ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q46108 | MEVKAKQLDSVNATASVKIPSGMIKSEVENLAKKASKSVKMDGFRPGKVPVSAVLKRYERELTQDAEQNLFKSAVNSALQELKKENKELVGEPYFEKFDRKDGEIIAELILSFKPEIKLEGYEKLIPEYQTPKVSKKEIDEKKDELLKRFATPEAIKTKRALKEGDFAKFDFEGFVDDKAFEGGKAENYVLEIGSKQFIPGFEDGMVGMKIGEEKDIKVTFPKEYGAAHLAGKDAVFKVKLHEIQELKIPELDDEMLKKLLPGEEKASVEVLDEKLKEQIKNEKLFKLVNDELKGKFADALIEKYNFDLPKGIVEQETDM... | Function: Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase (By similarity).
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 50968
Se... |
Q3AF97 | MKVTKETLEKSRVELTIEVEAEEVSKAYEKAYKKIAQKVVIPGFRKGKAPRVLVERHVGKEYILEEALDELLPESYVKAVNEAGIEPVDKPEVSLVSYGVNEPLVYKAVVDVKPEVELGQYTGLEVTKMPVEVTDEEVEKELEYLQNRYAKLITVEDGEAKFGDIVVIDFAGKMNGEPLEGGSADNYRLELGSKVFIPGFEEQIVGMKPGETKEINVTFPEDYQKEDLAGKPAVFTVTLKEIKRKELAPLDDEFAKDVSEFSTLAELKEDLKKKIAQTKENISREKMEAEVVEKAVDNANVEIPASMVNHEVEHILHHFE... | Function: Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 48608
Sequence Length: 4... |
P0CAX0 | MQIVEKSGEGLSRVFGVTVPASELATRLEARIAEVAPQMNVKGFRPGKVPTAHVRRLYGKALMGEVIEQALNETTTKVLEDNKLRPAGQPELNPSSDMDKVIAGGEDLSFDLAVEVMPEFEPIDPTSIELVKPVYKVSDEEVQEALDELAKQARTYEPRTGKSLKAKDGDQLLIDFVGTIDGVEFAGGKAEGAELVLGSGQFIPGFEDQLVGAKPGDDVVVKVKFPEEYQAKDLAGKDAEFATKVQEVRAPVDGKADDELAKRLGLSDLAALTELLKSNLAGRYDNSSRFKLKRALLDVLDTKHDFPLPPRMVDAEFAGI... | Function: Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase (By similarity).
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 49767
Se... |
P56420 | MNLEVKKIDTANARLSAKLSIENLEKRYDKIAQKIAQKVKIDGFRRGKVPLSLVKTRYQAQIEQDAQEEMIQEVLKNAFKELGIENKDLIGSPNLTKFEKKDTHFEIEADIGLKPTIVLDKIKECVPSVGVEVPNEEKIDERLKQLAKDYAKFVDTNTQRKAQNDDKLTIDFEGFIDNAPFEGGKAENFNLILGSKQMLEDFEKALLGMQAGEEKEFPLTFPSKYHAEHLAGKEAFFKVKLHQIQAREMLEINDELAKIVLANEENATLKLLKERVEGQLFLENKARLYNEELKEKLIENLDEKIVFDLPKTIIEQEMDL... | Function: Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase (By similarity).
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 51989
Se... |
A9AUT1 | MKVTTEQLPKRIVALEIEPDAATIEKELNKAAQRIASKVAIPGFRKGKAPRFIVENYYGKAAILEEATDEIINVAFRAALEQENIKPVAQASLEKLEPEPFRFRILVPVEPEVILPDYKAITVDLTEEPVTDATLEVALDQAREKHVVLSAPEGEPEAAEGDQLTATVQTLVDGVPLHKLDEEDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDEGEPTTLIMEERRIVPELYAGLKGIKAGETREISAHLPADHPDARVADKDVVFKVTVSEIQNRQLPAWEELPGLEEFEGDLDAYKADL... | Function: Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 53732
Sequence Length: 4... |
Q31GF2 | MQVTVEKPETGLEHKINVTLPAGDLDSKVEQRLAQMRRTVKMDGFRPGKVPMSVVKKRYGGQVRQEMMGETVQQSFYDAVAKESLNIAGYPQFQELDEKDGHIVYSATFEVFPEVELPKFSSLKVETVTSEVTDKDVEKMVTRLREQKMAWKPANGNKKAKEGDQVIIDFVGKKDGEEFEGGKAEEVPLELGSGRMIPGFEDGIIGMKKNEEKTIEVTFPEDYQSDELKGQTVTFDITVHSVQTKVLPEIDEEFVKSFGIEEGTEEALVNEIRSNMEKELKRSVENKNRTAVLDALAEKVEVELPQAMVDQEASALMERQ... | Function: Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 49093
Sequence Length: 4... |
B2GGB4 | MKSAVEKLNPTEAKITIDIAYTDLKPFVQETYKELANQIQIPGFRKGKVPSKLIDQRVGFDFVVENALNEGLNAFYQQALTENELTPLSQPQVEVLSKPEENDREADTKVEISVAIRPEIELPDYKGLEIQVEAREATAEDEQKALDELRARFGTLKTVDRPAAEGDHVTLDLQALVDGEEVDAANDLSYEVGSGTMLEGIDEAVTGLSAGEDATFETTLAGGEHSGAEATVKVKVTAVKERELPEADDEFAQLASEFDTIAELKEDLKKQAAESAVVEQGIEARDKVLDKLVELIEVPVPEKVIEDQLAQHFDSEQAQA... | Function: Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 48943
Sequence Length: 4... |
Q1IRD7 | MTTEASNPEVNATAEVAVPVNPLLRSVTVEIPSDVVDAERNKHVQQYAKLARVPGFRKGKVPPSVIRTRFAQDINEEIVRTLIPHYFREETGKQNLQPVSQPQVTDLHLHDGEPLKFTAEFEILPEIPTTGYENIKVEHPPVEVTDAEIEDTIKSLQEQRATYDPIEDRAAEDGDFVQISFEGRDKSDPEAKPVEVPSIMVELGGSNTVQEFTENLRGTKAGDEKTFDVVYPADYGDQRLAGKSVEYHVSVKSLKKKIFPELDEAFISELGADVKTPDELRAKIREGAEHEKKHHAEHEGKDKLVDALVKLNDFPVPESM... | Function: Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 49200
Sequence Length: 4... |
C5CGV0 | MEKNVVKAEKNVEIVEFTFGPDEIAEAENEIVRYVNKNYTIPGFRKGKAPKRIIETFFGENFRDMVLEELSRKIEDTLKDEELFIPAVIADRKIEGDVAVFVVELHREPKVELKDYTGLELSVPKQEEVLANYVDNKLEELRNEAAIVEPKDGPAEIGDVINIEYTIEKDGKIIADHKTQEILIVEDDDRPIVTNVIGKKKGDIVEFDRTFENSNNKYHYKIEIKEVLKRTLMELNDEFAKSVASEVNTLEELKKKLEEEGLEAFESWKKDFLRQQVQDKLAELVELEISEKTLDYFVNRAIENAKKENTYDSYLKQAGS... | Function: Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 50877
Sequence Length: 4... |
Q88KJ1 | MQVSVENTSALERRMTIAVPAERVENEVNKRLQQTAKRAKIAGFRPGKVPMTVIRQRFEADARQEAFGDLVQASFYEAIVEQKLNPAGAPAVEPKSFEKGKDLEFVAIFEVFPEFTVAGLESIKVERLSAEVADSDLDNMLEVLRKQNTRFEAVERAAQNDDQVNIDFVGKVDGEAFAGGSAKGTLLVLGSGRMIPGFEEGLVGAKAGEERVVNVTFPEDYQNLDLAGKAAEFTITVNSVSAPVLPELNEEFFAQFGIKESTLEGFRAEVRKNMERELRQAIKTKVKNQVMDGLLAANPIEVPKALLENEVNRLRVQAVQ... | Function: Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 48517
Sequence Length: 4... |
A9WUW4 | MKSAVENLSPTRVKLDVEVPFEELQPSIAEAYKTIAEQVQIPGFRKGKFPNRLIDQRVGRGYVLETAINEGLNGWYQNAVAETGLRPLSRPEVEITEVPDPAATDGELKFKVEVDVRPEVELPDYAGITVEVAPAEQSDEDRQKALDDLRGRFGTLKPADRPAAKDDFITIDINAKIADEDVDSATGLSYQVGAGTMLEGLDEAVEGLSTDEEAIFDTKLVGGEHAGEAAQVTVKLTAVKVRELPEADDDFAQLASEFDTIAELREDLVKQVNQSKTVEQGVEARDKVMEKLVELIEVPIPESVIEEQLEQHFDPANAHG... | Function: Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 51532
Sequence Length: 4... |
Q6F880 | MRSALPTFDEIWQRKFRHRLLIQAQQFPADTVFLIGCSGGMDSMLLLHLMSELFPHKVRAIYIDHQLQSSSRAWGVFVQNFAQQSHIPFTIQPVIVDTGNLENQAREARYAAFESHLKSNEVLVLAHHQQDQTETVLLRLLSGSGVKGLGAMKEIEQKKNICCWRPMLSVSRQQIEHWVEHLKIPYIQDLTNFDTTYDRAWCRETVWPVLQKRFPKMQEAISRTSILMQDADEILHEVLQQDLNQCGDLNHLDLSRLQQLSLARQRQLLSFWMKGKAIYRPAFEMVERVQQEVICAKADAKAALHWNHHYYVRYQNILYR... | Function: Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine.
