wanglab/gogpt-training-data huggingface dataset:
Protein: Dol-P-Man:Man(5)GlcNAc(2)-PP-Dol alpha-1,3-mannosyltransferase (EC 2.4.1.258) (Asparagine-linked glycosylation protein 3 homolog) (Dol-P-Man-dependent alpha(1-3)-mannosyltransferase) (Dolichyl-P-Man:Man(5)GlcNAc(2)-PP-dolichyl mannosyltransferase) (Dolichyl-phosphate-mannose--glycolipid alpha-mannosyltransferase) (Not56-like protein) (Q92685)
Organism: Homo sapiens (Human)
Function: Adds the first Dol-P-Man derived mannose in an alpha-1,3 linkage to Man5GlcNAc2-PP-Dol.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305|PubMed:10581255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Dol-P-Man:Man
- Dolichyl pyrophosphate Man9GlcNAc2 alpha-1,3-glucosyltransferase
- Dolichyl-phosphate beta-glucosyltransferase
- GDP-Man:Man
- Dolichol phosphate-mannose biosynthesis regulatory protein
- Dol-P-Glc:Glc
- Alpha-1,2-mannosyltransferase ALG9
- Dolichol-phosphate mannosyltransferase subunit 3
- Dolichol-phosphate mannosyltransferase subunit 1
- Alpha-1,3/1,6-mannosyltransferase ALG2
Sequence:
MAAGLRKRGRSGSAAQAEGLCKQWLQRAWQERRLLLREPRYTLLVAACLCLAEVGITFWVIHRVAYTEIDWKAYMAEVEGVINGTYDYTQLQGDTGPLVYPAGFVYIFMGLYYATSRGTDIRMAQNIFAVLYLATLLLVFLIYHQTCKVPPFVFFFMCCASYRVHSIFVLRLFNDPVAMVLLFLSINLLLAQRWGWGCCFFSLAVSVKMNVLLFAPGLLFLLLTQFGFRGALPKLGICAGLQVVLGLPFLLENPSGYLSRSFDLGRQFLFHWTVNWRFLPEALFLHRAFHLALLTAHLTLLLLFALCRWHRTGESILSLLRDPSKRKVPPQPLTPNQIVSTLFTSNFIGICFSRSLHYQFYVWYFHTLPYLLWAMPARWLTHLLRLLVLGLIELSWNTYPSTSCSSAALHICHAVILLQLWLGPQPFPKSTQHSKKAH
Protein: Collagenase ColT (EC 3.4.24.3) (Microbial collagenase) (Q899Y1)
Organism: Clostridium tetani (strain Massachusetts / E88)
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 (By similarity). The activator domain (residues 57-330) and catalytic subdomain (340-611) open and close around substrate allowing digestion when the protein is closed.
Subcellular location: Secreted {ECO:0000250|UniProtKB:Q9X721}.
Interaction partners:
Sequence:
MKKKFIKMLCSIAIGCMISTSYSIKVSAFSNGNTKTNPNGEFKSLSLNSTNPYKTKYSFNDLNKLSNKEILDLTSKIKWSDISDLFQYNKDSYTFYSNKERVQALIDGLYEKGCNYTSTDDKGIDTLVEILRSGFYLGYYNDSLKYLNDKSFKDKCIPAMIAIENNKNFKLGENGQDTVVHALGKLIGNTSCNDEVVNKTIPILEQYYNEIDKYSKDRLKSNAVYNFMKEINYDISQYEYAHNIRDYKNTPWSGKIDSFIDTISKFASISNVTKDNGWIINNSIYYTAKLSKYHSNPSIPHSVIDNCIEIFPDYSEQYFTAIEAIKEDFNSRDSKGNVIDINKLIEEGKKHYLPKTYTFDNGKIIIKAGDKVEESKIQKLYWASKEVKSQFHRIIGNDKPLEVGNADDILTIVIYNNPEEYKLNKTLYGYSVDNGGIYIEGIGTFFTYERTPQESIYSLEELFRHEFTHYLQGRYLIPGLFNKGDFYKGNNGRITWFEEGSAEFFAGSTRTSVLPRKSMVGGLSKNPKERFNADKLLHSKYSDGWDFYKYGYAFSDYMYNNNKKLFSDLVSTMKNNDVKGYEALIEESSKDSKINKDYEYHMENLVNNYDNYTIPLVSDDYMKQYDNKSLHEIKSDIEKAMDVKNSQITKESSQYFDTYNLKATYTLSSNKGEISNWNYMNNKINEALNKLDNLSWGGYKTVTAYFSNPRLNSNNEVVYDIVFHGLLSHNKNSNEKVEVKEEPEIKDKDSFENVIYEKENNDSFDKANKIHKNQIVMATLDTEDYRDTFYFDALTSGSIDITIENIHGNSDAFNWLVYNDEDLNNYIAYPTKKEDNKLMGSFKVHKPGRYYILVYKTSLNKVNYKLNISDATNMAPVIKKIHEKENNDSFETANKITLDTLVLGNLDYKDVSDIYSFDIENTKDLNIKLTNLNNLGIAWNLYKESDLNNYIAYGAKSDNAIVGKCNLSPGKYYLYVYKYSGDKGNYSVIIN
Protein: LIM/homeobox protein Lhx1 (LIM homeobox protein 1) (Homeobox protein Lim-1) (P53411)
Organism: Gallus gallus (Chicken)
Function: Transcriptional factor that defines subclasses of motoneurons that segregate into columns in the spinal cord and select distinct axon pathways. Acts in conjunction with ISL-2.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Paired-box containing protein Pax-2
- Uncharacterized protein
- T-cell leukemia homeobox protein 3
- Pancreas transcription factor 1 subunit alpha
- Sine oculis-related homeobox 2 homolog
- Uncharacterized protein.
