wanglab/gogpt-training-data huggingface dataset:
Protein: Sorting nexin-20 (Selectin ligand-interactor cytoplasmic 1) (SLIC-1) (Q7Z614)
Organism: Homo sapiens (Human)
Function: May play a role in cellular vesicle trafficking. Has been proposed to function as a sorting protein that targets SELPLG into endosomes, but has no effect on SELPLG internalization from the cell surface, or on SELPLG-mediated cell-cell adhesion.
Subcellular location: Early endosome membrane {ECO:0000269|PubMed:18196517}; Peripheral membrane protein {ECO:0000269|PubMed:18196517}; Cytoplasmic side {ECO:0000269|PubMed:18196517}. Cell membrane {ECO:0000269|PubMed:18196517}. Cytoplasm {ECO:0000269|PubMed:18196517}. Nucleus {ECO:0000269|PubMed:18196517}.
Interaction partners:
- P-selectin glycoprotein ligand 1
- Headcase protein homolog
Sequence:
MASPEHPGSPGCMGPITQCTARTQQEAPATGPDLPHPGPDGHLDTHSGLSSNSSMTTRELQQYWQNQKCRWKHVKLLFEIASARIEERKVSKFVVYQIIVIQTGSFDNNKAVLERRYSDFAKLQKALLKTFREEIEDVEFPRKHLTGNFAEEMICERRRALQEYLGLLYAIRCVRRSREFLDFLTRPELREAFGCLRAGQYPRALELLLRVLPLQEKLTAHCPAAAVPALCAVLLCHRDLDRPAEAFAAGERALQRLQAREGHRYYAPLLDAMVRLAYALGKDFVTLQERLEESQLRRPTPRGITLKELTVREYLH
Protein: Viral late gene transcription factor 3 (VLTF-3) (Trans-activator protein A2) (P68319)
Organism: Vaccinia virus (strain Western Reserve) (VACV) (Vaccinia virus (strain WR))
Function: Acts with RNA polymerase to initiate transcription from late gene promoters.
Interaction partners:
Sequence:
MNLRLCSGCRHNGIVSEQGYEYCIFCESVFQKCTKVQKKSNFHVSNKLIHLRNVLRRLLSHQCSGEIISELLDIMEKNQISTDDVDANFVSSFLKANERINKKDYKLVFEIINQVKDEKLNLSTEKINEVVEIFKHLVFFCQENTPSKTINYSFFLDKIFDITSVTKNLKPQTVKNYTKNNSNQLVWENFLAHMRSKKRVTMVEDYGHEYVFVDERFSTCSLEV
Protein: Bcl2-associated agonist of cell death (BAD) (Bcl-2-binding component 6) (Bcl-xL/Bcl-2-associated death promoter) (Bcl2 antagonist of cell death) (O35147)
Organism: Rattus norvegicus (Rat)
Function: Promotes cell death. Successfully competes for the binding to Bcl-X(L), Bcl-2 and Bcl-W, thereby affecting the level of heterodimerization of these proteins with BAX. Can reverse the death repressor activity of Bcl-X(L), but not that of Bcl-2 (By similarity). Appears to act as a link between growth factor receptor signaling and the apoptotic pathways.
Subcellular location: Mitochondrion outer membrane. Cytoplasm {ECO:0000250|UniProtKB:Q61337}. Note=Colocalizes with HIF3A in the cytoplasm. Upon phosphorylation, locates to the cytoplasm. {ECO:0000250|UniProtKB:Q61337}.
Interaction partners:
- Bcl-2-like protein 1
- Apoptosis regulator Bcl-2
- RAC-alpha serine/threonine-protein kinase
- 14-3-3 protein zeta/delta
- 14-3-3 protein theta
- 14-3-3 protein beta/alpha
- 14-3-3 protein epsilon
- RAF proto-oncogene serine/threonine-protein kinase
- RAC-beta serine/threonine-protein kinase
- RAC-gamma serine/threonine-protein kinase
Sequence:
MGTPKQPSLAPAHALGLRKSDPGIRSLGSDAGGRRWRPAAQSMFQIPEFEPSEQEDASTTDRGLGPSLTEDQPGPYLAPGLLGSIVQQQPGQAANNSHHGGAGTMETRSRHSSYPAGTEEDEGMEEELSPFRGRSRSAPPNLWAAQRYGRELRRMSDEFEGSFKGLPRPKSAGTATQMRQSASWTRIIQSWWDRNLGKGGSTPSQ
Protein: Cystatin-C (Cystatin-3) (P21460)
Organism: Mus musculus (Mouse)
Function: As an inhibitor of cysteine proteinases, this protein is thought to serve an important physiological role as a local regulator of this enzyme activity.