Catalytic Activity: ATP + cytidine(34)... |
Q8U9L7 | MPVDARTPNEKTVAPLAAASAFVESLRKPTHILVAISGGSDSTGLLLALQEAKAADDDGLRLSAVTVDHALRPESADEARKVAMLCAELGIPHTTRRWDGPKPASGLSEASRLARYRLIADVAREIGADLVVSGHTIGDQRETVAMRAARSGGSDNLGLSGMADAVLYDAHLWIMRPFLACERQVIRDYVSSRSRHWLDDPSNENIRYERVRVRQTLPHSPIALDDSTAVRRQMLSERTAVFLRERAQVFHAALARLADDDVNPDLPEFRHGLAALIAALGGRSYFPAASSMERVLRFLKTGETGRMTVGRVLLDRRRDG... | Function: Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine.
Catalytic Activity: ATP + cytidine(34)... |
Q5WAE0 | MEARVEQFIENNRLFGMETNVLVAVSGGPDSMALLAIMANLREKWKLNLFGVHVNHRLRGEESNKDAELVQSFSARLGVPCNVKDVDVAAFKAEHHVGTQQAARALRYQVFQGEMERVHATVLLTAHHGDDEVETAFMKLTRGTTPLTKLGIAATRPFANGVLARPLLEETKRSIVAYCHEKAIPYRIDQSNFSDAYTRNRFRMNMAPYLVEENPHIHKHIGRFDRWQEEDNHYLMEQAKAHLDQILTKKSEKSIELEIQALCLAPFPLQRRMIHLILNYLHLNVYGVNDMRVFPDAIEQIQAFLQTSAPSAQLDLPGRV... | Function: Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine.
Catalytic Activity: ATP + cytidine(34)... |
Q0A7K1 | MAPTPELSPETLARHLAVLGPASGYCVAYSGGLDSTVLLHLMAALSAARELPLRAVHIHHGLQPQADAWAEHCRQQAAALGVDCLVLPVEVRRDSGEGLEAAARQARYAALASHLQSGEALLTAHHADDQAETVLLHLLRGSGPRGLAGMRAQRPLGRGRLLRPLLPWPRERLRAYGDTHALCWVEDPSNAHVAHDRNWLRHTLWPVLTQRWPDASRRVGRAAGEQAEAEALLRELAGEDLARHPPGPGLAVSVLARLSPARARNLVRHWLLMSGLRPPPRARLEQGLADLIRAGRDRQPVLTWPEGELRRYRDRIHRLP... | Function: Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine.
Catalytic Activity: ATP + cytidine(34)... |
Q5P9R1 | MSGVRIPLFPRFIPHGTVKLESAALKKLNSLELSGGYAVAVSGGVDSITLLNLVAALHKTQATSRPVVLTGNHGFRAEADHETRFVQKRAVALGLDCEILRWNRHRTSSKSQETAREIRYSLLHQWCTEHSVKFLLTAHNKSDQAETVLMHLERGSGIDGLSGMHERSVFGDITIYRPLLGFTRQEILEYATQKQLSWVEDPSNQDPKYRRTFFRNLIAESKNPGVVVDRLCRTTSHMHRALACILHYVRSSLDYCLEFSPLGFITVKSQELRSVPEEIASRLLLLSLMAMGGKDHKPRYSAFWPILTKILQGQDFTPRT... | Function: Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine.
Catalytic Activity: ATP + cytidine(34)... |
O67728 | MNPESRVIRKVLALQNDEKIFSGERRVLIAFSGGVDSVVLTDVLLKLKNYFSLKEVALAHFNHMLRESAERDEEFCKEFAKERNMKIFVGKEDVRAFAKENRMSLEEAGRFLRYKFLKEILESEGFDCIATAHHLNDLLETSLLFFTRGTGLDGLIGFLPKEEVIRRPLYYVKRSEIEEYAKFKGLRWVEDETNYEVSIPRNRIRHRVIPELKRINENLEDTFLKMVKVLRAEREFLEEEAQKLYKEVKKGNCLDVKKLKEKPLALQRRVIRKFIGEKDYEKVELVRSLLEKGGEVNLGKGKVLKRKERWLCFSPEV | Function: Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine.
Catalytic Activity: ATP + cytidine(34)... |
Q5P2I9 | MLVAAAVAPRQRLCVAFSGGADSTTLLHLLARLRPRFGFDLCAAHVHHALSPNADAWLDFCARQCAALDVAFHPFREQVARDHPAGLEAAAREVRHAALSRVTCDWLVFGHHQDDQAETLLFRLLRGAGVRGAAAMAAIEPGFPGRLRPLLGVRRADIRAFAQAASLEWIEDESNADPRHARNFLRHHVFPLFGEAFPGAVPALARASGHFREADGLLGDLAALDYAACGGSPWLRDRLLMLSDERVRNLLRWRIRQMGCEAPARARLVEAVRQLRATHAPLYLPLGTAACCTYRDRLWLEPQRDGAPEQPLPWRQEPAL... | Function: Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine.
Catalytic Activity: ATP + cytidine(34)... |
Q2NIN4 | MENIKLACSLETNQTYIIAVSGGVDSMALLHYLVAQKIKLQVVHFNHLTNSNTWKNKELVKNYCLQNSLGFHYFELNCPQKNFQAQARLLRQQKLMQIAAKHRTPFILTAHHLDDLAETILQKISRSSTLLGYSGMQIQTSWTDFIFLKPFLYIPKAKIISYAAFYKIPFLEDYTNQKLTYQRNQIRHQVIPYLKTQTSFLQNIQKYQQTLLQAYNFIRKQTLLFLTKHTNHSCNQPNSIALAPFLNLDLVIQKDIILLLLEQKNITQSFIFIQNIIKGINNPYKPNLSWHLNSDWHLIKDYKHIKLMNPALPLPFALTK... | Function: Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine.
Catalytic Activity: ATP + cytidine(34)... |
Q81VX7 | MKDTFVEKVDDFVRQHDVLKERSTIVVGVSGGPDSLALLYYLLEKRAAKQFEIVVAHVDHMFRGDESHEDLQFVQDLCKGLGVICETIRINVSQYQKQYGMNAQVAARECRYAFLERIMKKYDARYVALGHHGDDQVETILMRLVRGSTPKGYAGIAVKRPFHNGYLIRPLLGVTKEEIVNYCNELKIIPRIDPSNKKEVYTRNRLRKYVLPHLKEENPQVHEKFQKFSMQMQEDEAYLQELAFEKMNKVITKKSDKQISLSIPTFESMSMPLQRRGIQLILNYLYEYKIPSSLSSIHIDKVIEFFKRTQPSGSLDFPGD... | Function: Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine.
Catalytic Activity: ATP + cytidine(34)... |
B3CUJ5 | MNIEVDFCHNMECFGAFEKNPKLAIAVSGGSDSLALMLLVKHWNEKVKGEITILTIDHHLRSESTSEADYVSSICQNIKLQHVTLHWIHKGITGNIQAQARKARYQLLTNYCQEHDILHLITGHHADDIVENFFIRLLRGAGLAGLSSHNLFFVNNVRIIRPLFNITKQDLKKYLEQQNIKWINDPSNSSNKYLRTQVRDLLKSMLISFQHNFTVELLKKRIMLSQMHLTQALESVNNEIIHYVVHVVKIYSAGFAVIDRKLFKKASPEARYAILSYLLMIVGANTKPPRFSSLQRISLHDIQEYNTYKTLHGCIVEYSI... | Function: Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine.
Catalytic Activity: ATP + cytidine(34)... |
Q7UA26 | MGEQRPLALAWSPWHDRLHRRLHQHPQLLPQRQPLLLAVSGGQDSMALLVLLQELQRLHHWPLNIWHGDHGWHSGSAVIAADLRSWCQQRDLPIQVDQAPQGSTASEASARHWRYSQLQQRAEELGADVVTGHTASDRAETLLLQLARGTDLAGLGALRPVRPLFNDSPDGAQLRRPLLGFSRADTAAVCRDLQVPIWHDPSNQSPAFARNRIRAEVLPVLEQLHPGCSQRMANLAERTSQLRDTQQELSQLALQPLRTSTGLDRRRLGALQPSTRRQLLVIWLAQQGVTALNAALLEQLTDRLALSAAGGSCDLPGGWR... | Function: Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine.
Catalytic Activity: ATP + cytidine(34)... |
Q6MDI6 | MSCICLKNEKLNVINQVKRFIKKYCKSTQPLLLALSGGADSLSLFYCLLACRLEGILSFHVAHVDHGWREESAKEATILKNLAEQHQVPYHQLKIDLSQLAGNLEDACRKQRQKFFKEICLQNNLQAVCLGHQENDQVETVLKRILEGSHWSHFDGLKERMWHDQVQFLRPLLGIQKDEILAFLKGNQLKAFEDGTNCDERFMRARMRRTIIPDLNRSFGKKIDNSLVYIASEMSELKNFFLGRVSPLLGQIVKGPFGVYLNLANHPSIDLVEIKYLLRLISEQELFFLSRQILQRASEAIEKLEPQLSFEMGTKKIVID... | Function: Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine.
Catalytic Activity: ATP + cytidine(34)... |
Q6D8C5 | MDRTEPDDELLQTIVTQTAGCGSILLAYSGGLDSSVLLHLLVTVRQRSGQTIRAAYIHHGLNPLADSWAEHCRQQCERWQVPFSSLAVTVEAQNGGIEAAARTARYQALQVHLKEGETLLTAQHLDDQSETFLLALKRGSGPAGLSAMAANSFLGHHRLVRPLLGFSRLQLEAYAQRHQLRWIEDDSNQDERFDRNFLRRQILPRLTQRWPHFPSAVARSAELCAEQEQLLDELLEESLRTLRQPDGALSIDGLVPLSPVRRFALLRRWLAQQGATMPARDQLQRLWDEVAASRRDAEPILQLNQMQIRRFRQHLYLLPL... | Function: Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine.
