wanglab/gogpt-training-data huggingface dataset:
Protein: Succinate dehydrogenase [ubiquinone] flavoprotein subunit 2, mitochondrial (EC 1.3.5.1) (Flavoprotein subunit 2 of complex II) (FP) (Q9ZPX5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Flavoprotein (FP) subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q).
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:14671022}; Peripheral membrane protein {ECO:0000269|PubMed:14671022}; Matrix side {ECO:0000269|PubMed:14671022}.
Interaction partners:
- Succinate dehydrogenase iron-sulfur subunit 3, mitochondrial
- Succinate dehydrogenase iron-sulfur subunit 2, mitochondrial
- Succinate dehydrogenase iron-sulfur subunit 1, mitochondrial
- Fumarate hydratase 1, mitochondrial
- Succinate--CoA ligase subunit alpha-2, mitochondrial
- Succinate--CoA ligase subunit alpha-1, mitochondrial
- Fumarate hydratase 2
- Succinate--CoA ligase subunit beta, mitochondrial
- NADH dehydrogenase flavoprotein 1, mitochondrial
- NADH dehydrogenase iron-sulfur protein 1, mitochondrial
Sequence:
MWRCLRVASSSRRSESNGAFITSQLSRFFSAPPSAGDKSSYTIVDHTYDAVVVGAGGAGLRAAIGLSEHGFNTACITKLFPTRSHTVAAQGGINAALGNMSVDDWRWHMYDTVKGSDWLGDQDAIQYMCREAPKAVIELENYGLPFSRTEDGKIYQRAFGGQSLEFGIGGQAYRCACAADRTGHALLHTLYGQAMKHNTQFFVEYFALDLIMNSDGTCQGVIALNMEDGTLHRFHAGSTILATGGYGRAYFSATSAHTCTGDGNAMVARAGLPLQDLEFVQFHPTGIYGAGCLITEGARGEGGILRNSEGEKFMDRYAPTARDLASRDVVSRSMTMEIRQGRGAGPMKDYLYLYLNHLPPEVLKERLPGISETAAIFAGVDVTREPIPVLPTVHYNMGGIPTNYHGEVITLRGDDPDAVVPGLMAAGEAACASVHGANRLGANSLLDIVVFGRACANRVAEIQKPGEKLKPLEKDAGEKSIEWLDRIRNSNGSLPTSKIRLNMQRVMQNNAAVFRTQETLEEGCDLIDKTWDSFGDVKVTDRSMIWNSDLIETMELENLLVNACITMHSAEARKESRGAHAREDFTKRDDANWMKHTLGYWEEGNVKLEYRPVHMKTLDDEVDTFPPKPRVY
Protein: Uncharacterized protein Rv2325c (P9WPI7)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Uncharacterized ABC transporter ATP-binding protein Rv2326c
- UPF0102 protein Rv2898c
- Probable dipeptide-transport ATP-binding protein ABC transporter DppD
- Uncharacterized protein
- Probable export or membrane protein
- Integral membrane protein
- Conserved protein
- Conserved protein
- Probable multidrug-efflux transporter Rv1634
- Cobalamin biosynthesis protein CobIJ
Sequence:
MTTTSAPARNGTRRPSRPIVLLIPVPGSSVIHDLWAGTKLLVVFGISVLLTFYPGWVTIGMMAALVLAAARIAHIPRGALPSVPRWLWIVLAIGFLTAALAGGTPVVAVGGVQLGLGGALHFLRITALSVVLLALGAMVSWTTNVAEISPAVATLGRPFRVLRIPVDEWAVALALALRAFPMLIDEFQVLYAARRLRPKRMPPSRKARRQRHARELIDLLAAAITVTLRRADEMGDAITARGGTGQLSAHPGRPKLADWVTLAITAMASGTAVAIESLILHS
Protein: Epithelial cell adhesion molecule (Ep-CAM) (Epithelial glycoprotein 314) (EGP314) (Protein D5.7A) (Tumor-associated calcium signal transducer 1) (CD antigen CD326) (O55159)
Organism: Rattus norvegicus (Rat)
Function: May act as a physical homophilic interaction molecule between intestinal epithelial cells (IECs) and intraepithelial lymphocytes (IELs) at the mucosal epithelium for providing immunological barrier as a first line of defense against mucosal infection. Plays a role in embryonic stem cells proliferation and differentiation. Up-regulates the expression of FABP5, MYC and cyclins A and E (By similarity).
Subcellular location: Lateral cell membrane {ECO:0000269|PubMed:16054130}; Single-pass type I membrane protein {ECO:0000269|PubMed:16054130}. Cell junction, tight junction {ECO:0000269|PubMed:16054130}. Note=Colocalizes with CLDN7 at the lateral cell membrane and tight junction. {ECO:0000269|PubMed:16054130}.
