wanglab/gogpt-training-data huggingface dataset:
Protein: S-phase kinase associated protein 2 (A0A8I6AMP0)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MHRKHLQEIPDQSSNVTTSFTWGWDSSKTSELLSGMGVSALEKEEVDSENIPHGLLSNLGHPQSPPRKRLKSKGSDKDFVIIRRPKLNRENFPGVSWDSLPDELLLGIFSCLCLPELLRVSGVCKRWYRLSLDESLWQSLDLAGKNLHPDVTVRLLSRGVVAFRCPRSFMEQPLGESFSSFRVQHMDLSNSVINVSNLHGILSECSKLQNLSLEGLQLSDPIVTTLAQNENLVRLNLCGCSGFSESAVATLLSSCSRLDELNLSWCFDFTEKHVQAAVAHLPDTLTQLNLSGYRKNLQKTVHWLVVECGKDGKGRLSSSTLDPRGLTFFPFGCSDSIMLKNDCFPEFFQLNYLQHLSLSRCYDIIPETLLELGEIPTLKTLQVFGIVPDGTLQLLREALPRLQINCAYFTSIARPTMDNKKNPEIWGIKCRLTLQKPSL
Protein: Vimentin (P08670)
Organism: Homo sapiens (Human)
Function: Vimentins are class-III intermediate filaments found in various non-epithelial cells, especially mesenchymal cells. Vimentin is attached to the nucleus, endoplasmic reticulum, and mitochondria, either laterally or terminally.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:19386766, ECO:0000269|PubMed:21465480, ECO:0000269|PubMed:29496907}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:18408015, ECO:0000269|PubMed:29496907}. Nucleus matrix {ECO:0000250|UniProtKB:P31000}. Cell membrane {ECO:0000250|UniProtKB:P20152}.
Interaction partners:
- Desmin
- HLA class II histocompatibility antigen, DR alpha chain
- HLA class II histocompatibility antigen, DRB1 beta chain
- Caspase-7
- Plectin
- Zinc finger E-box-binding homeobox 1
- Gigaxonin
- Caspase-3
- Neurofilament medium polypeptide
- Zinc finger E-box-binding homeobox 2
Sequence:
MSTRSVSSSSYRRMFGGPGTASRPSSSRSYVTTSTRTYSLGSALRPSTSRSLYASSPGGVYATRSSAVRLRSSVPGVRLLQDSVDFSLADAINTEFKNTRTNEKVELQELNDRFANYIDKVRFLEQQNKILLAELEQLKGQGKSRLGDLYEEEMRELRRQVDQLTNDKARVEVERDNLAEDIMRLREKLQEEMLQREEAENTLQSFRQDVDNASLARLDLERKVESLQEEIAFLKKLHEEEIQELQAQIQEQHVQIDVDVSKPDLTAALRDVRQQYESVAAKNLQEAEEWYKSKFADLSEAANRNNDALRQAKQESTEYRRQVQSLTCEVDALKGTNESLERQMREMEENFAVEAANYQDTIGRLQDEIQNMKEEMARHLREYQDLLNVKMALDIEIATYRKLLEGEESRISLPLPNFSSLNLRETNLDSLPLVDTHSKRTLLIKTVETRDGQVINETSQHHDDLE
Protein: Cellulose synthase-like protein D2 (AtCslD2) (EC 2.4.1.-) (Q9LFL0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Thought to be a Golgi-localized beta-glycan synthase that polymerize the backbones of noncellulosic polysaccharides (hemicelluloses) of plant cell wall.
