 (EC 1.8.4.-) (Q7YTU4)
Organism: Caenorhabditis elegans
Function: Oxidoreductase involved in disulfide bond formation in the endoplasmic reticulum. Efficiently reoxidizes pdi-1, the enzyme catalyzing protein disulfide formation, in order to allow pdi-1 to sustain additional rounds of disulfide formation. Following pdi reoxidation, passes its electrons to molecular oxygen via FAD, leading to the production of reactive oxygen species (ROS) in the cell (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Lumenal side {ECO:0000250}.
Interaction partners:
- Protein disulfide-isomerase 1
- Protein disulfide-isomerase 2
- Probable protein disulfide-isomerase A4
- Thioredoxin domain-containing protein
- Protein disulfide-isomerase A6 homolog
- BZIP domain-containing protein.
- Thioredoxin domain-containing protein
- Translocon Sec61/SecY plug domain-containing protein
- Derlin-1
- Sulfhydryl oxidase
Sequence:
MREPLLQLIVLSLIIIVVNTQFESGRLCFCKGFEAVEPCDCSKPQTIDKLNNHRIYEKVQKLLKKDFFRFYKVNMDKTCPFWADDRQCGTNQCGIAFCDDEVPAGLRRRNAVNMEAAAVKEEEDDDAEKCADAGNNIDPMDRTLHDDEKRQLDAMDHHDDGLEDKFCEIEDDESDGMHYVDLSKNPERYTGYAGKSPQRVWKSIYEENCFKPDPKFDKNFLTNPSNFGMCLEKRVFYRLISGLHSAITISIAAYNYKPPPPSLGQFGSQMGTWFRNTEMFAGRFGTKWSWEGPQRLRNVYFIYLLELRALLKAAPYLQNELFYTGNDVEDAETRKAVEDLLEEIRAYPNHFDESEMFTGVESHARALREEFRSHFVNISRIMDCVECDKCRLWGKVQTHGMGTALKILFSDLPHSHYKQDSSKFQLTRNEVVALLQSFGRYSSSILEVDNFREDMYPGESVMNTAADGPPRKSNKIDL
Protein: Rho-related GTP-binding protein RhoN (Rho family GTPase 2) (Rho-related GTP-binding protein Rho7) (Rnd2) (P52198)
Organism: Homo sapiens (Human)
Function: May be specifically involved in neuronal and hepatic functions. Is a C3 toxin-insensitive member of the Rho subfamily (By similarity).
Subcellular location: Cytoplasmic vesicle, secretory vesicle, acrosome membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Note=Colocalizes with RACGAP1 in Golgi-derived proacrosomal vesicles and the acrosome. {ECO:0000269|PubMed:12590651}.
Interaction partners:
- Plexin-B1
- Rho GTPase-activating protein 35
- BTB/POZ domain-containing adapter for CUL3-mediated RhoA degradation protein 2
- BTB/POZ domain-containing adapter for CUL3-mediated RhoA degradation protein 1
- Inactive tyrosine-protein kinase PRAG1
- Plexin-B2
- Neurogenin-2
- UBX domain-containing protein 11
- Rho GTPase-activating protein 5
- Interferon-induced 35 kDa protein
Sequence:
MEGQSGRCKIVVVGDAECGKTALLQVFAKDAYPGSYVPTVFENYTASFEIDKRRIELNMWDTSGSSYYDNVRPLAYPDSDAVLICFDISRPETLDSVLKKWQGETQEFCPNAKVVLVGCKLDMRTDLATLRELSKQRLIPVTHEQGTVLAKQVGAVSYVECSSRSSERSVRDVFHVATVASLGRGHRQLRRTDSRRGMQRSAQLSGRPDRGNEGEIHKDRAKSCNLM
Protein: Zona pellucida sperm-binding protein 3 (Sperm receptor) (Zona pellucida glycoprotein 3) (Zp-3) (Zona pellucida glycoprotein 3B) (Zp-3B) (Zona pellucida protein C) [Cleaved into: Processed zona pellucida sperm-binding protein 3] (P48830)
Organism: Bos taurus (Bovine)
Function: Component of the zona pellucida, an extracellular matrix surrounding oocytes which mediates sperm binding, induction of the acrosome reaction and prevents post-fertilization polyspermy. The zona pellucida is composed of 3 to 4 glycoproteins, ZP1, ZP2, ZP3, and ZP4. ZP3 is essential for sperm binding and zona matrix formation.