Interaction partners:
- Claudin-7
- CD44 antigen
- Signal transducer CD24
- Receptor protein-tyrosine kinase
- Mucin-1
- Tetraspanin
- Cadherin-1
- Keratin, type I cytoskeletal 19
- CD9 antigen
- Prominin 1
Sequence:
MAPPKALAFGLLLAVVTATLAAAQKDCVCNNYKLTSRCYENENGECQCTSYGTQNTVICSKLASKCLVMKAEMTHSKSGRRMKPEGAIQNNDGLYDPECDEQGLFKAKQCNGTATCWCVNTAGVRRTDKDTEITCSERVRTYWIIIELKHKERAQPYNFESLHTALQDTFASRYMLNPKFIKSIMYENNVITIDLMQNSSQKTQDDVDIADVAYYFEKDVKGESLFHSSKSMDLRVNGELLDLDPGQTLIYYVDEKAPEFSMQGLTAGIIAVIVVVVLAVIAGIVVLVISTRKRSAKYEKAEIKEMGEIHRELNA
Protein: Tyrosine-protein phosphatase non-receptor type 21 (EC 3.1.3.48) (Protein-tyrosine phosphatase 2E) (Q62728)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250}.
Interaction partners:
Sequence:
MPLPFGLKLKRTRRYTVSSKSCLVARIQLLNNEFVEFTLSVESTGQESLEAVAQRLELREITYFSLWYYNKQNQRRWVDLEKPLKKQLDKHALEPTVYFGVVFYVPSVSQLQQEITRYQYYLQLKKDVLEGNLPCTLEQAIQLAGLAVQADFGDFDQYESQDFLQKFALLPVGWLQDEKLLEEAAQKVALLHQKYRGLTAPEAEMLYMQEVERMDGYGEESYPAKDSQGSDISIGACLDGIFVKHKNGRPPVVFRWHDIANMSHNKSFFALELANKEETIQFQTEDMETAKYVWRLCVARHKFYRLNQCNLQTQAATLNSVRRGSSSRMSLPKPQPYAMPPPPQLHYNGHYTEPFASSQDNVFVPNKNGFYCHSQTSLDRTQIDLSGRIRNGSVYSAHSTNSLNTPQPYLQPSPMSSNPSIPGSDVMRPDYIPSHRHSALIPPSYRPTPDYESVMKRLNRGMVHADRHSHSLRNLNIGSSYAYSRPDALVYSQPEIREHPHLASPQSAHYPFNLNYSFHSQAPYPYPVERRPVVGAVSVPELTNVQLQAQDYPAPNIMRTQVYRPPPPYPYPRPANSTPDLSRHLYISSSNPDLITRRVHHSVQTFQEDSLPVAHSLQEVSEPLTAARHAHLQKRNSIEIAGLTHGFEGLRLKEETMSASAADVAPRTFSAGSQSSVFSDKVKQEGTEEQGSGGYSHKKSLSDATMLIHSSEEDEDLEDDSSREHAVSEPRLTAAFSQEQQLNYPCASVTPVTGPLHIFEPKSHVTEPEKRAKDISPVHLVMETHQPRRHGLLTPSMSESDLTTSGRYRARRDSLKKRPVSDLLSGKKNTVEGLPPLGGMKKTRADAKKIGPLKLAALNGLSLSRLPLPDEGKEVSTRATNDERCKVLEQRLEQGTVFTEYERILKKRLVDGECSTARLPENAERNRFQDVLPYDDARVELVPTKENNTGYINASHIKVSVSGIEWDYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPRLGSRHNTVTYGRFKITTRFRTDSGCYATTGLKMKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYLEEIQSVRRHTNSTSEPRSPNPPLLVHCSAGVGRTGVVILSEIMVACLEHNEVLDIPRVLELLRQQRMMLVQTLSQYTFVYRVLIQFLKSSRLI
Protein: Keratin-associated protein 1-5 (High sulfur keratin-associated protein 1.5) (Keratin-associated protein 1.5) (Q9BYS1)
Organism: Homo sapiens (Human)
Function: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high-sulfur and high-glycine-tyrosine keratins.