Sequence:
MVHCAGCKRPILDRFLLNVLDRAWHVKCVQCCECKCNLTEKCFSREGKLYCKNDFFRCFGTKCAGCAQGISPSDLVRRARSKVFHLNCFTCMMCNKQLSTGEELYIIDENKFVCKEDYLNNSNTAKENSLHSATTGSDPSLSPDSQDPSQDDAKDSESANVSDKETGSNENDDQNLGAKRRGPRTTIKAKQLETLKAAFAATPKPTRHIREQLAQETGLNMRVIQVWFQNRRSKERRMKQLSALGARRHAFFRSPRRMRPLVDRLEPGELLPNGPFSFYGDYQSEYYGPGANYEFFPQGPPSSQAQTPVELPFGAAGGPPGTPLGALEHPLPGHHPPGEAQRFPDMLAHPAGDSPSPEPTLPGSLHSMSAEVFGPSPPFSSISVNGGANYGNHLSHPPEMNEAAVW
Protein: Phosphatidylserine lipase ABHD16A (EC 3.1.-.-) (Alpha/beta hydrolase domain-containing protein 16A) (Abhydrolase domain-containing protein 16A) (HLA-B-associated transcript 5) (hBAT5) (Monoacylglycerol lipase ABHD16A) (EC 3.1.1.23) (Protein G5) (O95870)
Organism: Homo sapiens (Human)
Function: Phosphatidylserine (PS) lipase that mediates the hydrolysis of phosphatidylserine to generate lysophosphatidylserine (LPS) (By similarity). LPS constitutes a class of signaling lipids that regulates immunological and neurological processes (By similarity). Has no activity towards diacylglycerol, triacylglycerol or lysophosphatidylserine lipase. Also has monoacylglycerol lipase activity, with preference for 1-(9Z,12Z-octadecadienoyl)-glycerol (1-LG) and 2-glyceryl-15-deoxy-Delta(12,14)-prostaglandin J2 (15d-PGJ(2)-G).
Subcellular location: Membrane {ECO:0000250|UniProtKB:Q9Z1Q2}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Lysophosphatidylserine lipase ABHD12
- Zinc finger and BTB domain-containing protein 12
- E3 ubiquitin-protein ligase RNF5
- Leukocyte-specific transcript 1 protein
- Protein PRRC2A
- Signal peptide peptidase
Sequence:
MAKLLSCVLGPRLYKIYRERDSERAPASVPETPTAVTAPHSSSWDTYYQPRALEKHADSILALASVFWSISYYSSPFAFFYLYRKGYLSLSKVVPFSHYAGTLLLLLAGVACLRGIGRWTNPQYRQFITILEATHRNQSSENKRQLANYNFDFRSWPVDFHWEEPSSRKESRGGPSRRGVALLRPEPLHRGTADTLLNRVKKLPCQITSYLVAHTLGRRMLYPGSVYLLQKALMPVLLQGQARLVEECNGRRAKLLACDGNEIDTMFVDRRGTAEPQGQKLVICCEGNAGFYEVGCVSTPLEAGYSVLGWNHPGFAGSTGVPFPQNEANAMDVVVQFAIHRLGFQPQDIIIYAWSIGGFTATWAAMSYPDVSAMILDASFDDLVPLALKVMPDSWRGLVTRTVRQHLNLNNAEQLCRYQGPVLLIRRTKDEIITTTVPEDIMSNRGNDLLLKLLQHRYPRVMAEEGLRVVRQWLEASSQLEEASIYSRWEVEEDWCLSVLRSYQAEHGPDFPWSVGEDMSADGRRQLALFLARKHLHNFEATHCTPLPAQNFQMPWHL
Protein: Glutamate racemase (EC 5.1.1.3) (Q6GHT5)
Organism: Staphylococcus aureus (strain MRSA252)
Function: Provides the (R)-glutamate required for cell wall biosynthesis.
