wanglab/gogpt-training-data huggingface dataset:
Protein: Ephrin type-B receptor 4 (EC 2.7.10.1) (Developmental kinase 2) (mDK-2) (Hepatoma transmembrane kinase) (Tyrosine kinase MYK-1) (P54761)
Organism: Mus musculus (Mouse)
Function: Receptor tyrosine kinase which binds promiscuously transmembrane ephrin-B family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Together with its cognate ligand/functional ligand EFNB2 it is involved in the regulation of cell adhesion and migration, and plays a central role in heart morphogenesis, angiogenesis and blood vessel remodeling and permeability. EPHB4-mediated forward signaling controls cellular repulsion and segregation from EFNB2-expressing cells.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P54760}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P54760}.
Interaction partners:
- Ephrin-B2
- Ephrin-B1
- Ephrin-B3
- Tyrosine-protein kinase ABL1
- Ras GTPase-activating protein 1
- Ephexin-1
- Ephrin-A1
- Ephrin-A2
- Ephrin-A5
- Ephrin-A4
Sequence:
MELRALLCWASLATALEETLLNTKLETADLKWVTYPQAEGQWEELSGLDEEQHSVRTYEVCDMKRPGGQAHWLRTGWVPRRGAVHVYATIRFTMMECLSLPRASRSCKETFTVFYYESEADTATAHTPAWMENPYIKVDTVAAEHLTRKRPGAEATGKVNIKTLRLGPLSKAGFYLAFQDQGACMALLSLHLFYKKCSWLITNLTYFPETVPRELVVPVAGSCVANAVPTANPSPSLYCREDGQWAEQQVTGCSCAPGYEAAESNKVCRACGQGTFKPQIGDESCLPCPANSHSNNIGSPVCLCRIGYYRARSDPRSSPCTTPPSAPRSVVHHLNGSTLRLEWSAPLESGGREDLTYAVRCRECRPGGSCLPCGGDMTFDPGPRDLVEPWVAIRGLRPDVTYTFEVAALNGVSTLATGPPPFEPVNVTTDREVPPAVSDIRVTRSSPSSLILSWAIPRAPSGAVLDYEVKYHEKGAEGPSSVRFLKTSENRAELRGLKRGASYLVQVRARSEAGYGPFGQEHHSQTQLDESESWREQLALIAGTAVVGVVLVLVVVIIAVLCLRKQSNGREVEYSDKHGQYLIGHGTKVYIDPFTYEDPNEAVREFAKEIDVSYVKIEEVIGAGEFGEVCRGRLKAPGKKESCVAIKTLKGGYTERQRREFLSEASIMGQFEHPNIIRLEGVVTNSVPVMILTEFMENGALDSFLRLNDGQFTVIQLVGMLRGIASGMRYLAEMSYVHRDLAARNILVNSNLVCKVSDFGLSRFLEENSSDPTYTSSLGGKIPIRWTAPEAIAFRKFTSASDAWSYGIVMWEVMSFGERPYWDMSNQDVINAIEQDYRLPPPPDCPTSLHQLMLDCWQKDRNARPRFPQVVSALDKMIRNPASLKIVARENGGASHPLLDQRQPHYSAFGSVGEWLRAIKMGRYEESFAAAGFGSFEVVSQISAEDLLRIGVTLAGHQKKILASVQHMKSQAKPGAPGGTGGPAQQF
Protein: Cell death abnormality protein 8 (O17386)
Organism: Caenorhabditis elegans
Function: Phospholipid scramblase that acts downstream of ced-9 and caspase ced-3 to promote phosphatidylserine exposure on apoptotic cell surface. Phosphatidylserine is a specific marker only present at the surface of apoptotic cells and acts as a specific signal for engulfment. Regulates apoptosis kinetics during embryonic development. Not required for engulfment of germ cell corpses.
Subcellular location: Cell membrane {ECO:0000269|PubMed:10882128, ECO:0000269|PubMed:24225442}; Multi-pass membrane protein {ECO:0000269|PubMed:10882128}.
