wanglab/gogpt-training-data huggingface dataset:
Protein: Transcription elongation factor Spt4 (Q8U440)
Organism: Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Function: Stimulates transcription elongation.
Interaction partners:
- Transcription elongation factor Spt5
- DNA-directed RNA polymerase subunit Rpo7
- Small ribosomal subunit protein eS31
- GTP-dependent dephospho-CoA kinase
- Small ribosomal subunit protein eS24
- DNA-directed RNA polymerase subunit Rpo1N
- Inorganic pyrophosphatase
Sequence:
MSEKACRHCHYITSEDRCPVCGSRDLSEEWFDLVIIVDVENSEIAKKIGAKVPGKYAIRVR
Protein: Protocadherin gamma B7 (Protocadherin gamma subfamily B, 7) (Q91XX3)
Organism: Mus musculus (Mouse)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
Interaction partners:
Sequence:
MGGSSARRKRPGRPQVLFILLLPLFCPALGQPVRYSIPEELDRGSVVGKLAKDLGLSVLEVSARKLRVSAEKLHFSVDSESGDLLVKDRIDREQICKGRRKCELQLEAVLENPLNIFHVVVEIEDVNDHAPQFPKDEINLEISESDSPGARTILESAKDLDIGMNSLSKYQLSPNDYFLLLVKDNPDGSKYPELELQKMLDREAESTHHLMLTAVDGGDPPRTGTTQLRIRVVDANDNRPVFSQDVYRVRLPEDLPPGTTVLRLKAMDQDEGINAEFTYSFLGVANKAQFSLDPITGDIVTRQSLDFEEVEQYTIDVEAKDRGSLSSQCKVIIEVLDENDNRPEIIITSLSDQISEDSPSGTVVALFKVRDRDSGENAEVMCSLSGNNPFKIHSSSNNYYKLVTDSILDREQTPGYNVTITATDRGKPPLSSSTTITLNVADVNDNAPVFQQQAYLINVAENNQPGTSITQVKAWDPDVGSNGLVSYSIIASDLEPKALSSFVSVNQDSGVVYAQRAFDHEQIRSFQLTLQARDQGSPALSANVSMRVLVDDRNDNAPRVLYPTLEPDGSALFDMVPRAAEPGYLVTKVVAVDADSGHNAWLSYHVLQASDPGLFSLGLRTGEVRTARALSDKDAARQRLLVAVRDGGQPPLSATATLLLVFADSLQEALPDLVDHPIPSDPQSELQFYLVVALALISVLFLLAVIFAIALRLRQSSSPSSTGCFGSVLGSKSRPVLPPNYSEGTLPYAYNLCVPGDQLKPEFNYFSSVGDCPAAQDILNKDSSSALLASILTPGVEADEKTFNQQAPPNTDWRFSQAQRPGTSGSQNGDETGTWPNNQFDTEMLQAMILASASEAADGSSTLGGGAGTMGLSARYGPQFTLQHVPDYRQNVYIPGSNATLTNAAGKRDGKAPAGGNGNKKKSGKKEKK
Protein: G-protein coupled receptor 42 (O15529)
Organism: Homo sapiens (Human)
Function: Probable G protein-coupled receptor that may be activated by a major product of dietary fiber digestion, the short chain fatty acids (SCFAs), and that may play a role in the regulation of whole-body energy homeostasis and/or in intestinal immunity.