Interaction partners:
Sequence:
MNKPIGVIDSGVGGLTVAKEIMRQLPNETIYYLGDIGRCPYGPRPGEQVKQYTVEIARKLMEFDIKMLVIACNTATAVALEYLQKTLSIPVIGVIEPGARTAIMTTRNQNVLVLGTEGTIKSEAYRTHIKRINPHVEVHGVACPGFVPLVEQMRYSDPTITSIVIHQTLKRWRNSESDTVILGCTHYPLLYKPIYDYFGGKKTVISSGLETAREVSALLTFSNEHASYTEHPDHRFFATGDTTHITNIIKEWLNLSVNVERISVND
Protein: Glutathione peroxidase (Q869A5)
Organism: Trypanosoma brucei
Interaction partners:
Sequence:
MLRSSRKKMSAASSIFDFEVLDADHKPYNLVQHKGSPLLIYNVASKCGYTKGGYETATALYNKYKSQGFTVLAFPCNQFGGQEPGTEEEIKEFVCTKFKAEFPIMAKINVNGENAHPLYEYMKKTKPGILATKAIKWNFTSFLIDRDGVPVERFSPGASVKDIEEKLIPLLGSARL
Protein: Protein phosphatase CheZ (EC 3.1.3.-) (Chemotaxis protein CheZ) (Q51434)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Plays an important role in bacterial chemotaxis signal transduction pathway by accelerating the dephosphorylation of phosphorylated CheY (CheY-P).
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Chemotaxis protein CheY
- Chemotaxis protein CheA
- Flagellar motor switch protein FliM
- Chemotaxis protein CheA
- RNA polymerase sigma factor FliA
- Chemotaxis protein CheA
- Protein-glutamate methylesterase/protein-glutamine glutaminase 1
- Chemotaxis protein methyltransferase 1
- Probable chemotaxis protein
- Chemotaxis protein MotB
Sequence:
MQLIQELSQARDRGLYQEVGKLTRELHNAIVDFQIDPHSPHAQEMSQIADATDRLSYVVEMTEKAANRTMDLVEQSAPLVNQLGDDSRELHQEWQRFMRREIDADGFRELAKRIEQFLVRSGENAGQLSSQLNDILLAQDYQDLTGQVIKRVTKLVTEVESNLVKLVWMAGQVDRYAGIEHDHVSMRHQAALERSAKGEGPQVAAEKREDVVSGQDDVDDLLSSLGF
Protein: ADP-glucose phosphorylase (EC 2.7.7.-) (ADP-glucose:phosphate adenylyltransferase) (Q9FK51)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the conversion of ADP-glucose and inorganic phosphate (Pi) into glucose-1-phosphate and ADP. Does not possess galactose-1-phosphate uridylyltransferase activity.
Interaction partners:
- UTP--glucose-1-phosphate uridylyltransferase 2
- UTP--glucose-1-phosphate uridylyltransferase 1
- UDP-glucose 4-epimerase 2
- Bifunctional UDP-glucose 4-epimerase and UDP-xylose 4-epimerase 3
- UDP-glucose 4-epimerase 4
- Bifunctional UDP-glucose 4-epimerase and UDP-xylose 4-epimerase 1
- UDP-glucose 4-epimerase 5
- UDP-sugar pyrophosphorylase
- Phosphoacetylglucosamine mutase
- Galactokinase
Sequence:
MTSPSHASDRGGGDGDSVENQSPELRKDPVTNRWVIFSPARAKRPTDFKSKSPQNPNPKPSSCPFCIGREQECAPELFRVPDHDPNWKLRVIENLYPALSRNLETQSTQPETGTSRTIVGFGFHDVVIESPVHSIQLSDIDPVGIGDILIAYKKRINQIAQHDSINYIQVFKNQGASAGASMSHSHSQMMALPVVPPTVSSRLDGTKDYFEETGKCCLCEAKSKHFVIDESSHFVSVAPFAATYPFEIWIIPKDHSSHFHHLDDVKAVDLGGLLKLMLQKIAKQLNDPPYNYMIHTSPLKVTESQLPYTHWFLQIVPQLSGVGGFEIGTGCYINPVFPEDVAKVMREVSLT
Protein: MIF4G domain containing (J3KSB8)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MGEPSREEYKIQSFDAETQQLLKTALKDPGAVDLEKVANVIVDHSLQDCVFSKEAGRMCYAIIQVNNMPMMALVNPVYDCLFRLAQPDSLSKEEEVDCLVLQLHRVGEQLEKMNGQRMDELFVLIRDGFLLPTGLSSLAQLLLLEIIEFRAAGWKTTPAAHKYYYSEVSD
Protein: Probable leucine--tRNA ligase, mitochondrial (EC 6.1.1.4) (Leucyl-tRNA synthetase) (LeuRS) (Q8VDC0)
Organism: Mus musculus (Mouse)
Subcellular location: Mitochondrion matrix {ECO:0000250}.