Catalytic Activity: ATP + cytidine(34)... |
C0QU23 | MVEKKFLEAVKKYSLISEGDRILVAFSGGIDSTVLTYLLIKFRDHLKISDIYLAHLNHSLRKESDEDQRFCEDFAKKYGLEIFTKKVDIKSLAEKEKKSIEQKAREERYSFFRKVMEERSINRLATGHHLSDLVETMIMWFIQGNRKGIKGFRPKERDIIRPLYLINKDQIENYAREKGIEYRIDITNFETDFLRNRIRHNIIPHIKGINPSLEGSLLTLSYFLSLDDQYLEEESEKISQKFLNGKIELEELLVYDKALVYRAIQNWIYRKTGVYPSYRQIMDIMEIIEKKEGTKSIRLSPEYNLIRRYSTLYIEKVKEK... | Function: Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine.
Catalytic Activity: ATP + cytidine(34)... |
A9BJK2 | MILQDFEKKIFKFIRDYKIFNKYDKILLGVSGGKDSMSLLHVMSKLSKTMGFEISVAHLNHCMREEADNDEAFVRQACWKLKIPFFSKKVDVFTYSKKNKVGVEVAGRKLRYEFFYETLRRLSYNKIATAHHMDDLFETMIYRILRGTGIYGLGGLIPIEEEITKPMLCVDLEEIKNYVTINNIEYVEDKYNYSLDYARNKIRYEITPLFKKINPRYKESFFRLAKIIWSYREEVKRKFEERSEISKDSLKLRLENDFFDGEIIRIAFLKFGKYPPNMEETEKIIKMRKGGVRKINGLSITKKSDSLLVKI | Function: Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine.
Catalytic Activity: ATP + cytidine(34)... |
Q7N8N0 | MANIDERLFVTLAKQLGEYKKILVGFSGGLDSSVLLHLLVNWRNQHNQKIQLRAIHIHHGLNLKADQWIEHCQLICDDWQVEFHSARVTIDARQKGIEAAARDARYQVFKSELQKDEVLVTAQHLDDQAETFLLALKRGSGPAGLASMPSIAVFADTLLLRPLLDYSRNELEKYASKHRLNWIEDDSNQDDRYDRNFLRLHIMPLLNQRWSHFPKAAARSASLCGEQEQLLDELLNESLKELITQDGALGIVSLAVCSEAKRNALLRRWFGYHGMKMPSREQLNRLWYEVALARTDAEPRLQFGKYDVRRYKQKLWLVPQ... | Function: Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine.
Catalytic Activity: ATP + cytidine(34)... |
A1VRB1 | MAAPVASLNPALAGIDSLFSAFPSSSSLPLGVAYSGGADSTALLLAAAERWPGQVQAFHIHHGLQAAADDFVRVCESVCAKAGLPLHIVQVDARHASGESPEDAARRARYAALATAATARGMQGVLLGQHADDQVETMLLALSRGAGLPGLSAMPASFGRGGMVFYRPLLHIPSAVLREWLVEQPIEFVDDPTNTDERYTRNRIRARLLPALAQAFPQFHATFARSARHAAQAQAVLVEVAAQDLAVVGNPPAIKALQALSPPRQANVLRHWLLLQYATPSAAQLEQLLHQVAACTTRGHRIHLKVASGHVTRLGGSLCY... | Function: Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine.
Catalytic Activity: ATP + cytidine(34)... |
B2RMB4 | MKISLTNRVRTTIRERKLFREGNRLVLVALSGGADSVALLCVLRELGYETVAAHCNFHLRGVESDEDAAFVEGLCRDLDVPLHRIDFDTVRYARERSISIEMAARELRYEWFGLLRKELAIEYVAVAHHADDNAETMVLNLCRGTGISGLCGMPYKRNDGIVRPLLDATRDEIEAYLLDQKITYRTDSSNEDTRFRRNLVRHRIMPLLKELNPSLQEALLRTRENLEGVAAFFSKATEDFHNTLRATASISIREVKETPAPFTLLYDLLHPYGFNRDQIREVVTSLDNPPGASFFSSSHRLLRERDRLTVLPLSPKMEVP... | Function: Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine.
Catalytic Activity: ATP + cytidine(34)... |
P51383 | MFLDSFLHKKFFSTIEKKSLLPSKSSLLVAFSGGQDSLTLVKLLYDLNPFYRWRITLIHFDHRWRWDSMLASKQVFSFARYYNFPLYYFECPDYLNTEEASRKWRYTTLIDLAVKNNFTKILLAHTATDSSETLLSNLFRGTSLDGLASIGWSCQLAQSVYIVRPLLNFYRFETSWFCRKYYLPIWVDRSNYDYIMFRNRLRQELVPYIKSYFQPNLEERCYSLSSLVKYDTDFLEQEALRIYFILIHQDLIAINHTALRLLHLSVQSRIFKIFFIANLNFNPNSRQIEDVIIFIKQNILSQINMNNYILVMDDIWFYVG... | Function: Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine.
Catalytic Activity: ATP + cytidine(34)... |
Q7V9L9 | MTNSTKVEKPWTKWHERLHKSLKSKSNLLPYGSSLLISVSGGQDSMALLKLILDLQRIYEWKVHVWHGDHGWHNQSRQIAEELEEWCKCQKLSFFCNRTNKQKVSTEEDARNWRYKSLIQQAKTLSKESPSLPCERVLTGHTANDRTETFIMNLARGAHLKGLSSLREDRTLETKIQLIRPILRFSRQETIQICDEMDLPIWIDPSNSNIAYSRNKIRAEIIPVLESLHPQSTIRISNLAERLTSLQKDQHQLAHLALGALLTSTGLSRSKMTKLSKTVRAIILAQWLEDNKAPLLSSKQLEELSQKIGKNKGPGNMDIS... | Function: Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine.
Catalytic Activity: ATP + cytidine(34)... |
B4F252 | MELKNCPLINEIKRQIGSHTHILVGFSGGVDSTVLLHGLVCLRDKYQLPLELTAIYVHHGLNSKADDWLTHCEHFCHNWQVSFISERVQVNGKEGGIEQGAREARYQAYRQYLQPNQVLVTAQHQDDQAETFLLALKRGSGPAGLSSMPAKMPFEQGYLLRPLLNITREQIEAYAHEHGLLWIEDDSNQDDRYDRNFLRLHVMPLLTQRWPHFSQAVTRSAALCGEQEALLDELLDVELQQLIDEHQSLDINLLSRCSEIKRNALLRRWFAKCNKSMPSRSQLSRLWQEVALAKADAEPRLRFFQDEVRRYQQRLYLVPV... | Function: Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine.
Catalytic Activity: ATP + cytidine(34)... |
Q7V987 | MASSSSTQLPWSAWHARLHHKLLANPDLLPAKASLLIAVSGGQDSMALLGLLIDLQRKHGWSLEVWHGDHNWHKQSATIATELKNWCESHNLSFCSDQAKPGQTNNEATARHWRYEQLTLHAERLSSNNPNHPCRYVLTGHTSSDRAETLLLNLARGTDLAGLSSMRQCRPISKDHPHKNVQLIRPLLGFSREDTALICSELGLPIWLDPANSNPDFSRNRVRQEVLPVLESLHPGCSLRMAALAERLNHHHADQQAIAMLALNNLSKQNGLCRKDLAQLPITARTTLLAYWLKRSGAPSLPAVQLEQISQSIAPGKPPG... | Function: Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine.
Catalytic Activity: ATP + cytidine(34)... |
Q7UZL1 | MSDKNSSQKNWTSWHHLLHKEILGNKTLIPDGANLLIAVSGGQDSMALLNLINDMKTQHNWFVNVWHGDHQWHKKSAKYALELKSYCNKKNISFFFDQANKNNISSEEKARDWRYKKLSERANQLLIENQKEIDIYLLTGHTNTDNAETFLLNLARGSNYAGLSNINKKRLLKHHIFLIRPLLIFSREDTKKFCQLQNIPIWEDPTNCDLTIKRNIVRKEIIPILETMYPGCSKRINSFAEKMSNYKNEQNDLSKLASLYCEDAIGVKRELLNSLCIEARCTILNTFLKKDCTKQLSSKNLTHLASSILVKDRGKIDLPD... | Function: Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine.
Catalytic Activity: ATP + cytidine(34)... |
Q46ID9 | MRLHKRLKQNKSLLPSNSTILLAISGGQDSMALLKLIIDLKRLHQWQVEVWHGNHQWHAKSEETEDELKLWCLKNQISFHSNKADKKEVANEEKARDWRYKNLIMKAKFLSSKNIHFPCTRILTGHTATDRAETVIMNLARGTDLTGLTTLKEQRTIENNIDLTRPLLIFNRNETLEICKDFNLPIWIDPSNENINLTRNKIRKEILPILNSIYKGADSRIASVANRLESYNEDQKLFAKIAIQFCQGEKINSLSRIKLFGLTNSIRQIILSNWLKTMGVKRVTALQIEEINTKVSQRKPPGSIHLHGDFLIRWNKEAIY... | Function: Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine.
Catalytic Activity: ATP + cytidine(34)... |
Q6FPU1 | MDGTGISDGSSVTGDAAAGFPAGATQAPGSKQGMDLYFDNALQYMGEHPVLAGVGGFLALYVGAGVYKGVQTRLNGGKAATQFLKGGFDPKMNAKEALQILNLKENNLTTKKLKEVHRKIMLANHPDKGGSPYLATKINEAKDFLEKKGIVRK | Function: Essential component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner. In the complex, it is required to stimulate activity of mtHSP70 (SSC1) (By similarity).
Location Topology: S... |
Q6PBT7 | MASTMVAVGLTLAAAGFTGRYAVRAMKHMEPQVKQALEASKSAFGSGYYRGGFDPKMNRREASLILGVSPTANKTKIREAHRKLMILNHPDRGGSPYLAAKINEAKDLLDGQAKK | Function: Mitochondrial co-chaperone which forms a complex with prohibitins to regulate cardiolipin remodeling (By similarity). May be a component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent... |
Q6BH37 | MAPFNMDIPTLAIPGDRNQSQAIELSQQAQQPQQPQQSQQAYTGHLQRKQADEGSAEYYFDKGCEWMGNHPWMTGMGVLGVAYFASGFVKSKQPGINGKAFVKGPFGQKMTPKEALQILNLKETNLSQAKLKEQHRKLMMANHPDKGGSSYLATKVNEAKDILEKRGGLKKK | Function: Essential component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner. In the complex, it is required to stimulate activity of mtHSP70 (SSC1) (By similarity).
