wanglab/gogpt-training-data huggingface dataset:
Protein: ATP-dependent helicase brm (EC 3.6.4.12) (Homeotic gene regulator) (Protein brahma) (P25439)
Organism: Drosophila melanogaster (Fruit fly)
Function: Transcriptional regulator. Acts as a coactivator, assisting one or more dedicated transcriptional activators of ANTC and BXC homeotic gene clusters. Can counteract the repressive effect of Polycomb protein. ATPase subunit of the Brahma complex, a multiprotein complex which is the equivalent of the yeast SWI/SNF complex and acts by remodeling the chromatin by catalyzing an ATP-dependent alteration in the structure of nucleosomal DNA. This complex can both serve as a transcriptional coactivator or corepressor, depending on the context. In type II neuroblast lineage, as part of the Brm remodeling complex, suppresses the formation of ectopic neuroblasts probably through interaction with erm and HDAC3.
Subcellular location: Nucleus.
Interaction partners:
- Brahma-associated protein of 60 kDa
- Brahma associated protein 111kD
- GH08712p
- Brahma associated protein 155 kDa
- Trithorax group protein osa
- Brahma associated protein 55kD
- Brahma associated protein 170kD
- Polybromo
- Supporter of activation of yellow protein
- Bromodomain containing 7/9
Sequence:
MASPSPANSPMPPPQAPSPMAPPSQSPAPSPHSPYPHQQPGPLQGPPPPGHPGAYGHPMQHGPPGQGPPGHHMPPHHQGMIFSKGPHMGMQMPPTGPNMSPYQTHGMPPNAPTQPCIVSPGGPPGGPPPPERSSQENLHALQRAIDSMEEKGLQEDPRYSQLLAMRATSKHQHLNGNQVNLLRTQITAYRLLARNKPISMQMQQALQAAQQQPPPGPPIGPPGAPGGPPPGSQHAGQPPVPPQQQQQPPPSAGTPPQCSTPPASNPYGPPVPGQKMQVAPPPPHMQQGQPLPPQPPQVGGPPPIQQQQPPQQQQQQSQPPPPEPHQHQLPNGGKPLSMGPSGGQPLIPSSPMQPQVRGTLPGMPPGSQVPQPGGGPQRQVPPAGMPMPKPNRITTVAKPVGLDPITLLQERENRIAARISLRMQELQRLPATMSEDLRLQAAIELRALRVLNFQRQLRMEFVQCTRRDTTLETALNIKLYKRTKRQGLREARATEKLEKQQKLEAERKRRQKHLEFLAAVLQHGKDLREFHRNNKAQLARMNKAVMNHHANAEREQKKEQERIEKERMRRLMAEDEEGYRKLIDQKKDKRLAFLLSQTDEYISNLTQMVKQHKDDQMKKKEEEGKRLIQFKKELLMSGEYIGIDEGSIVADMRVHVVEQCTGKKLTGDDAPMLKHLHRWLNMHPGWDWIDDEEDSCGSNDDHKPKVEEQPTATEDATDKAQATGNDEDAKDLITKAKVEDDEYRTEEQTYYSIAHTIHEKVVEQASIMVNGTLKEYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTISLVTYLMDRKKVMGPYLIIVPLSTLPNWVLEFEKWAPAVGVVSYKGSPQGRRLLQNQMRATKFNVLLTTYEYVIKDKAVLAKIQWKYMIIDEGHRMKNHHCKLTQVLNTHYIAPYRLLLTGTPLQNKLPELWALLNFLLPSIFKSCSTFEQWFNAPFATTGEKVELNEEETILIIRRLHKVLRPFLLRRLKKEVEHQLPDKVEYIIKCDMSALQRVLYKHMQSKGVLLTDGSEKGKHGKGGAKALMNTIVQLRKLCNHPFMFQHIEEKYCDHTGGHGVVSGPDLYRVSGKFELLDRILPKLKATNHRVLLFCQMTQCMTIIEDYLGWRQFGYLRLDGTTKAEDRGELLRKFNAKGSDVFVFLLSTRAGGLGLNLQTADTVVIFDSDWNPHQDLQAQDRAHRIGQRNEVRVLRLMTVNSVEERILAAARYKLNMDEKVIQAGMFDQKSTGSERQQFLQTILHQDDNEEEEENEVPDDEMINMMIARSEEEIEIFKRMDAERKKEDEEIHPGRERLIDESELPDWLTKDDDEVERFHYQYDEDTILGRGSRQRKEVDYTDSLTEKEWLKAIDDGAEFDEEEEEDDSKRKRRKRKNRKEESDDDSLILKRRRRQNLDKRSKKQMHKIMSAVIKHNQDGRTLSEPFMKLPSRQRLPDYYEIIKRPVDIKKILQRIEDCKYADLNELEKDFMQLCQNAQIYNEEASLIYLDSIALQKVFVGARQRITAAADAAAVAAGDNTGEAHGNGGSDNSDNDDDDGGDDGSDDEEIATTSAAAVKMKLKLNKSLASAPATPTQSSSNVSSGAATTSKKQTRRKRSQKKYTISDDDDDDMD
Protein: Multifunctional fusion protein [Includes: Delta-1-pyrroline-5-carboxylate dehydrogenase (P5C dehydrogenase) (L-glutamate gamma-semialdehyde dehydrogenase); L-glutamate gamma-semialdehyde dehydrogenase (EC 1.2.1.88)] (Q9VNX4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Delta-1-pyrroline-5-carboxylate synthase