Subcellular location: Golgi apparatus membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Glucomannan 4-beta-mannosyltransferase 7
- Xyloglucan 6-xylosyltransferase 1
- Glucomannan 4-beta-mannosyltransferase 9
- Xyloglucan 6-xylosyltransferase 2
- Xyloglucan glycosyltransferase 4
- Glucomannan 4-beta-mannosyltransferase 2
- At1g29770
- Probable glucomannan 4-beta-mannosyltransferase 3
- Probable arabinosyltransferase ARAD1
- Probable arabinosyltransferase ARAD2
Sequence:
MASNKHFDKSRSNLSNNSDIQEPGRPPAGHSVKFAQRTSSGRYINYSRDDLDSELGGQDFMSYTVHIPPTPDNQPMDPSISQKVEEQYVANSMFTGGFKSNTRAHLMHKVIETEPNHPQMAGSKGSSCAIPGCDAKVMSDERGQDLLPCECDFKICRDCFIDAVKTGGGICPGCKEPYKNTHLTDQVDENGQQRPMLPGGGGSKMERRLSMVKSTNKSALMRSQTGDFDHNRWLFETTGTYGYGNAFWTKDGDFGSGKDGDGDGDGMGMEAQDLMSRPWRPLTRKLKIPAGVISPYRLLIFIRIVVLALFLTWRVKHQNPDAVWLWGMSVVCELWFALSWLLDQLPKLCPINRATDLQVLKEKFETPTASNPTGKSDLPGFDVFVSTADPEKEPPLVTANTILSILAAEYPVEKLSCYVSDDGGALLTFEAMAEAASFANIWVPFCRKHAIEPRNPDSYFSLKRDPYKNKVKSDFVKDRRRVKREFDEFKVRVNSLPDSIRRRSDAYHAREEIKAMKMQRQNRDDEPMEPVKIPKATWMADGTHWPGTWLTSASDHAKGDHAGIIQVMLKPPSDEPLHGVSEGFLDLTDVDIRLPLLVYVSREKRPGYDHNKKAGAMNALVRASAIMSNGPFILNLDCDHYIYNSEALREGMCFMMDRGGDRLCYVQFPQRFEGIDPSDRYANHNTVFFDVNMRALDGLMGPVYVGTGCLFRRIALYGFNPPRSKDFSPSCWSCCFPRSKKKNIPEENRALRMSDYDDEEMNLSLVPKKFGNSTFLIDSIPVAEFQGRPLADHPAVKNGRPPGALTIPRELLDASTVAEAIAVISCWYEDKTEWGSRIGWIYGSVTEDVVTGYRMHNRGWKSVYCVTKRDAFRGTAPINLTDRLHQVLRWATGSVEIFFSRNNALLASSKMKILQRIAYLNVGIYPFTSIFLIVYCFLPALSLFSGQFIVQTLNVTFLVYLLIISITLCLLALLEIKWSGISLEEWWRNEQFWLIGGTSAHLAAVLQGLLKVVAGVEISFTLTSKSGGDDIDDEFADLYMVKWTSLMIPPITIIMVNLIAIAVGFSRTIYSVVPQWSKLIGGVFFSFWVLAHLYPFAKGLMGRRGRTPTIVYVWSGLVAITISLLWVAINPPAGNTEIGGNFSFP
Protein: Hydrazine-oxidizing enzyme (A0P951)
Organism: Candidatus Jettenia caeni
Interaction partners:
Sequence:
MRNFLKVTLMSALIGCGAMGAASSLMLKEAKAVEIITHWVPHEVYGQIGEPDNNGKVFFSGLGAKYMGYPKHENPPPYPGKYSKFWRTLPAYRYYIPDFMYNRDEVRPSNPIKGTFQLEQCIACHSVMTPGIVRDYKKSAHSRAEPNPTGCDTCHGNNHQKLTMPSSKACGTSECHETQYSEQGQGGIGSHASCSSFAQIECAWSIERPPGDTAGCTFCHTSSEERCSTCHQRHQFDPKVARRAEQCKTCHWGKDHRDWEAYDIGLHGVVYQVNKWDPKQFDWDKKLADADYVGPTCQYCHMRGGHHNVQRFSTVYTSMGMSMADRGAPIWKEKRDRWASVCDDCHSPRFAKENLQALDESVKDAGLKYRETFKVAEDLLKDGVADPMPKDLAPDWSGQHIWSLKIGAYHDGPEYGGKTGESGEFRMSNCSDIERLCFESVGYFQTYIYKGMAHGSWNDATYSDGSFGMDRWLVNVKQNASQARRLAALEKKVGISWVPESFWKTGEWLDQLTGPYIVKNHPGKTIFDLCPDPGWLDTHHAPAEEVEYINRKLEELGMRHESHGSAHH
Protein: WD repeat-containing protein 41 (Q9HAD4)
Organism: Homo sapiens (Human)
Function: Non-catalytic component of the C9orf72-SMCR8 complex, a complex that has guanine nucleotide exchange factor (GEF) activity and regulates autophagy. The C9orf72-SMCR8 complex promotes the exchange of GDP to GTP, converting inactive GDP-bound RAB8A and RAB39B into their active GTP-bound form, thereby promoting autophagosome maturation. As part of the C9orf72-SMCR8 complex, stimulates RAB8A and RAB11A GTPase activity in vitro, however WDR42 is shown not be an essential complex component for this function. The C9orf72-SMCR8 complex also acts as a negative regulator of autophagy initiation by interacting with the ULK1/ATG1 kinase complex and inhibiting its protein kinase activity.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:27193190}.