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
- Cathepsin B
- Cathepsin S
- Hepatitis A virus cellular receptor 1 homolog
- Neutrophil gelatinase-associated lipocalin
- Amyloid-beta precursor protein
- Beta-2-microglobulin
- C-reactive protein
- Albumin
- Cathepsin D
- Transthyretin
Sequence:
MASPLRSLLFLLAVLAVAWAATPKQGPRMLGAPEEADANEEGVRRALDFAVSEYNKGSNDAYHSRAIQVVRARKQLVAGVNYFLDVEMGRTTCTKSQTNLTDCPFHDQPHLMRKALCSFQIYSVPWKGTHSLTKFSCKNA
Protein: Legumain (EC 3.4.22.34) (Protease, cysteine 1) (G1SPJ6)
Organism: Oryctolagus cuniculus (Rabbit)
Interaction partners:
- H-2 class II histocompatibility antigen gamma chain
- Cathepsin B
- Cathepsin S
- Cathepsin Z
- Dipeptidyl peptidase 1
- Cathepsin V
- Cathepsin L1
- Cathepsin L
- Cathepsin L1
- Cystatin-C
Sequence:
MIWKVATFLSVALGIDAITVGVDSPENGGKHWVVIVAGSNGWYNYRHQADACHAYQIIHRNGIPDEQIVVMMYDDIANAKDNPTPGIVINRPNGTDVYQGVPKDYTGENVTSENFLAVLRGDAEAVKGKGSGRVLKSGPRDHVFVYFTDHGATGLLVFPNDDLHVRDLNKTIQYMHKHKKYGKMVFYIEACESGSMMDHLPDDINVYATTAANPTESSYACYYDEERGTYLGDWYSVNWMEDSDVEDLTKETLHRQYQLVKSHTNTSHVMQYGNKSIASMKLMQFQGMRHRASPPVSLPPVPHLDLTPGPDVPLEILKRKLKSRANSSQYRKLSAEMHRLQNARTILEKSVSKVVLLLADSQAEAARLLSTRSPLTKHDCYEAAVTHFRTHCFNWHSSTYEYALRYLYVLVNLCEKPYPLDRIKLSLDKVCLGYY
Protein: PDZ domain-containing protein (C1P635)
Organism: Caenorhabditis elegans
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004170}.
Interaction partners:
Sequence:
MTDKTAELCLKIGDEEKDDFTLEIEKLQATLQEMLDCTSSPSTSLDSTDKLPSGLAARRLIRIASEHHHISTTSSCHSDSGNSSSRDVITPFTVHGGASIGRLILIDIVRRDDLIGIVHPNDILLTIENIKVSGMVRSEVNRILEDMMREHDQIAIEILPAGAITDDICELLADRKSSGELQTIIRENLYQKTVPYTTRPPREGEVDGEHYRFVSVDDFNKLLDSGDLLENGTYQGHLYGTPRPVECYADDDMMLMGSEGLLPPNWETAYTENGDKYFIDHNTGTTTWDDPRELPPGWEQVDDQNYGTFYVDHINRKTQYERPYGFGGSSATIDQPVKYGTLPSSTNHNHNNIYSHYNSGTLKSSSSPRDSGFDSSPTRYRKFGDPPETATSSADYDHHSKMFSRSSNPLFTTDPARLGGELISTKIVKGAKGLGFTLIGNDSSSRGDEFIQVKSVLSGGPAAANGVLRSGDILVRVNGRLLLGATQKEACDVFVAIPVNEAVDIQVCRGYELFIDPANRIVTENVYAAAKSRDLHEIDIFKGSEGFGFTIADNLNGQRIKKILFPSQCPNLMEGDTIVELDGRNVRPIPHTQLVDMLRERPIGYRGKLVVKRGSPKTRSRTPSAAFRYGEPQTNMMDSAAPLPVRSKTPAERQTSRTEEDQNVRNTLQRQPAVTSEWEGMSSAIPASRMRPSSTTLGFATPNYIPLSQYNQKPSDLITVSLIRKPVGFGFRLLGGVESKTPLSVGQIVIGGAAEEDGRLQEGDEIVEIDGHNVEGASHSEAVVLLEAAAQNKHVKLIVRRPSRTDPARRGSLNSAGPSGSYDVLLHRNENDGFGFVLMSSQHKNGSTVGQIQPGSPAARCGRLSVGDRVIAVNGIDILSLSHPDTISLIKDSGLSVRLTIAPPNTAGPVLPMVSATLGRNFTMNGHYESNYGLPPPPPSVYEKHPPPSYLAFDGLSINDRMSMINCGTSQESLLAHLRSSSVMDTYSEEMELLDMEKHLRTEI
Protein: Protein YIPF (Q9VK46)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Golgi apparatus membrane {ECO:0000256|RuleBase:RU361264}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU361264}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Yip1-interacting factor 1, isoform C
- Protein YIPF
- Transcription initiation factor IIA subunit 2
- Protein YIPF
- FI01544p
- Derlin-1
- Receptor expression-enhancing protein
- Receptor expression-enhancing protein
- poly
- Protein transport protein SEC23
Sequence:
MSQFGGPNDFYGSAPSADASYNFDMPEFGQELNFQTFDNTQASVPPNYDASYAQPPSQGLGGFYDPTAYTDTSYGQDKSGKSAAGGGAGNEFDDEPPLLEELGINPNHIFQKTLAVLNPLRGTDQQILQDTDMAGPLVFCLTLGGFLLLSGKVTFSYIYGIGVMGCIFFYCLLSLMVSRSQVTFGAVASVLGYCLLPMVVLSGINILITIQGTLGLIVSGISIFWCAISASKLFATAFSMDHQQLLIAYPCAVLYGGFALITIY
Protein: Glycine cleavage system P protein (EC 1.4.4.2) (A0A0G2JUZ5)
Organism: Rattus norvegicus (Rat)
Subcellular location: Mitochondrion {ECO:0000256|RuleBase:RU364056}.