Interaction partners:
- Bifunctional glutamate/proline--tRNA ligase
- Methionine--tRNA ligase, cytoplasmic
- Tyrosine--tRNA ligase, cytoplasmic
- Isoleucine--tRNA ligase, cytoplasmic
- Probable arginine--tRNA ligase, mitochondrial
- Isoleucine--tRNA ligase, mitochondrial
- Methionine--tRNA ligase, mitochondrial
- Lysine--tRNA ligase
- Arginine--tRNA ligase, cytoplasmic
- Probable proline--tRNA ligase, mitochondrial
Sequence:
MASTCQRLSFYVSPLKRQLVSRPPVILWERLIPGCSRSIYSATGKWTKEYTLQTRKDVEKWWHQQIKEQASRVSEEDKLKPKFYLLSMFPYPSGKLHMGHVRVYTLSDTIARFQKMRGMQVINPMGWDAFGLPAENAAIERNLHPESWTQSNIKHMRKQLDRLGLCFSWDREITTCLPDYYKWTQYLFIKLYEAGLAYQKEALVNWDPVDQTVLANEQVNEYGCSWRSGAKVEKKYLRQWFIKTTAYAKAMQDALADLPEWYGIKGMQAHWIGDCVGCHLDFTLKVDGEDTGEKLTAYTATPEAIYGISHVAISPSHGLLHGCSSVKKALQKALVPGRDCLTPVMAVSMLTLQEVPIVIMANPDLEGSLDSKIGIPSTSSEDTRLAQALGLPYSEVIEASPDGTERLSGSAEFTGMTRQDAFVALTRKARGMRVGGHVTSNKLKDWLISRQRYWGTPIPIVHCPACGPVPVPLQDLPVILPSIASLTGRGGSPLATALEWVNCSCPRCKGSAKRETDTMDTFVDSAWYYFRYTDPHNTQSPFGSALADFWMPVDLYIGGKEHAVMHLFYARFLSHFCHDQKMVKHREPFHKLLAQGLIKGQTFRLPSGQCLKKEDIDFTGPAPVCAKTKEKLEVTWEKMSKSKHNGVDPEEIVAQYGIDTIRLYILFAAPPEKDILWDVKTDALPGVLRWQQRLWSLTTRFIEARTSGTVPQPQLLNSKEKTKAQNLWEYKNAVIAQVTTHFTEDFALNSVVSQLMGLSSALSQASQRVVLHSPEFEDALCALLVMAAPLAPHVTSELWAGLTLVPSKLCDHYAWDSGVMLQAWPTVDSQFLQKPDMVQMAVLINNKACGKIPVPQHVAQDQDKVHELVLQSELGMKLLQGRSIKKAFLSPRTALINFLVQE
Protein: F-box only protein 6 (Q9FZK1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Putative defensin-like protein 145
- Defensin-like protein 147
Sequence:
MEEELAMLRQLIGQLQELLHNGSPPPPSSSSSLSSSSPSFLVLHHPQYQNGWCLPCIEDTSADDCCDIVMAGGKRPGIFKMLETVKPPVKRTRKERTQGKSCTEVDEISGNMDQEIWQEFPQDLFEDVVSRLPMATFFQFRAVCRKWNALIDSDSFSRCFTELPQTIPWFYTITHENVNSGQVYDPSLKKWHHPIIPALPKKSIVLPMASAGGLVCFLDIGHRNFYVSNPLTKSFRELPARSFKVWSRVAVGMTLNGNSTSHGYKVLWVGCEGEYEVYDSLSNVWTKRGTIPSNIKLPVLLNFKSQPVAIHSTLYFMLTDPEGILSYDMVSGKWKQFIIPGPPDLSDHTLAACGERLMLVGLLTKNAATCVCIWELQKMTLLWKEVDRMPNIWCLEFYGKHIRMNCLGNKGCLILLSLRSRQMNRLITYNAVTREWTKVPGCTVPRGRKRLWIACGTAFHPSPTARA
Protein: Splicing factor 45 (RNA-binding motif protein 17) (Q7PL83)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|PIRNR:PIRNR031066}.