- Proline dehydrogenase 1, mitochondrial
- Glutamate dehydrogenase, mitochondrial
- Aspartate aminotransferase, cytoplasmic
- Aspartate aminotransferase
- Glutamine synthetase 2 cytoplasmic
- Pyrroline-5-carboxylate reductase
- Ornithine aminotransferase, mitochondrial
- Glutamine synthetase 1, mitochondrial
- Pyrroline-5-carboxylate reductase
Sequence:
MLRMMRSSSSRCSSLQQSLLKSSTRCLGSVIPDLKLKDFPIANEPILGYLKDSKERKALEQALKGTASSCEDIPIVIGGKEYKTPEVRYQVMPHDHQHKLASFYYADKKLIEKAIKTAVETQPKWDRVSIADRLKIWEKAADLMATTYRQDLNAATMLGQSKTAIQAEIDSAAELIDFIRMNAYFLKEVTKYQPISENIKVTKNSLRYRGIDGFIAAVSPFNFTAIGGNLSYTPALMGNGVLWKPSDTAMLSNWIIFKIMREAGVPDGVVNFVPADGPVFGDTITASPHLAGINFTGSVPTFNRLWKQVGNNIDNYVNFPRLTGECGGKNFHFIHASADVESVVTSTIRSAFEYCGQKCSACSRMYVPESLWPQIKEGLVCEAAKLKIGDVQDFSSFTSAVIDDKAFKRITGYIEHAKKSPNLEILAGGTYSDSKGYFVNPTIVLSKDPKDRIMTEEIFGPVLSIYVYKESDLLETMKLVHTSTKFALTGAVFGQDEDFVKCALQEFKMAAGNFYINDKSTGSVVGQQPFGGGRMSGTNDKAGGPHYILRWTSPQSIKETFVPLRDVNYPYMCE
Protein: Nucleotide excision repair protein (Q4U2H8)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSIDCQELLRLFGIPYIVAPMEAEAQCAFLNATDLTHGTITDDSDIWLFGGRTVYKNFFAQNKHVMEFRAEQIEQTFNCNRGKLIQLACLVGSDYTTGIHGIGAVTALEILASFSGQDANGPGICNQSVLQTLIKFRDWWQAHKCSNLPPGSSARLALRKKLKNIELHEGFPSGAVVEAYLAPTIDDNRDAFSWGTPDVESIREFTRKSFGWTTSKTDDILMPVMKKINEKKIQGSIRNYFTAKSALRVQQPHVSKRVQLAIDKMSGKIDETPEKPKKVTRTRRAKAAPPTDDDLAIADVATKAARPKRGKRKAAPESVVLDGELPSTSQSIPKPEKCPRIPSSVEVIPQREKDLEQMRLNKAKAAEILKNSAKANRK
Protein: Rhomboid-related protein 4 (RRP4) (EC 3.4.21.105) (Rhomboid domain-containing protein 1) (mRHBDD1) (Rhomboid-like protein 4) (Q8BHC7)
Organism: Mus musculus (Mouse)
Function: Intramembrane-cleaving serine protease that cleaves single transmembrane or multi-pass membrane proteins in the hydrophobic plane of the membrane, luminal loops and juxtamembrane regions. Involved in regulated intramembrane proteolysis and the subsequent release of functional polypeptides from their membrane anchors. Functional component of endoplasmic reticulum-associated degradation (ERAD) for misfolded membrane proteins. Required for the degradation process of some specific misfolded endoplasmic reticulum (ER) luminal proteins. Participates in the transfer of misfolded proteins from the ER to the cytosol, where they are destroyed by the proteasome in a ubiquitin-dependent manner. Functions in BIK, MPZ, PKD1, PTCRA, RHO, STEAP3 and TRAC processing. Involved in the regulation of exosomal secretion; inhibits the TSAP6-mediated secretion pathway. Involved in the regulation of apoptosis; modulates BIK-mediated apoptotic activity. Also plays a role in the regulation of spermatogenesis; inhibits apoptotic activity in spermatogonia.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:22795130}; Multi-pass membrane protein {ECO:0000305}. Mitochondrion membrane {ECO:0000250|UniProtKB:Q8TEB9}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Transitional endoplasmic reticulum ATPase
- Rhomboid-related protein 1
Sequence:
MQRRTRGINTGLLLLLSQVFQIGINNIPPVTLATLAVNVWFFLNPWKPLYHSCISVEKCYQQKDWQRLLLSPLHHGDDWHLYFNMVSMLWKGVKLERRLGSRWFAYVIATFSLLTGVVYLLLQFTVAELLNQPDFKRNCAVGFSGVLFALKVLSNHYCPGGFVNILGFPVPNRFACWAELVAIHFCTPGTSFAGHLAGILVGLMYTQGPLKKIMDTCAGIFISHAGPSGQQNHFNNAGPSGYQNHYADGRPVTYDATYRNYDVYTAGLSEEEQLERALRASIWDRGNTRNGPMPYGFRLPPEEMRRQRLHRFDGQ