Subcellular location: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- B-cell receptor CD22
- Galanin peptides
Sequence:
MDTGPDQSYFSGNHWFVFSVYLLTFLVGLPLNLLALVVFVGKLRCRPVAVDVLLLNLTASDLLLLLFLPFRMVEAANGMHWPLPFILCPLSGFIFFTTIYLTALFLAAVSIERFLSVAHPLWYKTRPRLGQAGLVSVACWLLASAHCSVVYVIEFSGDISHSQGTNGTCYLEFRKDQLAILLPVRLEMAVVLFVVPLIITSYCYSRLVWILGRGGSHRRQRRVAGLVAATLLNFLVCFGPYNVSHVVGYICGESPVWRIYVTLLSTLNSCVDPFVYYFSSSGFQADFHELLRRLCGLWGQWQQESSMELKEQKGGEEQRADRPAERKTSEHSQGCGTGGQVACAEN
Protein: Centromere protein S (CENP-S) (E1BSW7)
Organism: Gallus gallus (Chicken)
Function: DNA-binding component of the Fanconi anemia (FA) core complex. Required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. In complex with CENPX (MHF heterodimer), crucial cofactor for FANCM in both binding and ATP-dependent remodeling of DNA. Stabilizes FANCM. In complex with CENPX and FANCM (but not other FANC proteins), rapidly recruited to blocked forks and promotes gene conversion at blocked replication forks. In complex with CENPT, CENPW and CENPX (CENP-T-W-S-X heterotetramer), involved in the formation of a functional kinetochore outer plate, which is essential for kinetochore-microtubule attachment and faithful mitotic progression. As a component of MHF and CENP-T-W-S-X complexes, binds DNA and bends it to form a nucleosome-like structure. DNA-binding function is fulfilled in the presence of CENPX, with the following preference for DNA substates: Holliday junction > double-stranded > splay arm > single-stranded. Does not bind DNA on its own (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:19620631}. Chromosome, centromere {ECO:0000269|PubMed:19620631}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:19620631}. Note=Assembly of CENPS and CENPX and its partner subunits CENPT and CENPW at centromeres occurs through a dynamic exchange mechanism. Although exchange is continuous in the cell cycle, de novo assembly starts principally during mid-late S phase and is complete by G2. CENPS is more stably bound at the kinetochore than CENPX. During S phase, rapidly recruited to DNA interstrand cross-links that block replication. Recruited to DNA damage sites about 20 minutes following UV irradiation, reaching a plateau after approximately 40 minutes. {ECO:0000250|UniProtKB:Q8N2Z9}.
Interaction partners:
- Centromere protein X
- Centromere protein W
- Fanconi anemia group M protein
- Centromere protein T
- Centromere protein O
- Centromere protein N
- Centromere protein I
- Centromere protein Q
- Centromere protein M
- Centromere protein K
Sequence:
MEAAGGEQRELLIQRLRAAVHYTTGCLCQDVAEDKGVLFSKQTVAAISEITFRQCENFARDLEMFARHAKRSTITSEDVKLLARRSNSLLKYITQKSDELASSNMEQKEKKKKKSSAAKGRKTEENETPVTESEDSNMA
Protein: N-lysine methyltransferase SETD6 (SET domain-containing protein 6) (J3QT10)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MATQAKRPRVAGPVDGGDLDPVACFLSWCRRVGLELSPKVAVSRQGTVAGYGMVARESVQAGELLFVVPRAALLSQHTCSIGGLLERERVALQSQSGWVPLLLALLHELQAPASRWRPYFALWPELGRLEHPMFCLRVRSLELYHQLVALVMAYSFQEPLEEEEDEKEPNSPVMVPAADILNHLANHNANLEYSANCLRMVATQPIPKGHEIFNTYGQMANWQLIHMYGFVEPYPDNTDDTADIQMVTVREAALQGTKTEAERHLVYERWDFLCKLEMVGEEGAFVIGREEVLTEEELTTTLKVLCMPAEEFRELKDQDGGGDDKREEGSLTITNIPKLKASWRQLLQNSVLLTLQTYATDLKTDQGLLSNKEVYAKLSWREQQALQVRYGQKMILHQLLELTS
Protein: Uncharacterized protein (Q54FX9)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
Sequence:
MSLNWADETENEERENEMKAIVEPVQPQQPTQSSLPQASIQPEPVVEQQQQQPPQQQQPPQTQDDERDNYNNNNNRSSGGRGDYSGNSNNSNNYYNNNNNNNRQQGGYQNNNNNRYNNNNNQQGGYQNNNNNRYNNNNQQGGYQNRYNNNNNNQQGGYQNNNNRMQQGGGYQNNNNNNNNYNNNRMQQGGYQNNNYNNNNNNNNNNNQYTQKNSINYKRNEVSITGYDEANASKELFQEFLQSHLIEYSDINFAPNETIVSLKDSENYLKTMKLTGTKFNDSQITVLNYTRKQPGFVPPSYSNQSSSSSGDNQSFQPQSTSKVNPFGNATPIDTSKVHLSNSTQPQQPTQQQPQPTQQQQQQQQPTQQGQQGQQQPQQQNDNKYRPNSMRTNSGFKQNDNKFDNNNKFDNKKPFGQNKYNNKREEDGWKSTGPARHPKDQPSKEVSQPTVAKTSGNIFECLEQDD
Protein: N-acylethanolamine-hydrolyzing acid amidase (EC 3.5.1.60) (Acylsphingosine deacylase NAAA) (EC 3.5.1.23) (N-acylsphingosine amidohydrolase-like) (ASAH-like protein) [Cleaved into: N-acylethanolamine-hydrolyzing acid amidase subunit alpha; N-acylethanolamine-hydrolyzing acid amidase subunit beta] (Q5KTC7)
Organism: Rattus norvegicus (Rat)
Function: Degrades bioactive fatty acid amides to their corresponding acids, with the following preference: N-palmitoylethanolamine > N-myristoylethanolamine > N-stearoylethanolamine > N-oleoylethanolamine > N-linoleoylethanolamine > N-arachidonoylethanolamine.