Interaction partners:
- Keratin-associated protein 3-1
- Keratin-associated protein 1-1
- Keratin-associated protein 9-4
- Keratin-associated protein 3-2
- Keratin-associated protein 9-8
- Keratin, type I cuticular Ha4
- Keratin-associated protein 1-3
- Keratin-associated protein 4-8
- Keratin-associated protein 4-3
Sequence:
MTCCQTSFCGYPSFSISGTCGSSCCQPSCCETSCCQPRSCQTSFCGFPSFSTSGTCSSSCCQPSCCETSCCQPSCCETSCCQPSCCQISSCGTGCGIGGGISYGQEGSSGAVSTRIRWCRPDSRVEGTYLPPCCVVSCTPPSCCQLHHAQASCCRPSYCGQSCCRPVCCCEPTC
Protein: GrpE protein homolog 2, mitochondrial (Mt-GrpE#2) (Q8TAA5)
Organism: Homo sapiens (Human)
Function: Essential component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner. Seems to control the nucleotide-dependent binding of mitochondrial HSP70 to substrate proteins. Stimulates ATPase activity of mt-HSP70. May also serve to modulate the interconversion of oligomeric (inactive) and monomeric (active) forms of mt-HSP70 (By similarity).
Subcellular location: Mitochondrion matrix {ECO:0000250}.
Interaction partners:
- Stress-70 protein, mitochondrial
- 10 kDa heat shock protein, mitochondrial
- Mitochondrial disaggregase
- Mitochondrial import inner membrane translocase subunit TIM44
- Cytochrome c oxidase subunit 5B, mitochondrial
- 60 kDa heat shock protein, mitochondrial
- DnaJ homolog subfamily A member 3, mitochondrial
- Oxidoreductase-like domain-containing protein 1
- Mitochondrial import inner membrane translocase subunit TIM16
- Heat shock 70 kDa protein 12A
Sequence:
MAVRSLWAGRLRVQRLLAWSAAWESKGWPLPFSTATQRTAGEDCRSEDPPDELGPPLAERALRVKAVKLEKEVQDLTVRYQRAIADCENIRRRTQRCVEDAKIFGIQSFCKDLVEVADILEKTTECISEESEPEDQKLTLEKVFRGLLLLEAKLKSVFAKHGLEKLTPIGDKYDPHEHELICHVPAGVGVQPGTVALVRQDGYKLHGRTIRLARVEVAVESQRRL
Protein: Endoplasmic reticulum lectin 1 (ER lectin) (Erlectin) (XTP3-transactivated gene B protein) (Q96DZ1)
Organism: Homo sapiens (Human)
Function: Probable lectin that binds selectively to improperly folded lumenal proteins. May function in endoplasmic reticulum quality control and endoplasmic reticulum-associated degradation (ERAD) of both non-glycosylated proteins and glycoproteins.
Subcellular location: Endoplasmic reticulum lumen {ECO:0000269|PubMed:16531414, ECO:0000269|PubMed:18502753}.
Interaction partners:
- Protein sel-1 homolog 1
- E3 ubiquitin-protein ligase synoviolin
- Derlin-2
- Derlin-1
- Derlin-3
- Calnexin
- Protein OS-9
- E3 ubiquitin-protein ligase AMFR
- Endoplasmin
- Ubiquitin-conjugating enzyme E2 J1
Sequence:
MEEGGGGVRSLVPGGPVLLVLCGLLEASGGGRALPQLSDDIPFRVNWPGTEFSLPTTGVLYKEDNYVIMTTAHKEKYKCILPLVTSGDEEEEKDYKGPNPRELLEPLFKQSSCSYRIESYWTYEVCHGKHIRQYHEEKETGQKINIHEYYLGNMLAKNLLFEKEREAEEKEKSNEIPTKNIEGQMTPYYPVGMGNGTPCSLKQNRPRSSTVMYICHPESKHEILSVAEVTTCEYEVVILTPLLCSHPKYRFRASPVNDIFCQSLPGSPFKPLTLRQLEQQEEILRVPFRRNKEEDLQSTKEERFPAIHKSIAIGSQPVLTVGTTHISKLTDDQLIKEFLSGSYCFRGGVGWWKYEFCYGKHVHQYHEDKDSGKTSVVVGTWNQEEHIEWAKKNTARAYHLQDDGTQTVRMVSHFYGNGDICDITDKPRQVTVKLKCKESDSPHAVTVYMLEPHSCQYILGVESPVICKILDTADENGLLSLPN
Protein: Replication termination factor 2 (Q388D9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MGGDGQALSNKRRILEKSRVFLTADELRKGDNGGGETTRKLKEEKVLRWSHCGLSLEPLQLPVVFDLYGRLYSKKAVLDNILEKRSLHKQSSSDLNSDMKISKLSDVCEVSNVEEGKDRKVLIRCPVTGYDSASGLHQFLGFWSCGHVVACAAVNESVGKPAAAKKDCPVDDDPASVCPFCGATSFAVHLILDQESDEVKQYRRLRSLHRVFRKRGRSNT
Protein: Neurofascin (O94856)
Organism: Homo sapiens (Human)
Function: Cell adhesion, ankyrin-binding protein which may be involved in neurite extension, axonal guidance, synaptogenesis, myelination and neuron-glial cell interactions.