Location Topology: S... |
Q54QN1 | MATPIIVGATIAGIAYSSRFLIRVIQRAKSKQLFEMVSTPGFTVETIEDGFENKMTPAEAANILGLKEESTKEEIKIRHKLLMIKNHPDKGGSSYLATKINEARNVLSSKNSN | Function: Mitochondrial co-chaperone which forms a complex with prohibitins to regulate cardiolipin remodeling (By similarity). May be a component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent... |
Q9VTJ8 | MASSVILAGLSVAAVGFAGKHLMRRMPQMTTKFNEALKNLPKYDAESMAASKYYKGGFDPKMNKREASLILGVSPSASKIKIKDAHKKIMLLNHPDRGGSPYLAAKINEAKDFLDKAK | Function: Probable component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner. May act as a co-chaperone that stimulate the ATP-dependent activity (By similarity).
Location Topology: Singl... |
Q5B4H1 | MASALTLGLGVATAAFLGRAGLVAYRRSKGGVNALGKAFYKGGFEPRMNRREAALILELPERTLNKEKVRKKHRQLMLLNHPDRGGSPYLATKINEAKEFLDKHT | Function: Essential component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner. In the complex, it is required to stimulate activity of mtHSP70 (SSC1/sscA) (By similarity).
Location Topolo... |
Q4I7T5 | MASVMAWGAGAAVAAFLGRAGLVAWRRSRGGVGAMGKAFYKGGFEAKMTKKEATLILSLNERAITKDKVRKAHRTLMLLNHPDRGGSPYLATKVNEAKEFLDKNG | Function: Essential component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner. In the complex, it is required to stimulate activity of mtHSP70 (SSC1) (By similarity).
Location Topology: S... |
Q96DA6 | MASTVVAVGLTIAAAGFAGRYVLQAMKHMEPQVKQVFQSLPKSAFSGGYYRGGFEPKMTKREAALILGVSPTANKGKIRDAHRRIMLLNHPDKGGSPYIAAKINEAKDLLEGQAKK | Function: Mitochondrial co-chaperone which forms a complex with prohibitins to regulate cardiolipin remodeling (By similarity). May be a component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent... |
Q9CQV7 | MASTVVAVGLTIAAAGFAGRYVLQAMKHVEPQVKQVFQSLPKSAFGGGYYRGGFEPKMTKREAALILGVSPTANKGKIRDAHRRIMLLNHPDKGGSPYIAAKINEAKDLLEGQAKK | Function: Mitochondrial co-chaperone which forms a complex with prohibitins to regulate cardiolipin remodeling . May be a component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner. May ac... |
Q7RX75 | MSSAVAIGAGVAVAAFLGRAGLVAWRRSRGGVGALGKAFYKGGFEPRMNKKEASLILSLNERTITKDKIRKAHRTLMLLNHPDRGGSPYLATKVNEAKEFLEKSV | Function: Essential component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner. In the complex, it is required to stimulate activity of mtHSP70 (hsp70-5) (By similarity).
Location Topology... |
Q9UT37 | MSSAILLGVGIAATAAAGKIGVDAFRKYRNLNGGVKAFLKGGFESKMSRAEAIQILSLNNRTLTRQKIKEAHRRLMLANHPDRGGSPYVASKVNEAKSLLDADRSIRKFSSWALPVSKQRSMPSVLEAVKWLEYSSIPKA | Function: Essential component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner. In the complex, it is required to stimulate activity of mtHSP70 (ssc1) (By similarity).
Location Topology: S... |
Q6CEU0 | MSTTPVQPLQSEPLMDSETGVAPQIEAPQVPEGPKKGIDEQIFDYFAEHPVQATAATLVGLYALGAVFKRPAAGARGQFFKGGFENKMGPSEALQILSLRDAGLTMNKLKGQHRKIMLLNHPDRGGSPYVATKINEAKSVLEKRGGLK | Function: Essential component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner. In the complex, it is required to stimulate activity of mtHSP70 (SSC1) (By similarity).
Location Topology: S... |
Q07914 | MSSQSNTGNSIEAPQLPIPGQTNGSANVTVDGAGVNVGIQNGSQGQKTGMDLYFDQALNYMGEHPVITGFGAFLTLYFTAGAYKSISKGLNGGKSTTAFLKGGFDPKMNSKEALQILNLTENTLTKKKLKEVHRKIMLANHPDKGGSPFLATKINEAKDFLEKRGISK | Function: Essential component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner. In the complex, it is required to stimulate activity of mtHSP70 (SSC1).
Location Topology: Single-pass membr... |
O62250 | MPWRTALKVALAAGEAVAKALTRAVRDEIKQTQQAAARHAASTGQSASETRENANSNAKLGISLEESLQILNVKTPLNREEVEKHYEHLFNINDKSKGGTLYLQSKVFRAKERIDEEFGRIELKEEKKKEENAKTE | Function: Regulates ATP-dependent protein translocation into the mitochondrial matrix.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 15276
Sequence Length: 136
Domain: The J-like region, although related to the J domain does not have co-chaperone activity.
Subcellular Location: Mitochondrion inner ... |
Q59ZW9 | MAHRLLVNVIFTGASVFGRAFTEAYRQAAKASAAGAAGRPAKASSAGGIPVEEAMKILDLEKSELSLDKVEEKYEYLFNVNSKEQGNSFYLQSKVYYAMDTLKKELEYLEKLQNEKGAASN | Function: Essential component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner. In the complex, it is required to regulate activity of mtHSP70 (SSC1) via its interaction with PAM18/TIM14. ... |
P20614 | MAPLAALASSMLLLLWLVAPSRACTCVPPHPQTAFCNSDLVIRAKFVGAPEVNHTTLYQRYEIKTTKMFKGFDALGHATDIRFVYTPAMESVCGYSHKSQNRSEEFLIAGQLRNGLLHITTCSFVVPWNSLSFSQRSGFTKTYAAGCDMCTVFACASIPCHLESDTHCLWTDQLLLGSDKGFQSRHLACLPQEPGLCAWQSLRPRKD | Function: Metalloproteinase inhibitor that functions by forming one to one complexes with target metalloproteinases, such as collagenases, and irreversibly inactivates them by binding to their catalytic zinc cofactor. Acts on MMP1, MMP2, MMP3, MMP7, MMP8, MMP9, MMP10, MMP11, MMP12, MMP13 and MMP16. Does not act on MMP1... |
P50122 | MALFAPTVSGILLLLWLTAPSRACTCVPPHPQTAFCNSEVVIRAKFVGTAEVNETALYQRYEIKMTKMFKGFSALRDAPDIRFIYTPAMESVCGYFHRSQNRSEEFLIAGQLSNGHLHITTCSFVAPWNSMSSAQRRGFTKTYAAGCEECTVFPCSSIPCKLQSDTHCLWTDQLLTGSDKGFQSRHLACLPREPGMCTWQSLRPRGA | Function: Metalloproteinase inhibitor that functions by forming one to one complexes with target metalloproteinases, such as collagenases, and irreversibly inactivates them by binding to their catalytic zinc cofactor. Acts on MMP1, MMP2, MMP3, MMP7, MMP8, MMP9, MMP10, MMP11, MMP12, MMP13 and MMP16. Does not act on MMP1... |
Q60453 | RACSCSPVHPQQAFCNADVVIRAKAVSEKEVDSGNDIYGNPIKRIQYEIKQIKMFKGPDKDIEFIYTAPSSAVCGVSLDVGGKKEYLIAGKAEGDGKMHITLCDFIVPWDTLSTTQKKSLNHRYQMGCECKITRCPMIPCYISSPDECLWMDWVTEKSINGHQAKFFACIKRSDGSCAWYRGAAPPKQEFLDIEDP | Function: Complexes with metalloproteinases (such as collagenases) and irreversibly inactivates them by binding to their catalytic zinc cofactor.
PTM: The activity of TIMP2 is dependent on the presence of disulfide bonds.
Sequence Mass (Da): 21941
Sequence Length: 196
Subcellular Location: Secreted
|
O77717 | KAVSEKEVDSGNDIYGNPIKRIQYEIKQIKMFKGPDKDIEFIYTAPSSAVCGVSLDVGGKKEYLIAGKADGNGKMHITLCDFIVPWDTLST | Function: Complexes with metalloproteinases (such as collagenases) and irreversibly inactivates them.
PTM: The activity of TIMP2 is dependent on the presence of disulfide bonds.
Sequence Mass (Da): 9998
Sequence Length: 91
Subcellular Location: Secreted
|
P16035 | MGAAARTLRLALGLLLLATLLRPADACSCSPVHPQQAFCNADVVIRAKAVSEKEVDSGNDIYGNPIKRIQYEIKQIKMFKGPEKDIEFIYTAPSSAVCGVSLDVGGKKEYLIAGKAEGDGKMHITLCDFIVPWDTLSTTQKKSLNHRYQMGCECKITRCPMIPCYISSPDECLWMDWVTEKNINGHQAKFFACIKRSDGSCAWYRGAAPPKQEFLDIEDP | Function: Complexes with metalloproteinases (such as collagenases) and irreversibly inactivates them by binding to their catalytic zinc cofactor. Known to act on MMP-1, MMP-2, MMP-3, MMP-7, MMP-8, MMP-9, MMP-10, MMP-13, MMP-14, MMP-15, MMP-16 and MMP-19.