Subcellular location: Lysosome {ECO:0000250|UniProtKB:Q02083}. Membrane {ECO:0000250|UniProtKB:Q02083}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q02083}.
Interaction partners:
- Fatty-acid amide hydrolase 1
- N-acyl-phosphatidylethanolamine-hydrolyzing phospholipase D
- Monoglyceride lipase
- G protein-coupled receptor 55
- Monoacylglycerol lipase ABHD6
- Lysophosphatidylserine lipase ABHD12
- Glycerophosphodiester phosphodiesterase 1
- 
Sequence:
MGTPAIRAACHGAHLALALLLLLSLSDPWLWATAPGTPPLFNVSLDAAPELRWLPMLQHYDPDFVRAAVAQVIGDRVPQWILEMIGEIVQKVESFLPQPFTSEIRGICDYLNLSLAEGVLVNLAYEASAFCTSIVAQDSQGRIYHGRNLDYPFGNALRKLTADVQFVKNGQIVFTATTFVGYVGLWTGQSPHKFTISGDERDKGWWWENMIAALSLGHSPISWLIRKTLTESEDFEAAVYTLAKTPLIADVYYIVGGTSPQEGVVITRDRGGPADIWPLDPLNGAWFRVETNYDHWEPVPKRDDRRTPAIKALNATGQAHLSLETLFQVLSVFPVYNNYTIYTTVMSAAEPDKYMTMIRNPS
Protein: Pyridoxal 5'-phosphate synthase subunit SNZ1 (PLP synthase subunit SNZ1) (EC 4.3.3.6) (PDX1 homolog 1) (Pdx1.1) (p35) (Q03148)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the formation of pyridoxal 5'-phosphate from ribose 5-phosphate (RBP), glyceraldehyde 3-phosphate (G3P) and ammonia. The ammonia is provided by a SNO isoform. Can also use ribulose 5-phosphate and dihydroxyacetone phosphate as substrates, resulting from enzyme-catalyzed isomerization of RBP and G3P, respectively.
Interaction partners:
- Pyridoxal 5'-phosphate synthase subunit SNO1
- Probable pyridoxal 5'-phosphate synthase subunit SNO2
- Probable pyridoxal 5'-phosphate synthase subunit SNO3
- Probable pyridoxal 5'-phosphate synthase subunit SNZ2
- Probable pyridoxal 5'-phosphate synthase subunit SNZ3
- Putative pyridoxal kinase BUD16
- Pyridoxamine 5'-phosphate oxidase
- Transcription regulatory protein SNF12
- Chromatin structure-remodeling complex protein RSC6
- Putative pyridoxal kinase BUD17
Sequence:
MTGEDFKIKSGLAQMLKGGVIMDVVTPEQAKIAEKSGACAVMALESIPADMRKSGKVCRMSDPKMIKDIMNSVSIPVMAKVRIGHFVEAQIIEALEVDYIDESEVLTPADWTHHIEKDKFKVPFVCGAKDLGEALRRINEGAAMIRTKGEAGTGDVSEAVKHIRRITEEIKACQQLKSEDDIAKVAEEMRVPVSLLKDVLEKGKLPVVNFAAGGVATPADAALLMQLGCDGVFVGSGIFKSSNPVRLATAVVEATTHFDNPSKLLEVSSDLGELMGGVSIESISHASNGVRLSEIGW
Protein: FACT complex subunit SSRP1-A (Facilitates chromatin transcription complex subunit ssrp1-A) (HMG box-containing protein 4) (Structure-specific recognition protein 1-A) (P41848)
Organism: Caenorhabditis elegans
Function: Component of the FACT complex, a general chromatin factor that acts to reorganize nucleosomes. The FACT complex is involved in multiple processes that require DNA as a template such as mRNA elongation, DNA replication and DNA repair. During transcription elongation the FACT complex acts as a histone chaperone that both destabilizes and restores nucleosomal structure. It facilitates the passage of RNA polymerase II and transcription by promoting the dissociation of one histone H2A-H2B dimer from the nucleosome, then subsequently promotes the reestablishment of the nucleosome following the passage of RNA polymerase II. Binds specifically to double-stranded DNA (By similarity). In embryos, may function redundantly with hmg-3 in embryos to promote cell cycle progression and development of the anterior pharynx. In the germline, acts non-redundantly with hmg-3 to play a role in oocyte development.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267, ECO:0000269|PubMed:30336114}. Chromosome {ECO:0000250|UniProtKB:Q08945}.