Interaction partners:
- Glycine cleavage system H protein, mitochondrial
- Aminomethyltransferase
- Serine hydroxymethyltransferase
- Trifunctional purine biosynthetic protein adenosine-3
- Serine hydroxymethyltransferase
- Glycine cleavage system H protein
- Glycine cleavage system H protein
- Dimethylglycine dehydrogenase, mitochondrial
- Sarcosine dehydrogenase, mitochondrial
- Methylenetetrahydrofolate reductase
Sequence:
MQLCARAWGLRLGPGAGGGHRLARGTGLSWAPRSRDSSSGGGGGGGDRGAAGASRLLERLLPRHDDFARRHIGPGDKDRREMLQALGLASIDELIEKTVPASIRLKRPLKLEDPVCENEILETLHAIASKNQIWRSYIGMGYYNCSVPQTILRNLLENSGWVTQYTPYQPEVSQGRLESLLNYQTMVSDITGLDMANASLLDEATAAAEAMQLCHRHNKRKRFFIDPRCHPQTIAVVQTRAKYRGVIVELKLPHEMDFSGKDVSGVLFQYPDTEGKVEDFTELVERAHQTGSLTCCATDLLALCILRPPGEFGVDIALGNSQRFGVPLGYGGPHAAFFAVRESLVRMMPGRMVGVTRDATGKEVYRLALQTREQHIRRDKATSNICTAQALLANMAAMFAIYHGSHGLQHIAKRVHNATLILSEGLKRAGHQLQHDLFFDTLKVQCGCSLKEVLGRAAQRQINFRLFDDGTLGISLDETVTEKDLDDLLWIFGCESSTELVAEGMGEEWRGLLGSSFKRTSPFLTHQVFNSYHSETNLVRYMKKLENKDISLVHSMIPLGSCTMKLNSSSELTPITWREFANIHPFVPLDQAQGYQQLFQELEKDLCELTGYDRVSFQPNSGAQGEYAGLATIRAYLDQKGERHRTVCLIPKSAHGTNPASAYMAGMKIQPVEVDRYGNIDVAHLKAMVDKHKENLAAIMITYPSTNGVFEENISDVCALIHQHGGQVYLDGANMNAQVGICRPGDFGSDVSHLNLHKTFCIPHGGGGPGMGPIGVKKHLVPFLPSHPIVCLKPNEDTWPVGTVSAAPWGSSSILPISWAYIKTPLSSMMGGKGLKEATEIAILNANYMAKRLERYYRVLFRGARGYVAHEFILDTRPFKKSANIEAVDVAKRLQDYGFHAPTMSWPVAGTLMIEPTESEDKAELDRFCDAMISIRQEIADIEEGRIDPRVNPLKMSPHSLTCVTSSRWDRPYSREVAAFPLPFVKPENKFWPTIARIDDIYGDQHLVCTCPPMEVYESPFSEQKRASS
Protein: Integrator complex subunit 6 (G5E9X1)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MVIDKLPFDKYELEPSPLTQFILERKSPQTCWQVYVSNSAKYSELGHPFGYLKASTALNCVNLFVMPYNYPVLLPLLDDLFKVHKAKPTLKWRQSFESYLKTMPPYYLGPLKKAVRMMGAPNLIADSMEYGLSYSVISYLKKLSQQAKIESDRVIGSVGKKVVQETGIKVRSRSHGLSMAYRKDFQQLLQGISEDVPHRLLDLNMKEYTGFQVALLNKDLKPQTFRNAYDIPRRNLLDHLTRMRSNLLKSTRRFLKGQDEDQVHSVPIAQMGNYQEYLKQVPSPLRELDPDQPRRLHTFGNPFKLDKKGMMIDEADEFVAGPQNKHKRPGEPNMQGIPKRRRCMSPLLRGRQQNPVVNNHIGGKGPPAPTTQAQPDLIKPLPLHKISETTNDSIIHDVVENHVADQLSSDITPNAMDTEFSASSPASLLERPTNHMEALGHDHLGTNDLTVGGFLENHEEPRDKEQCAEENIPASSLNKGKKLMHCRSHEEVNTELKAQIMKEIRKPGRKYERIFTLLKHVQGSLQTRLIFLQNVIKEASRFKKRMLIEQLENFLDEIHRRANQINHINSN
