wanglab/gogpt-training-data huggingface dataset:
Protein: Cell division control protein (D3ZRK7)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR001767}.
Interaction partners:
- DNA helicase
- DNA replication licensing factor MCM4
- DNA replication licensing factor MCM3
- Origin recognition complex subunit 4
- Origin recognition complex subunit 1
- DNA replication licensing factor MCM2
- DNA replication factor Cdt1
- DNA replication licensing factor MCM6
- DNA replication licensing factor MCM7
- Cyclin-A2
Sequence:
MPQTRSQTQATIDFPKKKQSKTLSKTNSRDSEVKLRNVQPVPTTPCADIKILPLSPRKRLGDDNLCNTPHLSPCSPPKLGRKENGPPRSHTRKGCRLIFDDELAVKASAPKEQDRVPQHQILSSAQRGQESETNPEQKCPPEKESACMRLFKQEGTCYQQAKLVLNTAVPDRLPAREQEMGVIRDFLKEHICGKKAGSLYLSGAPGTGKTACLSRILQDFKKEVKGFKTIVLNCMSLRNAQAVFPAIAQEIGREELCRPTGKDLMRKLEKHLTAERGPMIVLVLDEMDQLDSKGQDVLYTLFEWPWLSNSRLVLIGIANTLDLTDRILPRLEAREGCKPKLLNFPPYTRNQIAAILQDRLSQVSKDQVLDSAAIQFCARKVSAVSGDIRKALDVCRRAIEIVESDVRSQTVLKPLSECKSPCESLVPKRVGLAHISQVISGVDGNRVTLSQENTQDSLPLQQKILVCSLLLLTKRLKIKEVTLGKLYEAYSSVCRKQQVAAVDQSECLSLSGLLESRGIVGLKKNKESRLTKVSLKIEEKEIEHVLKGKAFIGNILAAGLP
Protein: Heat shock protein 60 (60 kDa chaperonin) (Protein Cpn60) (Q5B041)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: May participate in assembly and/or disassembly of proteins imported into the mitochondrion. HSP60 are ATPases and have affinity for unfolded proteins (By similarity). Involved in osmoadaptation.
Subcellular location: Mitochondrion {ECO:0000305}.
Interaction partners:
- Chaperonin, putative
- Iron-sulfur cluster biogenesis chaperone, mitochondrial
- CCT-theta
- Heat shock protein 90
- GrpE protein homolog
- T-complex protein 1 subunit alpha
- ATP synthase subunit beta
- Cofilin
- Heat shock protein 70
- DnaJ homolog 1
Sequence:
MQRALSSRTSVLSAASKRAAFTKPAGLNLQQQRFAHKELKFGVEARAQLLKGVDTLAKAVTSTLGPKGRNVLIESPYGSPKITKDGVTVAKAVQLQDKFENLGARLLQDVASKTNELAGDGTTTATVLARAIFSETVKNVAAGCNPMDLRRGIQAAVEAAVDYLQQNKRDITTGEEIAQVATISANGDTHVGKLISTAMERVGKEGVITVKEGKTLEDELEVTEGMRFDRGYTSPYFITDAKAQKVEFEKPLILLSEKKISAVQDIIPALEASTTLRRPLVIIAEDIEGEALAVCILNKLRGQLQVAAVKAPGFGDNRKSILGDLGVLTNGTVFTDELDIKLEKLTPDMLGSTGSITITKEDTIILNGEGSKDAIAQRCEQIRGVMADPTTSEYEKEKLQERLAKLSGGVAVIKVGGASEVEVGEKKDRVVDALNATRAAVEEGILPGGGTALLKAAANGLENVKPANFDQQLGVSIVKSAITRPARTIVENAGLEGSVIVGKLTDEFSKDFNRGFDSAKGEYVDMIAAGIVDPLKVVRTALVDASGVSSLLGTTEVAIVEAPEEKGPAAPGGMGGMGGMGGMGGGMF
Protein: RNA polymerase-associated protein LEO1 (Q5XJE5)
Organism: Mus musculus (Mouse)
Function: Component of the PAF1 complex (PAF1C) which has multiple functions during transcription by RNA polymerase II and is implicated in regulation of development and maintenance of embryonic stem cell pluripotency. PAF1C associates with RNA polymerase II through interaction with POLR2A CTD non-phosphorylated and 'Ser-2'- and 'Ser-5'-phosphorylated forms and is involved in transcriptional elongation, acting both independently and synergistically with TCEA1 and in cooperation with the DSIF complex and HTATSF1. PAF1C is required for transcription of Hox and Wnt target genes. PAF1C is involved in hematopoiesis and stimulates transcriptional activity of KMT2A/MLL1. PAF1C is involved in histone modifications such as ubiquitination of histone H2B and methylation on histone H3 'Lys-4' (H3K4me3). PAF1C recruits the RNF20/40 E3 ubiquitin-protein ligase complex and the E2 enzyme UBE2A or UBE2B to chromatin which mediate monoubiquitination of 'Lys-120' of histone H2B (H2BK120ub1); UB2A/B-mediated H2B ubiquitination is proposed to be coupled to transcription. PAF1C is involved in mRNA 3' end formation probably through association with cleavage and poly(A) factors. Involved in polyadenylation of mRNA precursors. Connects PAF1C to Wnt signaling (By similarity).