Interaction partners:
- Guanine nucleotide exchange protein SMCR8
- Guanine nucleotide exchange factor C9orf72
- Ras-related protein Rab-39B
- Ras-related protein Rab-8A
- ADP-ribosylation factor 1
- Autophagy-related protein 101
- Ragulator complex protein LAMTOR1
- Ras-related protein Rab-1A
- Ragulator complex protein LAMTOR3
- Ragulator complex protein LAMTOR2
Sequence:
MLRWLIGGGREPQGLAEKSPLQTIGEEQTQNPYTELLVLKAHHDIVRFLVQLDDYRFASAGDDGIVVVWNAQTGEKLLELNGHTQKITAIITFPSLESCEEKNQLILTASADRTVIVWDGDTTRQVQRISCFQSTVKCLTVLQRLDVWLSGGNDLCVWNRKLDLLCKTSHLSDTGISALVEIPKNCVVAAVGKELIIFRLVAPTEGSLEWDILEVKRLLDHQDNILSLINVNDLSFVTGSHVGELIIWDALDWTMQAYERNFWDPSPQLDTQQEIKLCQKSNDISIHHFTCDEENVFAAVGRGLYVYSLQMKRVIACQKTAHDSNVLHVARLPNRQLISCSEDGSVRIWELREKQQLAAEPVPTGFFNMWGFGRVSKQASQPVKKQQENATSCSLELIGDLIGHSSSVEMFLYFEDHGLVTCSADHLIILWKNGERESGLRSLRLFQKLEENGDLYLAV
Protein: Activating signal cointegrator 1 (ASC-1) (Thyroid receptor-interacting protein 4) (TR-interacting protein 4) (TRIP-4) (Q9QXN3)
Organism: Mus musculus (Mouse)
Function: Transcription coactivator which associates with nuclear receptors, transcriptional coactivators including EP300, CREBBP and NCOA1, and basal transcription factors like TBP and TFIIA to facilitate nuclear receptors-mediated transcription. May thereby play an important role in establishing distinct coactivator complexes under different cellular conditions. Plays a role in thyroid hormone receptor and estrogen receptor transactivation (By similarity). Also involved in androgen receptor transactivation. Plays a pivotal role in the transactivation of NF-kappa-B, SRF and AP1. Acts as a mediator of transrepression between nuclear receptor and either AP1 or NF-kappa-B. May play a role in the development of neuromuscular junction (By similarity). May play a role in late myogenic differentiation. Also functions as part of the RQC trigger (RQT) complex that activates the ribosome quality control (RQC) pathway, a pathway that degrades nascent peptide chains during problematic translation (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q15650}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q15650}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q15650}. Note=Cytoplasmic under conditions of serum deprivation. Colocalizes with NEK6 in the centrosome. {ECO:0000250|UniProtKB:Q15650}.
