wanglab/gogpt-training-data huggingface dataset:
Protein: WUSCHEL-related homeobox 4 (Q6X7J9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Promotes differentiation and/or maintenance of the vascular procambium, the initial cells of the developing vasculature. Part of the TDIF-TDR-WOX4 signaling pathway that plays a crucial role in the maintenance of the vascular meristem organization during secondary growth. Is required for promoting the proliferation of procambial/cambial stem cells but not for repressing their commitment to xylem differentiation in response to the TDIF signal. Acts redundantly with WOX14 downstream of the TDR/PXY receptor kinase to regulate procambial cell proliferation and differentiation in vascular tissue, independently of any role in vascular. Acts as a cambium regulator in the inflorescence stem. Is required for auxin-dependent cambium stimulation in the inflorescence stem.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000269|PubMed:20729381}.
Interaction partners:
- Leucine-rich repeat receptor-like protein kinase TDR
- CLAVATA3/ESR
- CLAVATA3/ESR
- Protein CLAVATA 3
- Leucine-rich repeat receptor-like protein kinase
- Probable leucine-rich repeat receptor-like protein kinase At5g05160
- LOB domain-containing protein 4
- Homeobox-leucine zipper protein ATHB-8
- Receptor protein kinase CLAVATA1
- Dof zinc finger protein DOF5.3
Sequence:
MKVHEFSNGFSSSWDQHDSTSSLSLSCKRLRPLAPKLSGSPPSPPSSSSGVTSATFDLKNFIRPDQTGPTKFEHKRDPPHQLETHPGGTRWNPTQEQIGILEMLYKGGMRTPNAQQIEHITLQLGKYGKIEGKNVFYWFQNHKARERQKQKRNNLISLSCQSSFTTTGVFNPSVTMKTRTSSSLDIMREPMVEKEELVEENEYKRTCRSWGFENLEIENRRNKNSSTMATTFNKIIDNVTLELFPLHPEGR
Protein: BG antigen (A5HUK9)
Organism: Gallus gallus (Chicken)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
Sequence:
MHFLLGCNHPSFTLPWRTLLPYLVALHLLQPGSAQLRVVAPSLRVTANVGQDVVLRCQLSPCKDAWSSDIRWIQHRTSGFVHHYQNGEDLEQMEEYKGRTELLRDGLSDGNLDLRITAVSTSDSGSYSCAVQDGDGYADAVVDLEVSDPFSQITHPWKVALAVIVTILVGSFVITVFLYRKKAAETTKQKGKDAELERMDAKLGTLAAELERRDAKLETLVENLERRNAEFAEKLASELERRDAKLDKLASDLVQQTKAVEKLNSQWSKLQSLKLTKSDTIQNNCIGYEKSPQAVNYSPLSNPEKHHEAKRRWYIKSDYPQYPNQRGVGPAHVGTHGTPI
Protein: Secreted transmembrane peptide 3 (Phytocytokine STMP3) (Precursor of secreted transmembrane peptide 3) (B3H4Y2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Brassicaceae-specific phytocytokine (plant endogenous peptide released into the apoplast) perceived by MIK2 in a BAK1/SERK3 and SERK4 coreceptors-dependent manner, that modulates various physiological and antimicrobial processes including growth prevention and reactive oxygen species (ROS) response regulation.
Subcellular location: Cell membrane {ECO:0000269|PubMed:31001913}. Secreted, extracellular space, apoplast {ECO:0000269|PubMed:31001913}. Endoplasmic reticulum {ECO:0000269|PubMed:31001913}. Golgi apparatus {ECO:0000269|PubMed:31001913}. Note=Observed in a reticular pattern and a perinuclear ring (PubMed:31001913). The precursor of STMP3 accumulates at the plasma membrane and is proteolytically cleaved to release the STMP3 in the apoplasm (PubMed:31001913). {ECO:0000269|PubMed:31001913}.
