wanglab/gogpt-training-data huggingface dataset:
Protein: Fibrinogen beta chain [Cleaved into: Fibrinopeptide B; Fibrinogen beta chain] (P02675)
Organism: Homo sapiens (Human)
Function: Cleaved by the protease thrombin to yield monomers which, together with fibrinogen alpha (FGA) and fibrinogen gamma (FGG), polymerize to form an insoluble fibrin matrix. Fibrin has a major function in hemostasis as one of the primary components of blood clots. In addition, functions during the early stages of wound repair to stabilize the lesion and guide cell migration during re-epithelialization. Was originally thought to be essential for platelet aggregation, based on in vitro studies using anticoagulated blood. However subsequent studies have shown that it is not absolutely required for thrombus formation in vivo. Enhances expression of SELP in activated platelets. Maternal fibrinogen is essential for successful pregnancy. Fibrin deposition is also associated with infection, where it protects against IFNG-mediated hemorrhage. May also facilitate the antibacterial immune response via both innate and T-cell mediated pathways.
Subcellular location: Secreted {ECO:0000269|PubMed:10074346, ECO:0000269|PubMed:19296670, ECO:0000269|PubMed:9628725}.
Interaction partners:
- Fibrinogen alpha chain
- Fibrinogen gamma chain
- Prothrombin
- Antithrombin-III
- Integrin beta-3
- Heparin cofactor 2
- Plasminogen
- Protein AMBP
- Vitamin D-binding protein
- Integrin alpha-IIb
Sequence:
MKRMVSWSFHKLKTMKHLLLLLLCVFLVKSQGVNDNEEGFFSARGHRPLDKKREEAPSLRPAPPPISGGGYRARPAKAAATQKKVERKAPDAGGCLHADPDLGVLCPTGCQLQEALLQQERPIRNSVDELNNNVEAVSQTSSSSFQYMYLLKDLWQKRQKQVKDNENVVNEYSSELEKHQLYIDETVNSNIPTNLRVLRSILENLRSKIQKLESDVSAQMEYCRTPCTVSCNIPVVSGKECEEIIRKGGETSEMYLIQPDSSVKPYRVYCDMNTENGGWTVIQNRQDGSVDFGRKWDPYKQGFGNVATNTDGKNYCGLPGEYWLGNDKISQLTRMGPTELLIEMEDWKGDKVKAHYGGFTVQNEANKYQISVNKYRGTAGNALMDGASQLMGENRTMTIHNGMFFSTYDRDNDGWLTSDPRKQCSKEDGGGWWYNRCHAANPNGRYYWGGQYTWDMAKHGTDDGVVWMNWKGSWYSMRKMSMKIRPFFPQQ
Protein: Transcription factor TFIIIB component B'' Myb domain-containing protein (Q38AI0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- TATA box-binding protein-like 1
- Transcription factor, putative
- DNA-directed RNA polymerase III subunit RPC6
- DNA-directed RNA polymerase subunit
- DNA-directed RNA polymerase subunit beta
- Uncharacterized protein
- DNA-directed RNA polymerase III subunit RPC3
- RNA polymerase III subunit Rpc25 domain-containing protein
- Plastid-encoded RNA polymerase subunit alpha
- DNA-directed RNA polymerases I, II, and III subunit RPABC3
Sequence:
MDYSDFDFPPNPTDENDEHGAVPCLNNDIPLQALSSTPVEQLPPTTLPPNQQRPIRQAIQANQKLVMTARTQHRAVAVKKNEGDHDDREQKEEMDEDSEEEENAKKLFGWRKRSRFSWTEEELVDFYKFLSQYGTDFNAIAVLYTDKSRDEVKRLYHRELRRRPADVRAALASRTSIDLATFNTRLKKREEKRQQARNRKLDKEEEETLRQLEAGTLQLLPTSEVATDPGGTANADVEFSFDFKEESHAQKSDMVESLPLPAEGAVGEKEDDKGLVGSPENVLEGTEKTYTDDFIIDW
Protein: Leukotriene B4 receptor 1 (LTB4-R 1) (LTB4-R1) (O88855)
Organism: Mus musculus (Mouse)
Function: Receptor for leukotriene B4, a potent chemoattractant involved in inflammation and immune response.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Leukotriene B4 receptor 2
- Leukotriene A-4 hydrolase
- Polyunsaturated fatty acid 5-lipoxygenase
- Retinoic acid receptor responder protein 2
Sequence:
MAANTTSPAAPSSPGGMSLSLLPIVLLSVALAVGLPGNSFVVWSILKRMQKRTVTALLVLNLALADLAVLLTAPFFLHFLARGTWSFREMGCRLCHYVCGISMYASVLLITIMSLDRSLAVARPFMSQKVRTKAFARWVLAGIWVVSFLLAIPVLVYRTVKWNNRTLICAPNYPNKEHKVFHLLFEAITGFLLPFLAVVASYSDIGRRLQARRFRRSRRTGRLVVLIILAFAAFWLPYHLVNLVEAGRTVAGWDKNSPAGQRLRLARYVLIALAFLSSSVNPVLYACAGGGLLRSAGVGFVVKLLEGTGSEVSSTRRGGTLVQTPKDTPACPEPGPTDSFMTSSTIPESSK
Protein: Queuine tRNA-ribosyltransferase catalytic subunit (EC 2.4.2.64) (Guanine insertion enzyme) (tRNA-guanine transglycosylase) (O94460)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalytic subunit of the queuine tRNA-ribosyltransferase (TGT) that catalyzes the base-exchange of a guanine (G) residue with queuine (Q) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming queuine, allowing a nucleophilic attack on the C1' of the ribose to form the product.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03218, ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- tRNA
- Queuine tRNA-ribosyltransferase accessory subunit 2
- Queuosine 5'-phosphate N-glycosylase/hydrolase
- Probable thymidylate synthase
- Thioredoxin domain-containing protein plp1
- tRNA pseudouridine synthase 4
- tRNA
Sequence:
MASSFPALQFKVVARCSTTRARVTDIQLPHGLVESPVFMPVGTQASLKGVLPEQLDALGCKIMLNNTYHLGLKPGQEVLDTVGGAHRFQSWNKNILTDSGGFQMVSLLKLATITEDGVTFLSPRDGTPMLLTPEHSISLQNSIGSDIMMQLDDVVHTLTESKRMEEAMYRSIRWLDRCIQAHKRPETQNLFCIIQGGLDKRLREICCREMVKRNTPGIAVGGLSGGEEKHAFCETVYTCTSILPDNKPRYLMGVGYAEDLVVCVALGMDMFDCVYPTRTARFGNALTRKGVINLRNQKFRNDIGPLEEGCSCPCCKTELEGGWGITRAYFNSLVSKETVGANLMTIHNVHFQLQLMRDMRESIIKDEFPSFVKNFFHEWNHGDKSNYPSWAVDALRMVNIDLLA
Protein: Neuron navigator 2 (A0A5F8MPR0)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MPISINVWVPARDQSRDSCDHYKVIYTDWANHYLAKSGHKRLIKDLQQDVTDGVLLAQIIQVVANDKIEDINGCPKNRSQMIENIDACLNFLAAKGINTQGLSAEEIRNGNLKAIL
Protein: Metalloendoproteinase 3-MMP (At3-MMP) (EC 3.4.24.-) (Q5XF51)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Matrix metalloproteinases (MMPs) or matrixins may play a role in the degradation and remodeling of the extracellular matrix (ECM) during development or in response to stresses (By similarity). Active on McaPLGLDpaAR-NH(2) (QF24) and beta-casein and, to some extent, on myelin basic protein (MBP).
Subcellular location: Cell membrane {ECO:0000255}; Lipid-anchor, GPI-anchor {ECO:0000255}; Extracellular side {ECO:0000305}.
Interaction partners:
- Carboxypeptidase SOL1
- Expressed protein
- PLC-like phosphodiesterases superfamily protein
- Probable LRR receptor-like serine/threonine-protein kinase At4g37250
- At4g27652
- AT5g23340/MKD15_20
- IQ domain-containing protein IQM1
- Endochitinase At2g43580
- At4g27654
- At1g66080
Sequence:
MVRICVFMVFLLFFAPSPVSAGFYTNSSAIPPQLLRNATGNPWNSFLNFTGCHAGKKYDGLYMLKQYFQHFGYITETNLSGNFTDDFDDILKNAVEMYQRNFQLNVTGVLDELTLKHVVIPRCGNPDVVNGTSTMHSGRKTFEVSFAGRGQRFHAVKHYSFFPGEPRWPRNRRDLTYAFDPRNALTEEVKSVFSRAFTRWEEVTPLTFTRVERFSTSDISIGFYSGEHGDGEPFDGPMRTLAHAFSPPTGHFHLDGEENWIVSGEGGDGFISVSEAVDLESVAVHEIGHLLGLGHSSVEGSIMYPTIRTGRRKVDLTTDDVEGVQYLYGANPNFNGSRSPPPSTQQRDTGDSGAPGRSDGSRSVLTNLLQYYFWIIFGLFLYLV
Protein: Catalase (EC 1.11.1.6) (Q64405)
Organism: Cavia porcellus (Guinea pig)
Function: Catalyzes the degradation of hydrogen peroxide (H(2)O(2)) generated by peroxisomal oxidases to water and oxygen, thereby protecting cells from the toxic effects of hydrogen peroxide. Promotes growth of cells including T-cells, B-cells, myeloid leukemia cells, melanoma cells, mastocytoma cells and normal and transformed fibroblast cells.
