wanglab/gogpt-training-data huggingface dataset:
Protein: eEF1A lysine and N-terminal methyltransferase (eEF1A-KNMT) (Methyltransferase-like protein 13) [Includes: eEF1A lysine methyltransferase (EC 2.1.1.-); eEF1A N-terminal methyltransferase (EC 2.1.1.-)] (Q8N6R0)
Organism: Homo sapiens (Human)
Function: Dual methyltransferase that catalyzes methylation of elongation factor 1-alpha (EEF1A1 and EEF1A2) at two different positions, and is therefore involved in the regulation of mRNA translation. Via its C-terminus, methylates EEF1A1 and EEF1A2 at the N-terminal residue 'Gly-2'. Via its N-terminus dimethylates EEF1A1 and EEF1A2 at residue 'Lys-55'. Has no activity towards core histones H2A, H2B, H3 and H4. Negatively regulates cell proliferation at G1/S transition via transcriptional suppression of cell cycle regulatory genes such as CDK4 and CDK6.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:27659353}. Nucleus {ECO:0000269|PubMed:27659353}. Mitochondrion {ECO:0000269|PubMed:27659353}.
Interaction partners:
- N
- Pre-mRNA-splicing regulator WTAP
- Paired mesoderm homeobox protein 1
- EEF1A lysine methyltransferase 2
- Protein virilizer homolog
Sequence:
MNLLPKSSREFGSVDYWEKFFQQRGKKAFEWYGTYLELCGVLHKYIKPREKVLVIGCGNSELSEQLYDVGYRDIVNIDISEVVIKQMKECNATRRPQMSFLKMDMTQMEFPDASFQVVLDKGTLDAVLTDEEEKTLQQVDRMLAEVGRVLQVGGRYLCISLAQAHILKKAVGHFSREGWMVRVHQVANSQDQVLEAEPQFSLPVFAFIMTKFRPVPGSALQIFELCAQEQRKPVRLESAERLAEAVQERQQYAWLCSQLRRKARLGSVSLDLCDGDTGEPRYTLHVVDSPTVKPSRDNHFAIFIIPQGRETEWLFGMDEGRKQLAASAGFRRLITVALHRGQQYESMDHIQAELSARVMELAPAGMPTQQQVPFLSVGGDIGVRTVQHQDCSPLSGDYVIEDVQGDDKRYFRRLIFLSNRNVVQSEARLLKDVSHKAQKKRKKDRKKQRPADAEDLPAAPGQSIDKSYLCCEHHKAMIAGLALLRNPELLLEIPLALLVVGLGGGSLPLFVHDHFPKSCIDAVEIDPSMLEVATQWFGFSQSDRMKVHIADGLDYIASLAGGGEARPCYDVIMFDVDSKDPTLGMSCPPPAFVEQSFLQKVKSILTPEGVFILNLVCRDLGLKDSVLAGLKAVFPLLYVRRIEGEVNEILFCQLHPEQKLATPELLETAQALERTLRKPGRGWDDTYVLSDMLKTVKIV
Protein: Transcription initiation factor TFIID subunit 6 (Protein EMBRYO DEFECTIVE 2781) (TATA box associated factor II 59) (TBP-associated factor 6) (AtTAF6) (Transcription initiation factor TFIID subunit D5) (Q9MAU3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: TAFs are components of the transcription factor IID (TFIID) complex that is essential for mediating regulation of RNA polymerase transcription. Required for proper pollen function. May stabilize the interaction of TFIID with selected promoters. Not redundant with TAF6B.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Transcription initiation factor TFIID subunit 2
- Transcription initiation factor TFIID subunit 10
- Transcription initiation factor TFIID subunit 5
- Transcription initiation factor TFIID subunit 9
- Transcription initiation factor TFIID subunit 13
- Transcription initiation factor TFIID subunit 12
- Transcription initiation factor TFIID subunit 7
- Transcription initiation factor TFIID subunit 11
- Transcription initiation factor TFIID subunit 12b
- Transcription initiation factor TFIID subunit 4b
Sequence:
MSIVPKETVEVIAQSIGITNLLPEAALMLAPDVEYRVREIMQEAIKCMRHSKRTTLTASDVDGALNLRNVEPIYGFASGGPFRFRKAIGHRDLFYTDDREVDFKDVIEAPLPKAPLDTEIVCHWLAIEGVQPAIPENAPLEVIRAPAETKIHEQKDGPLIDVRLPVKHVLSRELQLYFQKIAELAMSKSNPPLYKEALVSLASDSGLHPLVPYFTNFIADEVSNGLNDFRLLFNLMHIVRSLLQNPHIHIEPYLHQLMPSVVTCLVSRKLGNRFADNHWELRDFAANLVSLICKRYGTVYITLQSRLTRTLVNALLDPKKALTQHYGAIQGLAALGHTVVRLLILSNLEPYLSLLEPELNAEKQKNQMKIYEAWRVYGALLRAAGLCIHGRLKIFPPLPSPSPSFLHKGKGKGKIISTDPHKRKLSVDSSENQSPQKRLITMDGPDGVHSQDQSGSAPMQVDNPVENDNPPQNSVQPSSSEQASDANESESRNGKVKESGRSRAITMKAILDQIWKDDLDSGRLLVKLHELYGDRILPFIPSTEMSVFL
Protein: Cytochrome c oxidase polypeptide 5, mitochondrial (Cytochrome c oxidase polypeptide V) (O74988)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:16823372}; Single-pass membrane protein {ECO:0000250|UniProtKB:P00424}.