Interaction partners:
- FACT complex subunit spt-16
- Suppressor of Ty 6 homolog
- RNA polymerase-associated protein CTR9
- RNA polymerase-associated protein RTF1 homolog
- Transcription elongation factor SPT5
- RNA polymerase-associated protein LEO1
- Transcription elongation factor SPT4
- Cell division cycle protein 73
- Probable DNA-directed RNA polymerases I, II, and III subunit RPABC3
- DNA-directed RNA polymerase RpoA/D/Rpb3-type domain-containing protein
Sequence:
MAELQFPGVYVEDVGHLAFGTLKLTEKSLNFKGDKGGKSVNVTGSDIDKLKWQKLGNKPGLRVGLNDGGAHRFGGFKDTDLEKIQSFTSSNWSQSIDQSNLFIKGWNYGQAEVKGKTVEFSWEDKPIFEIPCTNVSNVIANKNEAVLEFHQNDDSKVQLMEMRFHMPIDLENEEDADKVEEFKKAVLAYAGLEAETEQPICLLTDILCTTPRGRYDIKVYPTSIALHGKTYDYKIPIKSINRLFLVPHKDGRHVYFVLSLNPPIRQGQTRYSYLIFEFGKDEEQDLELALTDEQLESSNGNLRRDMTGPIYETISILFKSICNLKITVPGRFLGSSGTPAIQCTHRQNPGLLYPMEKGFLFIHKPAMYIRFEEISSCHFARSDSGTVTRTFDFEIDLKYGGPLTFNAMEKEENNKLFDYLNKKNIKIRNSQRVENTVADSSDDEIDPYKAAVTAEGRQRDDSDDDSTDEDYDLDKDIKKKKEDKESSEGTGSEPDDEYDSGSEQDSSGTGESEPDSEQDVPSKRRKGEPKEKREKKEKREKKEGKKGKKDKDPNAPKRATSAYMQWFLASRNELKEDGDSVADVAKKGGAKWKTMSSDDKKKWEEKAEEDKSRYEKEMKEYRKNGPPSSSSKPSSSKTSKKSSGPSSSKAISKEYISDSDDSDDEEPKKKEKKAAPKEESEESNNGSDGSDESDDSD
Protein: Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3A (Oligosaccharyl transferase subunit STT3A) (STT3-A) (EC 2.4.99.18) (B5) (Integral membrane protein 1) (Transmembrane protein TMC) (P46977)
Organism: Homo sapiens (Human)
Function: Catalytic subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity. This subunit contains the active site and the acceptor peptide and donor lipid-linked oligosaccharide (LLO) binding pockets (By similarity). STT3A is present in the majority of OST complexes and mediates cotranslational N-glycosylation of most sites on target proteins, while STT3B-containing complexes are required for efficient post-translational glycosylation and mediate glycosylation of sites that have been skipped by STT3A.
Subcellular location: Endoplasmic reticulum {ECO:0000269|PubMed:12887896}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P46978}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P46978}.