Subcellular location: [Processed zona pellucida sperm-binding protein 3]: Zona pellucida {ECO:0000250|UniProtKB:P21754}.; SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P48833}; Single-pass type I membrane protein {ECO:0000255}.
Interaction partners:
- Zona pellucida sperm-binding protein 2
- Zona pellucida sperm-binding protein 4
- Oviduct-specific glycoprotein
Sequence:
MGPCSRLFVCFLLWGSTELCSPQPFWDDETERFRPSKPPAVMVECQEAQLVVTVDKDLFGTGKLIRPADLTLGPDNCEPLASADTDGVVRFAVGLHECGNILQVTDNALVYSTFLLHNPRPAGNLSILRTNRAEVPIECHYPRQGNVSSWAIQPTWVPFRTTVFSEEKLVFSLRLMEENWSAEKMTPTFQLGDRAHLQAQVHTGSHVPLRLFVDHCVASLTPDWSTSPYHTIVDFHGCLVDGLTDASSAFKAPRPRPEILQFTVDVFRFANDSRNMIYITCHLKVTPVDRVPDQLNKACSFSKSSNRWSPVEGPTDICRCCSKGRCGISGRSMRLSHREGRPVPRSRRHVTEEADVTVGPLIFLRKMNDRGVEGPTSSPPLVMLGLGLATVMTLTLAAIVLGLTGRLRAASHPVCPVSASQ
Protein: RNA-binding protein CP31B, chloroplastic (Q9FGS0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Required for specific RNA editing events in chloroplasts and stabilizes specific chloroplast mRNAs.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:17450127}.
Interaction partners:
- Organelle RRM domain-containing protein 1
- Organelle RRM domain-containing protein 6
- AT3g09210/F3L24_8
- Translation initiation factor IF3-2, chloroplastic
- RNA-binding
- Pentatricopeptide repeat-containing protein At1g02150
- Pentatricopeptide repeat-containing protein At2g17033
Sequence:
MTSSVLTPSLKLLAMTNSSSSTLFCIPSIFNISSSESHRFNFSLSSRPVNLTLSLKSKTLRNSSPVVTFVSQTSNWAEEEEGEDGSIGGTSVTVDESFESEDGVGFPEPPEEAKLFVGNLPYDVDSQALAMLFEQAGTVEISEVIYNRDTDQSRGFGFVTMSTVEEAEKAVEKFNSFEVNGRRLTVNRAAPRGSRPERQPRVYDAAFRIYVGNLPWDVDSGRLERLFSEHGKVVDARVVSDRETGRSRGFGFVQMSNENEVNVAIAALDGQNLEGRAIKVNVAEERTRR
Protein: Kinesin-like protein klp-20 (Q965T6)
Organism: Caenorhabditis elegans
Function: Component of the kinesin II motor complex (composed of kap-1 and the heterodimeric motor proteins klp-11 and klp-20) which is required for intraflagellar transport (IFT). Heterodimerizes with klp-11 to form a 'processive' molecular motor upon IFT cargo binding, which, within the kinesin II motor complex, binds to and moves along microtubules in a unidirectional manner (without dissociation of the heterodimer), and in turn, is responsible for the IFT of cargo. Specifically, the kinesin II motor complex, together with the kinesin motor protein osm-3 moves along microtubules and is required for anterograde IFT along the middle segment of the sensory neuron cilia. In particular, the kinesin II motor complex delivers specific ciliary cargo proteins such as che-3 which are related to motility to ciliary tips. This is likely mediated by IFT complexes A and B.
Subcellular location: Cell projection, cilium {ECO:0000269|PubMed:28479320}. Cytoplasm, cytoskeleton {ECO:0000305}. Note=In particular, localizes to the base and transition zone of cilia. {ECO:0000269|PubMed:28479320}.