Subcellular location: Peroxisome matrix {ECO:0000250|UniProtKB:P04040}.
Interaction partners:
- Thiolase N-terminal domain-containing protein
- SCP2 domain-containing protein
- Peroxisomal multifunctional enzyme type 2
- Superoxide dismutase, mitochondrial
- Superoxide dismutase
- Superoxide dismutase
- Parkinson disease protein 7 homolog
- Hydroxysteroid dehydrogenase-like protein 2
- (S)-2-hydroxy-acid oxidase
- Kynureninase
Sequence:
MADSRDPASDQMKHWKEERAAQKPDVLTTAGGNPVGDKLNIMTVGPRGPLLVQDVVFTDEMAHFDRERIPERVVHAKGAGAFAYFEVTHDITKYCKAKVFEHIGKKTPIAVRFSTVAGESGSADTVRDPRGFAVKFYTEEGIWDLVGNNTPIFFIRDALLFPSFIHSQKRNPQTHLKDPDMMWDFWSLRPESLHQVSFLFSDRGIPDGHRHMNGYGSHTFKLVNGSGEAVYCKFHYKTDQGIKNLSVEDAARLSQEDPDYGLRDLFNAIATGNYPSWTLYIQVMTFQQAQSFPFNPFDLTKIWPHKDYPLIPVGKLVLNRNPVNYFAEVEQIAFDPSNMPPGIEPSPDKMLQGRLFAYPDTHRHRLGPNYLQIPVNCPYRTRVANYQRDGPMCVTDNQGGAPNYYPNSFSAPVEQRQALEHTSRCSGDVGRYNSTDDDNVTQVRAFYTQVLNEEQRRRLCENIAGHLKDAQLFIQKKAVKNFMDVHPDYGNRIQTLLDKYNVEKPKNAIHTFVQDGSHLSAKEKANL
Protein: Agmatinase (EC 3.5.3.11) (Agmatine ureohydrolase) (AUH) (P60651)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the formation of putrescine from agmatine.
Interaction partners:
- Polyamine aminopropyltransferase
- Constitutive ornithine decarboxylase
- Inducible ornithine decarboxylase
- Biosynthetic arginine decarboxylase
- Gamma-glutamylputrescine synthetase PuuA
- Biodegradative arginine decarboxylase
- Putrescine aminotransferase
- Spermidine N
- S-adenosylmethionine decarboxylase proenzyme
- S-adenosylmethionine synthase
Sequence:
MSTLGHQYDNSLVSNAFGFLRLPMNFQPYDSDADWVITGVPFDMATSGRAGGRHGPAAIRQVSTNLAWEHNRFPWNFDMRERLNVVDCGDLVYAFGDAREMSEKLQAHAEKLLAAGKRMLSFGGDHFVTLPLLRAHAKHFGKMALVHFDAHTDTYANGCEFDHGTMFYTAPKEGLIDPNHSVQIGIRTEFDKDNGFTVLDACQVNDRSVDDVIAQVKQIVGDMPVYLTFDIDCLDPAFAPGTGTPVIGGLTSDRAIKLVRGLKDLNIVGMDVVEVAPAYDQSEITALAAATLALEMLYIQAAKKGE
Protein: Zinc finger protein 354A (Kidney, ischemia, and developmentally-regulated protein 1) (Renal transcription factor Kid-1) (Transcription factor 17) (TCF-17) (Q02975)
Organism: Rattus norvegicus (Rat)
Function: It may play a role in renal development and may also be involved in the repair of the kidney after ischemia-reperfusion or folic acid administration.
Subcellular location: Nucleus {ECO:0000305|PubMed:8382778}.
