wanglab/gogpt-training-data huggingface dataset:
Protein: Histone-lysine N-methyltransferase, H3 lysine-36 specific (EC 2.1.1.359) (Lysine N-methyltransferase 3) (SET domain-containing protein 2) (P46995)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Histone methyltransferase that trimethylates histone H3 'Lys-36' forming H3K36me3. Involved in transcription elongation as well as in transcription repression. The methyltransferase activity requires the recruitment to the RNA polymerase II, which is CTK1 dependent.
Subcellular location: Nucleus. Chromosome {ECO:0000305}.
Interaction partners:
- Histone H3
- DNA-directed RNA polymerase II subunit RPB1
- Histone-lysine N-methyltransferase, H3 lysine-79 specific
- Histone H4
- Protein NAM8
- Histone-lysine N-methyltransferase, H3 lysine-4 specific
- Chromatin modification-related protein EAF3
- E3 ubiquitin-protein ligase BRE1
- Histone H2A.2
- Transcription elongation factor SPT6
Sequence:
MSKNQSVSASEDEKEILNNNAEGHKPQRLFDQEPDLTEEALTKFENLDDCIYANKRIGTFKNNDFMECDCYEEFSDGVNHACDEDSDCINRLTLIECVNDLCSSCGNDCQNQRFQKKQYAPIAIFKTKHKGYGVRAEQDIEANQFIYEYKGEVIEEMEFRDRLIDYDQRHFKHFYFMMLQNGEFIDATIKGSLARFCNHSCSPNAYVNKWVVKDKLRMGIFAQRKILKGEEITFDYNVDRYGAQAQKCYCEEPNCIGFLGGKTQTDAASLLPQNIADALGVTVSMEKKWLKLKKLSGEPIIKNENENINIEFLQSLEVQPIDSPVDVTKIMSVLLQQDNKIIASKLLKRLFTIDDDSLRHQAIKLHGYTCFSKMLKLFITEQPQVDGKGNETEEDDIKFIKGILDFLLELPKTTRNGIESSQIDNVVKTLPAKFPFLKPNCDELLEKWSKFETYKRITKKDINVAASKMIDLRRVRLPPGWEIIHENGRPLYYNAEQKTKLHYPPSGSSKVFSSRSNTQVNSPSSSGIPKTPGALDSKKHKLSDEEYERKKQKRLEYERIALERAKQEELESLKQKLKLENERKSVLEDIIAEANKQKELQKEEAKKLVEAKEAKRLKRKTVSQSQRLEHNWNKFFASFVPNLIKKNPQSKQFDHENIKQCAKDIVKILTTKELKKDSSRAPPDDLTKGKRHKVKEFINSYMDKIILKKKQKKALALSSASTRMSSPPPSTSS
Protein: Zinc-regulated GTPase metalloprotein activator 1C (EC 3.6.5.-) (Cobalamin synthase W domain-containing protein 3) (COBW domain-containing protein 3) (Q5JTY5)
Organism: Homo sapiens (Human)
Function: Zinc chaperone that directly transfers zinc cofactor to target metalloproteins, thereby activating them. Catalyzes zinc insertion into the active site of methionine aminopeptidase METAP1, which function to cleave the initiator methionine from polypeptides during or after protein translation. Mechanistically, the N-terminal psi-PxLVp motif binds to the C6H2-type zinc finger of inactive form of METAP1. After formation of the docked complex, zinc is transferred from the CXCC motif in the GTPase domain of ZNG1C to the zinc binding site in the peptidase domain of METAP1 in a process requiring GTP hydrolysis. GTP/GDP exchange is required for release of active METAP1.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q8VEH6}.
Interaction partners:
Sequence:
MLPAVGSVDEEEDPAEEDCPELVPIETTQSEEEEKSGLGAKIPVTIITGYLGAGKTTLLNYILTEQHSKRVAVILNESGEGSALEKSLAVSQGGELYEEWLELRNGCLCCSVKDNGLRAIENLMQKKGKFDDILLETTGLADPGAVASMFWVDAELGSDIYLDGIITIVDSKYGLKHLTEEKPDGLINEATRQVALADIILINKTDLVPEEDVKKLRTTIRSINGLGQILETQRSRVDLSNVLDLHAFDSLSGISLQKKLQHVPGTQPHLDQSIVTITFEVPGNAKEEHLNMFIQNLLWEKNVRNKDNHCMEVIRLKGLVSIKDKSQQVIVQGVHELYDLEETPVSWKDDTERTNRLVLIGRNLDKDILKQLFIATVTETEKQWTTHFKEDQVCT
Protein: Lipocalin Can f 6.0101 (Allergen Can f 6) (allergen Can f 6.0101) (H2B3G5)
Organism: Canis lupus familiaris (Dog) (Canis familiaris)
Subcellular location: Secreted {ECO:0000269|PubMed:23464525, ECO:0000305|PubMed:22515174}.