Interaction partners:
- Cytochrome c oxidase subunit 13, mitochondrial
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
- Cytochrome c1, heme protein, mitochondrial
- Cytochrome c oxidase subunit 6, mitochondrial
- Cytochrome b-c1 complex subunit 7
- Cytochrome c oxidase subunit 4, mitochondrial
- Cytochrome c oxidase subunit 2
- Cytochrome b-c1 complex subunit 8
- Cytochrome b-c1 complex subunit 2, mitochondrial
- Cytochrome c oxidase subunit 3
Sequence:
MYLSKIICKKVPMKLLCTRNAATVSAAATNALQKEQPSGEAMIARPRLVDLDKRWGIMSQEEKDGLITDLYARQKQPWTTLSIEEKKAAYWIAFGEHGPRAFSHISQKTVFWGTVAGLTIGVVLFGLIRTQAAPSPRTMTREWQEKSNEYMKENKINPISGEASEGFKGRGQISGGIFSPSEKDKK
Protein: Nucleosome assembly protein 1-like 4 (Q78ZA7)
Organism: Mus musculus (Mouse)
Function: Acts as histone chaperone in nucleosome assembly. In condensing spermatids, mediates the loading of the heterodimer composed of histones H2AB1 and H2BC1/TH2B onto the nucleosomes, thereby promoting the replacement of histones to protamine in male germ cells.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q99733}. Cytoplasm {ECO:0000250|UniProtKB:Q99733}. Note=Present in the cytoplasm and excluded from the nucleus during G0/G1 phase, then relocates to the nucleus by the time cells are in S phase. Phosphorylated form localizes in the cytoplasm during the G0/G1 transition, whereas dephosphorylation leads to relocalization into the nucleus at the G1/S-boundary. {ECO:0000250|UniProtKB:Q99733}.
Interaction partners:
- Solute carrier family 22 member 18
- Pleckstrin homology-like domain family A member 2
Sequence:
MAENSLSDGGPADSVEAAKNASNTEKLTDQVMQNPQVLAALQERLDNVSHTPSSYIETLPKAVKRRINALKQLQVRCAHIEAKFYEEVHDLERKYAALYQPLFDKRREFITGDVEPTDAESAWHSENEEEDKLAGDMKNKVVIAEKEAATVEELNPKGIPEFWFTIFRNVDMLSELVQEYDEPILKHLQDIKVKFSDPGQPMSFVLEFHFEPNDYFTNPVLTKTYKMKSEPDKADPFSFEGPEIVDCDGCTIDWKKGKNVTVKTIKKKQKHKGRGTVRTITKQVPNESFFNFFSPLKASGDGESLDEDSEFTLASDFEIGHFFRERIVPRAVLYFTGEAIEDDDNFEEGEEGEEEELEGDEEGEDEDDADVNPKV
Protein: Alpha-1-antitrypsin 1-5 (Alpha-1 protease inhibitor 5) (Serine protease inhibitor 1-5) (Serine protease inhibitor A1e) (Serpin A1e) (Q00898)
Organism: Mus musculus (Mouse)
Function: Does not inhibit elastase or chymotrypsin. No target protease has been identified to date.
Subcellular location: Secreted {ECO:0000269|PubMed:8619829}.