Interaction partners:
- Kinesin-associated protein
- Kinesin-like protein
- Kinesin motor domain-containing protein
- Tetratricopeptide repeat protein 30 homolog
- Intraflagellar transport protein 52 C-terminal domain-containing protein
- Intraflagellar transport protein 88 homolog
- Tetratricopeptide repeat protein 21 homolog
- WD repeat-containing protein dyf-2
- Intraflagellar transport protein 122 homolog
- Intraflagellar transport protein 56 homolog
Sequence:
MEGAEKVKVVVRCRPISTTEKLQGHKIAVTCNDEEKAVNIKSLSQEDPPRTFYFDAVFSPNTDQMTVYNVAARPIVENVLKGYNGTIFAYGQTGTGKTFTMAGDLEPVEMRGIIPNSFAHIFDHIAKCQHDTTFLVRVSYLEIYNEEIRDLLSKDHNGNLEIKERPDVGVYVRNLSNPTVENASKMQALMEFGSKNRKVGATAMNLESSRSHAMFTVTIESCRNGLVTQGKLQLVDLAGSERQSKTGAQGERLKEAAKINLSLSTLGNVISSLVDGKSTHIPYRNSKLTRLLQDSLGGNSKTVMIANVGPATYNYDETLSTLRYANRAKNIQNVAKINEDPKDAQLRKFQLEIEALRKILDEENPGDDENQEEAWEAKMQEREVEMEKKRKILEERVNSAVNDEETHRLVKEMMENEAELKKARSEHEKLRSKLEKIEKKLIVGGENLLEKVEEQAKLLEVNNKELEQSKFQEAHLRTQLEERTAVKVEIEERYSSLQEEAFVKSKKIKKVSNELKDARAELKDLEEDHQRQVEAMLDDIRQLRKELLLNIAIIDEYIPVEHVELIEKYVSWSEEHGDWQLKAIAYTGNNMRASAPPAKKEFSNNNQTVPMYYSYRADLGASTAEHRPRTSSKKHRASIRLQQLLT
Protein: Uncharacterized protein C19orf44 (Q9H6X5)
Organism: Homo sapiens (Human)
Interaction partners:
- Proline and serine-rich protein 3
Sequence:
MASARKASRPMRDVFGDFSDVSLEDSTMEEIRNFQISRNLTKIAPGHSRFLKRNQTLDEKHLLLKENPVLGSGPRLASCRPPTTASRIRANAALMKLAQLETRIMNRKLQRNLSDTESDSMTADAGLPKRADRILSGGALELASQNTDKTSQNQARELPVTENNAQNAKVSRFLKKKQAPVENISPEAPAGKERTLQTPKQKEPARTFDSPDSDEEEMKVLLGSLMDSSREKNTNQGFSSANVSEEEERKLFSVPSQLRAFTVPSVELSSAKPSQTSHLPTSLAADRTLHSTRSRADYPQSHVSSDTASHTPSVSITGAFSNSVSLKMGHVKLVSSPGRSEAETVDEPVSEGADDSLDEFRINILSLDGLAPAVSENSDLEQEEESAQRQKTAGKIFRAEASTGQDAPRQAQARSWASQGKAASAEGDESEVSEHLSASSASAIQQDSTSSMQPPSEAPMVNTVSSAYSEDFENSPSLTASEPTAHSKESLDRTLDALSESSSSVKTDLPQTAESRKKSGRHVTRVLVKDTAVQTPDPAFTYEWTKVASMAAMGPALGGAYVDPTPIANHVISADAIEALTAYSPAVLALHDVLKQQLSLTQQFIQASRHLHASLLRSLDADSFHYHTLEEAKEYIRCHRPAPLTMEDALEEVNKEL
Protein: Serine/threonine-protein kinase greatwall (GW) (GWL) (EC 2.7.11.1) (Microtubule-associated serine/threonine-protein kinase-like) (MAST-L) (Q6NTJ3)
Organism: Xenopus laevis (African clawed frog)
Function: Serine/threonine kinase that plays a key role in M phase by acting as a regulator of mitosis entry and maintenance. Acts by promoting the inactivation of protein phosphatase 2A (PP2A) during M phase: does not directly inhibit PP2A but acts by mediating phosphorylation and subsequent activation of arpp19 and ensa at 'Ser-67', 2 phosphatase inhibitors that specifically inhibit the ppp2r2d (PR55-delta) subunit of PP2A. Inactivation of PP2A during M phase is essential to keep cyclin-B1-CDK1 activity high. Following DNA damage, it is also involved in checkpoint recovery by being inhibited.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Nucleus. Note=During interphase is mainly nuclear, upon nuclear envelope breakdown localizes at the cytoplasm and during mitosis at the centrosomes. {ECO:0000250}.