Interaction partners:
Sequence:
MKLLLLCLGLILVHAHEEENDVVKGNFDISKISGDWYSILLASDIKEKIEENGSMRVFVKDIEVLSNSSLIFTMHTKVNGKCTKISLICNKTEKDGEYDVVHDGYNLFRIIETAYEDYIIFHLNNVNQEQEFQLMELYGRKPDVSPKVKEKFVRYCQGMEIPKENILDLTQVDRCLQARQSEAAQVSSAE
Protein: GH03118p (Q95U66)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MEVGDHSVEVRLPGGGHVEGSPFLLKAYSAEKVIVTDIRAGVVNKSVSFGINASQAGAGNLEIIVAVNGKNVPNFVQSEGNARFKVNFKPTEAATHSLSVRFNGHPVPGSPFSCHIAAAAASPSMGLPRAMAMGECLKQAAVKMDNTFELEGFDGVEPQIFVTSPSGDNEHCQLSQHDGGSYSASFRPTTVGRHLISVTANDQHINGSPFSCNVFDVSRVSISGLEQQYGPANLGVPVTFSVDAAGAGEGTLELVVSTDSSTVKAEVVACARGLYDVTFVPQSTEPHYVNITFNEVAVDGSPFRVDIQQHTQHIQIGSLAAIDFPADDQIVEIFSPDQKSVPYSINRQTAEFRTHMTGNYTLRFIDRETRQHIGSRTLCVFDPTLVKITEVSEAFCHRPASIGVSLNEAGQGDLSALVRCGATEVPHTIRGPSKTGVYEIVYQPTRVAPHKISILFNEVPISLKPLEINVLPASAGKEISVSGLGLYQSRVGKTTSFAIDTVKRPAREFDVVVSGPGGQALPVRCYQTKNGHLQAEFTINKPGQCVIEVLHQSKPLPGSPFTCESFDSSKVSTQGVTKEPLALHSPNSFTVRTDNAGTAELEAFAISPSNQSIPVLISEQSDGVYNVEFVPSQPGNYKLTLMYGGETIPSSPLNFTASSSGVRNDARAAGHGLEVCHRNKEASFVVYCPIAPNVQIERLDEYGERIEPKIKALGNNEWRISYTILSVGKYEIRASCPNRGSLPGSPWHISCVESNKVTPVGGWGTLVDHDGRLILPARIIFDVENAGPGKLVCSIDGIEIPVDKLVDGKMCLNITGENLAAGEHDLDLTWSGLTITQCPRSAFVTGQQAADKVQLMGRGLAAAQAGEAAHFTIDASNAPAGRPEVILTSQDNTSLPVSLAQPRPSENIWLASYTPLKSTTGTLNLSVKWNGRLVKGCPLTVAVGSSMDASKVIVSGEGLRHGIVGKDIKSWIDTRRAGPGELTAHCAGVRKVAYCELYDHGDATFTLNIKPQESGRHILTIKYGGQNVPGSPFALKVAGAPDASKVRVYGPGIEHGVLATFQSRFICDTRGAGAGQLTVRVRGPKGAFRVEMQRESQKDRTILCKYDPTEPGDYRVEVKWAGEFVPGSPFPVMIFDTEEELRRYLQGI
Protein: WAS/WASL-interacting protein family member 2 (WASP-interacting protein-related protein) (WIP- and CR16-homologous protein) (WIP-related protein) (Q8TF74)
Organism: Homo sapiens (Human)
Function: Plays an active role in the formation of cell surface protrusions downstream of activated PDGFB receptors. Plays an important role in actin-microspike formation through cooperation with WASL. May cooperate with WASP and WASL to induce mobilization and reorganization of the actin filament system.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:11829459, ECO:0000269|PubMed:12213210}. Note=Localized to stress fibers and bundles of actin filaments.
Interaction partners:
- Actin nucleation-promoting factor WASL
- Actin nucleation-promoting factor WAS
- Cytoplasmic protein NCK2
- SH2/SH3 adapter protein NCK1
- WAS/WASL-interacting protein family member 3
- WAS/WASL-interacting protein family member 1
- Growth factor receptor-bound protein 2
- Cell division control protein 6 homolog
- Actin-binding protein WASF1
- Unconventional myosin-If
Sequence:
MPIPPPPPPPPGPPPPPTFHQANTEQPKLSRDEQRGRGALLQDICKGTKLKKVTNINDRSAPILEKPKGSSGGYGSGGAALQPKGGLFQGGVLKLRPVGAKDGSENLAGKPALQIPSSRAAAPRPPVSAASGRPQDDTDSSRASLPELPRMQRPSLPDLSRPNTTSSTGMKHSSSAPPPPPPGRRANAPPTPLPMHSSKAPAYNREKPLPPTPGQRLHPGREGPPAPPPVKPPPSPVNIRTGPSGQSLAPPPPPYRQPPGVPNGPSSPTNESAPELPQRHNSLHRKTPGPVRGLAPPPPTSASPSLLSNRPPPPARDPPSRGAAPPPPPPVIRNGARDAPPPPPPYRMHGSEPPSRGKPPPPPSRTPAGPPPPPPPPLRNGHRDSITTVRSFLDDFESKYSFHPVEDFPAPEEYKHFQRIYPSKTNRAARGAPPLPPILR
Protein: Protein GMH1 homolog (Meiotically up-regulated gene 16 protein) (P87155)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Has a role in meiosis.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein {ECO:0000269|PubMed:16823372}.