PTM: The activity of TIMP2 is dependent on the presence of disulf... |
P30121 | MGAAARSLRLALGLLLLATLLRPADACSCSPVHPQQAFCNADVVIRAKAVSEKEVDSGNDIYGNPIKRIQYEIKQIKMFKGPDKDIEFIYTAPSSAVCGVSLDVGGKKEYLIAGKAEGDGKMHITLCDFIVPWDTLSITQKKSLNHRYQMGCECKITRCPMIPCYISSPDECLWMDWVTEKSINGHQAKFFACIKRSDGSCAWYRGAAPPKQEFLDIEDP | Function: Complexes with metalloproteinases (such as collagenases) and irreversibly inactivates them by binding to their catalytic zinc cofactor.
PTM: The activity of TIMP2 is dependent on the presence of disulfide bonds.
Sequence Mass (Da): 24356
Sequence Length: 220
Subcellular Location: Secreted
|
P0DTS9 | MSVLETKLKSQMSKSAKIARNMNKLPDEIDRLRKRIERINKKRKPTSSNIRDLEKSNKQLVTKQQKLADLQVEYTKIEKKINETKINLQKEQSRNQKKLSSMLDKNTKGNEEIMEKLLTNSDQINEISNQIKKAVNQKEIIEYDVFLSHSSLDKEDYVSKISEKLIEKGLKVFEDVKVFEIGKSQTETMNMGILNSRFVVVFLSPNFIESGWSRYEFLSFLNREINEEHVIILPIWHKVSVEDVRAYNPYLVDKYALNTSDFSIEEIVEKIYQVIVNSKN | Function: Virulence factor that suppresses host Toll-like receptor 2 (TLR2)-mediated NF-kappa-B signaling upon infection . NAD(+) hydrolase (NADase) that catalyzes cleavage of NAD(+) into ADP-D-ribose (ADPR) and nicotinamide . Also able to hydrolyze NADP(+), but not other NAD(+)-related molecules . Able to reduce NAD(+... |
B7UM99 | MPIGNLGNNVNGNHLIPPAPPLPSQTDGAARGGTGHLISSTGALGSRSLFSPLRNSMADSVDSRDIPGLPTNPSRLAAATSETCLLGGFEVLHDKGPLDILNTQIGPSAFRVEVQADGTHAAIGEKNGLEVSVTLSPQEWSSLQSIDTEGKNRFVFTGGRGGSGHPMVTVASDIAEARTKILAKLDPDNHGGRQPKDVDTRSVGVGSASGIDDGVVSETHTSTTNSSVRSDPKFWVSVGAIAAGLAGLAATGIAQALALTPEPDDPTTTDPDQAANAAESATKDQLTQEAFKNPENQKVNIDANGNAIPSGELKDDIVEQ... | Function: Multifunctional protein that is required for efficient pedestal formation in host epithelial cells during infection. The extracellular region acts as a receptor for bacterial intimin, allowing the bacterium to attach tightly to the host-cell surface. Simultaneously, the intracellular region initiates a signal... |
A5A627 | MNLVDIAILILKLIVAALQLLDAVLKYLK | Function: Toxic component of a type I toxin-antitoxin (TA) system (Probable). Overexpression causes cessation of growth, induces stress-response, a number of membrane protein genes, and leads to cell death . Inhibits ATP synthesis, ATP levels drop drastically quickly after induction . Part of the programmed response t... |
Q07352 | MTTTLVSATIFDLSEVLCKGNKMLNYSAPSAGGCLLDRKAVGTPAGGGFPRRHSVTLPSSKFHQNQLLSSLKGEPAPALSSRDSRFRDRSFSEGGERLLPTQKQPGGGQVNSSRYKTELCRPFEENGACKYGDKCQFAHGIHELRSLTRHPKYKTELCRTFHTIGFCPYGPRCHFIHNAEERRALAGARDLSADRPRLQHSFSFAGFPSAAATAAATGLLDSPTSITPPPILSADDLLGSPTLPDGTNNPFAFSSQELASLFAPSMGLPGGGSPTTFLFRPMSESPHMFDSPPSPQDSLSDQEGYLSSSSSSHSGSDSPT... | Function: Zinc-finger RNA-binding protein that destabilizes several cytoplasmic AU-rich element (ARE)-containing mRNA transcripts by promoting their poly(A) tail removal or deadenylation, and hence provide a mechanism for attenuating protein synthesis . Acts as a 3'-untranslated region (UTR) ARE mRNA-binding adapter pr... |
P23950 | MTTTLVSATIFDLSEVLCKGNKMLNYSTPSAGGCLLDRKAVGTPAGGGFPRRHSVTLPSSKFHQNQLLSSLKGEPAPSLSSRDSRFRDRSFSEGGERLLPTQKQPGSGQVNSSRYKTELCRPFEENGACKYGDKCQFAHGIHELRSLTRHPKYKTELCRTFHTIGFCPYGPRCHFIHNAEERRALAGGRDLSADRPRLQHSFSFAGFPSAAATAAATGLLDSPTSITPPPILSADDLLGSPTLPDGTNNPFAFSSQELASLFAPSMGLPGGGSPTTFLFRPMSESPHMFDSPPSPQDSLSDHEGYLSSSSSSHSGSDSPT... | Function: Zinc-finger RNA-binding protein that destabilizes several cytoplasmic AU-rich element (ARE)-containing mRNA transcripts by promoting their poly(A) tail removal or deadenylation, and hence provide a mechanism for attenuating protein synthesis . Acts as a 3'-untranslated region (UTR) ARE mRNA-binding adapter pr... |
Q805B4 | MSTTLLSAFYDIDLLYKNEKALNNLALSTMLDKKAVGSPVSSTNSNLFPGFLRRHSATNLQALSGSTNLAKFCPNNNNNPLKDPAVSSTALLNRENKFRDRSFSENGERSQHLLHLQQQQQQQKAGAQVNSTRYKTELCRPFEENGACKYGEKCQFAHGFHELRSLTRHPKYKTELCRTFHTIGFCPYGPRCHFIHNAEERRQAPGAGERPKLHHSLSFSGFPNHSLDSPLLESPTSRTPPPQSSGSLYCQELLQLNNNNPCANNAFTFSGQELGLIAPLAIHTQNQSYCRQPCSSPPLSFQPLRRVSESPVFDAPPSPP... | Function: Zinc-finger RNA-binding protein that destabilizes several cytoplasmic AU-rich element (ARE)-containing mRNA transcripts by promoting their poly(A) tail removal or deadenylation, and hence provide a mechanism for attenuating protein synthesis . Acts as a 3'-untranslated region (UTR) ARE mRNA-binding adapter pr... |
P47974 | MSTTLLSAFYDVDFLCKTEKSLANLNLNNMLDKKAVGTPVAAAPSSGFAPGFLRRHSASNLHALAHPAPSPGSCSPKFPGAANGSSCGSAAAGGPTSYGTLKEPSGGGGTALLNKENKFRDRSFSENGDRSQHLLHLQQQQKGGGGSQINSTRYKTELCRPFEESGTCKYGEKCQFAHGFHELRSLTRHPKYKTELCRTFHTIGFCPYGPRCHFIHNADERRPAPSGGASGDLRAFGTRDALHLGFPREPRPKLHHSLSFSGFPSGHHQPPGGLESPLLLDSPTSRTPPPPSCSSASSCSSSASSCSSASAASTPSGAPT... | Function: Zinc-finger RNA-binding protein that destabilizes several cytoplasmic AU-rich element (ARE)-containing mRNA transcripts by promoting their poly(A) tail removal or deadenylation, and hence provide a mechanism for attenuating protein synthesis . Acts as a 3'-untranslated region (UTR) ARE mRNA-binding adapter pr... |
Q9ZD67 | MLPPKIFFEKVKEIIWPIERKELKLFIPMALMMLCILFNFGALRSIKDSLVVPSMGAEIISFLKLWLVLPSCVIFTILYVKLSNKLNFEYIFYSIVGTFLLFFLLFAYIIYPNQDIYHPNDAMINNLIASYPNLKWFIKIGSKWSYALMYIFSELWSAVVINLMFWQFANHIFDTAKAKRFYPVLGMVGNIGLIIAGSVLVFFSSGQYIIDSELLTDSYNSSSNNSIMLQPIISIIVTAGIIAMFLFRIINKFILTNSINVLDVKKVAAKTKTKLALIESIKLIIHSKYIGRIALLIICYGLLINIVEGPWKAKIKELHP... | Function: Provides the rickettsial cell with host ATP in exchange for rickettsial ADP. This is an obligate exchange system. This energy acquiring activity is an important component of rickettsial parasitism.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 57182
Sequence Length: 501
Subcellular Locati... |
F1NZP5 | MGPGWRAPSAALVGGSVALFGALRRAALALPRPAAVRSRPGRVWRWRNLLVSFAHSVLAGLWALFSLWQSPELLSDIQDGYSVSGHLLVCFSSGYFIHDSLDIIFNQQSRSSWEYLVHHAMAISAFVSLIITGRFLVAAMLLLLVEVSNIFLTIRMLLKMSNVPSPALYEANKYVNLVMYFAFRLAPQVYLTWYFVRYVEVQGQGAFLMANLLLLDAMILMYFSRLLRSDFFPSLRKGSVGRDVDGEKFLID | Function: Regulates the composition and fluidity of the plasma membrane (By similarity). Inhibits the incorporation of membrane-fluidizing phospholipids containing omega-3 long-chain polyunsaturated fatty acids (LCPUFA) and thereby promotes membrane rigidity (By similarity). Does not appear to have any effect on LCPUFA... |
Q96CP7 | MPRLLHPALPLLLGATLTFRALRRALCRLPLPVHVRADPLRTWRWHNLLVSFAHSIVSGIWALLCVWQTPDMLVEIETAWSLSGYLLVCFSAGYFIHDTVDIVASGQTRASWEYLVHHVMAMGAFFSGIFWSSFVGGGVLTLLVEVSNIFLTIRMMMKISNAQDHLLYRVNKYVNLVMYFLFRLAPQAYLTHFFLRYVNQRTLGTFLLGILLMLDVMIIIYFSRLLRSDFCPEHVPKKQHKDKFLTE | Function: Regulates the composition and fluidity of the plasma membrane . Inhibits the incorporation of membrane-fluidizing phospholipids containing omega-3 long-chain polyunsaturated fatty acids (LCPUFA) and thereby promotes membrane rigidity . Does not appear to have any effect on LCPUFA synthesis .