Protein: Tubulin beta chain (Q5SU16)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
Sequence:
MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGTYHGDSDLQLDRISVYYNEATGGKYVPRAILVDLEPGTMDSVRSGPFGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVVRKEAESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYPDRIMNTFSVVPSPKVSDTVVEPYNATLSVHQLVENTDETYCIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCLRFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRALTVPELTQQVFDAKNMMAACDPRHGRYLTVAAVFRGRMSMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRGLKMAVTFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVSEYQQYQDATAEEEEDFGEEAEEEA
Protein: CYtochrome P450 family (G5ECD0)
Organism: Caenorhabditis elegans
Interaction partners:
- Fatty acid synthase
Sequence:
MFFILLFVSIISFLTARQFLKAKRLPPGPFSLPLIGNAHQVGYQLWRTGGVTNMLNHFRKEYGDIFTLWLGPIPHVNITNYELSHEVFVKNSTKYADKHVSPMIDYVRKGNGVFFSNGDKWQELRRFSMLTMRNMGMGRDLMEEKILSELDARCAEINEKSIDGTTVLQVNEFFDLTVGSIINNMLLGFRFDERTKSRFLTMKHMFDEGMDKMTPLFFTLPVWALQKFLAKDFNSIIKDQFEIIDYVSVDAIKRSRDFMNGDYEIDPNNVEDIVDAFLLKMKQNPKSDVYDENNLKMLITDLWITGQETTTTTLVSAFIQFLNNPQVMDTVQKELIKVTNGGSRQLSLRDKTETPYLNATIAEVQRHASILNINFWRINNEPTVIGGHPVDSGCLIASQLSALHTNEKIFENPEKFNPERFIRNENLMQQTIPFGIGKRSCLGESLARAELYLIIGNLLLRYNFESSGKMPSTRETVPFGFAKRCEAFDMKVTKI
Protein: Uncharacterized isomerase YHI9 (EC 5.1.-.-) (P38765)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Interaction partners:
- Uncharacterized protein YMR130W
- Ornithine decarboxylase
Sequence:
MTLMVPFKQVDVFTEKPFMGNPVAVINFLEIDENEVSQEELQAIANWTNLSETTFLFKPSDKKYDYKLRIFTPRSELPFAGHPTIGSCKAFLEFTKNTTATSLVQECKIGAVPITINEGLISFKAPMADYESISSEMIADYEKAIGLKFIKPPALLHTGPEWIVALVEDAETCFNANPNFAMLAHQTKQNDHVGIILAGPKKEAAIKNSYEMRAFAPVINVYEDPVCGSGSVALARYLQEVYKFEKTTDITISEGGRLKRNGLMLASIKKEADNSTSYYIAGHATTVIDGKIKV
Protein: Fgr3p (Q5A645)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Fgr51p
Sequence:
MARLRRVRGPKLSTDKVSIVHEMGRKYKHAKILVTIRLDPTRLKSISRSPSNGTEMENSNETTNEKDSNAETLPPMSSGLSETATPKNNDAGEDISDSEISSMDNELMDFLTEHSVLVTPGRPLIPNQPETAPTTEKNQEKKPSGKLSSVSPKKQPNSSIPDSPSVDETYKILPRNVSPIVRNELHSIEDEFAPVDRMVFSLRDPLGGGRINLPVKSTSCIHFQCFDYENFCLFNKISTATKEITRRNLVQSNRAYLARIQQQVNQQPTVSSSFPFSSQNSQFPNPTSNPNVSNKLPVALPGNNGTHNYLVLPTFHSNFTLNNRINNNNIYNSNSGHSSQSGEITSLYNRLGEPYIKVINNPKPEHSSRFVTPCHKFPMYKCPICDTQFPLSELCISDGFNYFIRATPKEIDRVELLIGLDKYRLIDDNRKTPAPTGEKKEQSAEVIVLTSDEEDEDDRNPVVSQTPVKTKKRFNFYERAQELLHQETDNEIHYGDGESWDDPIVLD
Protein: Fibronectin type III and SPRY domain-containing protein 1 (Q1LY10)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: May be involved in microtubule organization and stabilization.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Cleavage furrow {ECO:0000250}. Note=Cell-cycle-dependent association with the centrosome. Colocalizes with a subpopulation of microtubules. Does not associate with microtubules during mitosis but reassociates with microtubules during cytokinesis. Localizes to the central portions of a small subset of microtubules in interphase cells and a subpopulation of microtubules in the cleavage furrow, not present in the mitotic spindle (By similarity). {ECO:0000250}.