Interaction partners:
Sequence:
MSRSFRNGFRLLKLSQMDFERAWWDMANLFRAPRRVYRSITLRKQNINRYGREDFSFIVLFSCMIVISALLWALFYMNTPKGYVTTITFMLFVDFGAVGVIMATMYYFIAKRFLMKSNDTILSSTDYQLEWNYCFDVHCNSFFPSFVLLYVIQLFLLPVITRDNFISLFMGNTLYLVALCYYSYLTFIGYQILPFLKNTHALLLPIPMFFIMWALSLLGFNVPKHVVDVYFGKSA
Protein: Cyclin-B2-3 (G2/mitotic-specific cyclin-B2-3) (CycB2;3) (Q9LDM4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Cyclin-dependent kinase B1-2
- Cell division cycle 20.4, cofactor of APC complex
- Cyclin-dependent kinase B1-1
- Cyclin-dependent kinase B2-1
- Cyclin-dependent kinases regulatory subunit 1
- Cell division cycle 20.3, cofactor of APC complex
- Wee1-like protein kinase
- Cell division cycle 20.5, cofactor of APC complex
- Cyclin-dependent kinase B2-2
- Cell division cycle 20.2, cofactor of APC complex
Sequence:
MVRSDENSLGLIGSMSLQGGGVVGKIKTTATTGPTRRALSTINKNITEAPSYPYAVNKRSVSERDGICNKPPVHRPVTRKFAAQLADHKPHIRDEETKKPDSVSSEEPETIIIDVDESDKEGGDSNEPMFVQHTEAMLEEIEQMEKEIEMEDADKEEEPVIDIDACDKNNPLAAVEYIHDMHTFYKNFEKLSCVPPNYMDNQQDLNERMRGILIDWLIEVHYKFELMEETLYLTINVIDRFLAVHQIVRKKLQLVGVTALLLACKYEEVSVPVVDDLILISDKAYSRREVLDMEKLMANTLQFNFSLPTPYVFMKRFLKAAQSDKKLEILSFFMIELCLVEYEMLEYLPSKLAASAIYTAQCTLKGFEEWSKTCEFHTGYNEKQLLACARKMVAFHHKAGTGKLTGVHRKYNTSKFCHAARTEPAGFLI
Protein: Bromodomain PHD finger transcription factor (A0A8I6ALT2)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MRGRRGRPPKQPAAPAAERCAPAPPPPPPPPPPPPPPPPPPPASGPIGGLRSRHRGSSRGRWAAAQAEVAPKTRLSSPRGGGRRKQPPPPPASASSASGPGRGGRGGGGGRTGGGGGHLARTTSARRAVNKVVYDDHESEDDDEEEDMVSEEDEEEEEDGDAEETQDSEDDEEDDMEEDDDDSDYPEEMEDDDDDASYCTESSFRSHSTYSSTPGRRKPRVHRPRSPILEEKDIPPLEFPKSSEDLMVPNEHIMNVIAIYEVVRNFGNVLRLSPFCFEDFCAALVSQEQCTLMAEMHVALLKAVLREEDTSNTTFGPADLKDSVNSTLYFIDGMTWPEVLRVYCESDKEYHHVLPYQEAEDYPYGPVESKIKVLQFLVDQFLTTNIAREELMSEGVIQYDDHCRVCHKLGDLLCCETCSAVYHLECVKPPLEEVPEDEWQCEVCVAHKVPGVTDCVAEVQKNKPYVRHEPIGYDRSRRKYWFLNRRLIIEEDTENENEKKVWYYSTKVQLAELIDCLDKDYWEAELCRVLEDIREEMQQHMDVTEDLTNKARGSNKSFLAAANEEILDSLRIKRGEDIDCDQNPEDTEKDKNEGENDSSKGAEKSREESEDQSPDKDADGKVLEEEPGQGKPEGDFRLDKSNGEVSESPGTGKGTSGSTRIITRLRNPESKLSQLKSQQVAAAAHEANKLFKEGKEVLVVNSQGEVSRLSTKKEVVMKGNINNYFKLGQEGKYRVYHNQYSTNSFALNKHQHREDHDKRRHLAHKFCLTPAGEFKWNGSVHGSKVLTISTLRLTITQLESNIPSSFLHPNWASHRANWIKAVQMCSKPREFALALAILECAVKPVVMLPIWRESLGHTRLHRMTSIEREEKEKVKKKEKKQEEEETMQQATWVKYTFPVRHQVWKQKGEEYRVTGYGGWSWISKTHVYRFLPKLPGNTNVNYRKPLEGVKNNMDENKDESDKRKSPRSPKKMKTECDSEKGEARDADSTAGATAGTMELSKLPEKEEHDVKELLDPDNDKPFKEEPMEIDDSVKTESHMNSEESAQVDVVNVSEGFHLRTSYKKKTKSSKLDGLLERRIRQFTLEEKQRLEKLKLESGVKGAGKPPTGAVKSSSEPPVSTKADEGHQGDLLRQEQRSTPSQAGTADLGLGASQSDPLVLGISPPSLSTGKPDPKGQVLDDVSIQSPGPACQGQNSVESDLDARISEATSKGLELSQTKTKVTDSLTDDSKPTSADEGSTLICKSKKPLPQDDCSTAVSSSSKSTLPAPVPKSPRDRDARAFPKAMDLDGRLGGDSEYNSTLENNSGTMYMRDSSEEDMVVQNSNDTTSKRFITPDQGMESTEPTKCQLVSKSTENCDNRLQGKVTEANGKKLGQHQKPEERAVNRCADQVSLRHSADRKNSEARESEKRGQKANKFQINGKDSKAKGYLKGPGMKDVSDGKVMSGAVEPKVNNINKVIPGNIKSLAGKESAVKPFVNGDIIMEEFSEQNTSETNSYSLSSSDAKGNHQDGLHTLPSTKDSASTQVIIPPAPCPDRNSLNQVEDMETEGPEVKKVTPSPITTGEDSNLGKDVMDENGLPSSKDENVNGESQRKTVITEVTTMTSTVATESKTVIKVAKGDKQTVVSSTENCARSTVTTTTTTVTKLSTPSPDSDVDTVSVKEQSKTVVTTTVTDSLSTAGSTLVTSMTVSREYSTRDRVKLMKFSRPKKTRSGTALPSYRKFVTKSSKKSIFVLPNDDLKKLARKGGIREVPCFNYNAKPALDIWPYPSPRPTFGITWRYRLQTVKSLAGVSLMLRLLWASLRWDDMAAKAPPGGGSTRTETSETEITTTEIIKRRDVGPYGIRSEYCIRKIICPIGVPEAPKETPTPQRKGLRSSALRPKRPETPKQTGPVVIESWVAEEELELWEIRAFAERVEKEKAQAVEQQTKKRLEQQKPAVIAASTTSPTNSTSSTVSPAQKVMVAPLSGSVTPGTKMVLATKVGSPATVTFQQNKNFHQTFATWVKQGQSNSGVVQVQQKVLGIIPSTAGPSQQTFTSFQPRTATVTIRPNTSASAGTTTTSQVITGPQIRPGMTVIRAPLQQPALGKAVIRTPVTMQPGAPQQVVTQIIRGQPVSTAISASSTASSAPVQKGLTPGAAAGTLQPSAPHSPRPQQGQVKLTMAQLTQLTQGHGGNQGLTVVIQGQGQTTGQLQLIPQGMTVLPGPGQQLMQAAMPNGTVQRFLFTPLSTPVTAVSSSSSSSSTNATATGSGEQKQSKLSPQTQVQPATTLAPTQSSSVSPAEAQPQPAQPAAQPQPQPQPPAQPEVQTQPAASSHVPSETQPSQAQSSKPLVATQCQPQSSVQGQSPVRVQSPPLTRIRPSTPSQVTPGQQPQVQTTASQPIPIPPPTSLQAPSQGQPQSQPQVQSSTQTLSSGQTLNQVTVPSPSRPQPQTQQPQPQVIAVPQLQQVQVLSQIQSQVVAQIQAQQGGAPQQIKLQLPVHVQQNSAAQAQHAQSVLTVQAASVREQLQRVQQLRDQQQKKKQQIEMEREHTLQASNQSEIIQKQVVMKHNAVIEHLKQKKTMTPAEREENQRMIVCNQVMKYILDKIDKEEKQAAKKRKREESVEQKRSKQNASKLSALLFKHKEQLKAEILKKRALLDKELQMQVQEELKRDLKMKREREMAQVVQANAAAGPTPSVPAPVPAPAPAPAAPPAPPSPPPSTHSLPPAGHPTAPLPVTSQKRKREEEKDSKSKKKKMISTTSKEAKKDTRLYCICKTPYDESKFYIGCDLCTNWYHGDCVGITEKEAKKMDVYICNDCKRAQEGSSEELYCICRTPYDESQFYIGCDRCQNWFHGRCVGILQSEAELIDEYVCPQCQSTEDAMTVLTPLTEKDYEGLKRVLRSLQAHKMAWPFLEPVDPNDAPDYYGVIKEPMDLATMEERIQKRYYEKLTEFVADMTKIFDNCRYYNPSDSPFYQCAEVLESFFVQKLKGFKASRL
Protein: Uncharacterized protein (Q57YB6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Telomerase-associated protein, putative
- Uncharacterized protein
Sequence:
MFCFFQNRWESGLGAHLTEELISSAFSDFAPYAGAEQQQTRFVRRQSDGTTTRVAYGEDGGWSVSMGNPYAGGISFATTPDLLCDMQLRIPLKLARDVVEQNSERGIIGSADNCEVLPVSRISLTPITTPYDSRSPFQYSVPPPLGPTGCFGMVELLYSYVTHVYGAGLRVGPLSLRATASPGGMPSIDNSYVSALGQTACLVDGSWCAPLSAFPSCNLTVALQHPFMAVEGDTLAAICLESSAPKTPEGQGCNNFRLLVVQTLATSNRQNKQNPSDSHSHSFSSVLRGDKNWRELGTLVAVQKSFRNQRFRLSAAAMIHDRELDYETAALADVTAIFSRPTVLRLGFNRARRVAMGIATEILNGLTLTLGVHYTAGDLRFGLEAAL
Protein: Sex hormone-binding globulin (SHBG) (Sex steroid-binding protein) (SBP) (Testis-specific androgen-binding protein) (ABP) (P08689)
Organism: Rattus norvegicus (Rat)
Function: Functions as an androgen transport protein, but may also be involved in receptor mediated processes. Each dimer binds one molecule of steroid. Specific for 5-alpha-dihydrotestosterone, testosterone, and 17-beta-estradiol. Regulates the plasma metabolic clearance rate of steroid hormones by controlling their plasma concentration (By similarity).