Interaction partners:
- Cell death protein 3
- Phospholipid scramblase
- ABC transporter ced-7
- Cell death protein 6
- Anoctamin
- Apoptosis regulator ced-9
- CED-5
- Cell death abnormality protein 1
- Cell death abnormality protein 12
- Cell death abnormality protein 2
Sequence:
MFLKKHKSKLLLVPRDEEQEDAGIVAVLTDRIPSVLLVRWFDLFCFGFAMCSYALDFFSDIGIAIFHFWAGRYLSGSLVLAFALLPSVIINIISMVWMLDDEMHWKRRAHPRRTGTFELNQKRFIPLSKMIVLCICQMGPLFWYYKALYYGWMFRKSSNENTDGEKRKCFSKMVEAERDATLLRFFEAFLESAPQLIIQGSIAASYFQNYYQTGTYPYWLYFQAASLLLSIISISWSVVVQNRSLRMIRDDKVNIWPHEAVLQFCWRFLTILARIITLVALVLIFGINVVPLISVHLLVTLVHVIFLQAIHIDACTHIEKLLLLINTFIHIFIPFNMVEGNTRWRYLTAYSVEFIEMMLVCWLLPLSLNTFPYIEKVQVGVPISFIAGIAIMMMYYQFFHPNRRQLIVTQSQEDLSLNVQKSVETLTPKLESSLEISGEQNTSQDLVSELLLDVEHEN
Protein: GH07821p (Mitochondrial ribosomal protein S22) (Q9VAY9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Small ribosomal subunit protein mS40
- Small ribosomal subunit protein bS16m
- Small ribosomal subunit protein mS29
- Mitochondrial ribosomal protein S34
- Small ribosomal subunit protein mS26
- LD06441p
- Small ribosomal subunit protein mS39
- Small ribosomal subunit protein uS10m
- Mitochondrial ribosomal protein S11
- Small ribosomal subunit protein uS9m
Sequence:
MHLLRSLRQLNGLQGVRQAIRQVSSAPTKPAALQYERDPQPLFTDAETQRLLQSMTQLNLDKVYRKRTVPDNSSETKFMSNEQLDNEFQNLVVRAQQILQMPPIVQIKKDVERVIAKDTALKDFANSKFVFTDITFGRRQSERKVIVRDMDGTLAYATLDTTKRMNQLYFPLEGRQSYTPRMFALEELLAKCLAEHKYEFILDRLLVQYEPHEPEFHNISARVFEHLNESKEFDLLRSTRHFGPMAFFYAWHRCIDDLLYDMIRRDYLHNAVELIALSYKLHNIPVEYQATLTELGKLHATPAESALAELRSVFRRHDNKQNIEQEIHTAIGKTEHDFAADEISLKFIEQYIASEHALKKVQLELAVQTLKEVNREKLMLFQGLKKAHGVQAS
Protein: Histidine rich calcium binding protein (G3V8S6)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Triadin
- Sarcoplasmic/endoplasmic reticulum calcium ATPase 2
- Calcium-transporting ATPase
- Sarcoplasmic/endoplasmic reticulum calcium ATPase 3
- Creatine kinase S-type
Sequence:
MGFQEPWLYSCLLWATVAILLVPPVVTQELRGTGLGLGNWNNNAGIPGSSEDLSTEYGHHIHSHGAYQGEKDRHHREEDEDFSREYGHQVQDHRYPGHEVGEENVSEEVFRGHVRQLHGHHKPNSEDLGDSAESHFPRQQSHNREEEDGVVSGEDHRHIPRHDHHGNEEEDDDGEEEERVGVMENSDDKHQAHGHHSHSKERDGLHHAHSHRHQGHHDEDDDDEDGVSTEGEHQAHRYQDHDEEDDDDSDEESHAHRLQGQEDENDDEDGDSSENGHQTQDHQGHKEQDDDDDEEEEEEEEEEEEEEEEEEEEEEDDDDDSTEHRHRHQTQGHRKGKDEDESDEDDHVTRHGRRGHEDEDDDDDDDDDDDDDNDGGSTENVHQAHRHRGHEHEDDGDDSEEDYHHVPSHGHQSHQNEEEEDEAVSTEHWHQSPRHAHHDLGRENQEEATVKYSRHVASHRPQGHSAEEDSLEDSTNEVPGHHHHRVSRDGDEDISTEFGHKAPRHRLQDQDEWTRQGHGKSVQEDIGHQPLQPTGPGSGESRKEDDHSSQEGDEDLKQRQEAHSEEEEEEEEGHGLPMSLEDEEEEEKDKKESKGDRAAVSAPLSHHRKHDDDDDGDGDDDDDDNDDDDEILEENLLPFTIIPNPLAGREVAREGSSEEESREVTGQQDAQEYENYQPGSLCGYCSFCNRCSECESCHCDEENMGEHCDQCQHCQFCYLCPLVCDTLCTPGSYVDYFSSSVYQAVADMLETQEP
Protein: Large ribosomal subunit protein eL37A (60S ribosomal protein L37-A) (SP-L27) (P59289)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Binds to the 23S rRNA.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Elongation factor 3
- mRNA export factor elf1
- Small ribosomal subunit protein eS21
- Large ribosomal subunit protein uL24
- Small ribosomal subunit protein uS10
- Large ribosomal subunit protein eL29
- Large ribosomal subunit protein eL31
- Large ribosomal subunit protein eL14
- Large ribosomal subunit protein eL39
- Small ribosomal subunit protein uS14
Sequence:
MTKGTQSFGMRHNKSHTICRRCGKRSFHIQKSTCACCGYPAAKTRSYNWGAKAKRRRTTGTGRMSYLKKVHRSFKNGFRAGKPTSAATA
Protein: RNA polymerase II subunit A C-terminal domain phosphatase SSU72 (CTD phosphatase SSU72) (EC 3.1.3.16) (M9PHZ3)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU369031}.