Location Topology... |
A8WGS4 | MELNSVILTTGSSVGFFKLVNYGLGKLPIPETARRNAWKWNNISTSFVHSLITGVWSVLCFCMHPQMAEDLIETHSVFSHALVSVSIGYFIYDFLDMVINQKIIHSWELLFHHVVVITCFGISVLTCRYVGFAVVALLVEINSVFLHLRQVLRMANLAKSTFYRVNSMINLGTYVVFRINTLAWMTRWLVLNRDLIPLFSYTIGSVGLAIMTAMNIVLFYRLMRSDFMKASREKELRKEKEKEKDM | Function: Regulates the composition and fluidity of the plasma membrane (By similarity). Inhibits the incorporation of membrane-fluidizing phospholipids containing omega-3 long-chain polyunsaturated fatty acids (LCPUFA) and thereby promotes membrane rigidity (By similarity). Does not appear to have any effect on LCPUFA... |
A6NGC4 | MAPTGLLVAGASFLAFRGLHWGLRRLPTPESAARDRWQWWNLCVSLAHSLLSGTGALLGLSLYPQMAADPIHGHPRWALVLVAVSVGYFLADGADLLWNQTLGKTWDLLCHHLVVVSCLSTAVLSGHYVGFSMVSLLLELNSACLHLRKLLLLSRQAPSLAFSVTSWASLATLALFRLVPLGWMSLWLFRQHHQVPLALVTLGGIGLVTVGIMSIILGIRILVNDVLQSRPHPPSPGHEKTRGTRTRRDNGPVTSNSSTLSLKD | Function: Regulates the composition and fluidity of the plasma membrane . Inhibits the incorporation of membrane-fluidizing phospholipids containing omega-3 long-chain polyunsaturated fatty acids (LCPUFA) and thereby promotes membrane rigidity . Does not appear to have any effect on LCPUFA synthesis .
Location Topology... |
Q9ZD47 | MTINASNIENSFSKINSHFSKLTDYIWPIKRHEISKFLFITLLMFCILFIQNLIRALKDSIVTTMIGAETISFLKFWGVMPSAFLITVIYVKLVNRMKAENIFYLIISIFLTFFALFAYVIFPNHEMLHLRPVTVHNLTASLPNLKWFILLLSKWSFSLFYIIAELWPNVVFALLFWQFVNNITTVEESKRFYPLFGLLSQTGIYLAGHFLENLSNINYYVTNKFALQSSFHTLSIQIILTIVLILGIVSIKTFWLLNHKVLDKKHMALLRFKTKNKSITIAKSFQMILSSRHIRLIATLLICYGIAINLVEGPWKAAAT... | Function: Provides the rickettsial cell with host ATP in exchange for rickettsial ADP. This is an obligate exchange system. This energy acquiring activity is an important component of rickettsial parasitism (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 58208
Sequence Length: 512
Su... |
P50694 | MMKTLVVVLSLSLTILSFGGAHAATISFKNNCPYMVWPGTLTSDQKPQLSTTGFELASQASFQLDTPVPWNGRFWARTGCSTDASGKFVCATADCASGQVMCNGNGAIPPATLAEFNIPAGGGQDFYDVSLVDGFNLPMSVTPQGGTGDCKTASCPANVNAVCPSELQKKGSDGSVVACLSACVKFGTPQYCCTPPQNTPETCPPTNYSEIFHNACPDAYSYAYDDKRGTFTCNGGPNYAITFCP | Catalytic Activity: Hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-beta-D-glucans.
Sequence Mass (Da): 25707
Sequence Length: 245
Subcellular Location: Secreted
EC: 3.2.1.39
|
Q9BXR5 | MRLIRNIYIFCSIVMTAEGDAPELPEERELMTNCSNMSLRKVPADLTPATTTLDLSYNLLFQLQSSDFHSVSKLRVLILCHNRIQQLDLKTFEFNKELRYLDLSNNRLKSVTWYLLAGLRYLDLSFNDFDTMPICEEAGNMSHLEILGLSGAKIQKSDFQKIAHLHLNTVFLGFRTLPHYEEGSLPILNTTKLHIVLPMDTNFWVLLRDGIKTSKILEMTNIDGKSQFVSYEMQRNLSLENAKTSVLLLNKVDLLWDDLFLILQFVWHTSVEHFQIRNVTFGGKAYLDHNSFDYSNTVMRTIKLEHVHFRVFYIQQDKIY... | Function: Participates in the innate immune response to microbial agents. Acts via MYD88 and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response (By similarity).
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 94564
Sequence Length: 811
Subcellular Locati... |
Q6R5P0 | MPRMERHQFCSVLLILILLTLVSLTLTGWAWTIPDCIIADSLLFPNLSYYIPFCTSAPGLHLLASCSNVKNLNQTLKRVPRNTEVLCLQGMVPTLPAKAFIRFHSLQLLRLQLRTTSVTSRTFQGLDQLQYLFFDHHAPCCLSLFLSPNCFESLRSLSSLSFQGYCLTYSQSIYLPTSLRHLTLRNSCLTKFQDLQRLFPDLLLSTSSTPNIKPGAPFLETLDLSYNLQLKQAGVRDLYGLTLHSLILDGTPLKALDLTDSGLLHLHFLSLVGTGIEKVPASLTGYSELRALDLGKNQIQNILENGEIPGYKALEFLSLH... | Function: Participates in the innate immune response to microbial agents. Acts via MYD88 and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 105873
Sequence Length: 926
Subcellular Location: Membrane
|
Q6QNU9 | MGRYWLLPGLLLSLPLVTGWSTSNCLVTEGSRLPLVSRYFTFCRHSKLSFLAACLSVSNLTQTLEVVPRTVEGLCLGGTVSTLLPDAFSAFPGLKVLALSLHLTQLLPGALRGLGQLQSLSFFDSPLRRSLFLPPDAFSDLISLQRLHISGPCLDKKAGIRLPPGLQWLGVTLSCIQDVGELAGMFPDLVQGSSSRVSWTLQKLDLSSNWKLKMASPGSLQGLQVEILDLTRTPLDAVWLKGLGLQKLDVLYAQTATAELAAEAVAHFELQGLIVKESKIGSISQEALASCHSLKTLGLSSTGLTKLPPGFLTAMPRLQR... | Function: Participates in the innate immune response to microbial agents. Acts via MYD88 and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response. Plays a role in preventing infection of internal organs of the urogenital system.
Location Topology: Single-pass type I membrane protein... |
Q6R5N8 | MSGLYRILVQLEQSPYVKTVPLNMRRDFFFLVVTWMPKTVKMNGSSFVPSLQLLLMLVGFSLPPVAETYGFNKCTQYEFDIHHVLCIRKKITNLTEAISDIPRYTTHLNLTHNEIQVLPPWSFTNLSALVDLRLEWNSIWKIDEGAFRGLENLTLLNLVENKIQSVNNSFEGLSSLKTLLLSHNQITHIHKDAFTPLIKLKYLSLSRNNISDFSGILEAVQHLPCLERLDLTNNSIMYLDHSPRSLVSLTHLSFEGNKLRELNFSALSLPNLTNLSASRNGNKVIQNVYLKTLPQLKSLNLSGTVIKLENLSAKHLQNLR... | Function: Component of innate and adaptive immunity that recognizes and binds 23S rRNA from bacteria. TLRs (Toll-like receptors) control host immune response against pathogens through recognition of molecular patterns specific to microorganisms. Acts via MYD88 and TRAF6, leading to NF-kappa-B activation, cytokine secre... |
P30974 | MSEIVDTELLVNCTILAVRRFELNSIVNTTLLGSLNRTEVVSLLSSIIDNRDNLESINEAKDFLTECLFPSPTRPYELPWEQKTIWAIIFGLMMFVAIAGNGIVLWIVTGHRSMRTVTNYFLLNLSIADLLMSSLNCVFNFIFMLNSDWPFGSIYCTINNFVANVTVSTSVFTLVAISFDRYIAIVHPLKRRTSRRKVRIILVLIWALSCVLSAPCLLYSSIMTKHYYNGKSRTVCFMMWPDGRYPTSMADYAYNLIILVLTYGIPMIVMLICYSLMGRVLWGSRSIGENTDRQMESMKSKRKVVRMFIAIVSIFAICWL... | Function: Receptor for tachykinin-like peptides.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 58020
Sequence Length: 504
Subcellular Location: Cell membrane
|
Q86T26 | MYRHGISSQRSWPLWTTIFIFLGVAAILGVTIGLLVHFLAVEKTYYYQGDFHISGVTYNDNCENAASQASTNLSKDIETKMLNAFQNSSIYKEYVKSEVIKLLPNANGSNVQLQLKFKFPPAEGVSMRTKIKAKLHQMLKNNMASWNAVPASIKLMEISKAASEMLTNNCCGRQVANSIITGNKIVNGKSSLEGAWPWQASMQWKGRHYCGASLISSRWLLSAAHCFAKKNNSKDWTVNFGIVVNKPYMTRKVQNIIFHENYSSPGLHDDIALVQLAEEVSFTEYIRKICLPEAKMKLSENDNVVVTGWGTLYMNGSFPV... | Function: Serine protease.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 46337
Sequence Length: 416
Subcellular Location: Cell membrane
EC: 3.4.21.-
|
Q14C59 | MYRPVIASRKSIPPWLIILCVLGVLAALGIIIGLLVHFLAVENKIYYYQGGFKVLDIPYDRNYERETSLESNYLSKILENKMVEAFQNSNIYKQYINSQVITLVPDNNSVTAHIWLVFKDPWSNKENLRRRIESILRQMLENNPESLTTDPGSLKLTEISKVDAEKIINNRCGRRPRMSATYDRITGGSTAHKGEWPWQASLRVNGKHYCGASLIGERFLLTAAHCFQGTNNPKNLTVSFGTRVTPAYMQHSVQEIIIHEDYVKGEHHDDVAVIKLTEKVSFNNDVHRVCLPESTQIFPPGEGVVVTGWGSFSYNGKSPL... | Function: Serine protease.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 46713
Sequence Length: 416
Subcellular Location: Cell membrane
EC: 3.4.21.-
|
Q1JRP2 | MARGQPRRSEEQWTALQNRTECKTKIKLTRCGKITLGILTAVLAAVLIGLIAYFAACGKDSFYYHVSFKVNNIDYDSKFAKPYSQEYMDLNKRIVSLMNETFHESKLRKQYVKAHTVQVSKAKGKVVIHAVLKFKACYRNNVEKYWESVETTLYQKLKGQTGLLIDSSSFKFSDIAMPIAEDLLNTCCGRRTIIHRGHKVAGGQDAEEGEWPWQASLQQNSVHRCGATLISNYWLITAAHCFIRAANPKDWKVSFGFLLSKPQAPRAVKNIIIHENYSYPAHDNDIAVVRLSSPVLYESNIRRACLPEATQKFPPNSDVV... | Function: Serine protease which has a preference for Arg or Lys in position P1 and uncharged residues in positions P2 and P3. Shows specificity towards FGF2 in vitro.