Interaction partners:
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit DAD1
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 2
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 4
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 48 kDa subunit
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit TMEM258
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1
- Oligosaccharyltransferase complex subunit OSTC
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit MAGT1
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3B
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit TUSC3
Sequence:
MTKFGFLRLSYEKQDTLLKLLILSMAAVLSFSTRLFAVLRFESVIHEFDPYFNYRTTRFLAEEGFYKFHNWFDDRAWYPLGRIIGGTIYPGLMITSAAIYHVLHFFHITIDIRNVCVFLAPLFSSFTTIVTYHLTKELKDAGAGLLAAAMIAVVPGYISRSVAGSYDNEGIAIFCMLLTYYMWIKAVKTGSICWAAKCALAYFYMVSSWGGYVFLINLIPLHVLVLMLTGRFSHRIYVAYCTVYCLGTILSMQISFVGFQPVLSSEHMAAFGVFGLCQIHAFVDYLRSKLNPQQFEVLFRSVISLVGFVLLTVGALLMLTGKISPWTGRFYSLLDPSYAKNNIPIIASVSEHQPTTWSSYYFDLQLLVFMFPVGLYYCFSNLSDARIFIIMYGVTSMYFSAVMVRLMLVLAPVMCILSGIGVSQVLSTYMKNLDISRPDKKSKKQQDSTYPIKNEVASGMILVMAFFLITYTFHSTWVTSEAYSSPSIVLSARGGDGSRIIFDDFREAYYWLRHNTPEDAKVMSWWDYGYQITAMANRTILVDNNTWNNTHISRVGQAMASTEEKAYEIMRELDVSYVLVIFGGLTGYSSDDINKFLWMVRIGGSTDTGKHIKENDYYTPTGEFRVDREGSPVLLNCLMYKMCYYRFGQVYTEAKRPPGFDRVRNAEIGNKDFELDVLEEAYTTEHWLVRIYKVKDLDNRGLSRT
Protein: Serine/threonine-protein kinase PLK (EC 2.7.11.21) (Polo-like kinase) (F7HSC1)
Organism: Macaca mulatta (Rhesus macaque)
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000256|ARBA:ARBA00004300}. Cytoplasm, cytoskeleton, spindle {ECO:0000256|ARBA:ARBA00004186}. Midbody {ECO:0000256|ARBA:ARBA00004214}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- G2/mitotic-specific cyclin-B1
- Cell division cycle protein 20 homolog
- Cyclin dependent kinase 1
- M-phase inducer phosphatase
- G2/mitotic-specific cyclin-B2
- Mitotic checkpoint serine/threonine-protein kinase BUB1 beta
- Membrane-associated tyrosine- and threonine-specific cdc2-inhibitory kinase
- M-phase inducer phosphatase
- M-phase inducer phosphatase
- Fizzy-related protein homolog
Sequence:
MSAAVTAGKLARAPADPGKAGVPGVAAPGAPAAAPPAKEIPEVLVDPRSRRRYVRGRFLGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSLLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERKKTLCGTPNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPKHINPVAASLIQKMLQTDPTARPTINELLNDEFFTSGYIPARLPITCLTIPPRFSIAPSSLDPSNRKPLTVLNKGLENPLPERTREKEEPVVRETGEVVDCHLSDMLQQLHSVNASKPSERGLVRQEEAEDPACIPIFWVSKWVDYSDKYGLGYQLCDNSVGVLFNDSTRLILYNDGDSLQYIERDGTESYLTVSSHPNSLMKKITLLKYFRNYMSEHLLKAGANITPREGDELARLPYLRTWFRTRSAIILHLSNGSVQINFFQDHTKLILCPLMAAVTYIDEKRDFRTYRLSLLEEYGCCKELASRLRYARTMVDKLLSSRSASNRLKAS
Protein: Serine--tRNA ligase (EC 6.1.1.11) (Seryl-tRNA synthetase) (SerRS) (Seryl-tRNA(Ser/Sec) synthetase) (P0A8L1)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the attachment of serine to tRNA(Ser). Is also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec).