Interaction partners:
Sequence:
MTDPSKLAVAVVCSSNMNRSMEAHNFLAKKGFNVRSYGTGERVKLPGMAFDKPNVYEFGTKYEDIYRDLESKDKDYTQNGLLHMLDRNRRIKKCPERFQDTKEQFDIIVTVEERVYDLVVMHMESMESVDNRPVHVLNVDVVDNAEDALMGAFVITDMINMMAKSTDLDNDIDELIQEFEERRKRVILHSVLFY
Protein: Mitochondrial import inner membrane translocase subunit TIM50 (M0R047)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|RuleBase:RU365079}; Single-pass membrane protein {ECO:0000256|RuleBase:RU365079}.
Interaction partners:
Sequence:
XQVILEQEGPGTLESQSGRGSYFLCGVGGGEAAEIGSRGSTKAQGPQQQPGSEGPSYAKKVALWLAGLLGAGGTVSVVYIFGNNPVDENGAKIPDEFDNDPILVQQLRRTYKYFKDYRQMIIEPTSPCLLPDPLQEPYYQPPYTLVLELTGVLLHPEWSLATGWRFKKRPGIETLFQQLAPLYEIVIFTSETGMTAFPLIDSVDPHGFISYRLFRDATRYMDGHHVK
Protein: Transmembrane protein 250 (Herpes virus UL25-binding protein) (H0YL14)
Organism: Homo sapiens (Human)
Function: May play a role in cell proliferation by promoting progression into S phase.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Nucleus {ECO:0000269|PubMed:21667337}. Cytoplasm {ECO:0000269|PubMed:21667337}. Note=Upon HHV-1 infection, accumulates arround the nuclear membrane and translocates into the nucleus.
Interaction partners:
- Septin-1
- Uncharacterized protein C17orf47
- Septin-2
- Septin-7
- Septin-5
Sequence:
MPVMPIPRRVRSFHGPHTTCLHAACGPVRASHLARTKYNNFDVYIKTRWLYGFIRFLLYFSCSLFTAALWGALAALFCLQYLGVRVLLRFQRKLSVLLLLLGRRRVDFRLVNELLVYGIHVTMLLVGGLGWCFMVFVDM
Protein: histone acetyltransferase (EC 2.3.1.48) (Q38AD3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- RuvB-like helicase
- Histone H4
- Histone H4
- Histone H3 variant
- Histone H3, putative
- Histone H2A
- Transmembrane protein, conserved
- Bromo domain-containing protein
- Bromo domain-containing protein
- non-specific serine/threonine protein kinase
Sequence:
MKRQRSGDTVIKTLFREYQAHSVTGFVQQAIKDTEKIFLCEACLSQFSSLPDLIKHAEICTYRYWIPGDEIYRCDERKCVIMEIDGRKAVCSSFTRRIAYLSKFFLDEKTTLDDLHFFAFIVIFELDDYGYHFAGYFSKEWRKTLSCTNTLSCLMVLPPYRSKGYGSLLVELSYEMAKIEGIAGTPERPLSTGGKRIFSRIWREELLRAMFAIHKERLPLTLRTISSKSAINIEDTALALHHLGVVFSAPDGTTFITVPQSAINESEKTKRLNNKLLLWVPLS
Protein: 5'-3' exoribonuclease 2 (EC 3.1.13.-) (Protein Dhm1) (Q9DBR1)
Organism: Mus musculus (Mouse)
Function: Possesses 5'->3' exoribonuclease activity. May promote the termination of transcription by RNA polymerase II. During transcription termination, cleavage at the polyadenylation site liberates a 5' fragment which is subsequently processed to form the mature mRNA and a 3' fragment which remains attached to the elongating polymerase. The processive degradation of this 3' fragment by this protein may promote termination of transcription. Binds to RNA polymerase II (RNAp II) transcription termination R-loops formed by G-rich pause sites (By similarity).
Subcellular location: Nucleus, nucleolus {ECO:0000250|UniProtKB:Q9H0D6}.