Interaction partners:
Sequence:
MAPEQREGASQVSVTFEDVAVLFTRDEWKKLDLSQRSLYREVMLENYSNLASMAGFLFTKPKVISLLQQGEDPWQVEKEGPRYFSLGLKCSHRTTKSTQTQDSSFQELIVRKSKRTFAFEPLNMKSENLFIHEGKLEEKWDKNTLTVERSHKNNEFSPKSHREKRSSECKKQISYLSNPPGITPDKRYKCSMCEKTFINTSSLRKHEKNHSGEKLFKCKECSKAFSQSSALIQHQITHTGEKPYVCKECGKAFTLSTSLYKHLRTHTVEKSYRCKECGKSFGQRSGLFIHQKIHARENPHRYNPGRKASASLSGCQRAHSRKKTYLCNECGNTFKSSSSLRYHQRIHTGEKPFRCSECGRAFSQSASLIQHERIHTGEKPYRCGECGKGFTSISRLNRHRIIHTGEKLYNCNECGKALSSHSTLIIHERIHTGEKPCKCKVCGKAFRQSSALIQHQRMHTGERPYKCNECGKTFRCNSSLSNHQRIHTGEKPYQCIECGMSFGQSSALIQHRRIHTGEKPFKCNTCGKTFRQSSSRIAHQRIHTGEKPYECNTCGKLFNYRSSLTNHYKIHVDEDP
Protein: GDP-Man:Man(3)GlcNAc(2)-PP-Dol alpha-1,2-mannosyltransferase (EC 2.4.1.131) (Alpha-1,2-mannosyltransferase ALG11) (Asparagine-linked glycosylation protein 11) (Protein LEAF WILTING 3) (Q9XEE9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Required for N-linked oligosaccharide assembly. Has a role in the last step of the synthesis of the Man(5)GlcNAc(2)-PP-dolichol core oligosaccharide on the cytoplasmic face of the endoplasmic reticulum.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:19732381}; Single-pass membrane protein {ECO:0000250|UniProtKB:P53954}.
Interaction partners:
- Dol-P-Man:Man
- Dol-P-Man:Man
- Alpha-1,3/1,6-mannosyltransferase ALG2
- Dolichol-phosphate mannosyltransferase subunit 1
- Dolichol kinase EVAN
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3A
- UDP-glycosyltransferase TURAN
- Dol-P-Glc:Glc
- Alpha-1,2-mannosyltransferase ALG9
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 2
Sequence:
MAIYFILYTLLTIIFAVSLSLFLSVINARKSRKRAVGFFHPYTNDGGGGERVLWCAVKAIQEENPDLDCVIFTGDHDSSSDSLARRAVDRFGVHLQSPPKVIHLNKRKWIEESTYPHFTMIGQSLGSVYLAWEALRMFTPLYFLDTSGYAFTYPLARIFGCKVVCYTHYPTISLDMISRVRQRNSMYNNDASIAKSNWLSTCKLVYYRAFSWMYGMVGSCTHLAMVNSSWTKSHIEVLWRIPERITRVYPPCDTSGLQAFPLERSSDPPKIISVAQFRPEKAHMLQLEAFSLALEKLDADVPRPKLQFVGSCRNNSDEERLQKLKDRAVELKVDGDVQFYKNAMYRELVELLGNAVAGLHGMIDEHFGISVVEYMAAGAIPIAHNSAGPKMDIVLEEDGQKTGFLAETVEEYAEAILEIVKMNETERLKMAESARKRAARFSEQRFCEDFKTAIRPIFTGPLK
Protein: Ras family GTPase (A0A1D8PS50)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- GTPase activating protein BUD2
- Rho family guanine nucleotide exchange factor
- Rga2p
- Ras family guanine nucleotide exchange factor
- Ras GTPase activating protein
- Phosphatidylinositol-3-phosphate-binding protein
- Leucine-rich repeat-containing protein 58
- 14-3-3 protein homolog
- Protein farnesyltransferase subunit beta
- Lrg1p
Sequence:
MRDYKVVVLGAGGVGKSSITVQFVQGVYVESYDPTIEDSYRKQIEVDGRACDLEILDTAGVAQFTAMRELYIKSGKGFLLVYSVTDENSLKELLALREQVLRIKDSDNVPMVLVGNKCDLEDDRVLSIEDGVKVSQDWGLVPFYETSAMYKTNVDEAFIDVVRQIMRKEAAISAEKKQQKELQKQQQQQQQEQDAEGQQQQQKSGKSKSSATQKDATADGQTDVNARLKQSINDHPKSSSGSKCCTIM
Protein: Heat shock protein 70kDa (Heat shock protein family A (Hsp70) member 8) (A0PA16)
Organism: Coturnix japonica (Japanese quail) (Coturnix coturnix japonica)
Interaction partners:
Sequence:
MSKGPAVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTVFDAKRLIGRRFDDSVVQSDMKHWPFTVVNDAGRPKVQVEYKGETKSFYPEEISSMVLTKMKEIAEAYLGKTVTNAVVTVPAYFNDSQRQATKDAGTIAGLNVLRIINEPTAAAIAYGLDKKVGAERNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVNHFIAEFKRKHKKDISENKRAVRRLRTACERAKRTLSSSTQASIEIDSLYEGIDFYTSITRARFEELNADLFRGTLDPVEKALRDAKLDKSQIHDIVLVGGSTRIPKIQKLLQDFFNGKELNKSINPDEAVAYGAAVQAAILSGDKSENVQDLLLLDVTPLSLGIETAGGVMTVLIKRNTTIPTKQTQTFTTYSDNQPGVLIQVYEGERAMTKDNNLLGKFELTGIPPAPRGVPQIEVTFDIDANGILNVSAVDKSTGKENKITITNDKGRLSKEDIERMVQEAEKYKAEDEKQRDKVSSKNSLESYAFNMKATVEDEKLQGKISDEDKQKILDKCNEIINWLDKNQTAEKEEFEHQQKELEKVCNPIITKLYQSAGGMPGGMPGGFPGGGAPPSGGASSGPTIEEVD
Protein: Zinc fingers and homeoboxes protein 1 (Q8R515)
Organism: Rattus norvegicus (Rat)
Function: Acts as a transcriptional repressor. Increases DNMT3B-mediated repressive transcriptional activity when DNMT3B is tethered to DNA. May link molecule between DNMT3B and other co-repressor proteins (By similarity).