Subcellular location: Cell membrane {ECO:0000269|PubMed:30850329}; Single-pass type I membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Isoform 8]: Cell junction, paranodal septate junction {ECO:0000269|PubMed:30124836}.
Interaction partners:
- Contactin-associated protein 1
- Gliomedin
- Contactin-1
- Ankyrin-3
- Ankyrin-1
- Neuronal cell adhesion molecule
- Ankyrin-2
- Spectrin beta chain, non-erythrocytic 4
- Syntenin-1
- Sodium channel protein type 8 subunit alpha
Sequence:
MARQPPPPWVHAAFLLCLLSLGGAIEIPMDPSIQNELTQPPTITKQSAKDHIVDPRDNILIECEAKGNPAPSFHWTRNSRFFNIAKDPRVSMRRRSGTLVIDFRSGGRPEEYEGEYQCFARNKFGTALSNRIRLQVSKSPLWPKENLDPVVVQEGAPLTLQCNPPPGLPSPVIFWMSSSMEPITQDKRVSQGHNGDLYFSNVMLQDMQTDYSCNARFHFTHTIQQKNPFTLKVLTTRGVAERTPSFMYPQGTASSQMVLRGMDLLLECIASGVPTPDIAWYKKGGDLPSDKAKFENFNKALRITNVSEEDSGEYFCLASNKMGSIRHTISVRVKAAPYWLDEPKNLILAPGEDGRLVCRANGNPKPTVQWMVNGEPLQSAPPNPNREVAGDTIIFRDTQISSRAVYQCNTSNEHGYLLANAFVSVLDVPPRMLSPRNQLIRVILYNRTRLDCPFFGSPIPTLRWFKNGQGSNLDGGNYHVYENGSLEIKMIRKEDQGIYTCVATNILGKAENQVRLEVKDPTRIYRMPEDQVARRGTTVQLECRVKHDPSLKLTVSWLKDDEPLYIGNRMKKEDDSLTIFGVAERDQGSYTCVASTELDQDLAKAYLTVLADQATPTNRLAALPKGRPDRPRDLELTDLAERSVRLTWIPGDANNSPITDYVVQFEEDQFQPGVWHDHSKYPGSVNSAVLRLSPYVNYQFRVIAINEVGSSHPSLPSERYRTSGAPPESNPGDVKGEGTRKNNMEITWTPMNATSAFGPNLRYIVKWRRRETREAWNNVTVWGSRYVVGQTPVYVPYEIRVQAENDFGKGPEPESVIGYSGEDYPRAAPTEVKVRVMNSTAISLQWNRVYSDTVQGQLREYRAYYWRESSLLKNLWVSQKRQQASFPGDRLRGVVSRLFPYSNYKLEMVVVNGRGDGPRSETKEFTTPEGVPSAPRRFRVRQPNLETINLEWDHPEHPNGIMIGYTLKYVAFNGTKVGKQIVENFSPNQTKFTVQRTDPVSRYRFTLSARTQVGSGEAVTEESPAPPNEATPTAAPPTLPPTTVGATGAVSSTDATAIAATTEATTVPIIPTVAPTTIATTTTVATTTTTTAAATTTTESPPTTTSGTKIHESAPDEQSIWNVTVLPNSKWANITWKHNFGPGTDFVVEYIDSNHTKKTVPVKAQAQPIQLTDLYPGMTYTLRVYSRDNEGISSTVITFMTSTAYTNNQADIATQGWFIGLMCAIALLVLILLIVCFIKRSRGGKYPVREKKDVPLGPEDPKEEDGSFDYSDEDNKPLQGSQTSLDGTIKQQESDDSLVDYGEGGEGQFNEDGSFIGQYTVKKDKEETEGNESSEATSPVNAIYSLA
Protein: Calpastatin (Calpain inhibitor) (H0YA91)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
XAARRTHEHVSEKTSESPSKPGEKKGSDEKKAASLGSSQSSRTYAGGTASATKVSASSGATSKSSSMNPTETKAVKTEPEKKSQSTKLSVVHEKKSQEGKPKEHTEPKSLPKQASDTGSNDAHNKKAVSRSAEQQPSEKSTEPKKKEKKSLTPAVPVESKPDKPSGKSGMDAALDDLIDTLGGPEETEEENTTYTGPEVSDPMSSTYIEELGKREVTIPPKYRELLAKKEGITGPPADSSKPIGPDDAIDALSSDFTCGSPTAAGKKTEKEESTEVLKAQSAGTVRSAAPPQEKKRKVEKV
Protein: Isopenicillin-N N-acyltransferase (IAT) (IPN acyltransferase) (EC 2.3.1.164) (Acyl-coenzyme A:6-aminopenicillanic-acid-acyltransferase 40 kDa form) (Penicillin biosynthetis cluster protein aatA) [Cleaved into: Acyl-coenzyme A:6-aminopenicillanic acid acyltransferase 11 kDa subunit; Acyl-coenzyme A:6-aminopenicillanic acid acyltransferase 29 kDa subunit] (P15802)