Interaction partners:
- Decapping and exoribonuclease protein
- 5'-3' exoribonuclease 1
- Probable helicase senataxin
- Regulation of nuclear pre-mRNA domain-containing protein 1A
- Exosome complex component 10
- CDKN2A-interacting protein
- Pre-mRNA-processing factor 40 homolog A
- Regulation of nuclear pre-mRNA domain-containing protein 1B
- Fas-binding factor 1
- Regulator of nonsense transcripts 1
Sequence:
MGVPAFFRWLSRKYPSIIVNCVEEKPKECNGVKIPVDASKPNPNDVEFDNLYLDMNGIIHPCTHPEDKPAPKNEDEMMVAIFEYIDRLFNIVRPRRLLYMAIDGVAPRAKMNQQRSRRFRASKEGMEAAVEKQRVREEILAKGGFLPPEEIKERFDSNCITPGTEFMDNLAKCLRYYIADRLNNDPGWKNLTVILSDASAPGEGEHKIMDYIRRQRAQPNHDPNTHHCLCGADADLIMLGLATHEPNFTIIREEFKPNKPKPCALCNQFGHEVKDCEGLPREKKGKHDELADSLPCAEGEFIFLRLNVLREYLERELTMASLPFPFDVERSIDDWVFMCFFVGNDFLPHLPSLEIREGAIDRLVNIYKNVVHKTGGYLTESGYVNLQRVQMIMLAVGEVEDSIFKKRKDDEDSFRRRQKEKRKRMKRDQPAFTPSGILTPHALGSRNSPGCQVASNPRQAAYEMRMQRNSSPSISPNTSFASDGSPSPLGGIKRKAEDSDSEPEPEDNVRLWEAGWKQRYYKNKFDVDAADEKFRRKVVQSYVEGLCWVLRYYYQGCASWKWYYPFHYAPFASDFEGIADMSSEFEKGTKPFKPLEQLMGVFPAASGNFLPPTWRKLMSDPDSSIIDFYPEDFAIDLNGKKYAWQGVALLPFVDERRLRAALEEVYPDLTPEENRRNSLGGDVLFVGKLHPLRDFILELYQTGSTEPVDVPPELCHGIQGTFSLDEEAILPDQTVCSPVPMLRDLTQNTAVSINFKDPQFAEDYVFKAAMLPGARKPATVLKPGDWEKSSNGRQWKPQLGFNRDRRPVHLDQAAFRTLGHVTPRGSGTSVYTNTALPPANYQGNNYRPLLRGQAQIPKLMSNMRPQDSWRGPPPLFQQHRFERSVGAEPLLPWNRMIQNQNAAFQPNQYQMLGGPGGYPPRRDDHRGGRQGYPREGRKYPLPPPSGRYSWN
Protein: GDP-D-glycero-alpha-D-manno-heptose dehydrogenase (EC 1.1.98.-) (Q0P8I7)
Organism: Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168)
Function: NAD-dependent dehydrogenase involved in the biosynthesis of heptose moieties with a hydroxyl group at C6 found on the capsular polysaccharide (CPS) of C.jejuni. Catalyzes the initial oxidation of C4 of the GDP-D-glycero-alpha-D-manno-heptose to form GDP-D-glycero-4-keto-alpha-D-lyxo-heptose in the presence of alpha-ketoglutarate required to recycle the NADH nucleotide.
Interaction partners:
- dTDP-4-dehydrorhamnose 3,5-epimerase
- D-glycero-alpha-D-manno-heptose 7-phosphate kinase
- Methyltransferase family protein
- Small ribosomal subunit protein uS3
- Small ribosomal subunit protein uS19
- Small ribosomal subunit protein uS17
- Small ribosomal subunit protein uS8
- Small ribosomal subunit protein uS14
- Small ribosomal subunit protein uS12
- Small ribosomal subunit protein uS5
Sequence:
MSKKVLITGGAGYIGSVLTPILLEKGYEVCVIDNLMFDQISLLSCFHNKNFTFINGDAMDENLIRQEVAKADIIIPLAALVGAPLCKRNPKLAKMINYEAVKMISDFASPSQIFIYPNTNSGYGIGEKDAMCTEESPLRPISEYGIDKVHAEQYLLDKGNCVTFRLATVFGISPRMRLDLLVNDFTYRAYRDKFIVLFEEHFRRNYIHVRDVVKGFIHGIENYDKMKGQAYNMGLSSANLTKRQLAETIKKYIPDFYIHSANIGEDPDKRDYLVSNTKLEATGWKPDNTLEDGIKELLRAFKMMKVNRFANFN
Protein: TPR repeat-containing thioredoxin TTL1 (Tetratricopeptide repeat thioredoxin-like 1) (Q9MAH1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in responses to osmotic stress and abscisic acid (ABA). May act as a positive regulator of ABA signaling during germination and seedling development under stress.