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- L-seryl-tRNA
- Cysteine--tRNA ligase
- Arginine--tRNA ligase
- Threonine--tRNA ligase
- Isoleucine--tRNA ligase
- Leucine--tRNA ligase
- Valine--tRNA ligase
- Glutamine--tRNA ligase
- Lysine--tRNA ligase, heat inducible
- Histidine--tRNA ligase
Sequence:
MLDPNLLRNEPDAVAEKLARRGFKLDVDKLGALEERRKVLQVKTENLQAERNSRSKSIGQAKARGEDIEPLRLEVNKLGEELDAAKAELDALQAEIRDIALTIPNLPADEVPVGKDENDNVEVSRWGTPREFDFEVRDHVTLGEMHSGLDFAAAVKLTGSRFVVMKGQIARMHRALSQFMLDLHTEQHGYSENYVPYLVNQDTLYGTGQLPKFAGDLFHTRPLEEEADTSNYALIPTAEVPLTNLVRGEIIDEDDLPIKMTAHTPCFRSEAGSYGRDTRGLIRMHQFDKVEMVQIVRPEDSMAALEEMTGHAEKVLQLLGLPYRKIILCTGDMGFGACKTYDLEVWIPAQNTYREISSCSNVWDFQARRMQARCRSKSDKKTRLVHTLNGSGLAVGRTLVAVMENYQQADGRIEVPEVLRPYMNGLEYIG
Protein: Mucin 21 (F7C950)
Organism: Mus musculus (Mouse)
Interaction partners:
- Mucin-15
- Mucin-20
- Mucin-13
- Mucin-6
- Mucin-2
- Mucin-1
- Mucin-2
- Mucin-4.
Sequence:
MQRRSSLWCWLLLQILLLGSGYAHISSTTTSNPSSETKSIATDYETTPTTTISSTASGSMPTLTTKASSIASDSKPTLTTTASSTASGSMSTPTTPASSTASGSTPTTTTTASSTASGSTPTPTTPASSTASGSTPTPTTTASSKASRSVPTTVSSTGSGSTPTPTTTASSTASGSTPTLTTTPSSTASGSTPTPTTPASSTASGSSPTPTTPVSSTASGSTPTPTTTASSKASGSVPTTVSSTGSGSTPTLTTTVSSTVSDSTPTPTTTASSTASGSAPTPTTTASSTASGSTPTLTTTASSSGSGSTPTLPTTESSTASGSTPTRTTTTSSTASRSTPTPTTTASSTASGSTPTPTTTVSSTGSGSTPTLTTTASRSGSGSTPTLTTTESSTASGSSPTLTTTASSSASGSMPTPTTTASSTASGSSPTLTTTASSSASGSMPTLTTTASSSASGSSPTLTTTASSSASGSMPTPTTTVSSTGSGSTPTLTTTESSTASGSTPTWTTTTSSTASRSTPTPTTTASSTASGSTPTPTTTVSSTGSGSTPTLTTTASRSGSGSTPTLTTTESSTASGSIPTLTTAASSTASGSTPTPTTTASSTASGSMPTPTTTASSTGSGSTPTLTTTASSSGSGSTPTLTTTESSTASGSIPTLTSAASSSASGSMPTPTTTVSSTGSGSTPTLTTTASSSASGSMPTPTTTASSTASGSSPTLTTTASSSASGSAPNPTTTVSSTGSGSTPTLTTTASSSGSGSTPTLPTTESSTASGSTPTRTTTTSSTASRSTPTPTTTASSTASGSTPTPTTTVSSTASGSTPTLTTTASRSGSGSTPTLTTTESSTASGSTPTPTTTASSTASGSAPNPTTTVSSTASGSTPTLPTTASSSGSGSTPTLTTTESSTASGSSPTLTTTASSSASGSMPTPTTTASSTASGSSPTLTTTASSSASGSMPTLTTTASSSASGSSPTLTTTASSSASGSMPTPTTTVSSTGSGSTPTLTTTESSTASGSTPTWTTTTSSTASRSTPTPTTTASSTASGSTPTPTTTVSSTGSGSTPTLTTTASRRGSGSTPTLTTTESSTGSGSTPTLTTTASSSGSGSTPTLPTTESSTASGSTPTRTTTTSSTASRSTPTPTTTASSTASGSTPTPTTTVSSTASGSTPTLTTTASRSGSGSTPILTTTESSTASGSTPTLTTAASSSASGSTPTPTTTVSSTGSGSTPTLTTTASSSGSGSTPTLTTTESSTASGSTPTQTTTTSSTASRSTPTPTTTASSTASGSIPTPTTTASSIASGTTPTLTTTESSTASGSSPTPTTASSSSASDSKPTSTTTASSTVSDSTPTPTTNASSSASGSTPTQTTTASRSASGSVPTLTTIAFSTASGSTPTLTTTASNSASSSSPTPTTTGLSKTSASSLSLTSTMTSITSASTFTPASIRTSKASASTSTSASIRTSIAFASTSTPTTSGPSTASVSTLNSTSIRTSTGSSSSLSATHTSSSLTVSTGTHTTSNHTGTPVMEVKPSGSLKPWEIFLITLASVIVVMGLSAGLFIYVRRYLSLRNAADGIFYNSHPDPGGSAMTPGSPTCSWRRPRTFNVVEMTRI