Organism: Penicillium chrysogenum (Penicillium notatum)
Function: Isopenicillin-N N-acyltransferase; part of the gene cluster that mediates the biosynthesis of penicillin, the world's most important antibiotic. AatA catalyzes the exchange of the alpha-aminoadipyl side chain of isopenicillin N for phenylacetic acid to yield penicillin. This step occurs in the peroxisomal matrix and the penM and paaT transporters are involved in the isopenicillin N and phenylacetic acid import into the peroxisome, respectively. The penicillin biosynthesis occurs via 3 enzymatic steps, the first corresponding to the production of the tripeptide N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine (LLD-ACV or ACV) by the NRPS acvA. The tripeptide ACV is then cyclized to isopenicillin N (IPN) by the isopenicillin N synthase ipnA that forms the beta-lactam nucleus. Finally, the alpha-aminoadipyl side chain is exchanged for phenylacetic acid by the isopenicillin N acyltransferase aatA to yield penicillin in the peroxisomal matrix (Probable).
Subcellular location: Peroxisome matrix {ECO:0000269|PubMed:18439860}. Note=The unprocessed preprotein is translocated inside peroxisomes and regulates its self-processing. {ECO:0000269|PubMed:18439860}.
Interaction partners:
Sequence:
MLHILCQGTPFEIGYEHGSAAKAVIARSIDFAVDLIRGKTKKTDEELKQVLSQLGRVIEERWPKYYEEIRGIAKGAERDVSEIVMLNTRTEFAYGLKAARDGCTTAYCQLPNGALQGQNWDFFSATKENLIRLTIRQAGLPTIKFITEAGIIGKVGFNSAGVAVNYNALHLQGLRPTGVPSHIALRIALESTSPSQAYDRIVEQGGMAASAFIMVGNGHEAFGLEFSPTSIRKQVLDANGRMVHTNHCLLQHGKNEKELDPLPDSWNRHQRMEFLLDGFDGTKQAFAQLWADEDNYPFSICRAYEEGKSRGATLFNIIYDHARREATVRLGRPTNPDEMFVMRFDEEDERSALNARL
Protein: Sorbin and SH3 domain-containing protein 1 homolog (G5EC32)
Organism: Caenorhabditis elegans
Function: Required for organization of sarcomeres in body wall muscles and for maintaining normal mitochondrial position in myocytes.
Subcellular location: Cell junction, adherens junction {ECO:0000269|PubMed:28978740}. Cell membrane {ECO:0000269|PubMed:28978740}. Cell junction, focal adhesion {ECO:0000269|PubMed:28978740}. Note=Localizes to adhesion plaques and dense bodies between myocytes (PubMed:28978740). Co-localizes with deb-1 and atn-1 at dense bodies (PubMed:28978740). Predominantly localizes to the membrane-proximal region of dense bodies (PubMed:28978740). {ECO:0000269|PubMed:28978740}.