Interaction partners:
Sequence:
MGLKMSSNALLLSLFLLLLCLFSEIGGSETTHWKIVEEPVRGQIATPPSLTCGGQRLGGPQPRLSPCPRPRPRPRPRTGS
Protein: Candida glabrata strain CBS138 chromosome H complete sequence (Q6FR84)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
- Candida glabrata strain CBS138 chromosome A complete sequence
Sequence:
MRFKSIFSSAALISCWAFGVAKLYQNQEIIIDSATLGSQIFEDDELMQLLNAKVTLNNFTDIRLPQGISLNSRSVLKINAPPGHGKPYSLVINGQVTIGKDSKFIFDGSSLEYESQSAASSNFKFDINTGSKGVFIFTYCTMTIKLPKLSEGLIDSDSVAAIHIGGTFEAPNINSPLSILGTLEVLTSETTVDGSFDDKLWRVDLGPDQIVEDGEGYRYILTGNIHCQAYVSVYADIFKATKTVLHALGYRGYTVVSPMTIDLSEGPVFSGGLYLYYIVLPEGQDGLTFLNFAVHEDKGIPAPTLGFMFLYSGDQTDVVATANQNIINVMNLNSKKSISVIGDHNYNITTKYSDGKSIQQQGYSGVQSYPNELIVYLYAPPSEEPDYTTTIDKGNGEFETDVVSHITTKDSDGKPTTIVTTIPWKPSEEADYTTTIDKGNGEFETDVVSHITTKDSDGKPTTIVTTIPWKPSEEADYTTTIDKGNGEFETDVVSHITTKDSDGKPTTIVTTIPLKPSDAGEADYTTTITSDGHTITEVVSHITTTDSDGNTVTYTTMMASFDQVGDGVYTSAPPYSQPPVVTTTVTEDDGSSKTVVISYSPSEGEDGVTRTGTTTISTITPSGEADYTTTIDKGNGDFETDLVSHITTKDSNGNPTTIVTTIPLKPSDAGEADYTTTITSDGHTITEVVSHITTTDSDGNTVTYTTTMASFDQVGDGVYTSAPPYSQPPVVTTTVTEDDGSSKTVVISYSPSEGEDGVTRTGTTTISTITPSGEADYTTTIDKGNGDFETDLVSHITTTDSDGKPTTIVTTIPLKPSDAGEADYTTTITSDGHTITEVVSHITTTDSDGNTVTYTTMMASFDQVGDGVYTSAPPYSQPPVVTTTVTEDDGSSKTVVISYSPSEGEDGVTRTGTTTISTITPSGEADYTTTIDKGNGDFETDLVSHITTTDSDGKPTTIITTVTLIEEPDYTSVFVSDGHTITAVVSHVTTTNDIGQTVTTTVTVMSYDQVGEGVYTSAPAYSQPPVTTTTVSANTATATVVISYFPSIGDDGVTGTGTTTVSTVSVGGEVDYTTTVDRGNGSTETDVISHITTTDSNGNPTTITTTITNAPPPLNSKANIGSDYTSTVVSNGHTIVSTVTQTVGGQSHGNTVSSAAPVTTVSGASFNAPETAGVGGIVNSQNSQSQYVADQGSGNEKPTQAPGTAGGSGSGSVHQSAGNIVPSGSPSVQSPMNTASPVNGIHSSQTPHSVPSQAQQQGQGQAQAPSSRQQAATTVLSPSGSSVNNIGSGFNSTQTASVLQGKGASIKVTSISILFSIITVIVVGMI
Protein: Tubulin beta-4B chain (Tubulin beta-2 chain) (Tubulin beta-2C chain) (P68371)
Organism: Homo sapiens (Human)
Function: Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P68372}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000250|UniProtKB:P68372}.