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000269|PubMed:12062805}. Note=Colocalized in the nucleus with DNMT3B. {ECO:0000250}.
Interaction partners:
- Zinc finger MYND domain-containing protein 11
- DNA
Sequence:
MASRRKSTTPCMVLASEQDPDLELISDLEEGPPVLTPVENARAESVSSDEEVHESVDSDNQQNKKVEGGYECKYCTFQTPDLNMFTFHVDSEHPNVVLNSSYVCVECNFLTKRYDALSEHNLKYHPGEENFKLTMVKRNNQTIFEQTINDLTFDGSFVKEENTEQGESIDVSSSGISISKTPIMKMMKNKVENKRITVHHNSAEGTSEEKENGVKASREENAENTSSSASESNTSTSTVNQVHPSPAGTVVTPTAVLPGLAQVITAVSAQQNSNLVPKVLIPVNSIPTYNAALDNNPLLLNTYNKFPYPTMSEITVLSAQAKYTEEQIKIWFSAQRLKHGVSWTPEEVEEARRKQFNGTVHTVPQTITVIPTHISTGSNGLPSILQTCQIVGQPGLVLTQVAGANTLPVTAPIALTVAGVPNQTNVQKSQVPAAQPAAETKPATAAVPSSPSVRPEAALVNPDSFGIRAKKTKEQLAELKVSYLKNQFPHDSEIIRLMKITGLTKGEIKKWFSDTRYNQRNSKSNQCLHLNNDSSATIIIDSSDETPEPPAAAASQPKQSWNPFPDFAPQKFKEKTAEQLRVLQASFLNSSVLTDEELNRLRAQTKLTRREIDAWFTEKNKTKALKDEKVEVDESNVGSSKEEPGENSPGDEAVAPKSAGTGKICKKTPEQLHMLKSAFVRTQWPSPEEYDKLAEESGLARTDIVSWFGDTRYAWKNGNLKWYYYYQSSNSSSLNGLSSLRKRGRGRPKGRGRGRPRGRPRGGKRMNTWDRVPSLIKFKTGTAILKDYYLKHKFLNEQDLDELVNRSHMGYEQVREWFAERQRRSELGIELFEENEEEDEVIDDQEEDEEETDDSDTWEPPRHVKRKLSKSDD
Protein: Transcriptional coregulator SSA1 (Q5KKP4)
Organism: Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC MYA-565) (Filobasidiella neoformans)
Function: Transcriptional coregulator that functions together with transcription factor HSF1. Positively regulates the expression of laccase LAC1 during glucose starvation.
Subcellular location: Nucleus {ECO:0000269|PubMed:17040492}.
Interaction partners:
- Chaperone, putative
- Chaperone, putative
- ER organization and biogenesis-related protein, putative
- Chaperone regulator, putative
- Zuotin, putative
- Chaperone regulator, putative
- Chaperone regulator, putative
- Expressed protein
- Heat shock protein, putative
- Transcription factor, putative
Sequence:
MVKAVGIDLGTTYSCVAVWQNDRVEIIANDQGNRTTPSYVAFNDSERLIGDAAKNQVAMNPYNTVFDAKRLIGRKFEDAEVQADMKHWPFKVIDRAGKPAIQVEYRGEEKVFTPEEISSMVLIKMKETAEAYLGGTVSKAVVTVPAYFNDSQRQATKDAGAIAGLDVLRIINEPTAAAIAYGLDKKSEGEKNVLIFDLGGGTFDVSLLTIEEGIFEVKATAGDTHLGGEDFDNRLVNHFVQEFKRKNKKDLSSNARALRRLRTACERAKRTLSSAAQTSIEIDSLFDGIDFYTSITRARFEELCQDLFRSTMDPVEKVLRDSKIDKSSVNEIVLVGGSTRIPKIQKLVSDMFSGREPNRSINPDEAVAYGAAVQAAILTGDTSEATQDLLLLDVAPLSMGIETAGGIMTPLIKRNTTVPTKKSEVFSTYSDNQPGVLIQVFEGERAKTKDCNLLGKFDLSGIPPAPRGVPQIEVSFDVDANGILNVNAADKSTGKSSKITITNDKGRLSKEEIERMLAEAEKFKAEDEAAAATVQAKNGLESYSYSLKTTLSDNQDKFDAADHETLSKKVDEVISSLDTMQSASKEEFESLQKELEAVANPIMTKFYGAQGGAPGGAPGGFPGAGGAPAQEEGPSVEEVD
Protein: Protein sidekick-1 (Q3UH53)
Organism: Mus musculus (Mouse)
Function: Adhesion molecule that promotes lamina-specific synaptic connections in the retina. Expressed in specific subsets of interneurons and retinal ganglion cells (RGCs) and promotes synaptic connectivity via homophilic interactions.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q8AV58}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q8AV58}. Synapse {ECO:0000269|PubMed:20219992}.