Interaction partners:
- Vinculin
- GTP cyclohydrolase 1
- FERM domain-containing protein
- Integrin beta pat-3
- Paxillin homolog 1
- PDZ and LIM domain protein Zasp
- E3 ubiquitin-protein ligase CBL
Sequence:
MMHHPHPFGSNLANSSEPQQPSGQYLNPAADAYNFDTFEDSDKFSPKGNVAALRNVIHGQLDMKTPTGNSSRYQKPAPPPVDSTPSWAKNVKVYEPNGYVDPHLNKHNMGRVLDGPVNPNKYFQGVPPASYSQVKHNESKPPVPPSTKPPHSAAQALQAQVLQSSKAPSQPQQSQKTSYRIPYDVALDPRHHLGEFDIDDSASIISSCISTFGESSEIAGFSAAAEQRHLYEQYRKKLMEEKNELKEGSETPCVSLSEKVMTSSTENLKNGNNQQNQQPEPQPPSSSIFNSELTPFGHVAPVAKQFEPTNFPPFSPEKESEIKRSIDLESSQLLVKSKSPAPYSTSSTDHYGTIRRKHKPVAIDLSKSSPNLASQSPSNLFFGASFEEKQNRSPMTSTPSYKEQGFKNDSLNDSLNQAFEIASSIETTKNAYEAPPTPKSASHDRSISDTYPVSSSTTSTWPSHTTTPTTTTAAAPIAAVAPQTYTEQQPMSTSMSSSVMSTNMDEPIVVGSHQQIPQQSPDSSPERNEDMSQWYRKMFKQMHRKGEDGSNEGKEQHFINPSNVTDGIGRTTPTASNLGRSRENLSFNQHRPDHPSSYFDSLEHGPNDQYNNQERVKQSNEEELLRLKAEKLAEELRKEKERKHSFIPSSAPSLQNNMDRLNSLLYDFSSDIQEPAHRDYTPQPVMTATAVYKFEPRSARELPLNRGDIIRIIREVDGYWMEGERNGRSGIFPTSYVQINTGNQGDSQKMRAIYPFTARSDTELSLKRGEIITRRRQIDSNWLEGSNQIGIVGIFPASYVEPIEQVEQHIPTIVPNRPKTPKIEDQVYNQVYKPNETVIMQSNQGYYDKAAVVPNNKVRFDLPSGSDSNLQMSLNPHQNQFPPTHTQTSTQQPSNYGMKKIEYEREKVVEEVPPMHMDQYRKLNDEPKNPKKDTNILMNAASLIPKGSEMYRAVYPYQPQKEDELQLYTNDIIFVVEKCDDGWFIGTSLRTGDFGIFPGNYVKRH
Protein: Histocompatibility 2, Q region locus 1 (Major histocompability complex Q1b) (O19441)
Organism: Mus musculus (Mouse)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
- Killer cell lectin-like receptor subfamily C, member 1
- Natural killer cells antigen CD94
- Beta-2-microglobulin
- H-2 class II histocompatibility antigen, A-B alpha chain
- H-2 class II histocompatibility antigen, E-B beta chain
- Tapasin
- Class II histocompatibility antigen, M alpha chain
- H-2 class II histocompatibility antigen gamma chain
- T-cell surface glycoprotein CD8 alpha chain
- H2-O alpha
Sequence:
MALGRLLLLLAAALTLTKTGAGSHSLRYFETSVSRPGFGKPRFISVGYVDDTQFVRFDSDAKNPRYEPRAPWMEQEGPEYWERNTRRVKGSEKRFQESLSTLLSYYNQSKGGIHTFQKLSGCDLGSDGRLQSGYLQFAYDGLDYIALNEDLETWTAADVAAQETRRKWEQAGAAEKHRTYLEGKCLMWLHRYLELGKEMLLRTDPPKAHVTHHPRSQGDVTLRCWALGFYPADITLTWQLNGEELTQDMELVETRPAGDGTFQKWASVVVPLGKEQNYTCHVYHEGLPEPLTLRWEPPPYTVSNMVIIAVLVVLGAVIVIGAVVIIGVMVSFVMKRRRNKGGQGEDCALAPSRDSAQSSDISLLDCKA
Protein: Large ribosomal subunit protein uL22z (60S ribosomal protein L17-1) (Q93VI3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Large ribosomal subunit protein uL18y
- Large ribosomal subunit protein eL13x
- Large ribosomal subunit protein eL31x
- Large ribosomal subunit protein uL6x
- Large ribosomal subunit protein eL38z/eL38y
- Large ribosomal subunit protein eL28y
- Large ribosomal subunit protein eL29y
- Large ribosomal subunit protein eL8y
- Large ribosomal subunit protein uL1z
- Small ribosomal subunit protein uS14z/uS14y/uS14x
Sequence:
MVKYSQEPDNITKSCKARGADLRVHFKNTRETAHAIRKLPLNKAKRYLEDVIAHKQAIPFTRFCRGVGRTAQAKNRHSNGQGRWPAKSAQFVLDLLKNAESNAEVKGLDVDALFISHIQVNQAAKQRRRTYRAHGRINPYMSNPCHIELILSEKEEPVKKEPETQLAAKSKKGASS
Protein: Beta-nerve growth factor (Beta-NGF) (P01138)
Organism: Homo sapiens (Human)
Function: Nerve growth factor is important for the development and maintenance of the sympathetic and sensory nervous systems. Extracellular ligand for the NTRK1 and NGFR receptors, activates cellular signaling cascades to regulate neuronal proliferation, differentiation and survival (Probable). The immature NGF precursor (proNGF) functions as ligand for the heterodimeric receptor formed by SORCS2 and NGFR, and activates cellular signaling cascades that lead to inactivation of RAC1 and/or RAC2, reorganization of the actin cytoskeleton and neuronal growth cone collapse. In contrast to mature NGF, the precursor form (proNGF) promotes neuronal apoptosis (in vitro) (By similarity). Inhibits metalloproteinase-dependent proteolysis of platelet glycoprotein VI. Binds lysophosphatidylinositol and lysophosphatidylserine between the two chains of the homodimer. The lipid-bound form promotes histamine relase from mast cells, contrary to the lipid-free form (By similarity).