Protein: Ion_trans_2 domain-containing protein (H9G2R6)
Organism: Caenorhabditis elegans
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
METQKKVLPPKLQEERRRLLESDIARTDSEAEGTVYKNSYASLMNELQPTTSFDDFKQSITQLTDIFRADPARMQYGEKKNIKHKLQQWFIENPSISARIRSCNVLIKLLTCILYCIRVVNDERSYPDDFPFSEEEAGKQDVTLYKYLLWVDFDFKIWFLQTMFACISMVYTILVFYLSYSGSVVRLLINIHFLLELITSFPFIISIFIPSLTYLYVPVFLNCWLAKGALQAMMNDLNRKSFISSSALFRQLLLLFSVLACLIFTGMCSIEHLQRARGKRIDLFTSFYFVMVTFSTVGYGDWYPDYWASQLCVVILICVALGLIPKQLDELGQTWSERQKSGTDFSSWNGVESHVVVTITTLEVEFIRDFLEEFYAHPENQRIQIVLLSPAELDNQTRMLLKIPLWNNRVHYVRGSSLRDEDLERANVATSKACFILSARHVNRKVATDEHTILRSWAIKDFAPNVKQYVQIFRAETKMHIEHAEVLICEDEFKYALLANNCICPGISTFITLLMHTSRGEEGQKSTEPWHKVYGFHSGNEMYQIKVQDSKFFCEYVGKSFSSTSFHAHKEYGIGLIAVSPDGDTSRMKLNPGSSHIIQPTDTVYYMGLTNEESLTDFRKGIRSQQKRANVASTIANIGTVAVDVPRSDKTELVGRKKKKRKEKAADEIHLIEVGEHVQSSRRPSIAMVTEGKIDSSSDSDQEEICDKCRGPCIQHKLQRTYPQVRTYIGTSNTVCHMMKERRSLCCLKLDEKCAHKSATSAHEYQWRNRPIILAADRTSSGMYNLVIPLRAYYRPVHDLHPIIILLELEEQDSLNDAFLDAISYFPDVYWMKGKVGNLDCLLRAGVSSAEHVVVVKETAVMAEEHTADCNTIITVQKIHRMFPRLRMITELTHATNMRFVQFNPHNAYSLAQSRFEKKERKRGSHMPFMFRLPFAQGGVFSANMLDRLLYQAIIKPFVVDLVRLLLGIDQHSDGGYLTSFVITSDDLWIRNYGRLYQKLCSSVADIPIGIFRTKKMDTKTVSLDLQEQCKDFENTEMGRNKDMYDHVKNRMRLLNIKDTHTLLEGSDEKSQISYVIINPAQDLELESGDIVYVIRSPIRKDATNARINPRRGLRRSKNVSETIDSTNQVPTIVIDENNL
Protein: trypsin (EC 3.4.21.4) (Q9VRS4)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Secreted, extracellular space {ECO:0000256|ARBA:ARBA00004239}.
Interaction partners:
- Jonah 65Aiv
- GH01508p
- Trypsin beta
- Trypsin alpha
- GH20109p
- Zinc carboxypeptidase A 1
- Uncharacterized protein
- Trypsin epsilon
- RE65433p
- Uncharacterized protein, isoform A
Sequence:
MKVFVVLVLALASASAGLLPNIAPVHPRDRVSTPSITGRITNGKDAVAGQFPYQVGLSFSSSAGSWWCGGSIIGNEWVLTAAHCTDGAASVTIYYGATVRTSPEFTQVVSSSKFRQHESYLALTIRNDISLIQTSSVSFSATVNKISLPAVSNSYSTYEGKTAVASGWGLTSDQATAVSRDLQYVDLTIISNSKCQETFGSLIVTSRVLCVDTTNKASTCQGDSGGPLALDGVLIGATSFGSADGCESGAPAAFTRITYYRDWIKETSGI
Protein: Protein NEDD1 (Neural precursor cell expressed developmentally down-regulated protein 1) (NEDD-1) (Q8NHV4)
Organism: Homo sapiens (Human)
Function: Required for mitosis progression. Promotes the nucleation of microtubules from the spindle.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:14654843, ECO:0000269|PubMed:19029337, ECO:0000269|PubMed:27137183}.