Protein: Neuron specific zinc finger transcription factor (Q24140)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MPRCLIAKKWKAYPWLDRTEDTCNQQQQQEQSAPNSPRELEELHLKSRRSTLDDDEEIDVVGDKFLIKLEKQRTTADAAAAAATSSEAATSHSSNSSNMEASATTTTSKCWGPSSPTAGTTAPSPPPHSPEAATRVAGNVYNGYTRELSPLHYTAYLPRMESEITVIRAAATALVAARTSGNGSGDQHLAVYQTPPSSTTSSPSCSPSGAGDRYSPLSSGQTSSERKCFSSTGATLSLPPKKKDIYRPYSLDDKPAHGYRRRVPAEEDLHAAHAILDLSASTAFHPPTQPHQLQQQQQQQQQQHQHHHSQQQHLAPQQHHYLPLQQQQQQQAHHTHLPTLEAHAHLRSTSSIAELAAAASVVNEQRPASNASSASSNHMPSSPSSNSSSSSSQVQNENSNTTNTNQDGDGCLQDGEHNGASGASAKTVAYTYEAFFVSDGRSKRKHVADPAAAASGVPTPDQQKTKYTCSECGKQYATSSNLSRHKQTHVDSQSAKKCHTCGKAYVSMPALAMHLLTHKLSHSCGVCGKLFSRPWLLQGHLRSHTGEKPYGCAHCGKAFADRSNLRAHMQTHSVDKNFECKRCHKTFALKSYLNKHLESACLKDEEELMMSMSLSMHDSNSESGASMASSPPHEFLEARQTRRAVEEPLMPCKHRIHWARYRNL
Protein: Coiled-coil domain-containing protein 68 (Cutaneous T-cell lymphoma-associated antigen se57-1) (CTCL-associated antigen se57-1) (Q9H2F9)
Organism: Homo sapiens (Human)
Function: Centriolar protein required for centriole subdistal appendage assembly and microtubule anchoring in interphase cells. Together with CCDC120, cooperate with subdistal appendage components ODF2, NIN and CEP170 for hierarchical subdistal appendage assembly.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:28422092}. Note=Localizes to the subdistal appendages of centrioles (PubMed:28422092). {ECO:0000269|PubMed:28422092}.
Interaction partners:
- Ninein
- Coiled-coil domain-containing protein 120
- Centrosomal protein of 170 kDa
- Centrosomal protein of 128 kDa
- Melanoma inhibitory activity protein 2
- cTAGE family member 2
- Centriolin
- Outer dense fiber protein 2
- Dynactin subunit 1
- Kinesin-like protein KIF2A
Sequence:
MTTVTVTTEIPPRDKMEDNSALYESTSAHIIEETEYVKKIRTTLQKIRTQMFKDEIRHDSTNHKLDAKHCGNLQQGSDSEMDPSCCSLDLLMKKIKGKDLQLLEMNKENEVLKIKLQASREAGAAALRNVAQRLFENYQTQSEEVRKKQEDSKQLLQVNKLEKEQKLKQHVENLNQVAEKLEEKHSQITELENLVQRMEKEKRTLLERKLSLENKLLQLKSSATYGKSCQDLQREISILQEQISHLQFVIHSQHQNLRSVIQEMEGLKNNLKEQDKRIENLREKVNILEAQNKELKTQVALSSETPRTKVSKAVSTSELKTEGVSPYLMLIRLRK
Protein: Formamidopyrimidine-DNA glycosylase 1 (Fapy-DNA glycosylase 1) (EC 3.2.2.23) (DNA-(apurinic or apyrimidinic site) lyase MutM 1) (AP lyase MutM 1) (EC 4.2.99.18) (P9WNC3)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG) when paired with C, G or T, as well as methyl-faPy (formanidopyrimidine residues) in poly(dG-dC) and spiroiminodihydantoin:C base pairs. Unlike its E.coli ortholog has no activity on 8-oxoG:A. Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates. Cleaves ssDNA containing an AP site. Complements the H(2)O(2) sensitivity of an M.smegmatis fpg disruption mutant; upon expression in M.smegmatis excises 8-oxoG from dsDNA.
Interaction partners:
- Adenine DNA glycosylase
- Uncharacterized formamidopyrimidine-DNA glycosylase-like protein
- Endonuclease III lyase)
- DNA polymerase I
- Uncharacterized protein Rv2926c
- Protein RecA
- Ribonuclease 3
- Uncharacterized protein Rv2927c
- Acylphosphatase
- Uncharacterized protein Rv2923c
Sequence:
MPELPEVEVVRRGLQAHVTGRTITEVRVHHPRAVRRHDAGPADLTARLRGARINGTDRRGKYLWLTLNTAGVHRPTDTALVVHLGMSGQMLLGAVPCAAHVRISALLDDGTVLSFADQRTFGGWLLADLVTVDGSVVPVPVAHLARDPLDPRFDCDAVVKVLRRKHSELKRQLLDQRVVSGIGNIYADEALWRAKVNGAHVAATLRCRRLGAVLHAAADVMREALAKGGTSFDSLYVNVNGESGYFERSLDAYGREGENCRRCGAVIRRERFMNRSSFYCPRCQPRPRK
Protein: Leucine zipper putative tumor suppressor 3 (ProSAP-interacting protein 1) (ProSAPiP1) (Q8K1Q4)
Organism: Rattus norvegicus (Rat)
Function: May be involved in promoting the maturation of dendritic spines, probably via regulating SIPA1L1 levels at the postsynaptic density of synapses.
Subcellular location: Synapse {ECO:0000269|PubMed:27252646}. Postsynaptic density {ECO:0000269|PubMed:16522626, ECO:0000269|PubMed:27252646}. Cell projection, dendritic spine {ECO:0000269|PubMed:16522626}. Cell projection, dendrite {ECO:0000269|PubMed:16522626}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:16522626}. Note=Rather found at excitatory than inhibitory synapses (PubMed:27252646). {ECO:0000269|PubMed:16522626, ECO:0000269|PubMed:27252646}.
Interaction partners:
- SH3 and multiple ankyrin repeat domains protein 3
- Signal-induced proliferation-associated 1-like protein 1
Sequence:
MAPADLASEGPKLEDPPAPHLFGKCPSGLIMANVETLPVRADPGRDPLLAFAPRPAELGPPDPRLTMGSVGGGVTHAQEFPMKSVGTRTGGGGSQGSFPGPRSSGSGTNRERPGPGRYPSEDKVLANSLYLNGELRGSDHTDVCGNVVGSSGGSSSSGGSDKAPPQYREPNHPPKLLTTSGKLDQCSEPLVRPSAFKPVVPKNFHSMQNLCPPQTNGTPEGRQGPAGLKGGLEKSRTMTPAGGSGGGGLSDSGRNSLTSLPTYSSSYSQHLAPLSASTSHINRIGTPGYSSGGGGGGSGYQDLGTSDSGRASSKSGSSSSMGRSGHLGSGEGGNGGLPFAACSPPSPSALIQELEERLWEKEQEVAALRRSQEQSEAAVAQVLEERQKAWERELAELRQGCSGKLQQVARRAQRAQQGLQLQVLRLQQDKKQLQEEAAQLIRQREELEDKVAACQKEQADFLPRMEETKWEVCQKAGEISLLKQQLKDSQADVSQKLSEIVGLRSQLREGRASLREKEEQLLSLRDSFGSKQASLELSEGELPPACLKPALTPVDLVEPQEALASCESDEAKMRRQAGVAAAASLVSVDGEVDAGGEGGTRALRREVGRLQAELAAERRARERQGASFAEERRVWLEEKEKVIEYQKQLQLSYVEMYQRNQQLERRLRERGAAGGSRTPTPQHGEEEKAWTPSRLERIESTEI
Protein: Glutaredoxin-1 (Thioltransferase-1) (TTase-1) (P35754)
Organism: Homo sapiens (Human)
Function: Has a glutathione-disulfide oxidoreductase activity in the presence of NADPH and glutathione reductase. Reduces low molecular weight disulfides and proteins.
Subcellular location: Cytoplasm.