Interaction partners:
- Activating signal cointegrator 1 complex subunit 2
- Activating signal cointegrator 1 complex subunit 3
- Mediator of RNA polymerase II transcription subunit 23
- Mediator of RNA polymerase II transcription subunit 28
- Mediator of RNA polymerase II transcription subunit 1
- Mediator of RNA polymerase II transcription subunit 8
- Mediator of RNA polymerase II transcription subunit 17
- Mediator of RNA polymerase II transcription subunit 13
- Mediator of RNA polymerase II transcription subunit 12
- REST corepressor 1
Sequence:
MAVAGAAYREPLVHWCTQQLQKTFALDVSEEIIQYVLSIENAEEIREYVTDLLQGNEGKKGQFIEDLITKWQKNDQEFISDSFQQCLRKDEILDGQRSVDQLKRSRRKGRNKQEVPAFPEPDVAVEVKTPLDLAKAQESNNSVKKKTRFVNLYTREGQDKLAVLLPGRHPCDCLGQKHKLINNCLVCGRIVCEQEGSGPCLFCGSLVCTNEEQDILQRDSNKSQKLLKKLMSGAETSGKVDVSTKDLLPHQESRMKSGLEKAIKHKEKLLEFDRTSIRRTQVIDDESDYFASDSNQWLSKVEREMLQKREEELRELRHASRLSKKVTIDFAGRKILEDENPLAEYHSRLDETIQAIASGTLNQSLVTLDRSCEEPLGVLVNPNMYQASPQWVDNTGSTPQKKTSLSAGPRLEPSLHQHQLRIQDQEFQEGFDGGWCLSMHQPWASLLVRGIKRVEGRSWYTPHRGRLWIAATGKRPSPQEVSELQATYRLLRGKDVEFPNDYPSGCLLGCVDLIDCLSQKQFQEQFPDISQESDSSFVFICKNPQEMVVKFPIKGNPKIWKLDSKIHQGAKKGLMKQNKAV
Protein: Colony-stimulating factor 3 (granulocyte) a (Granulocyte colony stimulating factor) (B8ZHI7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Colony-stimulating factor 3 receptor
- Interleukin-6
- Colony-stimulating factor 3
Sequence:
MMGLCYYWSLVIVLLCFLIGVAIMNFQAQFFFTLVGIVVSAPVPQKLDIMNKDTIEQAHSLISKTLEDIPATHAAWVKSKSLAWGSSTDKLQHLKHYIPSAPVLQNITDISSLETCLDKIVRGLQLHLNLLKDLIEATTLSQTDQVTELQADIQELVLLIEELQNQSGFNPSQQTSEEQSQSFKLNLTQHLKSDFQTEAAAHLILHQLRDFSCDILQRILSIRV
Protein: Regucalcin (RC) (Gluconolactonase) (GNL) (EC 3.1.1.17) (Senescence marker protein 30) (SMP-30) (Q15493)
Organism: Homo sapiens (Human)
Function: Gluconolactonase with low activity towards other sugar lactones, including gulonolactone and galactonolactone. Can also hydrolyze diisopropyl phosphorofluoridate and phenylacetate (in vitro). Calcium-binding protein. Modulates Ca(2+) signaling, and Ca(2+)-dependent cellular processes and enzyme activities (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Probable gluconokinase
- Protein transport protein Sec16B
- Protein transport protein Sec16A
- Catalase
- Choline dehydrogenase, mitochondrial
- Intraflagellar transport protein 46 homolog
- Sorbitol dehydrogenase
- Parkinson disease protein 7
- Calmodulin-like protein 4
- Calmodulin-1
Sequence:
MSSIKIECVLPENCRCGESPVWEEVSNSLLFVDIPAKKVCRWDSFTKQVQRVTMDAPVSSVALRQSGGYVATIGTKFCALNWKEQSAVVLATVDNDKKNNRFNDGKVDPAGRYFAGTMAEETAPAVLERHQGALYSLFPDHHVKKYFDQVDISNGLDWSLDHKIFYYIDSLSYSVDAFDYDLQTGQISNRRSVYKLEKEEQIPDGMCIDAEGKLWVACYNGGRVIRLDPVTGKRLQTVKLPVDKTTSCCFGGKNYSEMYVTCARDGMDPEGLLRQPEAGGIFKITGLGVKGIAPYSYAG
Protein: Mitochondrial respiration co-chaperone MRJ1 (Mitochondrial respiration J-domain protein 1) (J9VP29)
Organism: Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487) (Filobasidiella neoformans var. grubii)
Function: Mitochondrial co-chaperone required for ubiquinol-cytochrome c oxidoreductase (mitochondrial respiratory chain complex III) activity.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:32518190}.