Subcellular location: Secreted. Note=In testis, it is synthesized by the Sertoli cells, secreted into the lumen of the seminiferous tubule and transported to the epididymis.
Interaction partners:
- Muellerian-inhibiting factor
- Corticosteroid-binding globulin
- Albumin
- Insulin-2
- Insulin-1
- Aromatase
- Insulin-like growth factor 1
- Estrogen receptor
- Androgen receptor
- Prolactin
Sequence:
MEKGEVASLRCRLLLLLLLLTLPPTHQGRTLRHIDPIQSAQDSPAKYLSNGPGQEPVTVLTIDLTKISKPSSSFEFRTWDPEGVIFYGDTNTEDDWFMLGLRDGQLEIQLHNLWARLTVGFGPRLNDGRWHPVELKMNGDSLLLWVDGKEMLCLRQVSASLADHPQLSMRIALGGLLLPTSKLRFPLVPALDGCIRRDIWLGHQAQLSTSARTSLGNCDVDLQPGLFFPPGTHAEFSLQDIPQPHTDPWTFSLELGFKLVDGAGRLLTLGTGTNSSWLTLHLQDQTVVLSSEAEPKLALPLAVGLPLQLKLDVFKVALSQGPKMEVLSTSLLRLASLWRLWSHPQGHLSLGALPGEDSSASFCLSDLWVQGQRLDIDKALSRSQDIWTHSCPQSPSNDTHTSH
Protein: cellulase (EC 3.2.1.4) (Q9L3J2)
Organism: Acetivibrio thermocellus (Hungateiclostridium thermocellum) (Clostridium thermocellum)
Interaction partners:
Sequence:
MGQKHFKRSLLSVLTISALIISCLFSFIFVNADDTSEEPALEGLSIHYMDGTLDVKYQSMRPYIIIHNNSGMDVDMADLRVRYYYEKEGVTEEVLTCFYTAIGADKIFAEFHPELGYAEIGFTSDAGIIKSGGNSGQLQLVLKKISNGYYDQSNDYSYDPSYTDYAEYDKITLYYKGKLVWGKEGPPPPPEPTPPPNNDDWLHVEGNLIKDAQGNTVYLTGINWFGFETDGANGFHGLNKCNLEDSLDLMAKLGFNILRIPISAEIILQWKNGERVETSFVNTYENPRLDGLSSLEILDYTINHMKKNGMKAMIDMHSSTKDSYQENLWYNKDITMEEFIEAWKWIVERYKDDDTVIAVDLKNEPHGKYSGPNIAKWDDSNDPNNWKRAAEIIAEEILAINPNLLIVVEGVEAYPMEGYDYTNCGEFTTYCNWWGGNLRGVADHPVVISAPDKLVYSVHDYGPDIYMQPWFKKDFDINTLYEECWYPNWYYIVEQNIAPMLIGEWGGKLINENNRKWLECLATFIAEKKLHHTFWAFNPNSADTGGLMLEDWKTVDEEKYAIIVPTLWKKGLDHVIPLGGITEDTFKYGDVNGDFAVNSNDLTLIKRYVLKNIDEFPSPHGLKAADVDGNEKITSSDAALVKRYVLRAITSFPVEENQNE
Protein: Cell surface protein (Q4WLV5)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Interaction partners:
Sequence:
MSGLMHKVKDAVTGHHHDSTHTSNTTGTHHGTHQTTADTTTTNHGPHHSKLANKLDPRVDSDGDHHPGSHATITRGPDGEKVAHTSTHGPRPIEPGHGHSAATGTTNTTHGPHSSKAANKLDPRVDSDADNRARHEAIGGAHGPHSSNIANKVDPRVDSDRDNHAHTGAGATTTTGAYASGAHNTYGTTSTNAGPHNSNMLNKVDPRIDSDMDNRARHETMGGAHGPHGSSIANKMDPRVDSDMDNRGAYGTTTTHGTGAGNTFGTHTSSNAGPHNSSMMNKVDPRVDSDMDNRARHQALGGAQGPHSSNLANKIDPRVDSDMDNRGTTHGTTGHAYGSGAGMNTSMGTGMGTHTSTNAGPHNSNLMNKVDPRVDSNRDNRARHETLASNSYNTPGATTHTAGPHNSNLMNKIDPPVDSDLDNRGTHTLGTQRGI
Protein: DnaJ heat shock protein family (Hsp40) member B1 (D3ZUU5)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Heat shock cognate 71 kDa protein
- Heat shock 70 kDa protein 4
- Heat shock cognate 71 kDa protein
- Heat shock protein 105 kDa
- Heat shock 70 kDa protein 1A
- Stress-induced-phosphoprotein 1
- DnaJ homolog subfamily C member 3
- Endoplasmic reticulum chaperone BiP
- Heat shock transcription factor 1
- MAP kinase-activated protein kinase 5
Sequence:
MGKDYYQTLGLARGASDDEIKRAYRRQALRYHPDKNKEPGAEEKFKEIAEAYDVLSDPRKREIFDRYGEEGLKGGGPSGGSSGGANGTSFSYTFHGDPHAMFAEFFGGRNPFDTFFGQRNGEEGMDIDDPFSSFPMGMGGFTNMNFGRSRPTQEPTRKKQDPPVTHDLRVSLEEIYSGCTKKMKISHKRLNPDGKSIRNEDKILTIEVKRGWKEGTKITFPKEGDQTSNNIPADIVFVLKDKPHNIFKRDGSDVIYPARISLREALCGCTVNVPTLDKASPSPKHLRNVETLLSNLKSSSLIGSPSHPEPSWSRFFPYSCLHSSRTEPGTFPELQISRPFHWLHTAGGPREGFCSAECFPQNILQSFKVAH
Protein: Cytochrome P450 4e3 (EC 1.14.-.-) (CYPIVE3) (Q9VL92)
Organism: Drosophila melanogaster (Fruit fly)
Function: May be involved in the metabolism of insect hormones and in the breakdown of synthetic insecticides.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. Microsome membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MWLAVLALLVLPLITLVYFERKASQRRQLLKEFNGPTPVPILGNANRIGKNPAEILSTFFDWWYDYGKDNFLFWIGYSSHIVMTNPKQLEYILNSQQLIQKSTIYDLLHPWLGHGLLTSFGSKWHKHRKMITPSFHFNILQDFHEVMNENSAKFMTQLKKASAGDTIIDFQEHANYLTLDVICDTAMGVPINAMEQRDSSIVQAFRDMCYNINMRAFHPFKRSNRVFSLTPEFSAYQKTLKTLQDFTYDIIEKRVYALQNGGSKEDHDPSLPRKKMAFLDTLLSSTIDGRPLTRQEIYEEVSTFMFEGHDTTTSGVSFSVYLLSRHPDVQRKLYREQCEVMGHDMNRSVSFQEIAKMKYLDLFIKEAQRVYPSVPFIGRYCDKDYDINGSIVPKGTTLNLALILLGYNDRIFKDPHHFRPERFEEEKPAPFEYLPFSAGPRNCIGQKFALLELKTVISKVVRSFEVLPAVDELVSTDGRLNTYLGLAPDEKLKREAGRHKYDPILSAVLTLKSDNGLHLRLRERRS
Protein: Solute carrier family 25 member 35 (Q5SWT3)
Organism: Mus musculus (Mouse)
Subcellular location: Mitochondrion inner membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
Sequence:
MDFLMSGVAACGACVFTNPLEVVKTRMQLQGELQAPGTYQRHYRNVFHAFFTIGKVDGLAALQKGLGPALLYQFLMNGIRLGTYGLAESRGYLHTNEGTHSPVRSAAAGALAGVMGAYLGSPIYMVKTHLQAQAASEIAVGHQYKHQGMFQALTEIGQKHGLVGLWRGAVGGLPRVVIGSSTQLCTFSSIKDLLSQWEIFPPQSWKVALAAAMVSGVAIVVAMTPFDVASTRLYNQPTDTRGKGLMYRGILDALLQTARTEGFFGMYKGIGASYFRLGPHTILSLFFWDQLRSFYNTYAK
Protein: BBSome complex member bbs-7 (Bardet-Biedl syndrome 7 protein homolog) (Osmotic avoidance abnormal protein 12) (Q9XW70)
Organism: Caenorhabditis elegans
Function: Component of the BBSome complex (By similarity). The BBSome complex is thought to function as a coat complex required for sorting of specific membrane proteins to the primary cilia (By similarity). The BBSome complex is required for ciliogenesis but is dispensable for centriolar satellite function (By similarity). Required for proper BBSome complex assembly and its ciliary localization (By similarity). Required for cilia biogenesis and both the assembly and movement of intraflagellar transport proteins along the ciliary axoneme. Plays a role in the removal of degraded mechanosensory receptors within the cilia. Plays a role in guanylyl cyclase localization in the ring-like structures at the base of the finger compartment in AFD sensory neurons. In ciliated sensory neurons, required for the sensation of nitric oxide and avoidance of NO-producing organisms like P.aeruginosa.