Interaction partners:
- Glutathione reductase, mitochondrial
- Ribonucleoside-diphosphate reductase large subunit
- Thioredoxin
- Thioredoxin reductase 1, cytoplasmic
- Glutaredoxin-related protein 5, mitochondrial
- Mitochondrial peptide methionine sulfoxide reductase
- Glutaredoxin-3
- Glutathione peroxidase 2
- Glutathione peroxidase 3
- Glutathione peroxidase 7
Sequence:
MAQEFVNCKIQPGKVVVFIKPTCPYCRRAQEILSQLPIKQGLLEFVDITATNHTNEIQDYLQQLTGARTVPRVFIGKDCIGGCSDLVSLQQSGELLTRLKQIGALQ
Protein: Neuropeptide-like 1 [Cleaved into: MTYamide peptide; IPNamide peptide; NAP peptide; NPLP1-1; NPLP1-2; NPLP1-3; NPLP1-4; NPLP1-5; NPLP1-6] (Q9W0W6)
Organism: Drosophila melanogaster (Fruit fly)
Function: Acts as a ligand for the receptor-type guanylate cyclase Gyc76C. Stimulates Gyc76c-dependent cGMP production and modulates the IMD innate immune pathway in response to salt stress by inducing nuclear translocation of NF-kappa-B protein Rel which leads to increased expression of the antimicrobial peptide diptericin. Does not appear to play a role in Gyc76C-mediated wing development.
Subcellular location: Secreted.
Interaction partners:
- FMRFamide-related peptides
- Protein dimmed
- Zinc finger protein squeeze
- Receptor-type guanylate cyclase Gyc76C
- Eclosion hormone
- Short neuropeptide F
Sequence:
MQAVLQSAHSSRRLMLLLSMLLNAAIQPRSIIVSATDDVANVSPCEMESLINQLMSPSPEYQLHASALRNQLKNLLRERQLAVGEEQPLGEYPDYLEEDKRSVAALAAQGLLNAPKRSLATLAKNGQLPTAEPGEDYGDADSGEPSEQKRYIGSLARAGGLMTYGKRNVGTLARDFQLPIPNGKRNIATMARLQSAPSTHRDPKRNVAAVARYNSQHGHIQRAGAEKRNLGALKSSPVHGVQQKREDEEMLLPAAAPDYADPMQSYWWYPSYAGYADLDWNDYRRAEKRFLGRVLPPTRATASTHRSRL
Protein: N-succinyl-L-Arg/Lys racemase (EC 5.1.1.-) (N-succinyl amino acid racemase) (NSAR) (Q81IL5)
Organism: Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711)
Function: Catalyzes efficient racemization of N-succinyl-L-Arg and N-succinyl-L-Lys, suggesting that these are physiological substrates of this enzyme. Has low activity with L-Asp-L-Lys, and even lower activity with L-Leu-L-Arg, L-Leu-L-Lys, N-succinyl-L-His and N-succinyl-L-Met (in vitro).
Interaction partners:
- Hypothetical protein.
- (S)-2-hydroxy-acid oxidase chain D.
- Cell wall-associated hydrolase.
Sequence:
MKITAIHLYAIRLPLRNPFVISYGSYSDMPSIIVKMETDEGIIGYGEGVADDHVTGESWESTFHTLKHTLTPALIGQNPMNIEKIHDMMDNTIYGVPTAKAAIDIACFDIMGKKLNQPVYQLIGGRYHEEFPVTHVLSIADPENMAEEAASMIQKGYQSFKMKVGTNVKEDVKRIEAVRERVGNDIAIRVDVNQGWKNSANTLTALRSLGHLNIDWIEQPVIADDIDAMAHIRSKTDLPLMIDEGLKSSREMRQIIKLEAADKVNIKLMKCGGIYPAVKLAHQAEMAGIECQVGSMVESSVASSAGFHVAFSKKIITSVELTGPLKFTKDIGNLHYDVPFIRLNEKPGLGIEINEDTLQELTVFQDIVR
Protein: AMP-activated protein kinase gamma 2 non-catalytic subunit (Q6V7V4)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MLEKLEFQEEEDSESGVYMRFMRSHKCYDIVPTSSKLVVFDTTLQVKKAFFALVANGVRAAPLWESKKQSFVGMLTITDFINILHRYYKSPMVQIYELEEHKIETWRELYLQETFKPLVNISPDASLFDAVYSLIKNKIHRLPVIDPISGNALYILTHKRILKFLQLFMSDMPKPAFMKQNLDELGIGTYHNIAFIHPNTPIIKALNIFVERRISALPVVDESGKVVDIYSKFDVINLAAEKTYNNLDITVTQALQHRSQYFEGVVKCSKLETLETIVDRIVRAEVHRLVVVNEADSIVGIISLSDILQALILTPAGAKQKETETE