Interaction partners:
- Chromatin structure-remodeling complex protein SYD
- Endoplasmin homolog
- At5g58530
- SH3 domain-containing protein
- Heat shock protein 90-4
- Heat shock protein 90-1
- Heat shock protein 90-6, mitochondrial
- Heat shock protein 90-2
- Heat shock protein 90-5, chloroplastic
- Heat shock protein 90-3
Sequence:
MPKSVKPISESDKLSDHLRDSSLTSEINKPDFRELDLGSPVSPLRSQPRGLTTTTTTTTTSSSSSSSSGSVTGRIKHAPVIGRSNSVRSQSNSSSGNNNLRPRSDSATTSSSSHSQPLLSSSSSSATSPAPTSPANVLPTGNICPSGKIQITGMTQSRSRSDVLGSGTGTYGHGSIMRGGGISPAKPTNTGGGSNSPVNVGSSSRSSSTVATGETPIWKKAILGSDSEEVKRVGNEMYRKGLFNEALKLYDRAIALSPTNAAYRSNRAAALIGLSRIGEAVKECEDAVRSDPNYGRAHHRLALLLIRLGQVNSARKHLCFLGRPSDPMELQKLEAVEKHLIKCVDARRVTDWKTVLIEADAAIVSGADFSPQLFMCKVEAFLKLHRLDDAQSKLLEVPKVEPFPVSCSQTRFSGMACEAYIYFVKAQIEMALGRFENAVMAAEKASQIDPRCNEVAMLHNTVTLVARARARGNDLYKSERYTEASSAYAEGLRLDPCNAILYCNRAACWFKLGMWERSIEDCNQALRYQPSYTKPLLRRAASNSKMERWGAAVSDYEALIRELPHDKEVAESLFHAQVALKKSRGEEVLNMEFGGEVEEIYSLEQFKSAMNLPGVSVIHFSTASDHQCKQISPFVDSLCTRYPSIHFLKVDIDKCPSIGNAENVRVVPTVKIYKNGSRVKEIVCPSKEVLEYSVRHYSG
Protein: Cyclic AMP-dependent transcription factor ATF-6 alpha (cAMP-dependent transcription factor ATF-6 alpha) (Activating transcription factor 6 alpha) (ATF6-alpha) [Cleaved into: Processed cyclic AMP-dependent transcription factor ATF-6 alpha] (G3V909)
Organism: Rattus norvegicus (Rat)
Function: Precursor of the transcription factor form (Processed cyclic AMP-dependent transcription factor ATF-6 alpha), which is embedded in the endoplasmic reticulum membrane. Endoplasmic reticulum stress promotes processing of this form, releasing the transcription factor form that translocates into the nucleus, where it activates transcription of genes involved in the unfolded protein response (UPR).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:22682248}; Single-pass type II membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:P18850}; Single-pass type II membrane protein {ECO:0000255}. Note=Translocates from the endoplasmic reticulum to the Golgi, where it is processed. {ECO:0000250|UniProtKB:P18850}.; SUBCELLULAR LOCATION: [Processed cyclic AMP-dependent transcription factor ATF-6 alpha]: Nucleus {ECO:0000269|PubMed:22682248}. Note=Under ER stress the cleaved N-terminal cytoplasmic domain translocates into the nucleus (PubMed:22682248). THBS4 promotes its nuclear shuttling (By similarity). {ECO:0000250|UniProtKB:F6VAN0, ECO:0000269|PubMed:22682248}.
Interaction partners:
- Endoplasmic reticulum chaperone BiP
- DNA damage-inducible transcript 3 protein
- Vesicle-associated membrane protein-associated protein B
- X-box-binding protein 1
- Wolframin
- Cyclic AMP-dependent transcription factor ATF-4
- Eukaryotic translation initiation factor 2-alpha kinase 3
- Atf6b protein