Interaction partners:
- Tubulin alpha-1A chain
- Tubulin alpha-1B chain
- Tubulin alpha-4A chain
- Tubulin alpha-1C chain
- Tubulin beta chain
- Tubulin alpha-3C chain
- Tubulin alpha chain-like 3
- Tubulin alpha-8 chain
- Tubulin alpha-3E chain
- Microtubule-associated protein tau
Sequence:
MREIVHLQAGQCGNQIGAKFWEVISDEHGIDPTGTYHGDSDLQLERINVYYNEATGGKYVPRAVLVDLEPGTMDSVRSGPFGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVVRKEAESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYPDRIMNTFSVVPSPKVSDTVVEPYNATLSVHQLVENTDETYCIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCLRFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRALTVPELTQQMFDAKNMMAACDPRHGRYLTVAAVFRGRMSMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRGLKMSATFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVSEYQQYQDATAEEEGEFEEEAEEEVA
Protein: THO complex subunit 1 (R4GMN4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
XFKSYKLDDTQASRKKMEELKTGGEHVYFAKFLTSEKLMDLQLSDSNFRRHILLQYLILFQYLKGQVKFKSSNYVLTDEQSLWIEDTTKSVYQLLSENPPDGERFSKMVEHILNTEENWNSWKNEGCPSFVKESVCFVHDRTSDTKPTRIIRKRTAPEDFLGKGPTKKILMGNEELTRLWNLCPDNMEACKSETREHMPTLEEFFEEAIEQADPENMVENEYKAVNNSNYGWRALRLLARRSPHFFQPTNQQFKSLPEYLENMVIKLAKELP
Protein: Probable pyridoxamine 5'-phosphate oxidase (EC 1.4.3.5) (PNP/PMP oxidase) (PNPOx) (Q9UTQ1)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP).
Interaction partners:
- Putative pyridoxal kinase C6F6.11c
- Putative pyridoxal kinase C18.10
- Uncharacterized glutaminase C222.08c
- Pyridoxal reductase
- Probable pyridoxal reductase 2
- Probable pyridoxal 5'-phosphate synthase subunit PDX1
- NAD
- Uncharacterized oxidoreductase C3A11.11c
- Uncharacterized oxidoreductase C215.11c
- 4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate synthase
Sequence:
MSENTDSTHEKLIFAPSRYQYEKSSLHRDALMGKDPLVLFNQWFQEATDDEGIKSPESTTLSTARLPSGRVSSRLVLLKELDHRGFIIFTNLGTSKKAKDLKSNPYASLSFWWEPLQRQVRVEGIIERLSREETEEYFKTRPRNSRIGAWASPQSEVIADREELEKRVEEYKKKFGEDESVPVPVPDFWGGIRIVPLEIEFWQGGKYRLHDRFSFRRNTLDEDYELVRLAP
Protein: Proteasome regulatory non-ATP-ase subunit 2 (Q8WRU7)
Organism: Trypanosoma brucei
Interaction partners:
Sequence:
MAVGLSSSKGVLALLRESDSDVLQFALKRLRPLVDTYWCEISDDLPLIESLSESSDLAEETRALAALIASHVYFHLGAYNDSVHCALAAGPAFSYVERSLFTDTILSCCIDKFVEYQQKPEGAREELDPRLESLFTALTSKWIGQEGMPVKELVGFTIRARRLDFLEKVLRQHIKSTKSAAILNFTFEVASVLLRDIAFRREILKLLSVLYAQGGLTTVDYFSQAQCLLFLGDSTGTADLIEDLIRSGDKATAYQLAFDLHEYGNQEFLSAVAGLIEKRATLSIPAPSQVQRVETATEDKSGSGADHSTSSQAAAGQTTQEGDKKDISEVHQKLLSALTGELTASLYLQFLSGQCKADSNVLNRIKQTTDQRKAVPHNALTIAHALMYCGTTIHTFLRNDMEWFGGATYWGKFIATASIGALHYGHVNEALKIMDSYLPKDNIGVLPHSEAGSLYALGLIHAPVGVGRNQEIILYLKEMLRKFSASEHIIHGASLGIGLAAMGLKDEKLHDSLFTCVGGCDAVASEGAALGIGLLMMGSGNLGAIGNLRALASEDNQKEKTIRGISMAMALMMLGREDECWSTANELLEDSDPWVRLGGCFMLGLGYAGAENTKVLERLLSVSVKDTSDDVRRNAATMIGFLTIKDPALFVELTRVLVDSYNPHISYGVGMALAVAAAGTGMPEVIDILWGLKDDIVDFVRQGAYIALALVMVQVTEVENPKVKELRDIFTKIIAGRKEDMCSKFGCIIATGLLDAWGRNCTFALHRQRHRLDKAVVGMFVFLQHWYWFPYLLMITLAMRPTCFIGLNSDLEVPEYVFKSNAPASRFALPKSVLAEKKEAKAAAVKAVILSTTKKEEEFVRLKRSAVAGKNQGTGGTGGAANAAASQSGATKEQETEKKREPEANFVILSNPARITARQFAVITHDVDKRFVPLKENPSSICLLRDTNPAEGKPKVVTDLGWNSSDDAPPPEPFTWP
Protein: Neurexin-3-beta (Neurexin III-beta) [Cleaved into: Neurexin-3-beta, soluble form; Neurexin-3-beta, C-terminal fragment (NRXN3-CTF)] (Q8C985)
Organism: Mus musculus (Mouse)
Function: Neuronal cell surface protein that may be involved in cell recognition and cell adhesion. May play a role in angiogenesis (By similarity).