Interaction partners:
Sequence:
MGIVAETSQNGDTSLCSEKKFTVPQPPSIEEFGIVKPISRGAFGKVYLARRKNNSKLFAVKVVKKADMINKNMVQQVQAERDALALSKSPFIVHLYYSLQSANNIYLVMEYLIGGDVKSLLHIYGYFDEEMAVKYISEVAMALDYLHRHGIIHRDLKPDNMLISNKGHIKLTDFGLSKVTLKRELCMMDILTTPSMAKPKRDYSRTPGQVLSLISSLGFNTPAGGRTQGSLNQQTEGMRGNASTPLLMKKRESLVKGNKLMISCPEASLSSPSIPVKCLTPNLLKCRTQFATSSTSSQSRICLSSLESECGSPRWENCSQDAEAPPYFNSSRVKDSSSEQARSKKPTGSSASQNLKRLEFAFSPIVDRRTGKKAGFQDETGELSDTPLATLNAKGVIRKCLYENKAQEKPKDFDKTGQGELGKFTSSPDSPPWLANGSVAPIQFNDEEKTEKMGVKRNYDLVEKSPEQELLQDKKTNTDYKRGCAITDYPVSQSTGLTMEINSLFLSELRNSANKYASDRKSEDKYISAPRTLEKLDSGNPVAKNLLCELDDNCERDGEVSSTSEGEDRKERLNQDSSSTGMSVTENQIDRDLSHVDKSIKELSFEESQSENSEEITPDNKGIPFMAENDERVQSKYEPNTSILPDSLQNVLASPAPASAMTNPRRKPMVAFRSYNSPINVSNVSEPSKISMNSADKIHFSLECTGSFPMAVTPAQNKVQGLIETPYRTPKSVRRGGIQVDHERILGTPDYLAPELLLRKSHGPAVDWWALGVCLFEFLTGIPPFNDETPSQVFQNILNRDIPWPEEEEEVLSVNAQSAIEILLTIDPTKRAGLKDLKAHPLFHGMEWEELQYQPMSFIPQPDDETDTTYFEARNNAQHLKVSGFSL
Protein: Dual specificity protein phosphatase 1 (EC 3.1.3.16) (EC 3.1.3.48) (Mitogen-activated protein kinase phosphatase 1) (MAP kinase phosphatase 1) (MKP-1) (Protein-tyrosine phosphatase 3CH134) (Protein-tyrosine phosphatase ERP) (P28563)
Organism: Mus musculus (Mouse)
Function: Dual specificity phosphatase that dephosphorylates MAP kinase MAPK1/ERK2 on both 'Thr-183' and 'Tyr-185', regulating its activity during the meiotic cell cycle.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q91790}.