Interaction partners:
- Neutrophil elastase
- Albumin
- Vitamin K-dependent protein C
- Haptoglobin
- Alpha-1-antitrypsin 1-2
- Pregnancy zone protein
- Alpha-1-antitrypsin 1-3
- Alpha-1-acid glycoprotein 1
- Alpha-1-acid glycoprotein 2
- Alpha-1-acid glycoprotein 3
Sequence:
MTPSISWCLLLLAGLCCLVPSFLAEDVQETDTSQKDQSPASHEIATNLGDFAISLYRELVHQSNTSNIFFSPVSIATAFAMLSLGSKGDTHTQILEGLQFNLTQTSEADIHNSFQHLLQTLNRPDSELQLSTGNGLFVNNDLKLVEKFLEEAKNHYQAEVFSVNFAESEEAKKVINDFVEKGTQGKIVEAVKKLEQDTVFVLANYILFKGKWKKPFDPENTKQAEFHVDESTTVKVPMMTLSGMLDVHHCSTLSSWVLLMDYAGNATAVFLLPDDGKMQHLEQTLNKELISKFLLNRRRRLAQIHIPRLSISGNYNLETLMSPLGITRIFNSGADLSGITEENAPLKLSQAVHKAVLTIDETGTEAAAATVLQGGFLSMPPILHFNRPFLFIIFEEHSQSPLFVGKVVDPTHK
Protein: Sodium/hydrogen exchanger (A0A060Y126)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Subcellular location: Apical cell membrane {ECO:0000256|ARBA:ARBA00004424}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004424}. Early endosome membrane {ECO:0000256|ARBA:ARBA00004520}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004520}. Recycling endosome membrane {ECO:0000256|ARBA:ARBA00004195}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004195}.
Interaction partners:
- EF-hand domain-containing protein
- EF-hand domain-containing protein
- EF-hand domain-containing protein
- EF-hand domain-containing protein
- EF-hand domain-containing protein
- FERM domain-containing protein
- FERM domain-containing protein
Sequence:
MACRTCLWLLGTTFFTCTVRLVVEGTEVGATQGSQPEPGVVESNHSQAGGGHGSSISGIQIVTFKWHHVEAPYLIALWILVAGVSKMVVELNHSLTSVIPESALLILIGWILGGIIYGADKMQTFTLTPTVFFFYLLPQVILDAGYFMPNKLFFSNMGAILVYAVIGTCWNAATVGLGLWGCWLGGAMGDIDIGLLQFLLFGSLIAAVDPVAVIAVFEEVHVNEVLFIMVFGESLLNDGVTVVLFNVFDAFVSLGGAEIDAVEIIKGIISFFVVAFGGSLVGIIFALLISLLTRCTKNIQIIEPGFIFILGYLSYLTAEMLSLSAILSIVFCGICCQKYINANMDERSVTTVRYVMKVFANGSETIIFVFLGISAIDPAVWVWNTGFILLTLLFIFVFRFIGVFLLTWILNKYRLVPLEFIDQVVMSYGGLRGAVAYGLVAMLDENKFKEKNLMVSTTLIVVYFTVMLQGITMKPLVTWLKVKRAAVTELTLAEKIQNRTFDHMLVAIEDISGQIGHNYMRDKWHNFEERWLCWFLMKPSARKSRDYIFNIFHQLNLKDAMSYVKEGERRGSLAFVRNETKADVDFNKKFRASFSEIMPDIMADNMGPVHVPLSSILQDIVPSVCLVMHEQDLTMRESEDFNAHHLLQQHLYRGRKQHRHRYSRSHLETNRDENEVQEIFQRTMRSRLESFKSAKMGVAPAKKIQTKHQKKDKPQKMPNGNSSDKSKNHPYGDKDFEFSEGDCGSGDEAAGDLFPMRAYRVEAGIVNPAFMAEMDPMDNMQQIPHVALLPQTLNSFDT