Interaction partners:
- ADAM metallopeptidase domain 10b.
Sequence:
MDDQKESLRKIITTLALKNEEIQNFICSLKQSLENLEANSNRVQEDLESEFSSLHSVLDDLKEGMVTRIKQERASRTYELQSQLGACTKALESSEELLEFANQTLCSSENDSFTQAAKDIKDSVTMAPAFRLSLKAKASDSMNHMMVDFTHERNLLQSITFLPVPATPEIHVADCQVFDNTVTVVWTLPEPDSKIDHYILEHRKTNHEGPPRAREDYPWMVVEGIKETEYTLTGVRFDTRYMTFRVKACNKAVAGEFSEPVTLETHAFVFKLDASSSHQNLKVEDLSVEWDSSGGKVAVQDIRKEKNRTNSPMHSPARTAMMSPKRAPSARVGRDRFTAESYTVLGDTMIDAGQHYWEVRFDKESKAFAAGVALRSLGRFDQLGKSNASWCIHLNNWLQQSLTAKHNNKARTLDCSIPDRIGIYCNYEEGTLSFYNSRNKTLLHTFRTKFQQPVIPAFMVWNGSFSVQTGLQVPSIVLSGQKRNSNTSSSNASLT
Protein: Uncharacterized protein (Q583H7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MEPRTVRAYLEQRVQHQYFDVIPSRWRPLLTRLAKLTQTLQRDGALAVGNNKAAAIRSDFDLANALLEEEHEIYREGLTYLRGRNNGEECANTAALRRFLHGMLSCIAAKEISITHWKNCLTSVSPDTLRVYCHMCVAHPHVQKDDTARICLLYSQPA
Protein: Vacuolar protein sorting-associated protein 1 (P21576)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Essential for protein sorting in meiotic cell division of S.cerevisiae; it binds microtubules. Could also be involved in microtubule-associated motility. Necessary for membrane protein retention in a late Golgi compartment. Interacts with the MVP1 protein.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:8344247}.
Interaction partners:
- Reduced viability upon starvation protein 167
- Clathrin heavy chain
- Protein SLA2
- Autophagy-related protein 36
- Mitochondrial fission 1 protein
- Peroxisomal membrane protein PMP27
- Reduced viability upon starvation protein 161
- Syntaxin VAM3
- SEC14 cytosolic factor
- Sorting nexin MVP1
Sequence:
MDEHLISTINKLQDALAPLGGGSQSPIDLPQITVVGSQSSGKSSVLENIVGRDFLPRGTGIVTRRPLVLQLINRRPKKSEHAKVNQTANELIDLNINDDDKKKDESGKHQNEGQSEDNKEEWGEFLHLPGKKFYNFDEIRKEIVKETDKVTGANSGISSVPINLRIYSPHVLTLTLVDLPGLTKVPVGDQPPDIERQIKDMLLKYISKPNAIILSVNAANTDLANSDGLKLAREVDPEGTRTIGVLTKVDLMDQGTDVIDILAGRVIPLRYGYIPVINRGQKDIEHKKTIREALENERKFFENHPSYSSKAHYCGTPYLAKKLNSILLHHIRQTLPEIKAKIEATLKKYQNELINLGPETMDSASSVVLSMITDFSNEYAGILDGEAKELSSQELSGGARISYVFHETFKNGVDSLDPFDQIKDSDIRTIMYNSSGSAPSLFVGTEAFEVLVKQQIRRFEEPSLRLVTLVFDELVRMLKQIISQPKYSRYPALREAISNQFIQFLKDATIPTNEFVVDIIKAEQTYINTAHPDLLKGSQAMVMVEEKLHPRQVAVDPKTGKPLPTQPSSSKAPVMEEKSGFFGGFFSTKNKKKLAALESPPPVLKATGQMTERETMETEVIKLLISSYFSIVKRTIADIIPKALMLKLIVKSKTDIQKVLLEKLYGKQDIEELTKENDITIQRRKECKKMVEILRNASQIVSSV
Protein: Similar to insulin-like growth factor II (Q862E7)
Organism: Bos taurus (Bovine)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
VEECCFRSCDLALLETYCATPAKSERDVSASTTVLPDDVTAYPVGKFFQYDIWKQSTQRLRRGLPAFLRARRGRTLAKELEALREAKSHRPLIALPTQDPATHG
Protein: Contig An01c0450, genomic contig (EC 1.10.3.2) (A2QB61)
Organism: Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513)
Interaction partners:
Sequence:
MYPFQFGLALLASVFSLLSWANGSNLHVRATGNTVRFNVTLTWEDWAPAGIPRKMILMNGQFPGPVLQLRQGDDVEFLVTNHLPTNTTVHFHGIEQLDTPWSDGVPGLSQRPIAPGDSFLYKWRATNYGSYFYHAHTRGQICDGLYGAIYILPSESVEKPFRLITNNTSELQAMQAAERRTKPIMLSDWRFLTSEELWSAEEATGLDAICINAVLINGKGSISCPGQQAFNELASAEQKQLIGNLSLTDTGCLPPTLVSAQGIFSHNYSAMPPSMFYGCRPGNGGTERLLVDPSTTYVSYDLISAAGVSMLTFSIDEHPMYVYAIDGRYIEPTLVDAVTVANGNRYSVLVKLDKPAGNYTVRAANSGINQVINATAVLTYNTPIKTQKGSSVPSIDIHGSLVSSNYTLLNETTIMPFPAETPSSKVDATHILRIGHYNASYRWTEGNSSFPLSLEAASPLLFYPSTAKPDLTVKTLNGTWVDLIFHVNGQIQPPHPIHKHSNKFYVIGQGNGAWNYSSVAEAMQYIPENFNLKTPQIRDTFITPAAATEDTWLAIRYHVVNPGAWLLHCHIQVHLSGGMALALLDGVDEWPVIPKEYQLSDS
Protein: Transmembrane matrix receptor MUP-4 (Muscle-positioning protein 4) (Q21281)
Organism: Caenorhabditis elegans
Function: Required for junctional attachments between hypodermis and muscle, and between the apical epithelial surface and the cuticular matrix. Essential for enclosure of the embryo by the hypodermis, hypodermal integrity, embryo elongation, and maintenance of hypodermal morphology in fully elongated embryos.
Subcellular location: Cell junction, hemidesmosome {ECO:0000269|PubMed:11470827}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:11470827}. Cell membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. Note=Detected in intermediate filaments and hemidesmosomes. {ECO:0000255}.
Interaction partners:
- Signal transducer and activator of transcription b
- Fibronectin type-III domain-containing protein
- Intermediate filament protein ifb-1
- Microtubule-actin cross-linking factor 1
- Leucine-rich repeat-containing protein let-4
- NOmpA Homolog
- Leucine-rich repeat-containing protein let-4
Sequence:
MRWVPLVLLPLIASAATTYQHRQTYSSLQCRVNDPLSCNQAKSEVCVFVNGQYRCECPVGVSRLADGRCLVVNECARPSLNACHKDAQCVDLAEGYTCRCNSGFADTSPDKVNKPGRQCQKTTNECGAKQTYGVDCDENAACVDTPEGFQCVCQPGYADVSTSISKLPGRKCVESVNECTNGEADCSNNADCFDRADGYECKCRPGFVDASPNVDKYPGRVCNKPKAPEYYGQQSRQPQCSEGSGCGPNEECRFNTAGEKVCQCRRGSVQQSNGVCKVFSQCEQANECDRNAFCSNTYDGPKCQCKDGFLDVSPDPVRLPGRKCQQVRNECADGSHDCSHQAACQDTPTGYICSCNSNCIDVSSRYNLPPGRKCSVAANQCSDKSLNSCDENADCVQLPDGYTCKCFAGYVDVSSNANLPPGRVCTLSTACPAQPTDLVFLIDGSGSIGSYVFQTEVLRFLAEFTELFDIAPQKTRVSVVQYSDQIRHEFGLDNYSDRKSLQNAIRNIEYLTGLTRTGAAIEHVANEAFSERRGARPVGQVSRVAIVITDGRSQDNVTRPSDNARRQDIQLFAVGVTNHVLDAELEEISGSKDRTFHVSGFEDLNTRLRSAIQRVACPHQNNEDTYNKGPCDPSNHNGCDRSLNQVCQQKNGKFVCACPAGFDIHPVTKVCGGDICNPEIATSCPDPEICEKTPFGNWRCTCPADLGWRDRLTGVCKIGEKPVQTSESNDECSPNDVHSCPANSKCEKGAGGEFICKCDAGFQRNGRTNKCEAPGTCDPRMPDSCDARKKEKCLPDGRGAFACMCDRHHKRHPVTDICLIDECAAGVADCDPNAKCTDTDESYICTCNEGFLDKSPEQNKKPGRVCSKQRNECLDGTHNCSMNADCIDLPDGFLCRCKEDFVDISPNPNAFGGIDCRALVNECLITGGHNCHEHAICIDTRDSYKCQCKEGYVDHDELRNPGRTCKKLNQICESGKHECDKNARCVEKGANDYECVCNAGFIDKSPLTHRPGRKCVEPICSDDSKHDCHSAAICEENDSVPEKYTCKCRDGYLDVGAVMGGGKSGRECKELVNECLSASLNSCDAAATCIDLDDGYTCKCPLGSKDESPVPKLPGRSCKGLVNECNIPHLNNCSHFATCIDLEEGYECKCKPEYHDQKPEQPGTECKFIINECLAENLNDCSPNAMCIDKIDGYDCKCKAPFQDEMPSNPGRICRFDECADPKDNDCDKHALCIDTDDSYTCQCKEGFFDEISDPKKPGRVCIGLVIEPQNQSEDPTTPDPNTIKCGNGLCHLDLGEVCVGGATCSCRPGESRDNEKEKCVPTTSIPLVVRVMEYDGEPIQYRTDYSKPDTQAHIEIVDAVKKSVGKIIGKTDVAPRFVTTDVNYITNPKVQNSEWDKGLLGNVSVHLAGKEEVDKCRFYEQFAEIVREMGGRVDRIKLSDDADLDPCKKEEEKKGIPCGNTFCSIELGEECIAGKICGCPKGQKRKDANSPCRAVESWNLPLYVIRDGHEKITYSPSLSNPLNDDHKDLVSRFESGVAQSYDKTPLKGAFVTAEVNEIENPESRKKSWDTGILYNFTSHFVKGSVAEPASVFTDLIDYIQKRNDFEVGKSKLFISPEQLNPFSNCYHSDCHPDAICKEVGKGYTCTCPDGFRDLNPSRPGRNCLSYRGVNECEKPELNECSPHARCIDLDYLYKCECIRPYVNSAVGDALPGSVCSIDYCQDVNYCPLNSTCVNVDEQARCDCKPGFVDLRKSGHLSEAGLGESICRRQSDIDECALGLHNCSAAAICIDKKIGYECQCQEGYEDGNPSQPGRICAASLCGLCNGHGDCIHDALSSNVTCACLDGYTGQFCETAPSNLPLILMTLLALLFLLLTLLCCLYMCARCRCFGARGRSEGSASGQEILGSDYYTIPRAKLARPLYGDEMGDDHAGALAAYLDDGASISSDGSIEEIERRVTTDVTTREVRTTTVRDDDGNIISQSQTISHGNPHETDTEQYGMISSDHYKTSASEAMDAAMSTSASGAAYNQSSGAMMSSASGHKSAYNQGYASDSEDSDAGHAVYDRTTRTNQSHDFEPGADPRTGTERSKREFVTTTKAEEVNYF
Protein: Katanin p60 ATPase-containing subunit A1 (Katanin p60 subunit A1) (EC 5.6.1.1) (Lipotransin) (p60 katanin) (Q9WV86)
Organism: Mus musculus (Mouse)
Function: Catalytic subunit of a complex which severs microtubules in an ATP-dependent manner. Microtubule severing may promote rapid reorganization of cellular microtubule arrays and the release of microtubules from the centrosome following nucleation. Microtubule release from the mitotic spindle poles may allow depolymerization of the microtubule end proximal to the spindle pole, leading to poleward microtubule flux and poleward motion of chromosome. The function in regulating microtubule dynamics at spindle poles seems to depend on the association of the katanin KATNA1:KATNB1 complex with ASPM which recruits it to microtubules. Reversely KATNA1:KATNB1 can enhance ASPM blocking activity on microtubule minus-end growth. Microtubule release within the cell body of neurons may be required for their transport into neuronal processes by microtubule-dependent motor proteins. This transport is required for axonal growth.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03023}. Midbody {ECO:0000255|HAMAP-Rule:MF_03023}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000255|HAMAP-Rule:MF_03023}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000255|HAMAP-Rule:MF_03023}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:O75449}. Note=Predominantly cytoplasmic. Localized diffusely in the cytoplasm during the interphase. During metaphase is localized throughout the cell and more widely dispersed than the microtubules. In anaphase and telophase is localized at the midbody region. Also localized to the interphase centrosome and the mitotic spindle poles. Enhanced recruitment to the mitotic spindle poles requires microtubules and interaction with KATNB1 (By similarity). Localizes within the cytoplasm, partially overlapping with microtubules, in interphase and to the mitotic spindle and spindle poles during mitosis (By similarity). {ECO:0000250|UniProtKB:O75449, ECO:0000255|HAMAP-Rule:MF_03023}.