Interaction partners:
- Mitogen-activated protein kinase 14
- Mitogen-activated protein kinase 3
- Stress-activated protein kinase JNK
- Mitogen-activated protein kinase 1
- Mitogen-activated protein kinase 11
- Mitogen-activated protein kinase 9
- Mitogen-activated protein kinase 10
- Mitogen-activated protein kinase 12
- Mitogen-activated protein kinase 13
- Protein c-Fos
Sequence:
MVMEVGILDAGGLRALLREGAAQCLLLDCRSFFAFNAGHIAGSVNVRFSTIVRRRAKGAMGLEHIVPNAELRGRLLAGAYHAVVLLDERSASLDGAKRDGTLALAAGALCREARSTQVFFLQGGYEAFSASCPELCSKQSTPTGLSLPLSTSVPDSAESGCSSCSTPLYDQGGPVEILSFLYLGSAYHASRKDMLDALGITALINVSANCPNHFEGHYQYKSIPVEDNHKADISSWFNEAIDFIDSIKDAGGRVFVHCQAGISRSATICLAYLMRTNRVKLDEAFEFVKQRRSIISPNFSFMGQLLQFESQVLAPHCSAEAGSPAMAVLDRGTSTTTVFNFPVSIPVHPTNSALNYLKSPITTSPSC
Protein: aromatase (EC 1.14.14.14) (Cytochrome P-450AROM) (Estrogen synthase) (H0Z9H2)
Organism: Taeniopygia guttata (Zebra finch) (Poephila guttata)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
Sequence:
MVLETLNPLHYNITSLVPDTMPVATVPILILMCFLFLIWNHEETSSIPGPGYCMGIGPLISHGRFLWMGVGNACNYYNKTYGDFVRVWISGEETFIISKSSSVSHVMKHWHYVSRFGSKLGLQCIGMYENGIIFNNNPAHWKEIRPFFTKALSGPGLVRMIAICVESTTEHLDRLQEVTTELGNINALNLMRRIMLDTSNKLFLGVPLDENAIVLKIQNYFDAWQALLLKPDIFFKISWLCKKYKDAVKDLKGAMEILIEQKRQKLSTVEKLDEHMDFASQLIFAQNRGDLTAENVNQCVLEMMIAAPDTLSVTLFFMLILIAEHPTVEEEMMREIETVVGDRDIQSDDMPNLKIVENFIYESMRYQPVVDLIMRKALQDDVIDGYPVKKGTNIILNIGRMHKLEFFPKPNEFSLENFEKNVPSRYFQPFGFGPRSCVGKFIAMVMMKAILVTLLRRCRVQTMKGRGLNNIQKNNDLSMHPIERQPLLEMVFTPRRNENENQGDGMDQH
Protein: Uncharacterized transporter YMR279C (Q03263)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Membrane; Multi-pass membrane protein.
Interaction partners:
- Azole resistance protein 1
- Protein SGE1
- Vacuolar basic amino acid transporter 5
- Vacuolar basic amino acid transporter 3
- Vacuolar basic amino acid transporter 1
Sequence:
MFSIFKKKTSVQGTDSEIDEKITVKAKDKVVVSTEDEEVTTIVSSTKSTQVTNDSPWQDPTYFSSFGKELMFIATCMLAQLLNQAGQTHALCIMNVLSKSFNSEANNQAWLMASFPLAAGSFILISGRLGDIYGLKKMLIVGYVIVIVWSIISGLSKYSNSDAFFITSRAFQGVGIAFILPNIMGLVGHVYKVGSFRKNIVISFIGACAPTGGMFGGLFGGLIVTEDPNQWPWVFYAFGIATFLSLLMAWYSIPNNVPTNIHGLSMDWTGSALAIIGLILFNFVWNQAPIVGWDKPYIIVLLIISVIFLVAFFVYESKYAEVPLLPRAMTKNRHMIMILLAVFLGWGSFGIWTFYYVSFQLNLRHYSPVWTGGTYFVFVIFGSMAAFFVAFSIKRLGPALLLCFSLMAFDAGSIMFSVLPVEQSYWKLNFAMQAILCFGMDLSFPASSIILSDGLPMQYQGMAGSLVNTVINYSASLCLGMGGTVEHQINKSGNDLLKGYRAAVYLGVGLASLGVVISVTYMLENLWNRHRKSEDRSLEA
Protein: Arginase 1, mitochondrial (EC 3.5.3.1) (Agmatinase ARGAH1) (EC 3.5.3.11) (Arginine amidohydrolase 1) (AtARGAH1) (P46637)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the hydrolysis of L-arginine to urea and L-ornithine (Probable). The latter can be utilized in the urea cycle or as a precursor for the synthesis of both polyamines and proline (Probable). Possesses agmatinase activity. Catalyzes the formation of putrescine from agmatine.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:18567826, ECO:0000305|PubMed:25732537}.