Protein: Cytosolic Fe-S cluster assembly factor NAR1 homolog (Nuclear architecture-related protein 1 homolog) (Q9Y7N7)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component of the cytosolic Fe/S protein assembly machinery. Required for maturation of extramitochondrial Fe/S proteins. May play a role in the transfer of pre-assembled Fe/S clusters to target apoproteins (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Probable cytosolic Fe-S cluster assembly factor SPAC806.02c
- Cytosolic Fe-S cluster assembly factor nbp35
- DNA repair/transcription protein mms19
- Fe-S cluster assembly protein dre2
- MIP18 family protein C144.16
- NADPH-dependent diflavin oxidoreductase 1
- Heme A synthase-mitochondrial ferredoxin fusion protein
- Protein isd11
- Translation initiation factor rli1
- Iron-sulfur clusters transporter atm1, mitochondrial
Sequence:
MAKLSVNDLNDFLSPGAVCIKPAQVKKQESKNDIRIDGDAYYEVTKDTGETSELGIASISLNDCLACSGCITSAETVLVNLQSYQEVLKHLESRKSQEILYVSLSPQVRANLAAYYGLSLQEIQAVLEMVFIGKLGFHAILDTNASREIVLQQCAQEFCNSWLQSRAHKNQNQVTNSVVNEHPLIPHSTSQISGVHSNTSSNSGINENAVLPILSSSCPGWICYVEKTHSNLIPNLSRVRSPQQACGRILKDWAVQQFSMQRNDVWHLSLMPCFDKKLEASRDEFSENGVRDVDSVLTPKELVEMFKFLRIDPIELTKNPIPFQQSTDAIPFWYPRITYEEQIGSSSGGYMGYVLSYAAKMLFGIDDVGPYVSMNNKNGDLTEYTLRHPETNEQLISMATCYGFRNIQNLVRRVHGNSSVRKGRVLLKKRVRSNAQNPTEEPSRYDYVEVMACPGGCINGGGQLPFPSVERIVSARDWMQQVEKLYYEPGTRSVDQSAVSYMLEQWVKDPTLTPKFLHTSYRAVQTDNDNPLLLANKW
Protein: Large ribosomal subunit protein eL42 (60S ribosomal protein L36a) (60S ribosomal protein L44) (Cell growth-inhibiting gene 15 protein) (Cell migration-inducing gene 6 protein) (P83881)
Organism: Homo sapiens (Human)
Function: Component of the large ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:23636399}.
Interaction partners:
- Small ribosomal subunit protein eS26
- Large ribosomal subunit protein eL20
- Large ribosomal subunit protein eL19
- Large ribosomal subunit protein eL34
- Small ribosomal subunit protein uS14
- Small ribosomal subunit protein eS24
- Large ribosomal subunit protein uL5
- Small ribosomal subunit protein uS17
- Small ribosomal subunit protein eS21
- Large ribosomal subunit protein eL18
Sequence:
MVNVPKTRRTFCKKCGKHQPHKVTQYKKGKDSLYAQGKRRYDRKQSGYGGQTKPIFRKKAKTTKKIVLRLECVEPNCRSKRMLAIKRCKHFELGGDKKRKGQVIQF
Protein: Neutral ceramidase (N-CDase) (NCDase) (OsCDase) (EC 3.5.1.23) (Acylsphingosine deacylase) (N-acylsphingosine amidohydrolase) (Q0JL46)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Hydrolyzes the sphingolipid ceramide into sphingosine and free fatty acid. Uses ceramide instead of phytoceramide as substrate.
Subcellular location: Secreted {ECO:0000250}. Endoplasmic reticulum {ECO:0000269|PubMed:18547394}. Golgi apparatus {ECO:0000269|PubMed:18547394}.