Subcellular location: Secreted {ECO:0000269|PubMed:20978020}. Endosome lumen {ECO:0000250|UniProtKB:P01139}. Note=ProNGF is endocytosed after binding to the cell surface receptor formed by SORT1 and NGFR. {ECO:0000250|UniProtKB:P01139}.
Interaction partners:
- BDNF/NT-3 growth factors receptor
- High affinity nerve growth factor receptor
- Tumor necrosis factor receptor superfamily member 16
- NT-3 growth factor receptor
- Sortilin
- GDNF family receptor alpha-1
- VPS10 domain-containing receptor SorCS2
- Glial cell line-derived neurotrophic factor
- Neurotrophin-4
- Transient receptor potential cation channel subfamily A member 1
Sequence:
MSMLFYTLITAFLIGIQAEPHSESNVPAGHTIPQAHWTKLQHSLDTALRRARSAPAAAIAARVAGQTRNITVDPRLFKKRRLRSPRVLFSTQPPREAADTQDLDFEVGGAAPFNRTHRSKRSSSHPIFHRGEFSVCDSVSVWVGDKTTATDIKGKEVMVLGEVNINNSVFKQYFFETKCRDPNPVDSGCRGIDSKHWNSYCTTTHTFVKALTMDGKQAAWRFIRIDTACVCVLSRKAVRRA
Protein: Dipeptidyl aminopeptidase A (DPAP A) (EC 3.4.14.-) (YSCIV) (P33894)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Responsible for the proteolytic maturation of the alpha-factor precursor.
Subcellular location: Vacuole membrane; Single-pass type II membrane protein. Note=Lysosome-like vacuoles.
Interaction partners:
- Kexin
- Intermediate cleaving peptidase 55
- Pheromone-processing carboxypeptidase KEX1
- Vacuolar protein sorting/targeting protein VPS10
- Sorting nexin-3
- Mating factor alpha-1
- Protein-S-isoprenylcysteine O-methyltransferase
- Mating factor alpha-2
- Putative protease AXL1
Sequence:
MSASTHSHKRKNSHLFPQRKSSNSSMDKPFFPNNDSVANTDPQSNENGHTINEIRPTEATIDVTDVPQTPFLQEQYSMRPRRESFQFNDIENQHHTHSFFSVNKFNRRWGEWSLPEKRSYVLVFTLIALSVLVLLVILIPSKLLPTKITRPKTSAGDSSLGKRSFSIENVLNGDFAIPEDTFHFIDPPQRLLGQDSDPGLYFTTKEIDGHTNFIAKQLFDETFEVNLGGNRFLYEGVEFTVSTVQINYKLDKLIFGTNLESEFRHSSKGFYWIKDLNTGNIEPILPPEKSDDNYELGLSKLSYAHFSPAYNYIYFVYENNLFLQQVNSGVAKKVTEDGSKDIFNAKPDWIYEEEVLASDQAIWWAPDDSKAVFARFNDTSVDDIRLNRYTNMNEAYLSDTKIKYPKPGFQNPQFDLFLVNLQNGIIYSINTGGQKDSILYNGKWISPDTFRFEITDRNSKILDVKVYDIPSSQMLTVRNTNSNLFNGWIEKTKDILSIPPKPELKRMDYGYIDIHADSRGFSHLFYYPTVFAKEPIQLTKGNWEVTGNGIVGYEYETDTIFFTANEIGVMSQHLYSISLTDSTTQNTFQSLQNPSDKYDFYDFELSSSARYAISKKLGPDTPIKVAGPLTRVLNVAEIHDDSILQLTKDEKFKEKIKNYDLPITSYKTMVLDDGVEINYIEIKPANLNPKKKYPILVNIYGGPGSQTFTTKSSLAFEQAVVSGLDVIVLQIEPRGTGGKGWSFRSWAREKLGYWEPRDITEVTKKFIQRNSQHIDESKIAIWGWSYGGFTSLKTVELDNGDTFKYAMAVAPVTNWTLYDSVYTERYMNQPSENHEGYFEVSTIQNFKSFESLKRLFIVHGTFDDNVHIQNTFRLVDQLNLLGLTNYDMHIFPDSDHSIRYHNAQRIVFQKLYYWLRDAFAERFDNTEVLHL
Protein: Outer surface protein C (pC) (P23) (Q07337)
Organism: Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31) (Borrelia burgdorferi)
Function: A major immunodominant protein in mammalian hosts. Required for the initial stages of mammalian infection. Interaction with tick I.ricinus salivary protein Salp15 protects the bacteria from antibody-mediated killing in vitro and in vivo. Inhibits macrophage-mediated phagocytosis of the bacteria. Binds human plasminogen; this probably confers an extracellular protease activity on the bacteria that allows it to traverse tissue. Binds human complement C4-B, which may inhibit the complement cascade (Probable). Experiments in mice suggest it may play another role after initial infection (Probable).