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- RNA polymerase II-associated factor 1 homolog
- RNA polymerase-associated protein RTF1 homolog
- RNA polymerase-associated protein CTR9 homolog
- Superkiller complex protein 8
- Parafibromin
- FACT complex subunit SPT16
- Transcription elongation factor SPT6
- Transcription elongation factor SPT4-A
- FACT complex subunit SSRP1
- Transcription elongation factor SPT5
Sequence:
MADMEDLFGSEAESEAERKDSESESDSDSDQDNGASGSNASGSESDQDDRGDSGQPSNKELFGDDSEEEGASHHSGSDNHSERSDNRSEASERSDHEDNEPSDEDQHSGSEAHNDDDDEGHRSDEGSRHSEAEGSEKAQSDDEKWDGEDKSDQSDDEKLQNSDDEDREQGSDEDKLQNSDDDEEKMQNTDDEDRAQISDDDRQQLSEEEKGNSDDEHPVASDNDEEKQNSDDEDQPQVSDEEKMQNSDDERPQVSDEDGRRSDGEEEQDQKSESARGSDSEDEVLRLKRKNAIPSDSEADSDTEVPKDNNGTMDLFGGADDISSGSDGEDKPPTPGQPVDENGLPQDQQEEEPIPETRIEVEIPKVNTDLGNDLYFVKLPNFLSVEPRPFDPQYYEDEFEDEEMLDEEGRTRLKLKVENTIRWRIRRDEEGNEIKESNARIVKWSDGSMSLHLGNEVFDVYKAPLQGDHNHLFIRQGTGLQGQAVFKTKLTFRPHSTDSATHRKMTLSLADRCSKTQKIRILPMAGRDPECQRTEMIKKEEERLRASIRRESQQRRMREKQHQRGLSASYLEPDRYDEEEEGEESVSLAAIKNRYKGGIREERARIYSSDSDEGSEEDKAQRLLKAKKLNSDEEGESSGKRKAEDDDKANKKHKKYVISDEEEEEDD
Protein: Serine/threonine protein phosphatase 2A regulatory subunit (F4JBC4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MWKQILSKLPNKKSSKHEHRGREHGGHSSSSSHTSGASTSKSTDNGAAKSHAKNASPAGKSAASDSGFKDGNLKSSGNNNNNNNNGVFTPYEALPSFKDVPNTEKQNLFIKKLNLCRVVFDFTDPTKNIKEKDIKRQTLLELVDYVNSPNGKFSEVGIQEVVRMVSANIFRTLNPQPRENKVIDALDLEEEEPSMDLAWPHLQLVYELFLRFVASPETDTKLAKRYIDQSFVLRLLDLFDSEDPRERDCLKTILHRIYGKFMVHRPFIRKSINNIFYRFVFETEKHNGIAEFLEILGSIINGFALPLKDEHKFVEKDCKLADTVIRGLLKYWPVTNSSKEVMFLNELEEVLEATQPPEFQRCMVPLFRQIARCLNSLHFQAISFRHTLTALLMRSRYSLPVISNEQMEELILRYGKYQCLGLLYSALGVAERALFLWNNNHIENLIMQNRKVILPIIFPALERNAQKHWNQAVHSLTLNVRKIFHDLDPELFKECLAKFKEDESKAAETEAKREATWKRLEELGVRKAS
Protein: TCP pilus virulence regulatory protein (A5F384)
Organism: Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 / O395)
Function: Probable regulatory protein for the tcp operon.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
Sequence:
MIGKKSFQTNVYRMSKFDTYIFNNLYINDYKMFWIDSGIAKLIDKNCLVSYEINSSSIILLKKNSIQRFSLTSLSDENINVSVITISDSFIRSLKSYILGDLMIRNLYSENKDLLLWNCEHNDIAVLSEVVNGFREINYSDEFLKVFFSGFFSKVEKKYNSIFITDDLDAMEKISCLVKSDITRNWRWADICGELRTNRMILKKELESRGVKFRELINSIRISYSISLMKTGEFKIKQIAYQSGFASVSYFSTVFKSTMNVAPSEYLFMLTGVAEK
Protein: Ras-related protein Rab-7a (Q23146)
Organism: Caenorhabditis elegans
Interaction partners:
- Vacuolar protein sorting-associated protein 18 homolog
- Vacuolar protein sorting-associated protein 16 homolog
- Vacuolar protein sorting-associated protein 39 homolog
- Vacuolar protein sorting-associated protein 11 homolog
- Rab GDP dissociation inhibitor
- Vacuolar protein sorting-associated protein 41 homolog
- Vacuolar fusion protein CCZ1 homolog
- TBC1 domain family member 15
- Vacuolar fusion protein MON1 homolog