Interaction partners:
- Ceramide kinase
- Non-lysosomal glucosylceramidase
- Non-lysosomal glucosylceramidase
- Alkaline phytoceramidase family protein, expressed
- 3-dehydrosphinganine reductase
- Os07g0444000 protein
- Sphingolipid delta
- Very-long-chain aldehyde decarbonylase GL1-9
- aldehyde oxygenase
- sphingosine kinase
Sequence:
MEASSWLCYQARGFGSSRVWLWLLLALVLLNCSLVLSASPYLVGMGSFDITGPAADVNMMGYANTEQIASGIHFRLKSRAFIVAEPNGKRVVFVNIDACMASQIVTIKVLERLKARYGDLYNENNVAISGIHTHAGPGGYLQYVVYIVTSLGFVRQSFDVIVDGIEQSIVEAHNNLRPGKIFVNKGDLLDAGVNRSPSAYLNNPAEERSKYEYNVDKEMTLIKFVDDELGPVGSFNWFATHGTSMSRTNSLISGDNKGAAARFMEDWAEQMGLPKQSAHANSDDLRSLHKTSVLPRRVSTIIPEPNEITDDLIQLASSYEASGGRRLAGSSITRRIRSTQQNKPKFVSAFCQSNCGDVSPNVLGTFCIDTNLPCDFNHSTCNGKNELCYGRGPGYPDEFESTRVIGNRQFLKARDLFDSASEEIQGKIDYRHTYLDFSKLEVKVSTSAGGQQTVKTCPAAMGFAFAAGTTDGPGAFDFRQGDVKGNPFWKLVRNLLKTPGKDQVECHSPKPILLDTGEMKEPYDWAPAILPVQMIRIGQLVILCVPGEFTTMAGRRLRDAVKTVLTSGNSEFDKNIHVVLAGLTNSYSQYITTFEEYQIQRYEGASTLYGPHTLSAYIQEFQKLAMAMIANKEVPTNFQPPDMLDKQIGLLPGVVFDSTPLGVKFGDVNSDVPGNSTFNKGSTVNATFYSACPRNDLLTDGTFALVEKLDGNNNWVPVYDDDDWSLRFKWSRPARLSSRSFATLEWTVPEDAAAGVYRLRHFGASKPMFGSVRHFTGTSRAFAVR
Protein: Anti-bacteriophage protein B (Probable helicase AbpB) (P52126)
Organism: Escherichia coli (strain K12)
Function: Part of an antiviral system composed of AbpA and AbpB; when both are expressed from a plasmid they confer resistance to phages T2, T4, T7 and lambda but not RB32 or RB69. Resistance is temperature dependent, it can be seen at 30 degrees Celsius but not at 37 or 42 degrees Celsius. The system impairs phage but not bacterial DNA synthesis (shown for T4, T7 and lambda). Partially suppressed by mutations in T4 gene 41, a replicative helicase.
Interaction partners:
- Anti-bacteriophage protein A
- Elongation factor G
- Ion-translocating oxidoreductase complex subunit B
Sequence:
MTEIYEQAKHSLQGEDFSSFNYLFAVNKLLSNPVSYDLGRDLIVRALDSRERFSEHTTILKNMVRKSGLFPYLKKEFTSLTPDDLRVLELYRTPFSDGYVFHSMQFHIFDLLKSGQNVVLSAPTSMGKSAIVDSLLGMGTLKRLVLVVPTVALADETRRRLQERFGDRYQIIHHSSQVCHSDQAVYVLTQERVNERDDIVDIDLFVIDEFYKLAFRQLKSGDIDHQDERVIELNIALSKLLKVSRQFYLTGPFVNSIRGLEKLGYPHTFVSTDFNTVALDVKTFGIKANDDKAKLKALGEIAHACVDATIIYCKSPTVAGLVARELIRLGHGTPTENPHVDWVSEEFDADWDYTVALRNGIGLHFGALPRALQQYTADQFNAGKLRFLLCTSTIIEGVNTIAKNVVIYDNRDGTRSIDKFTHGNIKGRAGRMGVHFVGKIFCLEEIPEDNLNQEVDIPLGIQGIDTPINLLASVQPDHLSEFSQDRFDEVFINDRVSIDLVKKHSYFRVEQFEMLQSMFEMMDDNEFSSLVFHWTPATNFLKTFAKIIARLVPHTFSRNGVPVKPTDVMIAKLAGYLSAESYSEYLKNQIDYARQWISEGEKRTLSIALNNDLKLITNTFGYTLPKVLSLMEDVVKHHAVKRGIRSKVDYTHVKLAFESFHLPPGVNALEEIGIPIQTLHRLVDLLEFSDEADVDELSQYLRDTQDIWSRSIGYVDQMFIRRALGIRRH
Protein: Orphan receptor COUP-TFI (Q62681)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|RuleBase:RU004334}.
Interaction partners:
Sequence:
MAMVVSSWRDPQDDVAGGNPGGPNPAAQAARGGGGGEQQQAGSGAPHTPQTPGQPGAPATPGTAGDKGQGPPGSGQSQQHIECVVCGDKSSGKHYGQFTCEGCKSFFKRSVRRNLTYTCRANRNCPIDQHHRNQCQYCRLKKCLKVGMRREAVQRGRMPPTQPNPGQYALTNGDPLNGHCYLSGYISLLLRAEPYPTSRYGSQCMQPNNIMGIENICELAARLLFSAVEWARNIPFFPDLQITDQVSLLRLTWSELFVLNAAQCSMPLHVAVLAAAGLHASPMSADRVVAFMDHIRIFQEQVEKLKALHVDSAEYSCLKAIVLFTSDACGLSDAAHIESLQEKSQCALEEYVRSQYPNQPSRFGKLLLRLPSLRTVSSSVIEQLFFVRLVGKTPIETLIRDMLLSGSSFNWPYMSIQCS
Protein: Pbxy homeodomain protein (Pre-B-cell leukemia homeobox 2) (Pre-B-cell leukemia transcription factor 2) (Q9I9B4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00108}.