Interaction partners:
Sequence:
MARARPSVAGGGVAAPPERAGPGRPRRSRTGHHCDPECPGLRAAPRTPGPGAGRRAAKLRPGRGWWALLLLQLHLLRALAQDDVAPYFKTEPGLPQIHLEGNRLVLTCLAEGSWPLEFKWIRNDSELTTYSSEYKYIIPSLQKLDAGFYRCVVRNRMGALLQRKSEIQVAYMGNFMDTDQRKTVSQGHAALLNLLPIVSCPQPQVTWFREGHKIIPSSRIAITLENQLVILATTASDAGAYYVQAVNEKNGENKTSPFIHLSVARDTGTHEAMAPIIVVAPGNRSVVAGSSETTLECIANARPVEELSVHWKRNGVRLTSGLHSYGRRLTITNPTSADTGMYVCEATLRGSTFEPARARAFLSIIEPPYFTAEPESRILGEVEETMDIPCRAMGVPLPTLQWYKDAVPLSKLQNPRYKVLPSGGLHIQKLSPEDSGIFQCFASNEGGEVQTHTYLDVTNIAPAFTQRPVDTTVTDGMTAVLRCEVSGAPKPAITWKRGNHILASGSVRIPRFMLLESGGLRIAPVFIQDAGNYTCYAANTEASVNASAMLTVWNRTSIVHPPEDRVVIKGTTATLCCGATHDPRTSLRYVWKKDNVVITASSSSRIVVEKDGSLVISQTWSGDIGDYTCEIISEGGSDSRTARLEVIELPHPPQNLLASLSPARSHSVTLSWVRPFDGNSPVLYYIVQVSENNSPWKVHLSNVGPEMTGVTVSGLTPARTYQFRVCAVNQVGKGQYSTETSRLMLPEEPPSAPPKNIVASGRTNQSIMVQWQPPPETEHNGVLRGYILRYRLAGLPGEHQQRNISSPEVNYCLVTDLIIWTQYEIQVAAYNGAGLGVFSRAVTEYTLQGVPTAPPQNVQAEAVNSTTVHFLWNPPPQQFINGINQGYKLLAWPADAPETVTVVTIAPDFHGIHHGYITNLKKFTAYFTSVLCFTTPGDGPPSSPQLVWTHEDKPGAVGHLSFTEILDTSLKVSWQEPLERNGIIMGYQISWEVYGRNDSRLTHTLNSTMHEYKIQGLSSLTTYTIDVAALTAAGVGVTTSSTISSGVPPDLPGAPSNLVISNISPRSATLQFRPGYDGKTAICRWIVEGQVGAIGDEEEWVTLYEEENEPDAQMLEIPNLTPYTHYRFRMRQVNIVGPSPFSQSSRVIQTLQAPPDVAPTSLTVRTASETSLRLRWVPLPDSQYNGNPESVGYRVKYWRSDQPSSALAQVVSDRLERELTIEELEEWTEYELRMQAFNAIGAGPWSELVRGRTRESVPSAAPENVSAEAVSSTQILLTWASVPEQDQNGLILGYKVLYCAKDLDPEPRSHVVRGNHTQSALLAGLRKFVVYELQVLAFTRIGNGVPSSPLILERTKDDTPGPPVRLVFPEVRLTAVRIVWQPPEEPNGVILGYQIAYRLASGSPHTFTTVEVGATVRQFTATELAPESAYIFRLSAKTRQGWGEPLEATVITTEKRERPAPPRELLVPQAEVTARSLRLQWVPGSDGASPIRYFTVQVRELPGGEWQTYSSSISHEATACAVERLRPFTSYKLRLKATNDIGDSDFSAETEAVTTLQDVPGEPPGSVSATPHTTSSVLIQWQPPRDESLNGLLQGYRIYYRELESETGMSPEPKTLKSPSALRAELTAQSSFKTVNSSSSLTTYELTHLKKYRRYEVIMTAYNIIGESPASVPVEVFVGEAAPAMAPQNVQVTPLTASQLEVTWDPPPPESQNGNIQGYKVYYWEADSRNETEKMKVLFLPEPVVKIKDLTSHTKYLISISAFNAAGDGPKSDPCQGRTHQAAPGPPSFLAFSEITSTTLNVSWGEPSAANGILQGYRVVYEPLAPVQGVSKVVTVDVKGNWQRWLKVRDLTKGVTYFFRVQARTIAYGPELQANVTAGPAEGSPGSPRNVLVTKSASELTLQWTEGNAGTTPTTGYVIEARPSDEGLWDMFAKDIPRSATSYTVDLDKLRQGVTYEFRVVAVNKAGFGEPSRPSIAVSAQAEAPFYEEWWFLLVMALSSLLLILLVVFVLVLHGQSKKYKSCSTGKGISNMEETVTLDNGGFAALELNSRHLNVKSTFSKKNGTRSPPRPSPGGLHYSDEDICNKYNGAVLTESVNLKEKSVDGSESEASDSDYEEALPKHSFVNHYMSDPTYYNSWKRRPPAAAPHRYEAVAGAEAGPHLHTVITTQSAGGVYTPAGPGARAPLTGFSSFV