- PH domain-containing protein
Sequence:
MSGTRKKALLKVIILGDSGVGKTSLMNQYVNRRFSNQYKATIGADFLTRDVNIDDRTVTLQIWDTAGQERFQSLGVAFYRGADCCVLAFDVTNAASFKSLDSWRDEFLIQASPRDPDHFPFVLLGNKVDLESQRAVSSKRAQSWCQTKGNIPYYEVSAKEALNVEAAFLAIARDALARESQETNDFPEFPDQIRLNPNQQNQQNSGCNC
Protein: Sialic acid-binding Ig-like lectin 9 (Siglec-9) (CDw329) (Protein FOAP-9) (CD antigen CD329) (Q9Y336)
Organism: Homo sapiens (Human)
Function: Putative adhesion molecule that mediates sialic-acid dependent binding to cells. Preferentially binds to alpha-2,3- or alpha-2,6-linked sialic acid. The sialic acid recognition site may be masked by cis interactions with sialic acids on the same cell surface.
Subcellular location: Membrane; Single-pass type I membrane protein.
Interaction partners:
- Amine oxidase [copper-containing] 3
- Mucin-1
- Mucin-16
- Kallikrein-14
- Kallikrein-13
- Sialic acid-binding Ig-like lectin 7
- Neural cell adhesion molecule 1
- Tyrosine-protein phosphatase non-receptor type 11
- Low affinity immunoglobulin gamma Fc region receptor III-A
Sequence:
MLLLLLPLLWGRERAEGQTSKLLTMQSSVTVQEGLCVHVPCSFSYPSHGWIYPGPVVHGYWFREGANTDQDAPVATNNPARAVWEETRDRFHLLGDPHTKNCTLSIRDARRSDAGRYFFRMEKGSIKWNYKHHRLSVNVTALTHRPNILIPGTLESGCPQNLTCSVPWACEQGTPPMISWIGTSVSPLDPSTTRSSVLTLIPQPQDHGTSLTCQVTFPGASVTTNKTVHLNVSYPPQNLTMTVFQGDGTVSTVLGNGSSLSLPEGQSLRLVCAVDAVDSNPPARLSLSWRGLTLCPSQPSNPGVLELPWVHLRDAAEFTCRAQNPLGSQQVYLNVSLQSKATSGVTQGVVGGAGATALVFLSFCVIFVVVRSCRKKSARPAAGVGDTGIEDANAVRGSASQGPLTEPWAEDSPPDQPPPASARSSVGEGELQYASLSFQMVKPWDSRGQEATDTEYSEIKIHR
Protein: D-rhamnosyltransferase WbpZ (EC 2.4.1.-) (GDP-D-Man:GlcNAc-diphosphate-lipid alpha-1,3-D-mannosyltransferase) (EC 2.4.1.348) (GDP-D-Man:GlcNAc/GalNAc-diphosphate-lipid alpha-1,3-D-mannosyltransferase) (GDP-D-rhamnose:GlcNAc/GalNAc-diphosphate-lipid alpha-1,3-D-rhamnosyltransferase) (Q9HTC0)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Non-processive alpha-1,3-D-rhamnosyltransferase. Catalyzes the transfer of one D-rhamnose (D-Rha) residue from donor substrate GDP-D-Rha in alpha-1-3 linkage to both GlcNAc- and GalNAc-diphosphate-lipid acceptor substrates. Is also able to transfer D-mannose (D-Man) to these acceptors at a lower level. Nucleotide sugars GDP-D-Rha, GDP-Fuc, UDP-Gal, UDP-GalNAc, UDP-GlcNAc and CMP-sialic acid cannot act as donor substrates. Only compounds with a diphosphate as the aglycone group can act as acceptor substrates. No activity is detected with compounds containing a diphosphate mimic. Fluorescent undecyl-anthracenyl group-containing compounds, such as GlcNAc-PO(3)-PO(3)-AnthrU and GalNAc-PO(3)-PO(3)-AnthrU, are also good acceptor substrates. Involved in the biosynthesis of the common polysaccharide antigen (CPA), also called A band, which is one of the two major cell surface O-antigens of the P.aeruginosa lipopolysaccharide. Involved in susceptibility to antibiotic colistin.