Interaction partners:
Sequence:
MLSFQATVRPLAVSSRLHSPAAHIWRRNAHTAAMSDDSLDQGSSSSYGDSASQPHLGKGKGRQDSLAQSYRFPEKGMNGGPPDPFEVMALDRSATQQEVKQQYYKLALLLHPDSSHPSSSPDHFATLNKAYNLLSKQSSRSAFLKTGYGWDVSTSSGGNQTWSDSLMRAEIARRRNGGAAAWNGASRRYRDSDAGRGAWGGFDGSQGWRPYEDPSKGFSPPTSGPAEERYMSNPRFLAVVGVASAVIAWVHWHRLGYAAETHRDMLDKQNIDASRALAQARYEAATHGHIRREQIRRRVREAEVLKELEKADQGHIAVAGPPTAYPPSHRE
Protein: Thioredoxin reductase-like selenoprotein T (SelT) (EC 1.8.1.9) (P62342)
Organism: Mus musculus (Mouse)
Function: Selenoprotein with thioredoxin reductase-like oxidoreductase activity (By similarity). Protects dopaminergic neurons against oxidative stress and cell death. Involved in ADCYAP1/PACAP-induced calcium mobilization and neuroendocrine secretion (By similarity). Plays a role in fibroblast anchorage and redox regulation. In gastric smooth muscle, modulates the contraction processes through the regulation of calcium release and MYLK activation (By similarity). In pancreatic islets, involved in the control of glucose homeostasis, contributes to prolonged ADCYAP1/PACAP-induced insulin secretion.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:23913443}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Selenoprotein F
- Selenoprotein K
- Protein adenylyltransferase SelO, mitochondrial
- Selenoprotein W
- Selenoprotein S
- Selenoprotein M
- Selenide, water dikinase 2
- Selenoprotein N
- Selenoprotein H
- Selenoprotein V
Sequence:
MRLLLLLLVAASAVVRSEASANLGGVPSKRLKMQYATGPLLKFQICVSUGYRRVFEEYMRVISQRYPDIRIEGENYLPQPIYRHIASFLSVFKLVLIGLIIVGKDPFAFFGMQAPSIWQWGQENKVYACMMVFFLSNMIENQCMSTGAFEITLNDVPVWSKLESGHLPSMQQLVQILDNEMKLNVHMDSIPHHRS
Protein: Bombesin (P86483)
Organism: Sanguirana varians (Palawan frog) (Rana varians)
Function: Stimulates smooth muscle contraction in isolated rat stomach strip.
Subcellular location: Secreted {ECO:0000269|PubMed:19857598}.
Interaction partners:
Sequence:
MSLLPAVKVLPLGYLGIVLVFSLILRSAMVDFIQDAGKLERIDTYKREAQMIFGAPMWALGHLMGRK
Protein: Small ribosomal subunit protein eS24A (40S ribosomal protein S24-A) (O13784)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Small ribosomal subunit protein uS10
- Small ribosomal subunit protein uS14
- Small ribosomal subunit protein uS15
- Small ribosomal subunit protein eS7
- Elongation factor 3
- mRNA export factor elf1
- Small ribosomal subunit protein eS27
- Small ribosomal subunit protein uS5
- Small ribosomal subunit protein uS3
- Small ribosomal subunit protein eS21
Sequence:
MSEAVTIRTRKFMTNRLLQRKQMVVDILHPGKANISKNDLREKLGQMYKTDASAVQAFGLRTHYGGGRTTGFALIYDDVEAMKKFEPHYRLVRVGHAEPIQKVARQQRKQRKNRGKKVFGTGKRLAKRKSKQQD
Protein: Probable lactoylglutathione lyase, chloroplastic (EC 4.4.1.5) (Glyoxalase I) (Q8W593)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione.
Subcellular location: Plastid, chloroplast stroma {ECO:0000269|PubMed:11719511}.