Protein: SOS Ras/Rho guanine nucleotide exchange factor 2 (F1MAI3)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Growth factor receptor-bound protein 2
- Tyrosine-protein phosphatase non-receptor type 11
- SHC-transforming protein 1
- Receptor protein-tyrosine kinase
- GTPase NRas
- GTPase HRas
- GRB2-associated-binding protein 1.
- SHC-transforming protein 3
- Fibroblast growth factor receptor
- Fibroblast growth factor receptor
Sequence:
MQQAPQPYEFFSEENSPKWRGLLVPALRKVQEQVHPTLSANEESLYYIEELIFQLLNKLCLAQPRTVQDVEERVQKTFPHPIDKWAIADAQSAIEKRKRRNPLLLPVDKIHPSLKEVLGYKVDYHVSLYIVAVLEYISADILKLAGNYVFNIRHYEISQQDIKVSMCADKVLMDMFDQDDDIGLVSLCEEEPCSSGELNYYDLVRTEIAEERQYLRELNMIIKVFREAFLSDKKLFKSSEIEKIFSNISDIHELTVKLLGLIEDTVEMTDESSPHPLAGSCFEDLAEEQAFDPYETLSQDILAPEFNDHFSKLMARPAVALHFQSIADGFKEAVRYVLPRLMLVPVYHCWHYFELLKQLKACSEEQEDRECLNQAITALMNLQGSMDRIYKQHSPRRRPGDPVCLFYNRQLRSKHLAIKKMNEIQKNIDGWEGKDIGQCCNEFIMEGPLTRIGAKHERHIFLFDGLMISCKPNHCQTRLPGYSSAEYRLKEKFVMRKIQICDKEDACEYKHAFELVSKDENSVIFAAKSAEEKNNWMAALISLHYRSTLDRMLDSVLLKEENEQPLRLPRPDVYRFVVTDSEENIVFEDNLQSRSGIPIIKGGTVVKLIERLTYHMYADPNFVRTFLTTYRSFCKPQELLSLLIERFEIPDPEPTEADKLALEKGEQPISADLKRFRKEYVQPVQLRVLNVFRHWVEHHFYDFERDLELLERLEAFISSVRGKAMKKWVESIAKIIKRKKQAQANGVSHNITFESPPPPVEWHISRAGQSETFDLMTLHPIEIARQLTLLESDLYRRVQPSELVGSVWTKEDKEINSPNLLKMIRHTTNLTLWFEKCIVEAENFEERVAVLSRIVEILQVFQDLNNFNGVLEIVSAVNSVSVYRLDHTFEALQERKRRVLDDAVELSQDHFKKYLVKLKSINPPCVPFFGIYLTNILKTEEGNSDFLKRKGKDLINFSKRRKVAEITGEIQQYQNQPYCLRTEPEMRRFFENLNPMGLLSEKEFTDYLFNKSHEIEPRNCKQPPRFPRKSTFSLKSPGIRPNASRHGSTSGTFRGHPTPLEREPYKISFSRIAETELESTVSAPTSPNTPSTPPVSASSDHSVFLDVDLNSSCGSNTIFAPVLLPHSKSFFSSCGSLHKLSEEPLVPPPLPPRKKFDHDAPNSKGAMKSDDDPPAIPPRQPPPPKVKPRAPVLTGTFEGPVPSPPPPPPRDPLPDTPPPVPLRPPEHFINCPFNLQPPPLGHPHRDPDWLRDVSTCPNSPSTPPPTPSPRIPRRCHLPSPSHNNLAHPPAPPVPPRQNSSPHLPKLPPKTYKRELSHPPLYRLPLFENAETPQ
Protein: Epothilone C/D epoxidase (EC 1.14.15.-) (Cytochrome P450 167A1) (Cytochrome P450epoK) (Q9KIZ4)
Organism: Sorangium cellulosum (Polyangium cellulosum)
Function: Involved in the biosynthesis of epothilones, macrolactones which have a narrow anti-fungal spectrum and microtubule-stabilizing activity. Catalyzes the epoxidation of epothilones C and D to epothilones A and B, respectively.