Interaction partners:
- LD21442p
- ATP-dependent RNA helicase DHX15 homolog
- U2 snRNP-associated SURP motif-containing protein
- Splicing factor 3B subunit 1
- Uncharacterized protein, isoform D
- U1 small nuclear ribonucleoprotein A
- Probable U2 small nuclear ribonucleoprotein A'
- Splicing factor 3A subunit 2
- Splicing factor 3A subunit 1
- Splicing factor 3A subunit 3
Sequence:
MDLYDGIDTRARSSQIDGWSSGIKMLQTQLAVKMAVKKPLMTPVVNLRSKRLADPEVTCFAPITTVVSKPLISGKALPSILERINRGDWDVADEYDPQRPNEYEKLKEKSNGSDKNRAGVSDREDRDDKEKDRKRGRVGRREFYRDEVSAPNLKLSGFGHRQNDDDMYLPSPGLVAKQGGATIAPPPSLQEMSIDSGCEATNTMPYSASSVAAKIMAKYGFKDGQGLGKSEQGMAIALQVEKTSKRGGRIIHEKDVFLPPLALSPPSIGSQIGTSPSHKAMPPPQMVDTAAESGDIGYSITEIMKSPSKVVLLRNMVGPGDVDEELEPEVKDECNTKYGEVNSVIIHESFGTVPEDAVKIFVEFRRIESAIKAVVDLNGRFFGGRQVRAGFYNYDKFKCFQLH
Protein: Adenomatous polyposis coli protein 2 (A0A0C4DGQ0)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MASSVAPYEQLVRQVEALKAENSHLRQELRDNSSHLSKLETETSGMKEVLKHLQGKLEQEARVLVSSGQTEVLEQLKALQMDITSLYNLKFQPPTLGPEPAARTPEGSPVHGSGPSKDSFGELSRATIRLLEELDRERCFLLNEIEKEEKEKLWYYSQLQGLSKRLDELPHVETQFSMQMDLIRQQLEFEAQHIRSLMEERFGTSDEMVQRAQIRASRLEQIDKELLEAQDRVQQTEPQALLAVKSVPVDEDPETEVPTHPEDGTPQPGNSKVEVVFWLLSMLATRDQEDTARTLLAMSSSPESCVAMRRSGCLPLLLQILHGTEAAAGGRAGAPGAPGAKDARMRANAALHNIVFSQPDQGLARKEMRVLHVLEQIRAYCETCWDWLQARDGGPEGGGAGSAPIPIEPQICQATCAVMKLSFDEEYRRAMNELGGLQAVAELLQVDYEMHKMTRDPLNLALRRYAGMTLTNLTFGDVANKATLCARRGCMEAIVAQLASDSEELHQVVSSILRNLSWRADINSKKVLREAGSVTALVQCVLRATKESTLKSVLSALWNLSAHSTENKAAICQVDGALGFLVSTLTYKCQSNSLAIIESGGGILRNVSSLVATREDYRQVLRDHNCLQTLLQHLTSHSLTIVSNACGTLWNLSARSARDQELLWDLGAVGMLRNLVHSKHKMIAMGSAAALRNLLAHRPAKH
Protein: Intraflagellar transport protein 57 homolog (Dermal papilla-derived protein 8) (Estrogen-related receptor beta-like protein 1) (HIP1-interacting protein) (MHS4R2) (Q9NWB7)
Organism: Homo sapiens (Human)
Function: Required for the formation of cilia. Plays an indirect role in sonic hedgehog signaling, cilia being required for all activity of the hedgehog pathway (By similarity). Has pro-apoptotic function via its interaction with HIP1, leading to recruit caspase-8 (CASP8) and trigger apoptosis. Has the ability to bind DNA sequence motif 5'-AAAGACATG-3' present in the promoter of caspase genes such as CASP1, CASP8 and CASP10, suggesting that it may act as a transcription regulator; however the relevance of such function remains unclear.
Subcellular location: Cell projection, cilium {ECO:0000250|UniProtKB:Q8BXG3}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q5EA95}. Note=Concentrates within the inner segment of cilia. {ECO:0000250}.
Interaction partners:
- Intraflagellar transport protein 52 homolog
- Clusterin-associated protein 1
- Intraflagellar transport protein 46 homolog
- TRAF3-interacting protein 1
- Intraflagellar transport protein 172 homolog
- Intraflagellar transport protein 81 homolog
- Intraflagellar transport protein 20 homolog
- Intraflagellar transport protein 88 homolog
- Intraflagellar transport protein 80 homolog
- Intraflagellar transport protein 22 homolog
Sequence:
MTAALAVVTTSGLEDGVPRSRGEGTGEVVLERGPGAAYHMFVVMEDLVEKLKLLRYEEEFLRKSNLKAPSRHYFALPTNPGEQFYMFCTLAAWLINKAGRPFEQPQEYDDPNATISNILSELRSFGRTADFPPSKLKSGYGEHVCYVLDCFAEEALKYIGFTWKRPIYPVEELEEESVAEDDAELTLNKVDEEFVEEETDNEENFIDLNVLKAQTYHLDMNETAKQEDILESTTDAAEWSLEVERVLPQLKVTIRTDNKDWRIHVDQMHQHRSGIESALKETKGFLDKLHNEITRTLEKISSREKYINNQLENLVQEYRAAQAQLSEAKERYQQGNGGVTERTRLLSEVMEELEKVKQEMEEKGSSMTDGAPLVKIKQSLTKLKQETVEMDIRIGIVEHTLLQSKLKEKSNMTRNMHATVIPEPATGFY
Protein: Sensor kinase CckA [Includes: Protein histidine kinase (EC 2.7.13.3); Response regulator] (P0DOA0)
Organism: Brucella abortus (strain 2308)
Function: Component of a regulatory phosphorelay system that controls B.abortus cell growth, division, and intracellular survival inside mammalian host cells. This signaling pathway is composed of CckA, ChpT, CtrA and CpdR. CckA autophosphorylates in the presence of ATP on a conserved His residue and transfers a phosphoryl group to a conserved Asp residue on its C-terminal receiver domain. CckA-P transfers phosphoryl groups to the ChpT phosphotransferase.