Subcellular location: Cytoplasm {ECO:0000305|PubMed:23664878}.
Interaction partners:
- Glycosyltransferase WbpY
- Glycosyltransferase WbpX
- ABC subunit of A-band LPS efflux transporter
- Transport permease protein
- Alginate biosynthesis protein AlgA
- GDP-6-deoxy-D-mannose reductase
- GDP-mannose 4,6-dehydratase
- Methyltransferase type 11 domain-containing protein
- Glycosyltransferase
- Uncharacterized protein
Sequence:
MRVLHFYKTYLSETVGGIEQVIFQLCESSGSWGIDNHVLTLSSDPHPPVVPFGGHVVHRARLDLQLASTGFSLSVFKQFRELAAEADVVNYHFPWPFMDLVHFLTGMNKPSVVTYHSDIIRQRVLLKLYRPLMSRFLHSVDRIVAASPNYFSTSDVLRQYREKTRVITYGLDKDGYPKPATQRLEHWREKLGPRFFLFVGVMRYYKGLHILLDALQGTDYPVVIVGAGPLQAELYAQAAALGLRNVHFLGRVDDEDKVALLQLSYAMVFPSHLRSEAFGISLLEGAMYGKPMISSEIGTGTSYINIHGETGLVVPPSQPAAFRQAMRWLWEHPQQAEEMGRNAEARYRQLFTAEEMGRRWSELYRELLEEKASSRYVKAAR
Protein: Trans-2-enoyl-CoA reductase [NADH] (TER) (EC 1.3.1.44) (Q97LU2)
Organism: Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / IAM 19013 / LMG 5710 / NBRC 13948 / NRRL B-527 / VKM B-1787 / 2291 / W)
Function: Involved in the fatty acid synthesis (FAS II). Catalyzes the reduction of the carbon-carbon double bond of crotonyl-CoA to yield butyryl-CoA.
Interaction partners:
- Acyl-CoA dehydrogenase, short-chain specific
- 3-hydroxyacyl-[acyl-carrier-protein] dehydratase FabZ
- Short-chain-enoyl-CoA hydratase
- 3-oxoacyl-
- 3-oxoacyl-[acyl-carrier-protein] synthase 2
- Probable nitronate monooxygenase
- Phosphate butyryltransferase
- CBS-domain containing protein, YHDP B.subtilis ortholog
- Mercuric resistance operon regulatory protein, MerR family
Sequence:
MIVKAKFVKGFIRDVHPYGCRREVLNQIDYCKKAIGFRGPKKVLIVGASSGFGLATRISVAFGGPEAHTIGVSYETGATDRRIGTAGWYNNIFFKEFAKKKGLVAKNFIEDAFSNETKDKVIKYIKDEFGKIDLFVYSLAAPRRKDYKTGNVYTSRIKTILGDFEGPTIDVERDEITLKKVSSASIEEIEETRKVMGGEDWQEWCEELLYEDCFSDKATTIAYSYIGSPRTYKIYREGTIGIAKKDLEDKAKLINEKLNRVIGGRAFVSVNKALVTKASAYIPTFPLYAAILYKVMKEKNIHENCIMQIERMFSEKIYSNEKIQFDDKGRLRMDDLELRKDVQDEVDRIWSNITPENFKELSDYKGYKKEFMNLNGFDLDGVDYSKDLDIELLRKLEP
Protein: Caveolin-3 (M-caveolin) (P56539)
Organism: Homo sapiens (Human)
Function: May act as a scaffolding protein within caveolar membranes. Interacts directly with G-protein alpha subunits and can functionally regulate their activity. May also regulate voltage-gated potassium channels. Plays a role in the sarcolemma repair mechanism of both skeletal muscle and cardiomyocytes that permits rapid resealing of membranes disrupted by mechanical stress (By similarity). Mediates the recruitment of CAVIN2 and CAVIN3 proteins to the caveolae.