- Interferon-induced, double-stranded RNA-activated protein kinase
- Endoplasmin
Sequence:
MESPFSPVLPHGPGEDWESTLFAELGYFTDTDDVQFDAAHETYENNFDHLNFDLDLMPWESDIWSPSSHFCSDIKAEPQPLSPASSSCSVSSPRSTDSCSSTQHVPEELDLLSSSQSPLSLYGDSCHSPSSAEPLKEEKPVTGPGNKTEHGLTPKKKIQMSSKPSVQPKPLLLPAAPKTPANASVPAKTIIIQTLPALMPLAKQQSIISIQPAPTKGQTVLLSQPAVVQLQTPGVLPSAQPVLAVTGGATQLPNHVVNVVPAPVVNSPVNGKLCVTKPVLQSSTRSTGSDIAVLRRQQRMIKNRESACQSRKKKKEYMLGLEARLKAALSENEQLKKENGSLKRQLDQVVSENQRLKVPSPKRRAVCVMIVLAFIMLNYGPMSMLEQDSRRVKPSVSPANQRRHLLEFSAKEVKDTSDGDNQKNSYRYDHSVSNDKALMVLSEEPLLYIPPPPCQPLINTTESLRLNHELRGWVHRHEVERTKSRRMTNSQQKTRILQGALEQGSNSQLMAVQYTETTSISRNSGSELQVYYASPGSYQGFFDAIRRRGDTFYVVSFRRDHLLLPATTHNKTTRPKMSIVLPAININDNVINGQDYEVMMQIDCQVMDTRILHIKSSSVPPYLRDHQRNQTSTFFGSPPTATETTHVVSTLPESVQ
Protein: Dipeptidyl peptidase 3 (EC 3.4.14.4) (Dipeptidyl aminopeptidase III) (Dipeptidyl peptidase III) (G3V1D3)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MGEPEAGSEFANGAAAAGPMADTQYILPNDIGVSSLDCREAFRLLSPTERLYAYHLSRAAWYGGLAVLLQTSPEAPYIYALLSRLFRAQDPDQLRQHALAEGLTEEEYQAFLVYAAGVYSNMGNYKSFGDTKFVPNLPKEKLERVILGSEAAQQHPEEVRGLWQTCGELMFSLEPRLRHLGLGKEGITTYFSGNCTMEDAKLAQDFLDSQNLSAYNTRLFKEVDGEGKPYYEVRLASVLGSEPSLDSEVTSKLKSYEFRGSPFQVTRGDYAPILQKVVEQLEKAKAYAANSHQGQMLAQYIESFTQGSIEAHKRGSRFWIQDKGPIVESYIGFIESYRDPFGSRGEFEGFVAVVNKAMSAKFERLVASAEQLLKELPWPPTFEKDKFLTPDFTSLDVLTFAGSGIPAGINIPNYDDLRQTEGFKNVSLGNVLAVAYATQREKLTFLEEDDKDLYILWKGPSFDVQVGLHELLGHGSGKLFVQDEKGAFNFDQETVINPETGEQIQSWYRSGETWDSKFSTIASSYEECRAESVGLYLCLHPQVLEIFGFEGADAEDVIYVNWLNMVRAGLLALEFYTPEAFNWRQAHMQARFVILRVLLEAGEGLVTITPTTGSDGRPDARVRLDRSKIRSVGKPALERFLRRLQVLKSTGDVAGGRALYEGYATVTDAPPECFLTLRDTVLLRKESRKLIVQPNTRLEGSDVQLLEYEASAAGLIRSFSERFPEDGPELEEILTQLATADARFWKGPSEAPSGQA
Protein: Sodium- and chloride-dependent transporter XTRP3 (Sodium/imino-acid transporter 1) (Solute carrier family 6 member 20) (Transporter rB21A homolog) (Q9NP91)
Organism: Homo sapiens (Human)
Function: Mediates the Na(+)- and Cl(-)-dependent uptake of imino acids such as L-proline, N-methyl-L-proline and pipecolate as well as N-methylated amino acids. Also transports glycine, regulates proline and glycine homeostasis in the brain playing a role in the modulation of NMDAR currents.
Subcellular location: Apical cell membrane {ECO:0000250|UniProtKB:Q8VDB9}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q8VDB9}. Note=Located in the apical brush border membrane of kidney proximal tubule cells and in the apical membrane of enterocytes lining the intestinal villi. {ECO:0000250|UniProtKB:Q8VDB9}.
Interaction partners:
- Angiotensin-converting enzyme 2
- Proton-coupled amino acid transporter 2
- Xylosyltransferase 2
- Leucine zipper transcription factor-like protein 1
- FYVE and coiled-coil domain-containing protein 1
Sequence:
MEKARPLWANSLQFVFACISYAVGLGNVWRFPYLCQMYGGGSFLVPYIIMLIVEGMPLLYLELAVGQRMRQGSIGAWRTISPYLSGVGVASVVVSFFLSMYYNVINAWAFWYLFHSFQDPLPWSVCPLNGNHTGYDEECEKASSTQYFWYRKTLNISPSLQENGGVQWEPALCLLLAWLVVYLCILRGTESTGKVVYFTASLPYCVLIIYLIRGLTLHGATNGLMYMFTPKIEQLANPKAWINAATQIFFSLGLGFGSLIAFASYNEPSNNCQKHAIIVSLINSFTSIFASIVTFSIYGFKATFNYENCLKKVSLLLTNTFDLEDGFLTASNLEQVKGYLASAYPSKYSEMFPQIKNCSLESELDTAVQGTGLAFIVYTEAIKNMEVSQLWSVLYFFMLLMLGIGSMLGNTAAILTPLTDSKIISSHLPKEAISGLVCLVNCAIGMVFTMEAGNYWFDIFNDYAATLSLLLIVLVETIAVCYVYGLRRFESDLKAMTGRAVSWYWKVMWAGVSPLLIVSLFVFYLSDYILTGTLKYQAWDASQGQLVTKDYPAYALAVIGLLVASSTMCIPLAALGTFVQRRLKRGDADPVA
Protein: Poly [ADP-ribose] polymerase (PARP) (EC 2.4.2.-) (A0A0G2JTB0)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MSGRRCAGGGAACSSAVAEAVEPSARELFEACRNGDVERVKRLVTPEKVNSRDTAGRKSTPLHFAAGFGRKDVVEYLLQNGANVQARDDGGLIPLHNACSFGHAEVVNLLLQHGADPNARDNWNYTPLHEAAIKGKIDVCIVLLQHGAEPTIRNTDGRTALDLADPSAKAVLTGDYKKDELLESARSGNEEKMMALLTPLNVNCHASDGRKSTPLHLAAGYNRVKIVQLLLQHGADVHAKDKGDLVPLHNACSYGHYEVTELLVKHGACVNAMDLWQFTPLHEAASKNRVEVCSLLLSYGADPTLLNCHNKSAIDLAPTAQLKERLSYEFKGHSLLQAAREADVTRIKKHLSLEMVNFKHPQTHETALHCAAASPYPKRKQICELLLRKGANTNEKTKEFLTPLHVASENAHNDVVEVVVKHEAKVNALDSLGQTSLHRAAHCGHLQTCRLLLSYGCDPNIISLQGLTALQMGNENVQQLLQEGVSLGHSEADRQLLEAAKAGDVETVKKLCTVQSVNCRDIEGRQSTPLHFAAGYNRVSVVEYLLQHGADVHAKDKGGLVPLHNACSYGHYEVAELLVKHGAVVNVADLWKFTPLHEAAAKGKYEICKLLLQHGADPTKKNRDGNTPLDLVKDGDTDIQDLLRGDAALLDAAKKGCLARVKKLSSPDNVNCRDTQGRHSTPLHLAAGYNNLEVAEYLLQHGADVNAQDKGGLIPLHNAASYGHVDVAALLIKYNACVNATDKWAFTPLHEAAQKGRTQLCALLLAHGADPTLKNQEGQTPLDLVSADDVSALLTAAMPPSALPTCYKPQVLSGVRSPGATADALSSGPSSPSSLSAASSLDNLAGSFSELSAVVSSSTTEGATGLERKEDSGIDFSITQFIRNLGLEHLMDIFEREQITLDVLVEMGHKELKEIGISAYGHRHRLIKGVERLISGQQGLNPYLTLNNSGSGTILIDLSPDDKEFQSVEEEMQSTVREHRDGGHAGGIFNRYSILKIQKVCNKKLWERYTHRRKEVSEENHNHANERMLFHGSPFVNAIIHKGFDERHAYIGGMFGAGIYFAENSSKSNQYVYGIGGGTGCPVHKDRSCYICHRQLLFCRVTLGKSFLQFSAMKMAHSPPGHHSVTGRPSVNGLALAEYVIYRGEQAYPEYLITYQIVRPEGMGDG
Protein: p60=60 kDa stress-related protein (Q9PSQ5)
Organism: Gallus gallus (Chicken)
Interaction partners:
Sequence:
EEAQALKERGNQALAAGDIGAAVRHYTAAIALDAXNFLNRFEEALLGDPSLRELLEQLRQQDLNENAKQALKETYITNQAAVYFEKGDYNXEXELEEKYKDAVHFYNKLLEFPLALKDQEEQIR
Protein: Coatomer subunit beta (Beta-coat protein) (Beta-COP) (Q23924)
Organism: Dictyostelium discoideum (Social amoeba)
Function: The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Golgi apparatus membrane {ECO:0000269|PubMed:10887966}; Peripheral membrane protein {ECO:0000269|PubMed:10887966}; Cytoplasmic side {ECO:0000269|PubMed:10887966}. Cytoplasmic vesicle, COPI-coated vesicle membrane {ECO:0000269|PubMed:10887966}; Peripheral membrane protein {ECO:0000269|PubMed:10887966}; Cytoplasmic side {ECO:0000269|PubMed:10887966}. Note=The coatomer is cytoplasmic or polymerized on the cytoplasmic side of the Golgi, as well as on the vesicles/buds originating from it. {ECO:0000250}.