Interaction partners:
- Probable hydroxyacylglutathione hydrolase 2, chloroplastic
- Hydroxyacylglutathione hydrolase 2, mitochondrial
- Hydroxyacylglutathione hydrolase 1, mitochondrial
- Hydroxyacylglutathione hydrolase cytoplasmic
- Protein DJ-1 homolog D
- DJ-1 protein homolog E
- DJ-1 protein homolog F
- Persulfide dioxygenase ETHE1 homolog, mitochondrial
- Lactoylglutathione lyase
- Lactoylglutathione lyase GLX1
Sequence:
MVRIIPMAASSIRPSLACFSDSPRFPISLLSRNLSRTLHVPQSQLFGLTSHKLLRRSVNCLGVAESGKAAQATTQDDLLTWVKNDKRRMLHVVYRVGDMDRTIKFYTECLGMKLLRKRDIPEEKYTNAFLGYGPEDSHFVIELTYNYGVDKYDIGAGFGHFGIAVDDVAKTVELVKAKGGKVSREPGPVKGGKTVIAFIEDPDGYKFELLERGPTPEPLCQVMLRVGDLDRAIKFYEKAFGMELLRTRDNPEYKYTIAMMGYGPEDKFPVLELTYNYGVTEYDKGNAYAQIAIGTDDVYKTAEAIKLFGGKITREPGPLPGISTKITACLDPDGWKSVFVDNIDFLKELE
Protein: Large ribosomal subunit protein bL28 (50S ribosomal protein L28) (P0A7M2)
Organism: Escherichia coli (strain K12)
Interaction partners:
- Large ribosomal subunit protein bL32
- Small ribosomal subunit protein uS15
- Small ribosomal subunit protein uS9
- Large ribosomal subunit protein bL27
- Small ribosomal subunit protein uS8
- Large ribosomal subunit protein uL10
- Large ribosomal subunit protein uL11
- Large ribosomal subunit protein uL3
- Large ribosomal subunit protein bL34
- Small ribosomal subunit protein uS12
Sequence:
MSRVCQVTGKRPVTGNNRSHALNATKRRFLPNLHSHRFWVESEKRFVTLRVSAKGMRVIDKKGIDTVLAELRARGEKY
Protein: Importin-9 (Imp9) (Importin-9a) (Imp9a) (Importin-9b) (Imp9b) (Ran-binding protein 9) (RanBP9) (Q91YE6)
Organism: Mus musculus (Mouse)
Function: Nuclear transport receptor that mediates nuclear import of proteins, such as histones, proteasome and actin. Serves as receptor for nuclear localization signals (NLS) in cargo substrates. Is thought to mediate docking of the importin/substrate complex to the nuclear pore complex (NPC) through binding to nucleoporin and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to the importin, the importin/substrate complex dissociates and importin is re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. Mediates the import of pre-assembled proteasomes into the nucleus; AKIRIN2 acts as a molecular bridge between IPO9 and the proteasome complex (By similarity). Mediates the nuclear import of histones H2A, H2B, H4 and H4. In addition to nuclear import, also acts as a chaperone for histones by preventing inappropriate non-nucleosomal interactions (By similarity). Mediates the nuclear import of actin.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q96P70}. Nucleus {ECO:0000250|UniProtKB:Q96P70}.