Interaction partners:
- Homeobox protein Hox-B1b
- Homeobox protein Hox-B7a
- Homeobox protein Hox-B1a
- Ral guanine nucleotide dissociation stimulator-like 2.
- Homeobox protein PKNOX1.1
- Homeobox protein Hox-A1a
- PHD finger protein 1.
- Homeobox protein Meis1b
Sequence:
MLQPQQPITGNGPSASRGGGLSVHPGMHPLNSIHPAAQHRPDGADPAGLEGTENGHDNRRDIGDILQQIMTITDQSLDEAQAKKHALNCHRMKPALFSVLCEIKEKTGLSMRNVQEEEPPDPQLVRLDNMLLAEGVAGPEKGGGAAAAVSAATSSGGMSPDSSLEHSDYKSKLSQIRNIYHTELEKYEQACSEFTTHVMNLLREQSRTRPVSPREIERMVAIIHRKFSSIQTQLKQSTCEAVMILRSRFLDARRKRRNFSKQATEVLNEYFYSHLSNPYPSEEAKEELAKQCSITVSQVSNWFGNKRIRYKKNIGKYQEEANLYAMKTALGATQSEDSPHTPNSTGSGSFSLSGSADCFLGVPPMNGEQPPYHMGAQTNGNWQEQNSPPSAASPGTDHSVDSD
Protein: UDP-glucuronate decarboxylase (EC 4.1.1.35) (F4KHU8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MTFNAYSGLRSLSQAMAATSEKQNTTKPPPSPSPLRNSKFCQPNMRILISGGAGFIGSHLVDKLMENEKNEVVVADNYFTGSKENLKKWIGHPRFELIRHDVTEPLLIEVDRIYHLACPASPIFYKYNPVKTIKTNVIGTLNMLGLAKRVGARILLTSTSEVYGDPLIHPQPESYWGNVNPIGVRSCYDEGKRVAETLMFDYHRQHGIEIRIARIFNTYGPRMNIDDGRVVSNFIAQALRGEALTVQKPGTQTRSFCYVSDMVDGLIRLMEGNDTGPINIGNPGEFTMVELAETVKELINPSIEIKMVENTPDDPRQRKPDISKAKEVLGWEPKVKLREGLPLMEEDFRLRLNVPRN
Protein: Opsin 1 (cone pigments), long-wave-sensitive, 1 (W5KG21)
Organism: Astyanax mexicanus (Blind cave fish) (Astyanax fasciatus mexicanus)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU004951}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU004951}.
Interaction partners:
Sequence:
MGDQWGDAVFAARRRGDDTTREAAFTYTNSNNTKDPFEGPNYHIAPRWVYNLATCWMFFVVVASTVTNGLVLVASAKFKKLRHPLNWILVNLAIADLLETLLASTISVCNQFFGYFILGHPMCVFEGFTVATCGIAGLWSLTVISWERWVVVCKPFGNVKFDGKMATAGIVFTWVWSAVWCAPPIFGWSRYWPHGLKTSCGPDVFSGSEDPGVQSYMIVLMITCCFIPLGIIILCYIAVWWAIRTVAQQQKDSESTQKAEKEVSRMVVVMIMAYCFCWGPYTFFACFAAANPGYAFHPLAAAMPAYFAKSATIYNPVIYVFMNRQFRVCIMQLFGKKVDDGSEVSTSKTEVSSVAPA
Protein: SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 1 (A0A0A0MRP6)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MEQDTAAVAATVAAADATATIVVIEDEQPGPSTSQEEGAAAAATEATAATEKGEKKKEKNVSSFQLKLAAKAPKSEKEMDPEYEEKMKADRAKRFEFLLKQTELFAHFIQPSAQKSPTSPLNMKLGRPRIKKDEKQSLISAGDYRHRRTEQEEDEELLSESRKTSNVCIRFEVSPSYVKGGPLRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHNWMNEFKRWVPSLRVICFVGDKDARAAFIRDEMMPGEWDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKLSEIVREFKSTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDTKNCLGDQKLVERLHAVLKPFLLRRIKTDVEKSLPPKKEIKIYLGLSKMQREWYTKILMKDIDVLNSSGKMDKMRLLNILMQLRKCCNHPYLFDGAEPGPPYTTDEHIVSNSGKMVVLDKLLAKLKEQGSRVLIFSQMTRLLDILEDYCMWRGYEYCRLDGQTPHEEREEAIEAFNAPNSSKFIFMLSTRAGGLGINLASADVVILYDSDWNPQVDLQAMDRAHRIGQKKPVRVFRLITDNTVEERIVERAEIKLRLDSIVIQQGRLIDQQSNKLAKEEMLQMIRHGATHVFASKESELTDEDITTILERGEKKTAEMNERLQKMGESSLRNFRMDIEQSLYKFEGEDYREKQKLGMVEWIEPPKRERKANYAVDAYFREALRVSEPKIPKAPRPPKQPNVQDFQFFPPRLFELLEKEILYYRKTIGYKVPRNPDIPNPALAQREEQKKIDGAEPLTPEETEEKEKLLTQGFTNWTKRDFNQFIKANEKYGRDDIDNIAREVEGKSPEEVMEYSAVFWERCNELQDIEKIMAQIERGEARIQRRISIKKALDAKIARYKAPFHQLRIQYGTSKGKNYTEEEDRFLICMLHKMGFDRENVYEELRQCVRNAPQFRFDWFIKSRTAMEFQRRCNTLISLIEKENMEIEERERAEKKKRATKTPMSQKRKAESATESSGKKDVKKVKS
Protein: CheA signal transduction histidine kinase (Q725K1)
Organism: Nitratidesulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / CCUG 34227 / NCIMB 8303 / VKM B-1760 / Hildenborough) (Desulfovibrio vulgaris)
Interaction partners:
Sequence:
MHFRPAIVYPALDRHRIFRKVRELGAVDRPPDHRPAHLCHFEAAMTPQEANRPQPGDDIIELTDIIEKGTVPAAADAVDFDKELEDLFADSDIEAAISNLSLPDEAPSPAKAAVQEPADTGLDSDIDAFLDALDGPGHAAPENVAPKLAQPTPTPGGRPVNPDEQLQMPDMSDMDSLLEQLDAPAATKSAGNIEDLDAGDLDALLDDILGGAPASPKAATMTPPPATEAEPAPMSLDDLDALLDAPVAPAAPAAPEPAAERAPGTATMSLDDIDALLDTPVAPATPPAPEPAAERAPGTAAMSLDDIDALFDAPVAPAAPAAPEPASEPTPGTAAMSLDDIDALLDAPVAPAAPAAPEPASEPTPGTATMSLDDIDALLDAPVAPAAPAAPEPASEPTPGTATMSLDDIDALLDAPVAPAAPAAPEPAAEPTPGTAAMSLDDIDALLDAAPMPPAPEEAMPAHDTAAEETVIAAMPPVQEEPVAALAAETMAVAAAATAMAPQEPVISPASGPMSAPVMDANALEGLLSRLQALEDEVAGLRATVVHGNEVTAGLEERLAALDAESAVAASPEPAPAAESAPPAEPLMPDADALGRILSEMLAEGHPAMEWLVEQVRAVVMNGMSDHIASAVERAVEQTTAPMRDALSGVDATAEGMVELDNRLSSLEATRITADDIAKLESALREALRDDTDKAAAAAAARVIRQEIAALAEIL
Protein: ANUBL1 protein (Q86WR3)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MELENDYCLNDYNISEGWTLKLVLAMRGGPINTRRVPTDDPLRTMAEYLDSSRVEVWEKTSCSKQVTFLVYQEGDQLNFFPAVDRGDGTLTPLSDSSKKIDFHLHVLRRKGEHRMSGGSMYNSDTDEDEETEPSSSGQQIIENSITMNKMKLLKAKMKNMNLSKKPKKAVKIKPHPPVAPRPSSGSTAPSRHRLLRVLPNIGQSCSPAFGNAYPPEISRNGISSLATQLSAERYISSITGEFLKEDNSWENNTLSHFSSNVKLPPQIPHLELGNDQELADSVLHLGSSLPRQTKHFLGNLPSSNGNIVLPSEECVTEQSLLPKVGSLASFAEGNADEQSSGLEGACKVNLELLLTNADKGLKAPEQHLKHVAGVLNGESVETSVLNYRELSPHKNRLLSPLRCSAPMSLHNSLVKPERQSKCFEFGKLQPSSSQSLDVQNITDSSFSRTTCFQGVKVDSLGKRSDVISKVEARDITEMTNKASKEPVGCVNNISFLASLAGSTSRNRLQSTRGAGRLQNSGTGLSTNLQHFQEENFRKSSPQLEHTGVFLSTHGVGMNGNNAAAGKSVGECTTHHLPPVKAPLQTKKKTTNHCFLCGKKTGLASSYECRCGNNFCASHRYAETHGCTYDYKSAGRRYLHEANPVVNAPKLPKI