Subcellular location: Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cell membrane {ECO:0000250|UniProtKB:P51638}; Peripheral membrane protein {ECO:0000250}. Membrane, caveola {ECO:0000250|UniProtKB:P51637}; Peripheral membrane protein {ECO:0000250}. Cell membrane, sarcolemma {ECO:0000250|UniProtKB:P51637}. Note=Potential hairpin-like structure in the membrane. Membrane protein of caveolae (By similarity). {ECO:0000250}.
Interaction partners:
- Dysferlin
- Caveolin-2
- Caveolin-1
- Dystroglycan 1
- Tripartite motif-containing protein 72
- Dystrophin
- Alpha-1-syntrophin
- Caveolae-associated protein 1
- Delta-sarcoglycan
- Proto-oncogene tyrosine-protein kinase Src
Sequence:
MMAEEHTDLEAQIVKDIHCKEIDLVNRDPKNINEDIVKVDFEDVIAEPVGTYSFDGVWKVSYTTFTVSKYWCYRLLSTLLGVPLALLWGFLFACISFCHIWAVVPCIKSYLIEIQCISHIYSLCIRTFCNPLFAALGQVCSSIKVVLRKEV
Protein: Peptidyl-lysine N-acetyltransferase YiaC (EC 2.3.1.-) (KAT) (P37664)
Organism: Escherichia coli (strain K12)
Function: N-epsilon-lysine acetyltransferase that catalyzes acetylation of a large number of proteins. Overexpression inhibits motility.
Interaction partners:
- Aminoalkylphosphonate N-acetyltransferase
- [Ribosomal protein bS18]-alanine N-acetyltransferase
- Peptidyl-lysine N-acetyltransferase PatZ
- Uncharacterized N-acetyltransferase YafP
- Uncharacterized N-acetyltransferase YjgM
- DNA-3-methyladenine glycosylase 1
- Protein ElaA
- Threonine efflux protein
- HTH-type transcriptional activator AaeR
- Uncharacterized protein YciQ
Sequence:
MIREAQRSELPAILELWLESTTWGHPFIKANYWRDCIPLVRDAYLANAQNWVWEEDGKLLGFVSIMEGRFLAAMFVAPKAVRRGIGKALMQYVQQRHPHLMLEVYQKNQPAINFYQAQGFHIVDCAWQDETQLPTWIMSWPVVQTL
Protein: LD24721p (MIP20650p) (Small glutamine-rich tetratricopeptide containing protein, isoform A) (Small glutamine-rich tetratricopeptide containing protein, isoform B) (Q9VJD4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Golgi to ER traffic protein 4 homolog
- ATPase ASNA1 homolog
- Large proline-rich protein BAG6
- Hsc70Cb, isoform G
- RE23139p1
- UV excision repair protein RAD23
- UV excision repair protein RAD23
- LD43819p
Sequence:
MPDAVQQSFVRSFIDYLKKQGDVMSPDQTESIEVAIQCLQAAFDLGDDVEAAPAAAGEEQATTQSSSTASAPDDDAVASGSAGIGAAAAAVPNNIDMFELFQSLYTERNPESLALAESIKNEGNRLMKENKYNEALLQYNRAIAFDPKNPIFYCNRAAAHIRLGENERAVTDCKSALVYNNNYSKAYCRLGVAYSNMGNFEKAEQAYAKAIELEPDNEVYKSNLEAARNARNQPPQTGRLREDLINMLSQPMVRNLFNNAEIDVEQLLSMLQNPMIMNTIRQQFGGGNAPTLPNDMVQMIYNMTSQLTGFPNSNANPGNEQQPGNQPPPST
Protein: Putative nudix hydrolase 1 (EC 3.6.1.-) (O45830)
Organism: Caenorhabditis elegans
Function: Probably mediates the hydrolysis of some nucleoside diphosphate derivatives.