Interaction partners:
- Importin-5
- Importin-7
- Exportin-6
- Importin-8
- Importin-13
- Importin-4
- Transportin-1
- Cofilin-1
- Exportin-1
- Importin subunit beta-1
Sequence:
MAAAAAAGAASGLPGPVAQGLKEALVDTLTGILSPVQEVRAAAEEQIKVLEVTEEFGVHLAELTVDPQGALAIRQLASVILKQYVETHWCAQSEKFRPPETTERAKIVIRELLPNGLRESISKVRSSVAYAVSAIAHWDWPEAWPQLFNLLMEMLVSGDLNAVHGAMRVLTEFTREVTDTQMPLVAPVILPEMYKIFTMAEVYGIRTRSRAVEIFTTCAHMICNMEELEKGAAKVLIFPVVQQFTEAFVQALQMPDGPTSDSGFKMEVLKAVTALVKNFPKHMVSSMQQILPIVWNTLTESAAFYVRTEVNYTEEVEDPVDSDGEVLGFENLVFSIFEFVHALLENSKFKSTVKKALPELIYYIILYMQITEEQIKVWTANPQQFVEDEDDDTFSYTVRIAAQDLLLAVATDFQNESAVALATAATRHLQEAEQTKASGTEHWWKIHEACMLALGSVKSIITDSVKNGRIHFDMHGFLTNVILADLNLSASPFLLGRALWAASRFTVAMSPELIQQFLQATVSGLHETQPPSVRISAVRAIWGYCDQLKVSESTHVLQPFLPSILDGLIHLAAQFSSEVLNLVMETLCIVCTVDPEFTASVENKICPFTIAIFLKYSNDPVVASLAQDIFKELSQIEACQGPMQMRLIPTLVSIMQAPADKIPAGLCATAIDILTTVVRNTKPPLSQLLICQAFPAVAQCTLHTDDNATMQNGGECLRAYVSVTLEQVAQWHDEQGHNGLWYVMQVVSQLLDPRTSEFTAAFVGRLVSTLISKAGRELGENLDQILRAILSKMQQAETLSVMQSLIMVFAHLVHTQLEPLLEFLCSLPGPTGKPALEFVMAEWTSRQHLFYGQYEGKVSSVALCKLLQHGINADDKRLQDIRVKGEEIYSMDEGIRTRSKSAKNPERWTNIPLLVKILKLIINELSNVMEANAARQATPAEWNQDDSNDMWEDQEEEEEEEEDGLAGQLLSDILATSKYEEDYYEDDEEDDPDALKDPLYQIDLQAYLTDFLCQFAQQPCYIMFSCHLNDNERRVLQTIGI
Protein: Vacuolar protein sorting-associated protein 33A (r-vps33a) (Q63615)
Organism: Rattus norvegicus (Rat)
Function: Plays a role in vesicle-mediated protein trafficking to lysosomal compartments including the endocytic membrane transport and autophagic pathways. Believed to act as a core component of the putative HOPS and CORVET endosomal tethering complexes which are proposed to be involved in the Rab5-to-Rab7 endosome conversion probably implicating MON1A/B, and via binding SNAREs and SNARE complexes to mediate tethering and docking events during SNARE-mediated membrane fusion. The HOPS complex is proposed to be recruited to Rab7 on the late endosomal membrane and to regulate late endocytic, phagocytic and autophagic traffic towards lysosomes. The CORVET complex is proposed to function as a Rab5 effector to mediate early endosome fusion probably in specific endosome subpopulations. Required for fusion of endosomes and autophagosomes with lysosomes; the function is dependent on its association with VPS16 but not VIPAS39. The function in autophagosome-lysosome fusion implicates STX17 but not UVRAG.
Subcellular location: Cytoplasmic vesicle {ECO:0000269|PubMed:11382755}. Late endosome membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Lysosome membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Early endosome {ECO:0000305}. Cytoplasmic vesicle, autophagosome {ECO:0000250|UniProtKB:Q96AX1}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000305}.