Interaction partners:
- Katanin p80 WD40 repeat-containing subunit B1
- KATNB1-like protein 1
- Kelch-like protein 42
- Abnormal spindle-like microcephaly-associated protein homolog
- Cullin-3
- Kelch-like protein 13
- Kelch-like protein 12
- Speckle-type POZ protein
- Gigaxonin
- Kelch-like protein 21
Sequence:
MSLQMIVENVKLAREYALLGNYDSAMVYYQGVLDQMNKYLYSVKDTHLRQKWQQVWQEINVEAKQVKDIMKTLESFKLDITSLQAAQHELPAAEGEVWSLPVPVERRPLPGPRKRQSSQHSDPKPHSNRPSTVVRAHRPSPQNLHNDRGKAVRSREKKEQSKGREEKNKLPAAVTEPEANKFDGTGYDKDLVEALERDIISQNPNVRWYDIADLVEAKKLLQEAVVLPMWMPEFFKGIRRPWKGVLMVGPPGTGKTLLAKAVATECKTTFFNVSSSTLTSKYRGESEKLVRLLFEMARFYSPATIFIDEIDSICSRRGTSEEHEASRRMKAELLVQMDGVGGASENDDPSKMVMVLAATNFPWDIDEALRRRLEKRIYIPLPSAKGREELLRISLRELELADDVNLASIAENMEGYSGADITNVCRDASLMAMRRRIEGLTPEEIRNLSREAMHMPTTMEDFEMALKKISKSVSAADIERYEKWIVEFGSC
Protein: Biosynthetic arginine decarboxylase (ADC) (EC 4.1.1.19) (P21170)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the biosynthesis of agmatine from arginine.
Subcellular location: Periplasm {ECO:0000269|PubMed:2198270}.
Interaction partners:
- Agmatinase
- Biodegradative arginine decarboxylase
- Arginine N-succinyltransferase
- Large ribosomal subunit protein bL34
- Small ribosomal subunit protein bS20
- Argininosuccinate lyase
- Uncharacterized protein YqgB
- S-adenosylmethionine decarboxylase proenzyme
Sequence:
MSDDMSMGLPSSAGEHGVLRSMQEVAMSSQEASKMLRTYNIAWWGNNYYDVNELGHISVCPDPDVPEARVDLAQLVKTREAQGQRLPALFCFPQILQHRLRSINAAFKRARESYGYNGDYFLVYPIKVNQHRRVIESLIHSGEPLGLEAGSKAELMAVLAHAGMTRSVIVCNGYKDREYIRLALIGEKMGHKVYLVIEKMSEIAIVLDEAERLNVVPRLGVRARLASQGSGKWQSSGGEKSKFGLAATQVLQLVETLREAGRLDSLQLLHFHLGSQMANIRDIATGVRESARFYVELHKLGVNIQCFDVGGGLGVDYEGTRSQSDCSVNYGLNEYANNIIWAIGDACEENGLPHPTVITESGRAVTAHHTVLVSNIIGVERNEYTVPTAPAEDAPRALQSMWETWQEMHEPGTRRSLREWLHDSQMDLHDIHIGYSSGIFSLQERAWAEQLYLSMCHEVQKQLDPQNRAHRPIIDELQERMADKMYVNFSLFQSMPDAWGIDQLFPVLPLEGLDQVPERRAVLLDITCDSDGAIDHYIDGDGIATTMPMPEYDPENPPMLGFFMVGAYQEILGNMHNLFGDTEAVDVFVFPDGSVEVELSDEGDTVADMLQYVQLDPKTLLTQFRDQVKKTDLDAELQQQFLEEFEAGLYGYTYLEDE
Protein: Protein unc-93 homolog A (HmUnc-93A) (Unc-93A) (Q86WB7)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000269|PubMed:12381271}; Multi-pass membrane protein {ECO:0000269|PubMed:12381271}.
Interaction partners:
Sequence:
MDRSLRNVLVVSFGFLLLFTAYGGLQSLQSSLYSEEGLGVTALSTLYGGMLLSSMFLPPLLIERLGCKGTIILSMCGYVAFSVGNFFASWYTLIPTSILLGLGAAPLWSAQCTYLTITGNTHAEKAGKRGKDMVNQYFGIFFLIFQSSGVWGNLISSLVFGQTPSQETLPEEQLTSCGASDCLMATTTTNSTQRPSQQLVYTLLGIYTGSGVLAVLMIAAFLQPIRDVQRESEGEKKSVPFWSTLLSTFKLYRDKRLCLLILLPLYSGLQQGFLSSEYTRSYVTCTLGIQFVGYVMICFSATDALCSVLYGKVSQYTGRAVLYVLGAVTHVSCMIALLLWRPRADHLAVFFVFSGLWGVADAVWQTQNNALYGVLFEKSKEAAFANYRLWEALGFVIAFGYSMFLCVHVKLYILLGVLSLTMVAYGLVECVESKNPIRPHAPGQVNQAEDEEIQTKM
Protein: Perilipin-3 (Cargo selection protein TIP47) (Mannose-6-phosphate receptor-binding protein 1) (Q9DBG5)
Organism: Mus musculus (Mouse)
Function: Structural component of lipid droplets, which is required for the formation and maintenance of lipid storage droplets. Required for the transport of mannose 6-phosphate receptors (MPR) from endosomes to the trans-Golgi network.