Interaction partners:
- Ornithine aminotransferase, mitochondrial
- Arginine decarboxylase 1, chloroplastic
- Ornithine transcarbamylase, chloroplastic
- Arginine decarboxylase 2
- Argininosuccinate lyase, chloroplastic
- Arginine biosynthesis bifunctional protein ArgJ
- Acetylornithine deacetylase
- Urease
- At1g44820
- Aminoacylase, putative
Sequence:
MSRIIGRKGINYIHRLNSASFTSVSASSIEKGQNRVIDASLTLIRERAKLKGELVRLLGGAKASTSLLGVPLGHNSSFLQGPAFAPPRIREAIWCGSTNSATEEGKELKDPRVLTDVGDVPVQEIRDCGVDDDRLMNVISESVKLVMEEEPLRPLVLGGDHSISYPVVRAVSEKLGGPVDILHLDAHPDIYDCFEGNKYSHASSFARIMEGGYARRLLQVGIRSINQEGREQGKRFGVEQYEMRTFSKDRPMLENLKLGEGVKGVYISIDVDCLDPAFAPGVSHIEPGGLSFRDVLNILHNLQADVVGADVVEFNPQRDTVDGMTAMVAAKLVRELAAKISK
Protein: Dystrophin (F1QDK4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Utrophin
- Actin alpha 1, skeletal muscle b.
- Uncharacterized protein.
- Nebulin.
- Dystroglycan 1
- Delta-sarcoglycan)
- Dysferlin
- Syntrophin alpha 1.
- Alpha-sarcoglycan
- Beta-1-syntrophin
Sequence:
MRENLRNHQTQTTCWDHPKMAELYQSLADLNNVRFSAYRTAMKLRRMQKALCLDLLSMPAACEAFEQHNLKQNEQFMDIVQVINCLTSIYDRLEQQHSSLVNVPLCVDMCLNWLLNVYDTGRAGKIRTLSFKTGIISLCKAHLEDKYRFLFREVASATGFCDQRRLGLLLHDAIQIPRQLGEVASFGGSNIEPSVRSCFQFANNKPELEASVFLDWMRLEPQSMVWLPVLHRVAAAETAKHQAKCNICKECPIIGFRYRSLKHFNYDICQSCFFSGRVAKGHKMQYPMVEYCTPTTSGEDVRDFAKVLKNKFRTKRYFAKHPRMGYLPVQTILEGDNMETPASSPQLSHDDTHSRIEHYASRLAEMENRNGSYVNDNVSPNESMDDEHLLIQHYCQSLNQGSPLSQPQSPAQILISMETEEKGELERVLNDLEQENRKLQAEYDRLKKAHDHKGLSPLPSPPQMLPVSPQSPRDAELIAEAKLLRQHKGRLEARMQILEDHNKQLESQLTRLRQLLEQTESKVNGTALSSPSTASPRSDTSLASLRVAASQTTETMGDDELSSPTQDASTGLEDVIEQLNNSFPHSQGGGRLNP
Protein: Type IV secretion system protein VirB10 (Q2GIA5)
Organism: Anaplasma phagocytophilum (strain HZ)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
- Type IV secretion system protein VirB9
- Type IV secretion protein VirB8-1
- Type IV secretion system protein VirB9-2
- Type IV secretion system protein VirD4
- Type IV secretion system protein
- Type IV secretion system protein virB4
- Type IV secretion system protein VirB3
- Type IV secretion system protein VirB4-2
- Type IV secretion system protein VirB6 family
- Type IV secretion system protein VirB8-2
Sequence:
MADEIRGSSSGENIEDNVNVVGVAKSKKLFVIIVVLIATGLMYYFFFFNKESSDNEEDTQIPRVIEEKEVEKLRKDAGRPAQETAPRILTPPPRLPELPPLVMPTVPDIPVVTKLLKPPVEEEFVEEYNVQEVPSPMGNIAPPEREEISLPLPYKTITTEQPSFLGYDKEKRGAPMIAFGGGGGEAAGSESGDGSVGGKEDARFTAWQGLEGTQSPSVRATRVGDTRYIILQGHMIDAVLETAINSDISGVLRAVVSRDVYASSGDAVVIPKGSRLIGSYFFDSAGNNVRVDVNWSRVILPHGVDIQIASSGTDELGRNGISGVVDNKVGSILTSTIFLAGISLGTAYVTEQIPSLRTETVKVETPADGKDGKKTTSSSLSTKIVSDAIKDFSDSMKEIVNKYSNRTPTVYVDQGTVMKVFVNQDVVFPRDAVR
Protein: At1g27330 (Ribosome associated membrane protein RAMP4) (Q84K46)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004389}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004389}.