Interaction partners:
Sequence:
MTQEQANQSETKPAFDFKPFAPGYAEDPFPAIERLREATPIFYWDEGRSWVLTRYHDVSAVFRDERFAVSREEWESSAEYSSAIPELSDMKKYGLFGLPPEDHARVRKLVNPSFTSRAIDLLRAEIQRTVDQLLDARSGQEEFDVVRDYAEGIPMRAISALLKVPAECDEKFRRFGSATARALGVGLVPRVDEETKTLVASVTEGLALLHGVLDERRRNPLENDVLTMLLQAEADGSRLSTKELVALVGAIIAAGTDTTIYLIAFAVLNLLRSPEALELVKAEPGLMRNALDEVLRFDNILRIGTVRFARQDLEYCGASIKKGEMVFLLIPSALRDGTVFSRPDVFDVRRDTSASLAYGRGPHVCPGVSLARLEAEIAVGTIFRRFPEMKLKETPVFGYHPAFRNIESLNVILKPSKAG
Protein: Peptidoglycan D,D-transpeptidase MrdA (EC 3.4.16.4) (Class B penicillin-binding protein 2) (Penicillin-binding protein 2) (PBP-2) (PBP2) (Transpeptidase PBP2) (TP PBP2) (P0AD65)
Organism: Escherichia coli (strain K12)
Function: Catalyzes cross-linking of the peptidoglycan cell wall. Responsible for the determination of the rod shape of the cell. Is probably required for lateral peptidoglycan synthesis and maintenance of the correct diameter during lateral and centripetal growth.
Subcellular location: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_02081, ECO:0000269|PubMed:1103132, ECO:0000269|PubMed:3009484, ECO:0000305|PubMed:37620344}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_02081, ECO:0000305|PubMed:37620344}. Note=Localizes preferentially in the lateral wall and at mid-cell in comparison with the old cell pole. Localization at mid-cell is dependent on active FtsI. {ECO:0000269|PubMed:12519203}.
Interaction partners:
- Cell shape-determining protein MreC
- Peptidoglycan glycosyltransferase MrdB
- Penicillin-binding protein 1A
- Probable peptidoglycan glycosyltransferase FtsW
- Rod shape-determining protein MreD
- Cell shape-determining protein MreB
- Cytoskeleton protein RodZ
- Penicillin-binding protein 1B
- D-alanyl-D-alanine carboxypeptidase DacA
- Peptidoglycan D,D-transpeptidase FtsI
Sequence:
MKLQNSFRDYTAESALFVRRALVAFLGILLLTGVLIANLYNLQIVRFTDYQTRSNENRIKLVPIAPSRGIIYDRNGIPLALNRTIYQIEMMPEKVDNVQQTLDALRSVVDLTDDDIAAFRKERARSHRFTSIPVKTNLTEVQVARFAVNQYRFPGVEVKGYKRRYYPYGSALTHVIGYVSKINDKDVERLNNDGKLANYAATHDIGKLGIERYYEDVLHGQTGYEEVEVNNRGRVIRQLKEVPPQAGHDIYLTLDLKLQQYIETLLAGSRAAVVVTDPRTGGVLALVSTPSYDPNLFVDGISSKDYSALLNDPNTPLVNRATQGVYPPASTVKPYVAVSALSAGVITRNTTLFDPGWWQLPGSEKRYRDWKKWGHGRLNVTRSLEESADTFFYQVAYDMGIDRLSEWMGKFGYGHYTGIDLAEERSGNMPTREWKQKRFKKPWYQGDTIPVGIGQGYWTATPIQMSKALMILINDGIVKVPHLLMSTAEDGKQVPWVQPHEPPVGDIHSGYWELAKDGMYGVANRPNGTAHKYFASAPYKIAAKSGTAQVFGLKANETYNAHKIAERLRDHKLMTAFAPYNNPQVAVAMILENGGAGPAVGTLMRQILDHIMLGDNNTDLPAENPAVAAAEDH