Subcellular location: Cell inner membrane {ECO:0000305|PubMed:26124143}; Multi-pass membrane protein {ECO:0000305|PubMed:26124143}; Cytoplasmic side {ECO:0000305|PubMed:26124143}.
Interaction partners:
Sequence:
MRPKWCKTTVLASFPRGSACTARQLKHSANRIYLDARASVPARRAGILNEDRIELPDDAIGASAERRSTRDLRKPSRAGIQHERAVGLMSRQTDNTYPKPLVMPKRGPSAALRLLIVGILLMGAAFIYFLFRDQLGDGFALVLMGVLSMVGVFYLFGAATGLIQFSQRSDHQDLAHSFMDTQPEGTVISDPRGQIVYANQAYARMTGATDADGIRPLDQVLASEPAASDAIYRLTNAVRDGLSAQEEVRISGGLSRGANGSLAPVWYRIKARALEGGAEFKGPLVAWQVADISEERAEQERFFQELQEAINHLDHAPAGFFSANPAGRIIYLNATLAEWLGVDLTQFTPGSLTLNDIVAGSGMALIKAVKAEPGTSRNTVIDLDLIKRNGQSLAVRFYHRVQTARDGMPGTTRTIVLDRAEGDDSSVAQRSAEVRFTRFFNSAPMAIAAVDAEGHTLRTNARFLDIFSGVVDRDAIDRRVKLENVVHERDRETFNKALAAAFAGQASISPVDTVLPGNEERHIRFYMSPVTDLGGEAAEEAAVISAVETTEQKALENQMAQSQKMQAVGQLAGGIAHDFNNVLTAIIMSSDLLLTNHRASDPSFPDIMNIKQNANRAASLVRQLLAFSRRQTLRPEVLDLTDVLADLRMLLARLVGKDIELKIDHGRDLWPVKADLGQFEQVAVNLAVNARDAMPEGGQITLRTRNIPAADAAKLHYRDLPEADYVVFEVEDTGTGIPADVLEKIFEPFFTTKEVGKGTGLGLSMVYGIIKQTGGFIYCDSEVGKGTTFKIFLPRLIEEKRADDAPVAAKEKKVEKATDLSGSATVLLVEDEDAVRMGGVRALQSRGYTVHEAASGVEALEIMEELGGEVDIVVSDVVMPEMDGPTLLRELRKTHPDIKFIFVSGYAEDAFARNLPADAKFGFLPKPFSLKQLATTVKEMLEKQD
Protein: Peroxidase 12 (Atperox P12) (EC 1.11.1.7) (ATP4a) (PRXR6) (Q96520)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/isoform in each plant tissue.
Subcellular location: Secreted {ECO:0000305}. Vacuole {ECO:0000305}. Note=Carboxy-terminal extension appears to target the protein to vacuoles.