Subcellular location: Cell projection, cilium {ECO:0000269|PubMed:15231740}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:15231740}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:15231740}. Note=Moves in anterograde and retrograde directions along the ciliary axonemes. {ECO:0000269|PubMed:15231740}.
Interaction partners:
- BBSome complex member bbs-5
- BBSome complex member bbs-2
- BBSome complex member BBS1
- BBSome complex member bbs-4
- Protein pthb1 homolog
- Tetratricopeptide repeat protein 8
- Intraflagellar transport protein 88 homolog
- WD_REPEATS_REGION domain-containing protein
- Intraflagellar transport protein 52 C-terminal domain-containing protein
- WD repeat-containing protein dyf-2
Sequence:
MQNYSRTDFAQVGTTNRGCMRVIPSDKEKEHDLIVVGGQNGSLICLSRKSNDTTIIFKTQPGYPVQSLALGGPASSKKKDKIFVASQNTVRGVNRKGKTFFSMETNMAEVANRMFVRGLDVVLTGRKSYSRYHDTVDSNSYLCTEDIHDVVSLVFEEAWGSREYTSILACGNSTLQIIEGNNFAYDVRLDSVPFTVSLFMGDGGHTKLLVLYGTKTGRLGLVSVPQGGGKILWEIDTTSGACVTTIVCFNVTGGQFPDIIVGKEDGLIEIYVIDETDHAHLFGTFSCDESITGISCGHVSSKSEIDIIICTFTGWLFSLAKTSRPMIENLPVAANFSVKMQQLRSEVEELQTKVNEERLRYEEITKRQGSGTGSTFFHSFQVHENFEYSAAHGAYNLTIELVIPIDFVVVQSQLPIRLMEVEKNASVVSEVRQDALNPWPLLASYRCQANVCRLELRVQANEGDSGVINLYVCPKVMPKCAQITTHYIKALSSHMRSHDFDLYRPMNTLQFTGNFSIAEAHAWLHNLLPNVPSKCPPADTITNNYQCSVNGGTQLQVVYSKGSAVFRSDCMTTICIIRDKVSEQTMKMQIRVEVACELNQDSVNHCLKLIDPKITSMLNIEKNKLYAAALKELESNNDDVFSFLSAANAKILKDHDAIYEKSEGVSIEDSGVLAILENLMVARGKLTGRSSKGRGDAIRDLISTDYSLENMQTLFKNAMND
Protein: Beta-centractin (Actin-related protein 1B) (ARP1B) (P42025)
Organism: Homo sapiens (Human)
Function: Component of a multi-subunit complex involved in microtubule based vesicle motility. It is associated with the centrosome.
Subcellular location: Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome.
Interaction partners:
- Dynactin subunit 2
- Dynactin subunit 4
- Dynactin subunit 1
- Actin-related protein 10
- Dynactin subunit 5
- Dynactin subunit 6
- Dynactin subunit 3
- Alpha-centractin
- F-actin-capping protein subunit beta
- F-actin-capping protein subunit alpha-2
Sequence:
MESYDIIANQPVVIDNGSGVIKAGFAGDQIPKYCFPNYVGRPKHMRVMAGALEGDLFIGPKAEEHRGLLTIRYPMEHGVVRDWNDMERIWQYVYSKDQLQTFSEEHPVLLTEAPLNPSKNREKAAEVFFETFNVPALFISMQAVLSLYATGRTTGVVLDSGDGVTHAVPIYEGFAMPHSIMRVDIAGRDVSRYLRLLLRKEGVDFHTSAEFEVVRTIKERACYLSINPQKDEALETEKVQYTLPDGSTLDVGPARFRAPELLFQPDLVGDESEGLHEVVAFAIHKSDMDLRRTLFANIVLSGGSTLFKGFGDRLLSEVKKLAPKDIKIKISAPQERLYSTWIGGSILASLDTFKKMWVSKKEYEEDGSRAIHRKTF
Protein: Actin, cytoplasmic 1 (EC 3.6.4.-) (Beta-actin) [Cleaved into: Actin, cytoplasmic 1, N-terminally processed] (P60706)
Organism: Gallus gallus (Chicken)
Function: Actin is a highly conserved protein that polymerizes to produce filaments that form cross-linked networks in the cytoplasm of cells. Actin exists in both monomeric (G-actin) and polymeric (F-actin) forms, both forms playing key functions, such as cell motility and contraction. In addition to their role in the cytoplasmic cytoskeleton, G- and F-actin also localize in the nucleus, and regulate gene transcription and motility and repair of damaged DNA.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P60710}. Nucleus {ECO:0000250|UniProtKB:O93400}.
Interaction partners:
- Profilin
- Cofilin-2
- Vinculin
- Profilin
- Profilin
- Ezrin
- Hematopoietic lineage cell-specific protein
- Talin-1
- Filamin B
- Uncharacterized protein.