Protein: receptor protein serine/threonine kinase (EC 2.7.11.30) (A0A0B4K7J3)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
- Protein decapentaplegic
- receptor protein serine/threonine kinase
- Protein screw
- Protein 60A
- Serine/threonine-protein kinase receptor
- Protein mothers against dpp
- Inhibin beta chain
- Mothers against decapentaplegic homolog
- receptor protein serine/threonine kinase
- Maverick
Sequence:
MESNIYLVFLLTFLLYNNARAEISDHLREDIPDLDMELSSASSAHLNGKELPAVPQNSVQTHPRRHIKSKRRMKRRYKCYSCEPPCRDPYEFTHTCQNAIQCWKSRTRDADGQVQESRGCSTSPDQLPMICSQNSLKINGPSKRNTGKFVNVVCCAGDYCNEGDFPELLPFDSNDVTVITADTSSISKMLVAVLGPFLVIALLGAVTIFFIRRSHRKRLAASRTKQDPEAYLVNDELLRATSAGDSTLREYLQHSVTSGSGSGLPLLVQRTLAKQVTLIECIGRGKYGEVWRGHWHGESIAVKIFFSRDEESWKRETEIYSTILLRHENILGFIGSDMTSRNSCTQLWLMTHYYPLGSLFDHLNRNALSHNDMVWICLSIANGLVHLHTEIFGKQGKPAMAHRDLKSKNILVTSNGSCVIADFGLAVTHSHVTGQLDLGNNPKVGTKRYMAPEVLDESIDLECFEALRRTDIYAFGLVLWEVCRRTISCGIAEEYKVPFYDVVPMDPSFEDMRKVVCIDNYRPSIPNRWSSDSLMTGMSKLMKECWHQNPDVRLPALRIKKTIHKLASADEKIRLDFDEVCV
Protein: Collagen alpha-3(IX) chain (Q14050)
Organism: Homo sapiens (Human)
Function: Structural component of hyaline cartilage and vitreous of the eye.
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000250}.
Interaction partners:
- Collagen alpha-1
- Collagen alpha-2
- Matrilin-3
- CD44 antigen
- Platelet glycoprotein VI
- Sulfate transporter
- Cartilage intermediate layer protein 1
- Multifunctional procollagen lysine hydroxylase and glycosyltransferase LH3
- Integrin alpha-2
- Integrin alpha-3
Sequence:
MAGPRACAPLLLLLLLGELLAAAGAQRVGLPGPPGPPGPPGKPGQDGIDGEAGPPGLPGPPGPKGAPGKPGKPGEAGLPGLPGVDGLTGRDGPPGPKGAPGERGSLGPPGPPGLGGKGLPGPPGEAGVSGPPGGIGLRGPPGPSGLPGLPGPPGPPGPPGHPGVLPEGATDLQCPSICPPGPPGPPGMPGFKGPTGYKGEQGEVGKDGEKGDPGPPGPAGLPGSVGLQGPRGLRGLPGPLGPPGDRGPIGFRGPPGIPGAPGKAGDRGERGPEGFRGPKGDLGRPGPKGTPGVAGPSGEPGMPGKDGQNGVPGLDGQKGEAGRNGAPGEKGPNGLPGLPGRAGSKGEKGERGRAGELGEAGPSGEPGVPGDAGMPGERGEAGHRGSAGALGPQGPPGAPGVRGFQGQKGSMGDPGLPGPQGLRGDVGDRGPGGAAGPKGDQGIAGSDGLPGDKGELGPSGLVGPKGESGSRGELGPKGTQGPNGTSGVQGVPGPPGPLGLQGVPGVPGITGKPGVPGKEASEQRIRELCGGMISEQIAQLAAHLRKPLAPGSIGRPGPAGPPGPPGPPGSIGHPGARGPPGYRGPTGELGDPGPRGNQGDRGDKGAAGAGLDGPEGDQGPQGPQGVPGTSKDGQDGAPGEPGPPGDPGLPGAIGAQGTPGICDTSACQGAVLGGVGEKSGSRSS
Protein: Interferon regulatory factor 7 (B5X2E7)
Organism: Salmo salar (Atlantic salmon)
Interaction partners:
- Serine/threonine-protein kinase TBK1
- Interferon regulatory factor 3
- TNF receptor-associated factor 6-like
- Myeloid differentiation primary response protein MyD88
- Inhibitor of nuclear factor kappa-B kinase subunit epsilon-like
- TNF receptor-associated factor 6-like
- TIR domain-containing adapter molecule 1-like
- Inhibitor of nuclear factor kappa-B kinase subunit alpha
- Inhibitor of nuclear factor kappa-B kinase subunit alpha
- Inhibitor of nuclear factor kappa-B kinase subunit alpha
Sequence:
MQSCKPQFADWLIEQVRTEQYTGLFFMDNNKFRVPWKHNSRKDCSEDDRKIFRAWAVVSGKITEHPNDKAKWKTNFRSALNSLCRRFKMVEDHSKDSNDPHKVYLVINEYNYESPLIEEITLENYGIDHALTTTENTPPGMEHDILNFSNLTLNHLDLNQHTENYIPVHTHHPVPPVLIQQPYAQVNPDALLNLPATRSSLWDLEITISYRGSEMLKTQVSGPRVQLHYQCNALEPNTQPLCFPSTDGLPDLKQIEYTNCILRSVQRGLLLEVQNTGIYGYRQDKCHVFSSTSNPREAHPEPRKMPQNEMVQLLNFQQYENELIAFKENRRGSPDYTIHMCFGEKFPDGKPPEKKLIVVKVVPLICRYFHEVAQEEGASSLQNDISLQISHHNSLMELINATWPDGPQHTMGQYF