Interaction partners:
- T29M8.11
- F-box/kelch-repeat protein At3g06240
- Large ribosomal subunit protein uL1c
- AT4g14420/dl3250c
- Membrane protein of ER body 1
- Protein disulfide-isomerase like 2-1
- Probable pectinesterase/pectinesterase inhibitor 58
- Glycoprotein membrane GPI-anchored
- S-protein homolog 12
- F-box protein At1g19070
Sequence:
MTTSKRLADRKIEKFDKNILKRGFVPETTTKKGKDYPVGPILLGFFVFVVIGSSLFQIIRTATSGGMA
Protein: Heparan-sulfate 6-O-sulfotransferase 2 (HS6ST-2) (EC 2.8.2.-) (Q96MM7)
Organism: Homo sapiens (Human)
Function: 6-O-sulfation enzyme which catalyzes the transfer of sulfate from 3'-phosphoadenosine 5'-phosphosulfate (PAPS) to position 6 of the N-sulfoglucosamine residue (GlcNS) of heparan sulfate.
Subcellular location: Membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
- Glypican-3
- Heparan sulfate 2-O-sulfotransferase 1
Sequence:
MALPACAVREFEPPRQPERGAPVRTTCPRRHSRVEAELAASRPGSVAASVRAGPPRGVSHGFHTRPLLDKPRKASSSLAGAACAPLFALLSRGRRRRMHVLRRRWDLGSLCRALLTRGLAALGHSLKHVLGAIFSKIFGPMASVGNMDEKSNKLLLALVMLFLFAVIVLQYVCPGTECQLLRLQAFSSPVPDPYRSEDESSARFVPRYNFTRGDLLRKVDFDIKGDDLIVFLHIQKTGGTTFGRHLVRNIQLEQPCECRVGQKKCTCHRPGKRETWLFSRFSTGWSCGLHADWTELTSCVPSVVDGKRDARLRPSRNFHYITILRDPVSRYLSEWRHVQRGATWKASLHVCDGRPPTSEELPSCYTGDDWSGCPLKEFMDCPYNLANNRQVRMLSDLTLVGCYNLSVMPEKQRNKVLLESAKSNLKHMAFFGLTEFQRKTQYLFEKTFNMNFISPFTQYNTTRASSVEINEEIQKRIEGLNFLDMELYSYAKDLFLQRYQFMRQKEHQEARRKRQEQRKFLKGRLLQTHFQSQGQGQSQNPNQNQSQNPNPNANQNLTQNLMQNLTQSLSQKENRESPKQNSGKEQNDNTSNGTNDYIGSVEKWR
Protein: Rubredoxin-2 (Rd-2) (Q93PP8)
Organism: Desulfovibrio desulfuricans (strain ATCC 27774 / DSM 6949 / MB)
Function: Rubredoxin is a small nonheme, iron protein lacking acid-labile sulfide. Its single Fe, chelated to 4 Cys, functions as an electron acceptor and may also stabilize the conformation of the molecule.
Interaction partners:
- Nitrogen fixation protein NifU
- BFD domain protein
- Ferric uptake regulator, Fur family
- Bacterioferritin
Sequence:
MAEPQDMWRCQMVNCGYVYDPDRGDKRRKVPAGTKFEDLPEDWRCPVCGAGKKSFRRLSDEA