Interaction partners:
- Putative nudix hydrolase 2
- GPS domain-containing protein
- Bis
- dUTP diphosphatase
Sequence:
MPLGKLDLVEEEYIAESGDHTPEASRLMGNGDSVVENLNGHTNGAVAKKKNEPRVPDMQLGKCRYVRLHDNVNYVAAAIILRNQGDDTEVLLIQEAKKSCRGKWYMPAGRVEAGETIEEAVVREVKEETGYSCDVVELLSLQVQGSGWYRYAFYCNITGGDLKTEPDQESLAAEWYNIKDLKANKVQLRGRDFIRLVDEAVTYRTHGPVDSIPRVMPLNQNVAGLFLEFMIVKHSRDGLRTEVLVHKSIKDETYLLEEEQPFPTVEFGFEYFFAMVVSKCYRHLLEEGANVVFTPSHVTRIKCHPKPMESLAHGVSIRVYCEHKQSASKAIIRSPRYHWISVESPETRQRFHMAQKQFRPSLHML
Protein: Leucine-rich tendon-specific protein, isoform B (A1ZBX8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MRPKLSAILMLLLLCTLAAANDLKDLLEDSTTSSSTSTTSSTIPSSVTSPTTPTAYVVSAAAVPALVAGRGKSKSTSGKYVNKSSPRKRKAEQVSSLPLPVDDALMEWKCPNITGTRNAELECGCDLPHTLRCNIDLHGMMLLADRLRTSPYSISLLDCSLRNVTFLSDAKIFDNVSLHGLVISSGEIKRVHKSAFLGIRGPLQALGLPGNALMSVPWNALSTLSALERLDLANNKIKALGTADFVGLTSLVYLELSNNQISSISQRTFVNLRKLEVLKLGGNRLGDYAQSLRSLSQCLSLRQLDLQANNLNGPLSEQTLPGMRNLESLNLNRNLIKSIQNKALANFSRLVSLSLRHNQIDVLQDHAFFGLGALDSLDLSYNGIVAISSASLQHLSRLTVLDLTHNFLRALTSDLIAPLPSLRELRLAGNDISIVARNAMDGARELESLQMQENPLSCDCSIRPFAEWLQESQLHSSLSASCVTPPRLEGAPLLQVPVETLSCDMDNVEKDNANIMQHLETLAKPNQTSPIKDLSEEIILHELHFSTDYGLILTWLLNLSKKDYMCDAIFVYKEEHINEILIDNSPIHCESKVVNGQNTVSVIVPDSSSLEIGESYRFCLVMIQEQKPDSELNIGCSNITRLERSSPGAVPVSRQYQRRPYYNANELKPEVVHDAGEDYQVNQRRFNSVVGSQPQQTQQSTLLHSYTVIDSLNKSFLPGLGLGVLVTSVLVLIWGATRIRQTGGSSGGGGRNGDSIDSNSSSMHNNNNNSRPGTPTATTCYAASDHIARLADAENGTRYLKLQATTSL
Protein: 2-amino-4-ketopentanoate thiolase beta subunit (EC 2.3.1.263) (AKP thiolase) (AKPT) (C1FW07)
Organism: Unknown prokaryotic organism
Function: Involved in the ornithine fermentation pathway. Catalyzes the thiolytic cleavage of 2-amino-4-ketopentanoate (AKP) with coenzyme A (CoA) to form acetyl-CoA and alanine. It is strictly specific for AKP.
Interaction partners:
Sequence:
MAKDTSYDAVMDRRAEIMSRALGLNYDEFIISDIAFDYEGMMAKAGYSLEEVRQIQSESGVGNTPLLELRNITDLARKTSKRGFGARILIKDEAANPSGSFKDRRASVSIHHAKKLGYPGVLAATSGNYGAAVASQAAMKNLGCIIVQEVFDSRHVGQPEIIEKSRKCEAYGAEVVQLTVGPELFYVSLILLEETGYFNASLYSPFGISGVETLGYELVEQIRARYDKDPAYIVVTHAGGGNVTGTARGALKAGAKNSTIIGASVDLSGLHMASDNDFNKKSFTTGHTGFGVPFATWPDRTDVPKNAARPLRYLDRYVTVTQGEVFYVTEALAQVEGMERGPAGNTSLAAAIALARELPEDEIVVVQETEYTGAGKHPWAQLDFAKQNGIAVKRGAPKENKPGKTIVIPQNFSQITATEMDLNRMRRSYIRNALERNKVKNVTEEDIRFLAEDTKTDADFVTSVIRDLGVRL
Protein: Putative pentatricopeptide repeat-containing protein At5g59200, chloroplastic (Protein ORGANELLE TRANSCRIPT PROCESSING 80) (Q9FIF7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in RNA editing event in chloroplasts. Required for the editing of a single site in rpl23 transcript.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:19934379}.