Subcellular location: Presynaptic cell membrane {ECO:0000269|PubMed:34135511}; Single-pass type I membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MHLRIHPRRSPPRRPAWTLGIWSLFWGCIVSSVWSSSNVASSSSSSPGSHSQQEHHFHGSKHHSVPISIYRSPVSLRGGHAGATYIFGKSGGLILYTWPANDRPSTRSDRLAVGFSTTVKDGILVRIDSAPGLGDFLQLHIEQGKIGVVFNIGTVDISIKEERTPVNDGKYHVVRFTRNGGNATLQVDNWPVNEHYPTGNTDNERLQMVKQKIPFKYNRPVEEWLQEKGRQLTIFNTQAQIAIGGKDKGRLFQGQLSGLYYDGLKVLNMAAENNPNIKINGSVRLVGEVPSVSGTTQTTSMPPEMSTTVMETTTTMATTTTRKNRSTASIQPTSDDLVSSAECSSDDEDFVECEPSTGRSDKSLSTSIFEGGYKAHAPKWESKDFRPNKVSETSRTTTTSLSPELIRFTASSSSGMVPKLPAGKMNNRDLKPQPDIVLLPLPTAYELDSTKLKSPLITSPMFRNVPTANPTEPGIRRVPGASEVIRESSSTTGMVVGIVAAAALCILILLYAMYKYRNRDEGSYQVDETRNYISNSAQSNGTLMKEKQASSKSGHKKQKNKDKEYYV
Protein: Wolf-Hirschhorn syndrome candidate 2 (Human) (Q5U2N1)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Negative elongation factor E
- Negative elongation factor complex member C/D
- Negative elongation factor complex member B
- DNA-directed RNA polymerases I, II, and III subunit RPABC3
- DNA-directed RNA polymerase subunit
- Transcription elongation factor SPT5
- Transcription elongation factor SPT4
- DNA-directed RNA polymerases I, II, and III subunit RPABC2
- DNA-directed RNA polymerase II subunit RPB3
- DNA-directed RNA polymerase subunit beta
Sequence:
MASMRESDTGLWLHNKLGATDELWAPPSIASLLTAAVIDNIRLCFHRLSSAVKLKLLLGTLHLPRRTVDEMKGALMDIIQLATLDSDPWVLMVADILKSFPDTGSLNLDLEEQNPNVQDILGELREKVSECEASAMLPLECQYLNKNALTTLAGPLTPPVKHFQLKRKPKSATLRAELLQKSTETAQQLKRSAGVPFHAKGRGLLRKMDTTTPLKGIPKQAPFRSPTTPSVFSPSGNRTPIPPSRTPLQKERGVKLLDISELNTVGAGREAKRRRKTLDTEVVEKPTKEETVVENATPDYAAGLVSTQKLGSLNSEPTLPSTSYLPSTPSVVPASSYIPSSETPPAPPSREASRPPEEPSAPSPTLPTQFKQRAPMYNSGLSPATPTPAAPASPLTPTAPPAVTPTAQTPPVAMVAPQTQAPAPVQQQPKKNLSLTREQMFAAQEMFKTANKVTRPEKALILGFMAGSRENPCPEQGDVIQIKLSEHTEDLPKADGQGSTTMLVDTVFEMNYATGQWTRFKKYKPMTNVS
Protein: 5'-nucleotidase, cytosolic IA (D3ZVD3)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- AMP deaminase 1
- Cytosolic purine 5'-nucleotidase
- 5'-nucleotidase
- 7-methylguanosine phosphate-specific 5'-nucleotidase
- Adenylosuccinate synthetase isozyme 2
- Adenine phosphoribosyltransferase
- Inosine-5'-monophosphate dehydrogenase 1
- 5',3'-nucleotidase, mitochondrial
- Bifunctional purine biosynthesis protein ATIC
- Guanylate kinase
Sequence:
MEPRQPPEAREPGPGAETAAVPRWEEAKTFYDNLSPKKKPKSPKPQNAVTIAVSSRALFRMDEEQRIYTEQGVEEYVRYQLEHENEPFSPGPAFPFVKALEAVNKQLRELYPDSEDIFDIVLMTNNHAQVGVRLINSINHYDLFIERFCMTGGNSPICYLKAYHTNLYLSADAEKVREAIDEGIAAATIFSPSKDVVVSQSQLRVAFDGDAVLFSDESERIVKAHGLDRFFEHEKAHENKPLAQGPLKGFLEALGRLQKKFYSKGLRLECPIRTYLVTARSAASSGARALKTLRSWGLETDEALFLAGAPKGPLLEKIRPHIFFDDQMFHVAGAQEMGTVAAHVPYGVAQNPRREKQSLGAQ
Protein: Large ribosomal subunit protein uL5 (50S ribosomal protein L5) (P62399)
Organism: Escherichia coli (strain K12)
Function: This is 1 of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance. Its 5S rRNA binding is significantly enhanced in the presence of L18.
Interaction partners:
- Small ribosomal subunit protein uS14
- Small ribosomal subunit protein uS12
- Small ribosomal subunit protein uS3
- Large ribosomal subunit protein bL17
- Small ribosomal subunit protein uS4
- Small ribosomal subunit protein uS19
- Large ribosomal subunit protein uL16
- Small ribosomal subunit protein uS5
- Large ribosomal subunit protein uL3
- Large ribosomal subunit protein uL23
Sequence:
MAKLHDYYKDEVVKKLMTEFNYNSVMQVPRVEKITLNMGVGEAIADKKLLDNAAADLAAISGQKPLITKARKSVAGFKIRQGYPIGCKVTLRGERMWEFFERLITIAVPRIRDFRGLSAKSFDGRGNYSMGVREQIIFPEIDYDKVDRVRGLDITITTTAKSDEEGRALLAAFDFPFRK
Protein: Sodium/potassium-transporting ATPase subunit alpha (A0A075Q735)
Organism: Salmo salar (Atlantic salmon)
Subcellular location: Cell membrane {ECO:0000256|RuleBase:RU362084}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU362084}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
YKLAATSEDDGNKKSKKELKKAKEKKDMDDLKKEVDLDDHKLTLDELHRKYGTDLARGLSSARAKEILLRDGPNTLTPPPTTPEWVKFCRQLFGGFSMLLWIGAMLCFLAYGIQAASEDEPANDNLYLGVVLSVVVIVTGCFSYYQEAKSSKIMDSFKNLVPQQALVVRDGEKKNINAEEVVVGDLVEVKGGDRIPADLRIVSASGCKVDNSSLTGESEPQTRTPDFSNDNPLETRNIAFFSTNCVEGTARGIVINTGDHTVMGRIATLATSLEGGKTPIAKEIEHFIHIITGVAVFLGVSFFVLSLILGYGWLEAVIFLIGIIVANVPEGLLATVTVCLTLTAKRMAKKNCLVKNLEAVETLGSTSTICSDKTGTLTQNRMTVAHMWFDNQIHEADTTENQSGTCFDKSSATWASLARVAGLCNRAVFLAEQNNVPILKRDVAGDASESALLKCIELCCGSVKAMREKYSKIAEIPFNSTNKYQLSIHKNIAAGESKHLLVMKGAPERILDRCSTILIHGKEQPLDDELKEAFQNAYEELGGLGERVLGFCHFQLPDDQFAECFNFDCEEVNFPTENLCFVGLMSMIDPPRAAVPDAVGKCRSAGIKVIMVTGDHPITAKAIAKGVGIISEGNETVED
Protein: D(1B) dopamine receptor (D(5) dopamine receptor) (Dopamine D5 receptor) (P25115)
Organism: Rattus norvegicus (Rat)