Interaction partners:
Sequence:
MTKAYSTRVLTFLILISLMAVTLNLFPTVEAKKRSRDAPIVKGLSWNFYQKACPKVENIIRKELKKVFKRDIGLAAAILRIHFHDCFVQGCEASVLLAGSASGPGEQSSIPNLTLRQQAFVVINNLRALVQKKCGQVVSCSDILALAARDSVVLSGGPDYAVPLGRRDSLAFASQETTLNNLPPPFFNASQLIADFANRNLNITDLVALSGGHTIGIAHCPSFTDRLYPNQDPTMNQFFANSLKRTCPTANSSNTQVNDIRSPDVFDNKYYVDLMNRQGLFTSDQDLFVDKRTRGIVESFAIDQQLFFDYFTVAMIKMGQMSVLTGTQGEIRSNCSARNTQSFMSVLEEGIEEAISMI
Protein: Amine sulfotransferase (EC 2.8.2.3) (SULT-X2) (Sulfotransferase 3A1) (ST3A1) (O35403)
Organism: Mus musculus (Mouse)
Function: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the N-sulfonation of amines.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Solute carrier family 22
- Sulfotransferase
- Sulfotransferase
- Flavin-containing monooxygenase 3
- Cytochrome P450
Sequence:
MDNKDEYLLNFKGYNFQKTLVKMEVVENIENYEIRDDDIFIVTYPKSGTIWTQQILSLIYFEGHRNRTENIETIDRAPFFEYNIHKLDYAKMPSPRIFSSHIPYYLVPKGLKDKKAKILYMYRNPKDVLISYFHFSNLMLIFQNPDTVESFMQTFLDGDVVGSLWFDHIRGWYEHRHDFNIMFMSFEDMKKDFRSSVLKICSFLEKELSEEDVDAVVRQATFQKMKADPRANYEHIIKDELGTRNEMGSFLRKGVVGAWKHYLTVDQSERFDKIFHRNMKNIPLKFIWDINEE
Protein: Gliomedin [Cleaved into: Gliomedin shedded ectodomain] (Q6ZMI3)
Organism: Homo sapiens (Human)
Function: Ligand for NRCAM and NFASC/neurofascin that plays a role in the formation and maintenance of the nodes of Ranvier on myelinated axons. Mediates interaction between Schwann cell microvilli and axons via its interactions with NRCAM and NFASC. Nodes of Ranvier contain clustered sodium channels that are crucial for the saltatory propagation of action potentials along myelinated axons. During development, nodes of Ranvier are formed by the fusion of two heminodes. Required for normal clustering of sodium channels at heminodes; not required for the formation of mature nodes with normal sodium channel clusters. Required, together with NRCAM, for maintaining NFASC and sodium channel clusters at mature nodes of Ranvier.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q80WL1, ECO:0000269|PubMed:27616481}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q80WL1}. Cell projection, axon {ECO:0000250|UniProtKB:Q80WL1}. Note=Detected at the nodes of Ranvier. Detected at immature heminodes. {ECO:0000250|UniProtKB:Q80WL1}.; SUBCELLULAR LOCATION: [Gliomedin shedded ectodomain]: Secreted {ECO:0000250|UniProtKB:Q80WL1}. Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:Q80WL1}. Note=Proteolytic processing gives rise to a soluble extracellular domain that is secreted. The gliomedin shedded ectodomain localizes to the nodes of Ranvier. {ECO:0000250|UniProtKB:Q80WL1}.
Interaction partners:
- Neurofascin
- Neuronal cell adhesion molecule
- Spectrin beta chain, non-erythrocytic 4
- Contactin-associated protein 1
Sequence:
MARGAEGGRGDAGWGLRGALAAVALLSALNAAGTVFALCQWRGLSSALRALEAQRGREQREDSALRSFLAELSRAPRGASAPPQDPASSARNKRSHSGEPAPHIRAESHDMLMMMTYSMVPIRVMVDLCNSTKGICLTGPSGPPGPPGAGGLPGHNGLDGQPGPQGPKGEKGANGKRGKMGIPGAAGNPGERGEKGDHGELGLQGNEGPPGQKGEKGDKGDVSNDVLLAGAKGDQGPPGPPGPPGPPGPPGPPGSRRAKGPRQPSMFNGQCPGETCAIPNDDTLVGKADEKASEHHSPQAESMITSIGNPVQVLKVTETFGTWIRESANKSDDRIWVTEHFSGIMVKEFKDQPSLLNGSYTFIHLPYYFHGCGHVVYNNSLYYHKGGSNTLVRFEFGQETSQTLKLENALYFDRKYLFANSKTYFNLAVDEKGLWIIYASSVDGSSILVAQLDERTFSVVQHVNTTYPKSKAGNAFIARGILYVTDTKDMRVTFAFDLLGGKQINANFDLRTSQSVLAMLAYNMRDQHLYSWEDGHLMLYPVQFLSTTLNQ
Protein: Serine protease FAM111B (EC 3.4.21.-) (Cancer-associated nucleoprotein) (Q6SJ93)
Organism: Homo sapiens (Human)
Function: Serine protease.