Sequence:
MDDDIAALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVTHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAASSSSLEKSYELPDGQVITIGNERFRCPEALFQPSFLGMESCGIHETTFNSIMKCDVDIRKDLYANTVLSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIVHRKCF
Protein: Protein tyrosine phosphatase, receptor type, O (Q62797)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
Sequence:
MGHLPRERRGGRRLLPLLGLFVLLKIVSTFHVTVRDDNNIVVSLEASDVVSPTSVYVVRVAGESKNYFFEFEESNGTLPPPVVFKATYHGLYYIISLVVVSGNVVTKPSRSITVLTKPLPVTSVSIYDYKPSPETGVLFEIHYPEKYNVFSRVNISYWEGKDFRTMLYKDFLKGKTVFNHWLPGICYSNITFQLVSEATFNKSTLVECSGVSHEPKQHRTAPYPPRNISVRFVNLNKNNWEEPSGSFPEDSFIKPQDAIGRDRPFHFPEETPETPASNASSGWPDPNGTEYESTSQPYWWDSASAAPENEEDFVSVLPADYDTEATLGRTEKPTADPFSAFPVQMTLSWLPPKPPTAFDGFNILIEREGNFTDYLTVDEEAHEFVAELKEPGKYRLSVTTFSSSGACETRKSQSAKSLSFYISPTGEWIEELTEKPQHVSVHVLSSTTALLSWTSSQENYNSTIVSVVSLTCQKQKESQRLEKQYCTQVNSSKPVIENLVPGAQYQVVMYLRKGPLIGPPSDPVTFAIVPTGIKDLMLYPLGPTAVVLSWTRPYLGVFRKYVVEMFYFNPTTMTSEWTTYYEIAATVSLTSSVRIANLLPAWYYNFRVTMVTWGDPELSCCDSSTISFITAPVAPEITSVEYFNSLLYISWTYGDATTDLSHSRMLHWMVVAEGRRKIKKSVTRNVMTAILSLPPGDIYNLSVTACTERGSNTSMLRLVKLEPAPPKSLFAVNKTQTSVTLLWVEEGVADFFEVLCQKLGSGHDGKLQEPVAVSSHVVTISSLLPATAYNCSVTSFSHDSPSVPTFIAVSTMVTEVNPNVVVISVLAILSILLIGLLLVTLVILRKKHLQMARECGAGTFVNFASLEREGKLPYSWRRSVFTFLTLLPSCLWTDYLLAFYINPWSKNGLKKRKLTNPVQLDDFDSYIKDMAKDSDYKFSLQFEELKLIGLDIPHFAADLPLNRCKNRYTNILPYDFSRVRLVSMNEEEGADYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSRIIVMLTQCNEKRRVKCDHYWPFTEEPIAYGDITVEMVSEEEQEDWASRHFRINYADEAQDVMHFNYTAWPDHGVPPANAAESILQFVYTVRQQATKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCVQLMWLKKKQQFCISDVIYENVSKS
Protein: D-alanyl-D-alanine carboxypeptidase DacC (DD-carboxypeptidase) (DD-peptidase) (EC 3.4.16.4) (Penicillin-binding protein 6) (PBP-6) (P08506)
Organism: Escherichia coli (strain K12)
Function: Removes C-terminal D-alanyl residues from sugar-peptide cell wall precursors.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:3330754}; Peripheral membrane protein {ECO:0000269|PubMed:3330754}; Periplasmic side {ECO:0000269|PubMed:3330754}. Note=N-terminus lies in the periplasmic space, targeted there by the C-terminal amphiphilic helix (PMID:3330754).
Interaction partners:
- D-alanyl-D-alanine carboxypeptidase DacB
- Putative D-alanyl-D-alanine carboxypeptidase
- Penicillin-binding protein 1A
- Peptidoglycan D,D-transpeptidase MrdA
- D-alanyl-D-alanine carboxypeptidase DacD
- D-alanyl-D-alanine carboxypeptidase DacA
- Penicillin-binding protein 1B
- Probable L,D-transpeptidase YcbB
- Peptidoglycan D,D-transpeptidase FtsI
- Penicillin-binding protein 1C
Sequence:
MTQYSSLLRGLAAGSAFLFLFAPTAFAAEQTVEAPSVDARAWILMDYASGKVLAEGNADEKLDPASLTKIMTSYVVGQALKADKIKLTDMVTVGKDAWATGNPALRGSSVMFLKPGDQVSVADLNKGVIIQSGNDACIALADYVAGSQESFIGLMNGYAKKLGLTNTTFQTVHGLDAPGQFSTARDMALLGKALIHDVPEEYAIHKEKEFTFNKIRQPNRNRLLWSSNLNVDGMKTGTTAGAGYNLVASATQGDMRLISVVLGAKTDRIRFNESEKLLTWGFRFFETVTPIKPDATFVTQRVWFGDKSEVNLGAGEAGSVTIPRGQLKNLKASYTLTEPQLTAPLKKGQVVGTIDFQLNGKSIEQRPLIVMENVEEGGFFGRVWDFVMMKFHQWFGSWFS