Interaction partners:
- Vacuolar protein sorting-associated protein 16 homolog
- VPS39 subunit of HOPS complex
- Vacuolar protein sorting-associated protein 18 homolog
- Vacuolar protein sorting-associated protein 11 homolog
- VPS8 subunit of CORVET complex
- Transforming growth factor, beta receptor associated protein 1
- Vacuolar protein sorting-associated protein 41 homolog
- Spermatogenesis-defective protein 39 homolog
- Vesicle-associated membrane protein 8
- Syntaxin-17
Sequence:
MAAHLSYGRVNLNVLREAVRRELREFLDKCAGSKAIVWDEYLTGPFGLIAQYSLLKEHEVEKMFTLKGSRLPAADVKNIIFLVRPRLELMDMIAENVLSEDRRGPTRDFHILFVPRRSLLCEQRLKDLGVLGSFIYREEYSLDLIPFDGDLLSMESESAFKECYLEGDQTSLYHAAKGLMTLQALYGTIPQIFGKGECARQVANMMVRMKREFTGSQNSVFPVFDNLLLLDRNVDLLTPLASQLTYEGLIDEIYGIQNSYVKLPPEKFAPKKQGGGGGKDLPTEAKKLQLNSAEELYAEIRDKNFNAVGSVLSKKAKIISAAFEERHNAKTVGEIKQFVSQLPHMQAARGSLANHTSIAELIKDVTTSEDFFDKLTVEQEFMSGIDTDKVNNYIEDCIAQKHPLIKVLRLVCLQSMCNSGLKQKVLDYYKREILQTYGYEHILTLNNLEKAGLLKAQTGGRNNYPTIRKTLRLWMDDVNEQNPTDISYVYSGYAPLSVRLAQLLSRPGWRSIEEVLRILPGPHFEERQPLPTGVQKKRQPGENRVTLVFFLGGVTFAEIAALRFLSQLEDGGTEYVIATTKLINGSSWLEALMEKPF
Protein: Rifin (Q8IK44)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MKLHYTKILLFFFPLNVLLTSYHAHNKNKASITPHHTRSTTSRLLSEYDTESSIYDSDEDINSVKEIFERQTSRRFEEYEERMITQRQKYKEQRDKDIQKIILKDKMEKNLAKKIEKGCLRCGFGLSGVAGSIGLFGAVAINIWKPAALKAAIAKAITEGTADIAAAGVKAGEVTGKVLVISGLKRMGISTLDGKDLGTYFATTSYKNITNITQAVSSEYVQKCISASSGSVRFRLVDAQRDIHFCHSVWKQTSAVSTPKKGISYKEVIERTVETMVSKAEGPANTAAEIAEAANKLAIEEAQEKVMEATIYNWYTTIGYSILAILIIVLIMLIIYLILRYRRKKKMKKKAQYTKLLNE
Protein: Probable polyamine oxidase 4 (AtPAO4) (EC 1.5.3.16) (Amine oxidase 2) (Q8H191)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Flavoenzyme involved in polyamine back-conversion. Catalyzes the oxidation of the secondary amino group of polyamines, such as spermine and spermidine. Substrate preference is spermine > spermidine. No activity detected when putrescine or N(1)-acetylspermine are used as substrates. Plays an important role in the regulation of polyamine intracellular concentration (Probable).
Subcellular location: Peroxisome {ECO:0000269|PubMed:18703589}.
Interaction partners:
- Spermine synthase
- Spermidine synthase 1
- Spermidine synthase 2
- N-carbamoylputrescine amidase
- Aldehyde dehydrogenase family 3 member H1
- Probable polyamine oxidase 5
- Aldehyde dehydrogenase family 3 member I1, chloroplastic
- Aldehyde dehydrogenase family 3 member F1
- Aldehyde dehydrogenase family 2 member B7, mitochondrial
- Polyamine oxidase 1
Sequence:
MDKKKNSFPDNLPEGTISELMQKQNNVQPSVIVIGSGISGLAAARNLSEASFKVTVLESRDRIGGRIHTDYSFGCPVDMGASWLHGVSDENPLAPIIRRLGLTLYRTSGDDSILYDHDLESYGLFDMHGNKIPPQLVTKVGDAFKRILEETEKIRDETANDMSVLQGISIVLDRNPELRQEGMAYEVLQWYLCRMEAWFAVDANLISLKCWDQDECLSGGHGLMVQGYEPVIRTIAKDLDIRLNHRVTKVVRTSNNKVIVAVEGGTNFVADAVIITVPIGVLKANLIQFEPELPQWKTSAISGLGVGNENKIALRFDRAFWPNVEFLGMVAPTSYACGYFLNLHKATGHPVLVYMAAGNLAQDLEKLSDEATANFVMLQLKKMFPDAPDPAQYLVTRWGTDPNTLGCYAYDVVGMPEDLYPRLGEPVDNIFFGGEAVNVEHQGSAHGAFLAGVSASQNCQRYIFERLGAWEKLKLVSLMGNSDILETATVPLQISRM