Interaction partners:
- Mitotic spindle organizing protein 2B
- HAUS augmin-like complex subunit 6
- Gamma-tubulin complex component 5
- Gamma-tubulin complex component 4
- Gamma-tubulin complex component 6
- Tubulin gamma-1 chain
- Mitotic-spindle organizing protein 1
- Serine/threonine-protein kinase PLK1
- Gamma-tubulin complex component 3
- Mitotic-spindle organizing protein 2A
Sequence:
MQENLRFASSGDDIKIWDASSMTLVDKFNPHTSPHGISSICWSSNNNFLVTASSSGDKIVVSSCKCKPVPLLELAEGQKQTCVNLNSTSMYLVSGGLNNTVNIWDLKSKRVHRSLKDHKDQVTCVTYNWNDCYIASGSLSGEIILHSVTTNLSSTPFGHGSNQSVRHLKYSLFKKSLLGSVSDNGIVTLWDVNSQSPYHNFDSVHKAPASGICFSPVNELLFVTIGLDKRIILYDTSSKKLVKTLVADTPLTAVDFMPDGATLAIGSSRGKIYQYDLRMLKSPVKTISAHKTSVQCIAFQYSTVLTKSSLNKGCSNKPTTVNKRSVNVNAASGGVQNSGIVREAPATSIATVLPQPMTSAMGKGTVAVQEKAGLPRSINTDTLSKETDSGKNQDFSSFDDTGKSSLGDMFSPIRDDAVVNKGSDESIGKGDGFDFLPQLNSVFPPRKNPVTSSTSVLHSSPLNVFMGSPGKEENENRDLTAESKKIYMGKQESKDSFKQLAKLVTSGAESGNLNTSPSSNQTRNSEKFEKPENEIEAQLICEPPINGSSTPNPKIASSVTAGVASSLSEKIADSIGNNRQNAPLTSIQIRFIQNMIQETLDDFREACHRDIVNLQVEMIKQFHMQLNEMHSLLERYSVNEGLVAEIERLREENKRLRAHF
Protein: Patatin-like protein 1 (AtPLP1) (EC 3.1.1.-) (Patatin-related phospholipase A IIgamma) (pPLAIIg) (Phospholipase A IVA) (AtPLAIVA) (O23179)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Possesses non-specific lipolytic acyl hydrolase (LAH) activity. Catalyzes the hydrolysis of the neutral lipids monogalactosyldiacylglycerol (MGDG), digalactosyldiacylglycerol (DGDG) and phosphatidylglycerol (PG), and less efficiently the polar lipids phosphatidylcholine (PC) and phosphatidylinositol (PI), but not the storage lipid triacylglycerol (TAG). May play a role in root development.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12226489}.
Interaction partners:
- Patatin
- Protein DETOXIFICATION 21
- F-box protein PP2-A12
Sequence:
MENKSPSKKNKPPSCGSLVTILSLDGGGVRGIIAGVILAFLEKQLQELDGEEARLADYFDVIAGTSTGGLVTAMLTVPDETGRPHFAAKDIVPFYLEHCPKIFPQPTGVLALLPKLPKLLSGPKYSGKYLRNLLSKLLGETRLHQTLTNIVIPTFDIKKLQPTIFSSYQLLVDPSLDVKVSDICIGTSAAPTFFPPHYFSNEDSQGNKTEFNLVDGAVTANNPTLVAMTAVSKQIVKNNPDMGKLKPLGFDRFLVISIGTGSTKREEKYSAKKAAKWGIISWLYDDGSTPILDITMESSRDMIHYHSSVVFKALQSEDKYLRIDDDTLEGDVSTMDLATKSNLENLQKIGEKMLTNRVMQMNIDTGVYEPVAENITNDEQLKRYAKILSDERKLRRLRSDTMIKDSSNESQEIK