Interaction partners:
- Phosphoglycerate mutase family protein
Sequence:
MISSLAAITGGPSTFRRDPDSNTLRLSRRKTLISVLRSCKNIAHVPSIHAKIIRTFHDQDAFVVFELIRVCSTLDSVDYAYDVFSYVSNPNVYLYTAMIDGFVSSGRSADGVSLYHRMIHNSVLPDNYVITSVLKACDLKVCREIHAQVLKLGFGSSRSVGLKMMEIYGKSGELVNAKKMFDEMPDRDHVAATVMINCYSECGFIKEALELFQDVKIKDTVCWTAMIDGLVRNKEMNKALELFREMQMENVSANEFTAVCVLSACSDLGALELGRWVHSFVENQRMELSNFVGNALINMYSRCGDINEARRVFRVMRDKDVISYNTMISGLAMHGASVEAINEFRDMVNRGFRPNQVTLVALLNACSHGGLLDIGLEVFNSMKRVFNVEPQIEHYGCIVDLLGRVGRLEEAYRFIENIPIEPDHIMLGTLLSACKIHGNMELGEKIAKRLFESENPDSGTYVLLSNLYASSGKWKESTEIRESMRDSGIEKEPGCSTIEVDNQIHEFLVGDIAHPHKEAIYQRLQELNRILRFKENQIDIIMGF
Protein: Tubulin monoglycylase TTLL3 (EC 6.3.2.-) (Tubulin--tyrosine ligase-like protein 3) (Q1ECV4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Monoglycylase which modifies alpha- and beta-tubulin, adding a single glycine on the gamma-carboxyl groups of specific glutamate residues to generate monoglycine side chains within the C-terminal tail of tubulin. Not involved in elongation step of the polyglycylation reaction (By similarity). Preferentially glycylates a beta-tail peptide over the alpha-tail, although shifts its preference toward alpha-tail as beta-tail glutamylation increases (By similarity). Competes with polyglutamylases for modification site on beta-tubulin substrate, thereby creating an anticorrelation between glycylation and glutamylation reactions (By similarity). Not involved in elongation step of the polyglycylation reaction (By similarity).
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:A4Q9E5}. Cell projection, cilium {ECO:0000250|UniProtKB:A4Q9E5}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250|UniProtKB:A4Q9E5}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000250|UniProtKB:A4Q9E5}.
Interaction partners:
- Tubulin tyrosine ligase-like family, member 12.
- Cilia- and flagella-associated protein 97
- Intraflagellar transport protein 70A
Sequence:
MHQHIQVPPLEGKSRINYVNLPLINGDKLRTAKTLVDKAIKEKKVFSVQGPYPVIRAGLRARGWVERRLPRPSFSQPRRHDHETETTDEGDSSDEDDLGEEVERDDEAEDLYDLMSRLVRHETPYFYWTTRRDSVDCRSLRKEQMTNHYAKAGSFTTKVGLCMHLRNLQWFDAADPDTFFPRCYRLGAQDEKHAFIDDFRRTACTSLLLYVLEKYEGDSEGEKMGEVHNAKSHGLRKTRKQHSSQRIETSVIDSALHVCQEYLNSLEHCDIDNNLETNSTISEQQWKVFLQNYYLVVHEGINIEGCEYYLERCKCMLEQMRQVCPQMENDGICNIWIIKPGAKSRGRGIMCMNKLDDMLGLVDGDHCIMKDSKWVVQKYIERPLLVHDTKFDVRQWFLVTDWNPLTVWFYRECYLRFSTQPYSTHTLDSSVHLCNNSIQKHYQPSPDRSPSLPAECMWSCSQFRSWLAASGRAALWKAVVVPGMQKAVIQTLLTAQDSVEPRKASFELYGADFMLGRDLRPWLLEINASPTMAPSTGVTARLCPAVQEDTLRVVLDRRSERNTDTGGFQLIYKQAAVDVPQYVGVNLLIEGTSIRRPRAPVHKSLIQSHPEPLSKSTNHKSSLLSSPCTSGKENQSEEVKRACPNLPNRKITMDQSLIFHPKRKRPHRLVLPSTCCVLPNPTELHHPQRLSHTQPQSDRPHTHRTRSNLPTLYRPTPSVEVINIRPRQALTSSHYIHKIHTVNLSYPVLRMQQNHRRSKNTFAEREGPKSS
Protein: Protein ElaB (P0AEH5)
Organism: Escherichia coli (strain K12)
Subcellular location: Cell inner membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Uncharacterized protein YqjD
- Protein ElaA
- Uncharacterized protein YgaM
- Uncharacterized protein YebV
- Potassium binding protein Kbp
- DNA protection during starvation protein
- Fructose-bisphosphate aldolase class 1
- Osmotically-inducible putative lipoprotein OsmE
- Uncharacterized protein YccJ
- Osmotically-inducible protein Y
Sequence:
MSNQFGDTRIDDDLTLLSETLEEVLRSSGDPADQKYVELKARAEKALDDVKKRVSQASDSYYYRAKQAVYRADDYVHEKPWQGIGVGAAVGLVLGLLLARR
Protein: Mitochrondria associated protein (T3SS secreted effector Map) (Q7DB76)
Organism: Escherichia coli O157:H7
Interaction partners:
Sequence:
MFSPMTMAGRSLVQATAQTLKPAVTRAAMQAGTGATGMRFMPVQSNFVINHGKLTNQLLQAVAKQTRNGDTQQWFQQEQTTYISRTVNRTLDDYCRSNNSVISKETKGHIFRAVENALQQPLDMNGAQSSIGHFLQSNKYFNQKVDEQCGKRVDPITRFNTQTKMIEQVSQEIFERNFSGFKVSEIKAITQNAILEHVQDTRL
Protein: Type 1 encapsulin shell protein (Maritimacin) (EC 3.4.-.-) (Thermotoga bacteriocin) (Q9WZP2)
Organism: Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)
Function: Shell component of a type 1 encapsulin nanocompartment. Assembles into proteinaceous shells 23-24 nm in diameter with 2-2.5 nm thick walls. Cargo protein Flp (ferritin-like protein, may store iron) is targeted to the interior via its C-terminal extension; empty intact shells can be isolated in the absence of cargo protein. Fe(2+) may be able to pass though the 5-fold and dimer channels in the protein shell (Probable).