PTM: Proteolytically cleaved via an autocatalytic mechanism.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 48073
Sequence L... |
O60235 | MYRPARVTSTSRFLNPYVVCFIVVAGVVILAVTIALLVYFLAFDQKSYFYRSSFQLLNVEYNSQLNSPATQEYRTLSGRIESLITKTFKESNLRNQFIRAHVAKLRQDGSGVRADVVMKFQFTRNNNGASMKSRIESVLRQMLNNSGNLEINPSTEITSLTDQAAANWLINECGAGPDLITLSEQRILGGTEAEEGSWPWQVSLRLNNAHHCGGSLINNMWILTAAHCFRSNSNPRDWIATSGISTTFPKLRMRVRNILIHNNYKSATHENDIALVRLENSVTFTKDIHSVCLPAATQNIPPGSTAYVTGWGAQEYAGHT... | Function: May play some biological role in the host defense system on the mucous membrane independently of or in cooperation with other substances in airway mucous or bronchial secretions. Plays a role in the proteolytic processing of ACE2. Proteolytically cleaves and activates the human coronavirus 229E (HCoV-229E) sp... |
Q8VHJ4 | MYRPRSMVSPSRFFNPFMVALIVIITVGLLAMTAGLLIHFLAFDKRAYFYHSNFHILNVDYTEALNSPATHEYRTLSERIESMITDAFRESNLRSEFIRTHVVKLRKEGSGVVADVVMKFRSSKRNNKKAIKTRIQSVLQRLSSSGNLEIAPSNGITSLTDQDTENVLTQECGARPDLITLSEERIIGGTQAETGDWPWQVSLQLNNVHHCGGTLISNLWVLTAAHCFRSYSNPQQWTATFGVSTISPRLRVRVRAILAHAEYNSITRDNDIAVVQLDRPVTFTRNIHRVCLPAATQNIMPDSVAYVTGWGSLTYGGNTV... | Function: May play some biological role in the host defense system on the mucous membrane independently of or in cooperation with other substances in airway mucous or bronchial secretions. Plays a role in the proteolytic processing of ACE2. Preferentially cleaves the C-terminal side of arginine residues at the P1 posit... |
Q9UL52 | MMYRPDVVRARKRVCWEPWVIGLVIFISLIVLAVCIGLTVHYVRYNQKKTYNYYSTLSFTTDKLYAEFGREASNNFTEMSQRLESMVKNAFYKSPLREEFVKSQVIKFSQQKHGVLAHMLLICRFHSTEDPETVDKIVQLVLHEKLQDAVGPPKVDPHSVKIKKINKTETDSYLNHCCGTRRSKTLGQSLRIVGGTEVEEGEWPWQASLQWDGSHRCGATLINATWLVSAAHCFTTYKNPARWTASFGVTIKPSKMKRGLRRIIVHEKYKHPSHDYDISLAELSSPVPYTNAVHRVCLPDASYEFQPGDVMFVTGFGALK... | Function: Serine protease which possesses both gelatinolytic and caseinolytic activities. Shows a preference for Arg in the P1 position.
PTM: N-glycosylated.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 47696
Sequence Length: 423
Subcellular Location: Cell membrane
EC: 3.4.21.-
|
Q5S248 | MYRSCVVRARKRTCVEPWVIGIISFLSLIVLAVCIGLTVHYVRYNHRRTYNYYSTLSFTSDKLYSEFGREASKNFTEMSQRIETMVKHAFHKSPLRGQLVKAHIIKFSKEDDGVLAHMLLIFRIRSTEDPETVHKIIEYVLHEKLKYATGPPNVDPESVKIKKINKTESDNYFNHCCGTRRNKSTVQTSVRIVGGTPVEEEEWPWQSSLRWDGSHRCGATLINNTWLVTAAHCFRTHKDPSRWSATFGATLQPRKLTTGIRRIIVHEKYKYPSHDYDIALAELSKPVPCTNAVHKVCLPDANHEFQPGQRMFVTGFGALK... | Function: Serine protease which possesses both gelatinolytic and caseinolytic activities. Shows a preference for Arg in the P1 position.
PTM: N-glycosylated.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 48065
Sequence Length: 423
Subcellular Location: Cell membrane
EC: 3.4.21.-
|
Q6ZWK6 | MMYAPVEFSEAEFSRAEYQRKQQFWDSVRLALFTLAIVAIIGIAIGIVTHFVVEDDKSFYYLASFKVTNIKYKENYGIRSSREFIERSHQIERMMSRIFRHSSVGGRFIKSHVIKLSPDEQGVDILIVLIFRYPSTDSAEQIKKKIEKALYQSLKTKQLSLTINKPSFRLTPIDSKKMRNLLNSRCGIRMTSSNMPLPASSSTQRIVQGRETAMEGEWPWQASLQLIGSGHQCGASLISNTWLLTAAHCFWKNKDPTQWIATFGATITPPAVKRNVRKIILHENYHRETNENDIALVQLSTGVEFSNIVQRVCLPDSSIK... | Function: Probable serine protease.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 49410
Sequence Length: 438
Subcellular Location: Membrane
EC: 3.4.21.-
|
Q5QSK2 | MYQPGILGRRKRVCKPWTVALTTTAALLALAVLIGLLVYFLVYEEKTHYYQASFWIPSIKYSSDLSEEQSKLQINLKQKINNEIDVIFQRSSLKHHYVKSQVVNFRPSNDGVKADILIKFQIPRKNADTLRSEADSILNKKLQSSQSFLKRDISLPYLREMNAAQAEHILNSNCGLGMEYPRIARIADGKPAGSNSWPWQSSLQVEGIHLCGASLIGSQWLVTSAHCFDNYKNPKLWTVSFGRTLGNPLTTRKVESIIIHENYAAHKHDDDIAVVKLSSPVLFSENLRTVCLPEATFQVLPKSKVFVTGWGALKANGPFP... | Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 46593
Sequence Length: 417
Subcellular Location: Membrane
EC: 3.4.21.-
|
Q8QFN3 | MVLPPPDKRHVCLTTIVIMTSMAFMDAYLVEQNQGPRKIGVCIIVLVGDICFLIVLRYVAVWVGAEVKTAKRGYAMILWFLYIFVLEIKLYFIFQNYKADKKNLETVARKALTLLLSICVPGLYLVLVALDSMEYIRTFRKKEDLRGRLFWVALDLLDILDIQANLWEPHRTGLPIWAEGLMFFYCYILLLILPCVSLSEISMQGEHIAPQKMMLYPVLSLVTINIVTIFIRAINMVLFQDSRVSTIFIGKNIIAIATKACTFLEYKRQVKEFPQNAIALELQQNSLSHNQTLHSTQGIPHEPSPTSEILDT | Function: May play a role in MAPK signaling.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 35676
Sequence Length: 312
Subcellular Location: Membrane
|
Q9BTD3 | MVLPPPDRRHVCLTTLVIMGSMAVMDAYLVEQNQGPRKIGVCIIVLVGDVCFLLVLRYVAVWVGAEVRTAKRGYAMILWFLYIFVLEIKLYFIFQNYKAARRGAADPVARKALTLLLSVCVPGLFLLLVALDRMEYVRTFRKREDLRGRLFWVALDLLDLLDMQASLWEPPRSGLPLWAEGLTFFYCYMLLLVLPCVALSEVSMQGEHIAPQKMMLYPVLSLATVNVVAVLARAANMALFRDSRVSAIFVGKNVVALATKACTFLEYRRQVRDFPPPALSLELQPPPPQRNSVPPPPPPLHGPPGRPHMSSPTRDPLDT | Function: May play a role in MAPK signaling.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 35814
Sequence Length: 319
Subcellular Location: Membrane
|
Q5ZK32 | MAPKGKAGTKGKKQIFEENRETLRFYLRIILGASAVYAAVNLVVFYPAASAWTWLAFAFSSAVYGASYRSMSSMARPAFADDGSLADGGIDLNMEQGWQSECPHPHEPRHLKDVILLTAMVQVLSCFSLYVWYFWLLAPGRALYLLWVNILGPWFTAESSAPGQEPNEKKQRRTGTPPE | Function: May function as a negative regulator of endoplasmic reticulum-stress induced autophagy.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 19967
Sequence Length: 179
Subcellular Location: Endoplasmic reticulum membrane
|
Q9BTX3 | MAPKGKVGTRGKKQIFEENRETLKFYLRIILGANAIYCLVTLVFFYSSASFWAWLALGFSLAVYGASYHSMSSMARAAFSEDGALMDGGMDLNMEQGMAEHLKDVILLTAIVQVLSCFSLYVWSFWLLAPGRALYLLWVNVLGPWFTADSGTPAPEHNEKRQRRQERRQMKRL | Function: May function as a negative regulator of endoplasmic reticulum-stress induced autophagy.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 19642
Sequence Length: 173
Subcellular Location: Endoplasmic reticulum membrane
|