Protein: Collagenase ColH (EC 3.4.24.3) (Class II collagenase) (Gelatinase ColH) (Microbial collagenase) (Q46085)
Organism: Hathewaya histolytica (Clostridium histolyticum)
Function: Clostridial collagenases are among the most efficient degraders of eukaryotic collagen known; saprophytes use collagen as a carbon source while pathogens additionally digest collagen to aid in host colonization. Has both tripeptidylcarboxypeptidase on Gly-X-Y and endopeptidase activities; the endopeptidase cuts within the triple helix region of collagen while tripeptidylcarboxypeptidase successively digests the exposed ends, thus clostridial collagenases can digest large sections of collagen. The full-length protein has collagenase activity, while both the 116 kDa and 98 kDa forms act on gelatin. In vitro digestion of soluble calf skin collagen fibrils requires both ColG and ColH; ColG forms missing the second collagen-binding domain is also synergistic with ColH, although their overall efficiency is decreased. Digestion of collagen requires Ca(2+) and is inhibited by EDTA. The activator domain (residues 119-388) and catalytic subdomain (330-601) open and close around substrate allowing digestion when the protein is closed.
Subcellular location: Secreted {ECO:0000269|PubMed:18374061, ECO:0000269|PubMed:22099748, ECO:0000269|PubMed:7961400}.
Interaction partners:
Sequence:
MKRKCLSKRLMLAITMATIFTVNSTLPIYAAVDKNNATAAVQNESKRYTVSYLKTLNYYDLVDLLVKTEIENLPDLFQYSSDAKEFYGNKTRMSFIMDEIGRRAPQYTEIDHKGIPTLVEVVRAGFYLGFHNKELNEINKRSFKERVIPSILAIQKNPNFKLGTEVQDKIVSATGLLAGNETAPPEVVNNFTPILQDCIKNIDRYALDDLKSKALFNVLAAPTYDITEYLRATKEKPENTPWYGKIDGFINELKKLALYGKINDNNSWIIDNGIYHIAPLGKLHSNNKIGIETLTEVMKVYPYLSMQHLQSADQIKRHYDSKDAEGNKIPLDKFKKEGKEKYCPKTYTFDDGKVIIKAGARVEEEKVKRLYWASKEVNSQFFRVYGIDKPLEEGNPDDILTMVIYNSPEEYKLNSVLYGYDTNNGGMYIEPEGTFFTYEREAQESTYTLEELFRHEYTHYLQGRYAVPGQWGRTKLYDNDRLTWYEEGGAELFAGSTRTSGILPRKSIVSNIHNTTRNNRYKLSDTVHSKYGASFEFYNYACMFMDYMYNKDMGILNKLNDLAKNNDVDGYDNYIRDLSSNYALNDKYQDHMQERIDNYENLTVPFVADDYLVRHAYKNPNEIYSEISEVAKLKDAKSEVKKSQYFSTFTLRGSYTGGASKGKLEDQKAMNKFIDDSLKKLDTYSWSGYKTLTAYFTNYKVDSSNRVTYDVVFHGYLPNEGDSKNSLPYGKINGTYKGTEKEKIKFSSEGSFDPDGKIVSYEWDFGDGNKSNEENPEHSYDKVGTYTVKLKVTDDKGESSVSTTTAEIKDLSENKLPVIYMHVPKSGALNQKVVFYGKGTYDPDGSIAGYQWDFGDGSDFSSEQNPSHVYTKKGEYTVTLRVMDSSGQMSEKTMKIKITDPVYPIGTEKEPNNSKETASGPIVPGIPVSGTIENTSDQDYFYFDVITPGEVKIDINKLGYGGATWVVYDENNNAVSYATDDGQNLSGKFKADKPGRYYIHLYMFNGSYMPYRINIEGSVGR