Interaction partners:
Sequence:
MNSMKTEENKSFSAMEDDQRTRPEVSKDTVMKQTHADTPVDHCLSGIRKCSSTFKLKSEVNKHETALEMQNPNLNNKECCFTFTLNGNSRKLDRSVFTAYGKPSESIYSALSANDYFSERIKNQFNKNIIVYEEKTIDGHINLGMPLKCLPSDSHFKITFGQRKSSKEDGHILRQCENPNMECILFHVVAIGRTRKKIVKINELHEKGSKLCIYALKGETIEGALCKDGRFRSDIGEFEWKLKEGHKKIYGKQSMVDEVSGKVLEMDISKKKALQQKDIHKKIKQNESATDEINHQSLIQSKKKVHKPKKDGETKDVEHSREQILPPQDLSHYIKDKTRQTIPRIRNYYFCSLPRKYRQINSQVRRRPHLGRRYAINLDVQKEAINLLKNYQTLNEAIMHQYPNFKEEAQWVRKYFREEQKRMNLSPAKQFNIYKKDFGKMTANSVSVATCEQLTYYSKSVGFMQWDNNGNTGNATCFVFNGGYIFTCRHVVHLMVGKNTHPSLWPDIISKCAKVTFTYTEFCPTPDNWFSIEPWLKVSNENLDYAILKLKENGNAFPPGLWRQISPQPSTGLIYLIGHPEGQIKKIDGCTVIPLNERLKKYPNDCQDGLVDLYDTTSNVYCMFTQRSFLSEVWNTHTLSYDTCFSDGSSGSPVFNASGKLVALHTFGLFYQRGFNVHALIEFGYSMDSILCDIKKTNESLYKSLNDEKLETYDEEKGKQESSLQDHQIEPMEC
Protein: Phosphomannomutase/phosphoglucomutase (PMM / PGM) (EC 5.4.2.2) (EC 5.4.2.8) (P26276)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Highly reversible phosphoryltransferase. The phosphomannomutase activity produces a precursor for alginate polymerization, the alginate layer causes a mucoid phenotype and provides a protective barrier against host immune defenses and antibiotics. Also involved in core lipopolysaccaride (LPS) biosynthesis due to its phosphoglucomutase activity. Essential for rhamnolipid production, an exoproduct correlated with pathogenicity. Required for biofilm production. The reaction proceeds via 2 processive phosphoryl transferase reactions; first from enzyme-phospho-Ser-108 to the substrate (generating a bisphosphorylated substrate intermediate and a dephosphorylated enzyme), a 180 degree rotation of the intermediate (probably aided by movement of domain 4), and subsequent transfer of phosphate back to the enzyme.
Interaction partners:
- Alginate biosynthesis protein AlgA
- Alginate biosynthesis protein AlgA
- UTP--glucose-1-phosphate uridylyltransferase
- Alginate biosynthesis protein AlgA
- Glucose-1-phosphate thymidylyltransferase
- Glucose-6-phosphate isomerase
- Ribose-phosphate pyrophosphokinase
- Glucokinase
- Alpha-1,4 glucan phosphorylase
- Transketolase
Sequence:
MSTAKAPTLPASIFRAYDIRGVVGDTLTAETAYWIGRAIGSESLARGEPCVAVGRDGRLSGPELVKQLIQGLVDCGCQVSDVGMVPTPVLYYAANVLEGKSGVMLTGSHNPPDYNGFKIVVAGETLANEQIQALRERIEKNDLASGVGSVEQVDILPRYFKQIRDDIAMAKPMKVVVDCGNGVAGVIAPQLIEALGCSVIPLYCEVDGNFPNHHPDPGKPENLKDLIAKVKAENADLGLAFDGDGDRVGVVTNTGTIIYPDRLLMLFAKDVVSRNPGADIIFDVKCTRRLIALISGYGGRPVMWKTGHSLIKKKMKETGALLAGEMSGHVFFKERWFGFDDGIYSAARLLEILSQDQRDSEHVFSAFPSDISTPEINITVTEDSKFAIIEALQRDAQWGEGNITTLDGVRVDYPKGWGLVRASNTTPVLVLRFEADTEEELERIKTVFRNQLKAVDSSLPVPF
Protein: Luc7-like protein (J3KPP4)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus speckle {ECO:0000256|RuleBase:RU369106}.
Interaction partners:
Sequence:
MISAAQLLDELMGRDRNLAPDEKRSNVRWDHESVCKYYLCGFCPAELFTNTRSDLGPCEKIHDENLRKQYEKSSRFMKVGYERDFLRYLQSLLAEVERRIRRGHARLALSQNQQSSGAAGPTGKNEEKIQVLTDKIDVLLQQIEELGSEGKVEEAQGMMKLVEQLKEERELLRSTTSTIESFAAQEKQMEVCEVCGAFLIVGDAQSRVDDHLMGKQHMGYAKIKATVEELKEKLRKRTEEPDRDERLKKEKQEREEREKEREREREERERKRRREEEEREKERARDRERRKRSRSRSRHSSRTSDRRCSRSRDHKRSRSRERRRSRSRDRRRSRSHDRSERKHRSRSRDRRRSKSRDRKSYKHRSKSRDREQDRKSKEKEKRGSDDKKSSVKSGSREKQSEDTNTESKESDTKNEVNGTSEDIKSEVQRKYAQMKMELSRVRRHTKASSEGKDSVVLQNILRYIVLSQLFCSRLVPPLVCLFGNYRPHL