Subcellular location: Encapsulin nanocompartment {ECO:0000269|PubMed:19172747, ECO:0000269|PubMed:27224728, ECO:0000269|PubMed:30376298, ECO:0000269|PubMed:32961724, ECO:0000269|PubMed:33769792, ECO:0000269|PubMed:33953921, ECO:0000269|PubMed:34815415, ECO:0000269|PubMed:35119930, ECO:0000305|PubMed:9872409}. Note=Globular particles 19-20 nm, with 60-80 nm long tails (Probable). Shells are 23-24 nm in diameter, walls are 2.0-2.5 nm thick (PubMed:19172747). {ECO:0000269|PubMed:19172747, ECO:0000305|PubMed:9872409}.
Interaction partners:
- Hypothetical protein
Sequence:
MEFLKRSFAPLTEKQWQEIDNRAREIFKTQLYGRKFVDVEGPYGWEYAAHPLGEVEVLSDENEVVKWGLRKSLPLIELRATFTLDLWELDNLERGKPNVDLSSLEETVRKVAEFEDEVIFRGCEKSGVKGLLSFEERKIECGSTPKDLLEAIVRALSIFSKDGIEGPYTLVINTDRWINFLKEEAGHYPLEKRVEECLRGGKIITTPRIEDALVVSERGGDFKLILGQDLSIGYEDREKDAVRLFITETFTFQVVNPEALILLKF
Protein: Conserved oligomeric Golgi complex subunit 7 (Component of oligomeric Golgi complex 7) (A0A0S2Z652)
Organism: Homo sapiens (Human)
Subcellular location: Golgi apparatus membrane {ECO:0000256|ARBA:ARBA00004395}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004395}.
Interaction partners:
Sequence:
MDFSKFLADDFDVKEWINAAFRAGSKEAASGKADGHAATLVMKLQLFIQEVNHAVEETSHQALQNMPKVLRDVEALKQEASFLKEQMILVKEDIKKFEQDTSQSMQVLVEIDQVKSRMQLAAESLQEADKWSTLSADIEETFKTQDIAVISAKLTGMQNSLMMLVDTPDYSEKCVHLEALKNRLEALASPQIVAAFTSQAVDQSKVFVKVFTEIDRMPQLLAYYYKCHKVQLLAAWQELCQSDLSLDRQLTGLYDALLGAWHTQIQWATQVFQKPHEVVMVLLIQTLGALMPSLPSCLSNGVERAGPEQELTRLLEFYDATAHFAKGLEMALLPHLHEHNLVKVTELVDAVYDPYKPYQLKYGDMEESNLLIQMSAVPLEHGEVIDCVQELSHSVNKLFGLASAAVDRCVRFTNGLGTCGLLSALKSLFAKYVSDFTSTLQSIRKKCKLDHIPPNSLFQEDWTAFQNSIRIIATCGELLRHCGDFEQQLANRILSTAGKYLSDSCSPRSLAGFQESILTDKKNSAKNPWQEYNYLQKDNPAEYASLMEILYTLKEKGSSNHNLLAAPRAALTRLNQQAHQLAFDSVFLRIKQQLLLISKMDSWNTAGIGETLTDELPAFSLTPLEYISNIGQYIMSLPLNLEPFVTQEDSALELALHAGKLPFPPEQGDELPELDNMADNWLGSIARATMQTYCDAILQIPELSPHSAKQLATDIDYLINVMDALGLQPSRTLQHIVTLLKTRPEDYRQVSKGLPRRLATTVATMRSVNY