Interaction partners:
- Coatomer subunit delta
- Coatomer subunit beta'
- Coatomer subunit alpha
- Coatomer subunit epsilon
- Coatomer subunit gamma
- Probable coatomer subunit zeta-A
- Probable coatomer subunit zeta-B
- Arf GTPase activating protein
- Clathrin heavy chain
- ADP-ribosylation factor 1
Sequence:
MSALTQSGSIEKPCTILINYDKGDPPQVNEFKQNFEHGTTEQKIETLKKVILYTINGEPIPQLLMPIILYVMPSNDHTIKKLLLIYWEVIEKTHLGKLKSEMILVCNSLLNDLNHPNEFVRGSTLRFLCKLREAEVLEPLVPSVRSNLENRHAYCRRNAVLAIYNIYSHFDYLIPDAPELIYNFLLQEKDASCKRNAFIMLFNCAPEKAVEYLSSVLDEVPSFGDMLQFIVVELIRKVCKTSPSERSKYIKCIFTLLNSSSPAVKYESAGTLLSLSSAPTAVRGAASAYIDLLCNESDNNVKMIVLDKLIEIKKNHSKIMEELVMDILRALSSPNIDICKKVLNIVLDSVTPKNIDEIILFLKKEINKTQSKEFDKGLEYRHILIRTIHVSSLKYPEVLGNVVPLLMEYLGDSYLPSAVDVVIFLREVVETYPSLRELIIKKLIENLSSIKVSKVYRVAVWVIAEYVTCLEDLQYAMTSITNDLEELLKPKQTEEVILETKAKVKIEKVSIQKLIADGDWYLASCISSSLTKLFFRAEQLNIDNADSNKLKAQVMMIISVLINLSKASQVSTSKSAYERMLSCIQVLIDSNATIKKIWLQDCRDSFANYLKYLLIKQSENKKKTEKEVLVKPNNIINIRQLKSKKAFGPVDTEDDLIKAVGNTGEANKDQNEYSKISQLSGFSDPIYVEAYVRVHQYDIVLDISVFNQTNDTLQNVTLELVTLGDLKICERVPPFTMAPREKTSAKASIKVSSTDNGVIMGTIAFDIAGSVSSMSDKNCVILNELHIDVIDYILPANHQYTDVLFRNHWLEFEWENKIPVNTNITDLVKYVHHISKVTNMGILTPEVHLSNDTGILSANLCAKSVFGEDALANICIEKQADGKISGYIRIRAKVQSIAVTLGEKIGNMGMKA
Protein: Kinesin motor domain-containing protein (P91400)
Organism: Caenorhabditis elegans
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
- Kinesin-like protein
- Protein regulator of cytokinesis 1
- Calponin-homology
- Kinesin motor domain-containing protein
- Kinesin-like protein
- Zygote defective protein 9
- Kinesin 1 cargo adaptor alternative variant a
- Kinesin motor domain-containing protein
- Kinesin like protein
- Kinesin-like protein klp-19
Sequence:
MNVARRRSGLFRSTIGATPKITRGRAAAPSTKEANSTTIPRQSAPGGITIGAAARRPPSRLPTPTTPATGRASLPERSAMAKPASCSRPIPTMQSTASRISTLTAASTFRQLRTGRPPPPSTQRSTATSSLKPSVTRARPVAQKPILPSKMALLEEKIAQLESAMAEATDFAEHQKSKIQILDGKLEGADRKLISLQDQLSTLKEVNKAKVEECEDYRVHNNDLRDLLNEKEAELRKLHNDVVDLRGQIRVAVRVRPLIKSEADASSSAIEYPAIDTIRINEGSKPGIVVKFEKVFTPVFSQKEVFANVEEFIRSSLHGYNVGLIAYGQTGSGKTHTMRGGNGEEEGIIPRAAAFLFAESRKLESLGWKFDFSLSFLEVYNNVAYDLLSDRAVVQLRLNDQTVSMIGLSEHTISNVSDVARLLRVADGGRKTAATKCNESSSRSHAVYMWKITAHQPSTGISTSCQLKLVDLAGSERAKESGVSGDQFKEMTNINQSLSILQMCISQQRSQKGHVSYRDSKLTQVLMDCLGRGNSKTMVVVNLNPCNEQATESKRSIEFASKMRSTNIGSAVQQRTLLGDVSQMSMN
Protein: 2,4-dienoyl-CoA reductase 2 (F7F3L0)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cleavage furrow {ECO:0000256|ARBA:ARBA00004626}. Midbody {ECO:0000256|ARBA:ARBA00004214}. Recycling endosome membrane {ECO:0000256|ARBA:ARBA00004654}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004654}.
Interaction partners:
Sequence:
MGSESTYSECETFTDEDTSTLVHPELQPEGDVDSAGGSGVPSECLDTMEEPDHGALLLLPGRSRPHSQAVVMVIGSEEHFEDYGEGSEAELSPETLCNGELDCEDPAFLTPSSNPLASKLCTVLTDEAFEFYCSQCHKQINRLEDLSARLTDLEMNSPAKRLSSRKVARYLHQSGTLTMEALEDPPPEPVECPEEDIADKVIFLERRVSELEKDSAAAGEQHGRLRQENLQLVHRANALEEQLKEQEFRAQEKVLEETRKQKELLCKMEREKSIEIENLQARLQQLDEENSELRSCTPCLKANIERLEEEKQKMLDEIEELTQRLSEEQENKRKMGDKLSHERHQFQRDKEATQELIEDLRKQLEHLQLLRLEMEQRRGRSSSLGLQEYNSRARESELEQEVRRLKQDNRNLKEQNDELNGQIITLSIQGAKSLFSTSFSESLAAEISSVSRDELMEAIQKQEEINFRLQDYIDRIIVAILETNPSILEVK