Subcellular location: Cell outer membrane; Lipid-anchor. Cell surface {ECO:0000269|PubMed:20199597, ECO:0000269|PubMed:22433849, ECO:0000269|PubMed:28873507, ECO:0000269|PubMed:8225587}. Note=Expressed in a punctate fashion on a subset of cells in vitro. {ECO:0000269|PubMed:22433849}.
Interaction partners:
Sequence:
MKKNTLSAILMTLFLFISCNNSGKDGNTSANSADESVKGPNLTEISKKITDSNAVLLAVKEVEALLSSIDEIAAKAIGKKIHQNNGLDTENNHNGSLLAGAYAISTLIKQKLDGLKNEGLKEKIDAAKKCSETFTNKLKEKHTDLGKEGVTDADAKEAILKTNGTKTKGAEELGKLFESVEVLSKAAKEMLANSVKELTSPVVAESPKKP
Protein: Glucosylceramidase (EC 3.2.1.45) (Q8IMY3)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Putative neutral sphingomyelinase
- ceramide glucosyltransferase
- Beta galactosidase, isoform A
- Beta-galactosidase
- Non-lysosomal glucosylceramidase
- Glucosylceramidase
- BcDNA.GH08312
- Sphingomyelin phosphodiesterase
- Ceramide kinase, isoform A
- Alkaline ceramidase
Sequence:
MPDMKTPLLGFLTTVIAISAGAPDWQLPCDLRETSHGSVCVCNSTYCDYLEPPQLTDISQIVVISSSKDGLRFKKTTGDLSKKKPITIDDKQFTDENFKADAIVVDQERAWLQLANIPQSLFINASIKTYRIFVKREQSFQNVSIFGGAFTGTVSYLLKELPVELQDHVYRSYFHPVGIAYNTIRMSIGGSDFDMEPWAYNELPLHDPKLSNFTELDPRDLQKVEQLKRLKIIGKVDSLKIMGAAWSAPTWMKSNNRWTGFGQLKSEYYQTWALYHLKFLELMRSKNMPIWAISTGNEPLNGVIGFFFVHFMSMGWTPWQQAIWLNDNLGPTIRNSAESKVLIFGNDDQRYTYPTWFRKMRSSRNNSLNYLDGLAVHWYWDELIGPQLIDQAHTDMPNKLLLNTESCIGDKPWQTHGPELGSWQRGESYMRAYTQDLTHNFNGWLDWNLVLDEQGGPNYVKNFVDAPIIVNATSRSEIYKQPIFYAIGHFSKFLPPDSVRIETRIENQSNPFTQLSVVGFQRPDGSVALIIYNGQNLPVDVTLDDSQRGAIQLRLPPRSWHTVLYK
Protein: C2H2-type domain-containing protein (Q387I5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSLQCEGDGAVCYTCGHFDFLPLKCNHCGNMFCGEHIKNHNIPGSEEACAAAYLGRVLPVTSMVQEGATEPRHACAICGSPLCVLIPCDLCQRDFCAIHRFHEHSDNHGERRRVQGTNGHDTTPFPKDVEEAFAHICGRYSPGRPLVLQPPAFRGTMLPVTALMCEVDDTGGTIKAVAVISLSVAAEMSVGQLLDRCTVSLVLPPSHLLKQPMFHISFSDRAVVDQIPLSLSASKADLSNRDVLLVVQQRGDPTEESERGVSDQVGKVTVSVEALENALTQLLSLALSDGLRPGSRLHSAASRIRLRSLGTKASKRGTSPPSQELSQSGQLPHCECTNRVKVSSVSDREVVRIGTHQQCDIGGTPWPFLRPPPLDEFIFSHTRMNPRRAAPKEPPSASIIVAVFVADCQLSREVAPFCISLNKELSIGRALDIIREIVDEVAGPRPGPGWNLFNLTTGELLTVPPLSSRSDLRDRDILFFGEVFSEALRAEVVRLREVKGKPLMALKMKMMKSCALM