Q9NX78 | MSPHGDGRGQAQGRAVRVGLRRSGGIRGGVAVFAAVAAVFTFTLPPSVPGGDSGELITAAHELGVAHPPGYPLFTLVAKLAITLFPFGSIAYRVNLLCGLFGAVAASLLFFTVFRLSGSSAGGILAAGVFSFSRLTWQWSIAAEVFSLNNLFVGLLMALTVHFEEAATAKERSKVAKIGAFCCGLSLCNQHTIILYVLCIIPWILFQLLKKKELSLGSLLKLSLYFSAGLLPYVHLPISSYLNHARWTWGDQTTLQGFLTHFLREEYGTFSLAKSEIGSSMSEILLSQVTNMRTELSFNIQALAVCANICLATKDRQNPS... | Function: O-mannosyl-transferase that transfers mannosyl residues to the hydroxyl group of serine or threonine residues of proteins . Specifically glycosylates the IPT/TIG domain of target proteins, such as MET and MST1R/RON . TMEM260-mediated O-mannosylated residues are composed of single mannose glycans that are not ... |
E9PQX1 | MWLQDRIATFFFPKGMMLTTAALMLFFLHLGIFIRDVHNFCITYHYDHMSFHYTVVLMFSQVISICWAAMGSLYAEMTENKYVCFSALTILMLNGAMFFNRLSLEFLAIEYREEHH | Function: Auxiliary component of the CatSper complex, a complex involved in sperm cell hyperactivation.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 13758
Sequence Length: 116
Subcellular Location: Cell projection
|
Q3SYV1 | MNQTDKNQQEIPSYLSDEPPEGSMKDHPQQQPGMLSRVTGGIFSVTKGAVGATIGGVAWIGGKSLEVTKTAVTTVPSMGIGLVKGGVSAVAGGVTAVGSAVVNKVPLTGKKKDKSD | Function: May play a role in bone development.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 11721
Sequence Length: 116
Subcellular Location: Membrane
|
Q5ZLA9 | MNQTDKSHQEVPSYLHDEPPEGSIKDHPQQQPSMLSRVTGGIFSVTKGAVGATIGGVAWIGGKSLEITKTAVTSVPSMGVGLVKGSVSAVAGGVTAVGSAVASKVPLTGKKKDKSD | Function: May be involved in the growth pathway.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 11712
Sequence Length: 116
Subcellular Location: Membrane
|
Q8WUH6 | MNQTDKNQQEIPSYLNDEPPEGSMKDHPQQQPGMLSRVTGGIFSVTKGAVGATIGGVAWIGGKSLEVTKTAVTTVPSMGIGLVKGGVSAVAGGVTAVGSAVVNKVPLTGKKKDKSD | Function: May play a role in bone development.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 11748
Sequence Length: 116
Subcellular Location: Membrane
|
Q2M3C6 | MAVAPSFNMTNPQPAIEGGISEVEIISQQVDEETKSIAPVQLVNFAYRDLPLAAVDLSTAGSQLLSNLDEDYQREGSNWLKPCCGKRAAVWQVFLLSASLNSFLVACVILVVILLTLELLIDIKLLQFSSAFQFAGVIHWISLVILSVFFSETVLRIVVLGIWDYIENKIEVFDGAVIILSLAPMVASTVANGPRSPWDAISLIIMLRIWRVKRVIDAYVLPVKLEMEMVIQQYEKAKVIQDEQLERLTQICQEQGFEIRQLRAHLAQQDLDLAAEREAALQAPHVLSQPRSRFKVLEAGTWDEETAAESVVEELQPSQE... | Function: Voltage-sensor protein present on the post-synaptic side of glutamatergic mossy fibers and granule cells in the cerebellum . Despite the presence of a voltage-sensor segment, does not form a functional ion channel and its precise role remains unclear . Undergoes both rapid and slow structural rearrangements i... |
Q8BZB3 | MALVTSFNMANPQPAIEGGISEVEIISQQVDEETKSIAPVQLVNFAYRDLPLAAVDLSTGGSQLLSNLDEEYQREGSDWLKPCCGKRAAVWQVFLLSASLNSFLVACVILVVILLTLELLIDTKLLQFSNAFQFAGVIHWISLVILSVFFSETVLRIVVLGIWDYIENKIEVFDGAVIILSLAPMVASTVANGPRSPWDAISLIIMFRIWRVKRVIDAYVLPVKLEMEMVTQQYEKAKAIQDEQLERLTQICQEQGFEIRQLRAHLAQQDLDLAAEREAALQAPHVLSQPRSRYKVVEAGTWAEETAAESIVEELRPSQE... | Function: Voltage-sensor protein present on the post-synaptic side of glutamatergic mossy fibers and granule cells in the cerebellum. Despite the presence of a voltage-sensor segment, does not form a functional ion channel and its precise role remains unclear. Undergoes both rapid and slow structural rearrangements in ... |
Q6UXY8 | MSAYYRNNWSEEDPDYPDYSGSQNRTQGYLKTQGYPDVPGPLNNPDYPGTRSNPYSVASRTRPDYPGSLAEPNYPRSLSNPDYSGTRSNAYSAASRTSPDHPTSLPEPDYSEFQSHPYHRASSRQPDYPGSQRNPDFAGSSSSGNYAGSRTHPDHFGSLEPDYPGAQSNSDHPGPRANLNHPGSRKNLEHTSFRINPYADSLGKPDYPGADIQPNSPPFFGEPDYPSAEDNQNLPSTWREPDYSDAENGHDYGSSETPKMTRGVLSRTSSIQPSFRHRSDDPVGSLWGENDYPEGIEMASMEMANSYGHSLPGAPGSGYV... | Function: Probable ion channel.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 114797
Sequence Length: 1006
Subcellular Location: Membrane
|
Q7Z403 | MAQPLAFILDVPETPGDQGQGPSPYDESEVHDSFQQLIQEQSQCTAQEGLELQQREREVTGSSQQTLWRPEGTQSTATLRILASMPSRTIGRSRGAIISQYYNRTVQLRCRSSRPLLGNFVRSAWPSLRLYDLELDPTALEEEEKQSLLVKELQSLAVAQRDHMLRGMPLSLAEKRSLREKSRTPRGKWRGQPGSGGVCSCCGRLRYACVLALHSLGLALLSALQALMPWRYALKRIGGQFGSSVLSYFLFLKTLLAFNALLLLLLVAFIMGPQVAFPPALPGPAPVCTGLELLTGAGCFTHTVMYYGHYSNATLNQPCG... | Function: Probable ion channel.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 90045
Sequence Length: 805
Subcellular Location: Endoplasmic reticulum membrane
|
Q7TN60 | MAQSLALALDVPETTGDEGLEPSPYEESEVHDSFHQLIQEQSLRVAEEGLELLPLGLGRGDQTLPGLEGAPALSSATLRILASMPSRTIGRSRGAIISQYYNRTVRLRRRSSRPLLGNVVPSARPSLRLYDLELDSTILEEDEKRSLLVKELQGLSAAQRDHMVRNMPLSLGEKRCLREKSWSPKGKRRHLQGRSGAFSCCSRLRYTCMLALHSLGLALLSGLYAARPWRYALKQIGGQFGSSVLSYFLFLKTLLAFNALMLLPLLAFLVGVQAAFPPDPAGPVPTFSGLELLTGGGRFTHTVMYYGYYSNSTLSPSCDA... | Function: Probable ion channel.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 90546
Sequence Length: 810
Subcellular Location: Endoplasmic reticulum membrane
|
Q5YCC5 | MSEFGAGAELPGWVTESRSRGEFFSPEESHAAAPAGFLQELPSYRSVLWRRAAAGDVQERWGNLRGIASAERREPQPDGGERGAIPLWELPFSIAEKRDSQQGDIKYSSGWNHWKRTSSKSWKKALKDIKELSSYMQLWRHDIHSIEGKFGTGIQSYFSFLRFLVLLNFLMFILMFSFVTLPAVISNYGIFNSSSTKISPNNTEPYCTVYTPSGNKGLVYFYTYLKDLLTGTGFLEVTVLFYGYYTIDAAWFSVLRYNLPLAYLLTTFAYLALSFVWIIKRSVERFRQHLVDDEDQFQSYCNKVFAGWDFCITDLNAARL... | Function: Probable ion channel.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 84377
Sequence Length: 735
Subcellular Location: Membrane
|
Q7Z402 | MSESSGSALQPGRPSRQPAVHPENLSLDSSCFSSPPVNFLQELPSYRSIARRRTTVHSRDKQSGTLLKPTDSYSSQLEDRIAENLSSHSLRNYALNISEKRRLRDIQETQMKYLSEWDQWKRYSSKSWKRFLEKAREMTTHLELWREDIRSIEGKFGTGIQSYFSFLRFLVLLNLVIFLIIFMLVLLPVLLTKYKITNSSFVLIPFKDMDKQCTVYPVSSSGLIYFYSYIIDLLSGTGFLEETSLFYGHYTIDGVKFQNFTYDLPLAYLLSTIASLALSLLWIVKRSVEGFKINLIRSEEHFQSYCNKIFAGWDFCITNR... | Function: Probable ion channel.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 83502
Sequence Length: 723
Subcellular Location: Membrane
|
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