Subcellular location: Lipid droplet {ECO:0000250|UniProtKB:O60664}. Endosome membrane {ECO:0000250|UniProtKB:O60664}; Peripheral membrane protein {ECO:0000250|UniProtKB:O60664}; Cytoplasmic side {ECO:0000250|UniProtKB:O60664}. Cytoplasm {ECO:0000250|UniProtKB:O60664}. Note=Membrane associated on endosomes. Detected in the envelope and the core of lipid bodies and in lipid sails. {ECO:0000250|UniProtKB:O60664}.
Interaction partners:
- Heat shock cognate 71 kDa protein
- Cation-independent mannose-6-phosphate receptor
- 1-acylglycerol-3-phosphate O-acyltransferase ABHD5
- Hormone-sensitive lipase
- Rab9 effector protein with kelch motifs
- Vesicle-associated membrane protein 3
- Rho-related BTB domain-containing protein 3
- Ras-related protein Rab-18
- Cation-dependent mannose-6-phosphate receptor
- Patatin-like phospholipase domain-containing protein 2
Sequence:
MSSNGTDAPAEAQAAMEEPVVQPSVVDRVAGLPLISSTYGMVSAAYTSTKENYPHVRTVCDVAEKGVKTLTTAAVSTAQPILSKLEPQIATASEYAHRGLDRLQESLPILQQPTEKVLADTKELVSSTVSGAQEMVSSSVSSAKETVATRVTGAVDVTLGAVQNSVDKTKSAMTSGVQSVMGSRVGQMVISGVDRVLVKSEAWADNRLPLTEAELALIATPPEDSDMASLQQQRQEQNYFVRLGSLSERLRNHAYEHSLGKLQNARQKAQETLQQLTSVLGLMESVKQGVDQRLGEGQEKLHQMWLSWNQKTPQDAEKDPAKPEQVEARALSMFRDITQQLQSMCVALGASIQGLPSHVREQAQQARSQVNDLQATFSGIHSFQDLSAGVLAQTRERIARAREALDNTVEYVAQNTPAMWLVGPFAPGITEKTPEGK
Protein: Pre-mRNA-processing factor 19 (EC 2.3.2.27) (Plant U-box protein 72) (OsPUB72) (RING-type E3 ubiquitin transferase PRP19) (U-box domain-containing protein 72) (Q9AV81)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Probable ubiquitin-protein ligase which is mainly involved pre-mRNA splicing and DNA repair.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q94BR4}.
Interaction partners:
- Os03g0339100 protein
- Os04g0348300 protein
- Os03g0387000 protein
- Os02g0602500 protein
- Os06g0106100 protein.
- Os02g0831300 protein.
- Os05g0495100 protein
- SNU114 homolog
- Peptidyl-prolyl cis-trans isomerase
- Os01g0582400 protein
Sequence:
MICAISGEVPDEPVVSKKSGLLFERRLVERYIEDHGKCPVTKEELTMDDIVAVKTNKVVKPRQLQAASIPGLLGMFQNEWDAIMLSSFALEQQLHTARQELSHALYQHDAACRVIARLKKERDEARALLAQAERQIPASMAGAAPTAVVSNGKRAFEDEVGPDGKKIRPGINPVMIDELTECNTMLSAHRKKRQVPPTLASIDAIERYTQISSHPLHKTNKPGILSMDIHPSKDIIATGGIDTNAVLFDRPSGQILCTLTGHSKKITSLKFVPRDELFVTGSADKTVKIWQGSEEGNYNCIHTLKDHTAEVEAVTVHATQKYFVTASKDNTWCFYDIPSGSCLTQVGESSGQEGYTSASFHPDGLILGTGTTEAVVKIWDVKTQSNVAKFEGHVGPVTAMSFSENGYFLATAALDGVKLWDLRKLRNFRTISPYDSDTPTNSVEFDFSGSYLAVGGSDTRVYQVANVKLEWNLVKTLPDLSGTGKVTNVKFGTDAKYIAVGSMDRNLRIFGHPGEDDQMDDAKPSEE