Protein: Flap endonuclease 1-A (FEN-1-A) (EC 3.1.-.-) (Flap structure-specific endonuclease 1-A) (OsFEN-1) (OsFEN-1a) (Q9SXQ6)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Structure-specific nuclease with 5'-flap endonuclease and 5'-3' exonuclease activities involved in DNA replication and repair. During DNA replication, cleaves the 5'-overhanging flap structure that is generated by displacement synthesis when DNA polymerase encounters the 5'-end of a downstream Okazaki fragment. It enters the flap from the 5'-end and then tracks to cleave the flap base, leaving a nick for ligation. Also involved in the long patch base excision repair (LP-BER) pathway, by cleaving within the apurinic/apyrimidinic (AP) site-terminated flap. Acts as a genome stabilization factor that prevents flaps from equilibrating into structures that lead to duplications and deletions. Also possesses 5'-3' exonuclease activity on nicked or gapped double-stranded DNA, and exhibits RNase H activity. Also involved in replication and repair of rDNA and in repairing mitochondrial DNA (By similarity). May be required for cell proliferation.
Subcellular location: Nucleus, nucleolus {ECO:0000255|HAMAP-Rule:MF_03140, ECO:0000269|PubMed:11851910}. Nucleus, nucleoplasm {ECO:0000255|HAMAP-Rule:MF_03140}. Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03140}. Note=Resides mostly in the nucleoli and relocalizes to the nucleoplasm upon DNA damage. {ECO:0000255|HAMAP-Rule:MF_03140}.
Interaction partners:
- Proliferating cell nuclear antigen
- Os01g0685500 protein
- DNA polymerase delta catalytic subunit
- Os01g0660500 protein
- ATP-dependent DNA helicase
- DNA ligase
- DNA polymerase delta small subunit
- DNA replication ATP-dependent helicase/nuclease
- Os05g0358200 protein
- Flap endonuclease 1-B
Sequence:
MGIKGLTKLLADNAPKAMKEQKFESYFGRRIAVDASMSIYQFLIVVGRTGMETLTNEAGEVTSHLQGMFNRTIRLLEAGIKPVYVFDGKPPDLKKQELAKRYSKREDATKELTEAVEEGDKDAIEKFSKRTVKVTKQHNEECKRLLRLMGVPVVEAPCEAEAECAALCINDMVYAVASEDMDSLTFGAPRFLRHLMDPSSKKIPVMEFEVAKVLEELELTMDQFIDLCILSGCDYCDSIKGIGGQTALKLIRQHGSIESILENINKDRYQIPEDWPYQEARRLFKEPNVTLDIPELKWNAPDEEGLVEFLVKENGFNQDRVTKAIEKIKFAKNKSSQGRLESFFKPVVSTSVPLKRKDTSEKPTKAVANKKTKGAGGKKK
Protein: Histocompatibility minor 13 (A0A3B3IUB5)
Organism: Homo sapiens (Human)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004477}. Membrane {ECO:0000256|ARBA:ARBA00004366}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004366}; Lumenal side {ECO:0000256|ARBA:ARBA00004366}.
Interaction partners:
Sequence:
MDSALSDPHNGSAEAGGPTNSTTRPPSTPEGIALAYGSLLLMALLPIFFGALRSVRCARGKNASDMPETITSRDAARFPIIASCTLLGLYLFFKVYFPNKSYAGSVLKTWKTQKSKKGKTAVIQNPTTRDSHSFPSEIFSQEYINLLLSMYFFVLGILALSHTISPFMNKFFPASFPNRQYQLLFTQGSGENKEEIINYEFDTKDLVCLGLSSIVGVWYLLRKHWIANNLFGLAFSLNGVELLHLNNVSTGCILLGGLFIYDVFWVFGTNVMVTVAKSFEAPIKLVFPQDLLEKGLEANNFAMLGLGDVVIPGIFIALLLRFDISLKKNTHTYFYTSFAAYIFGLGLTIFIMHIFKHAQPALLYLVPACIGFPVLVALAKGEVTEMFSYEESNPKDPAAVTESKEGTEASASKGLEKKEK