Function: Dopamine receptor whose activity is mediated by G proteins which activate adenylyl cyclase.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Neuroendocrine secretory protein 55
- Guanine nucleotide-binding protein G
- Pro-opiomelanocortin
- Pituitary adenylate cyclase-activating polypeptide
- VIP peptides
- Natriuretic peptides A
- Pro-glucagon
- Gastric inhibitory polypeptide
Sequence:
MLPPGRNRTAQPARLGLQRQLAQVDAPAGSATPLGPAQVVTAGLLTLLIVWTLLGNVLVCAAIVRSRHLRAKMTNIFIVSLAVSDLFVALLVMPWKAVAEVAGYWPFGTFCDIWVAFDIMCSTASILNLCIISVDRYWAISRPFRYERKMTQRVALVMVGLAWTLSILISFIPVQLNWHRDKAGSQGQEGLLSNGTPWEEGWELEGRTENCDSSLNRTYAISSSLISFYIPVAIMIVTYTRIYRIAQVQIRRISSLERAAEHAQSCRSRGAYEPDPSLRASIKKETKVFKTLSMIMGVFVCCWLPFFILNCMVPFCSSGDAEGPKTGFPCVSETTFDIFVWFGWANSSLNPIIYAFNADFRKVFAQLLGCSHFCFRTPVQTVNISNELISYNQDTVFHKEIATAYVHMIPNAVSSGDREVGEEEEEGPFDHMSQISPTTPDGDLAAESVWELDCEEEVSLGKISPLTPNCFDKTA
Protein: Rab-interacting lysosomal protein (Q5ND29)
Organism: Mus musculus (Mouse)
Function: Rab effector playing a role in late endocytic transport to degradative compartments. Involved in the regulation of lysosomal morphology and distribution. Induces recruitment of dynein-dynactin motor complexes to Rab7A-containing late endosome and lysosome compartments. Promotes centripetal migration of phagosomes and the fusion of phagosomes with the late endosomes and lysosomes.
Subcellular location: Late endosome membrane {ECO:0000250|UniProtKB:Q96NA2}. Lysosome membrane {ECO:0000250|UniProtKB:Q96NA2}. Cytoplasmic vesicle, phagosome membrane {ECO:0000250|UniProtKB:Q96NA2}. Note=Associated with late endosomal, lysosomal and phagosomal membranes. The interaction with RAB7A is necessary for its recruitment to phagosomes. {ECO:0000250|UniProtKB:Q96NA2}.
Interaction partners:
- Ras-related protein Rab-7a
- Oxysterol-binding protein-related protein 1
- Dynactin subunit 1
- Ras-related protein Rab-7b
- Cytoplasmic dynein 1 light intermediate chain 1
- Cytoplasmic dynein 1 light intermediate chain 2
- Cytoplasmic dynein 1 heavy chain 1
- Cytoplasmic dynein 2 heavy chain 1
- Cytoplasmic dynein 1 intermediate chain 2
- Cytoplasmic dynein 1 intermediate chain 1
Sequence:
MEPRRAAPRLPSQASSSVGAGSAAELVYHLAGALGTELQGLARRFGPDAAAGLVPLVVRALELLEKAAVGPAPDSLQVSAQQAEVELRRLREENQRLRQELGSGPQEERALLRQLKEVTDRQRDELRAHNRDLQRRSQETEALQEQLQRLLLINSELRHKLAAVQTQLRAAQDRERERQIAQDGSSQLAKEQSLEPDAATSDDPVDTQKQPGNLPEAVQCGFSREELKQILQERNELKANVFLLKEELAYFQRELLTDHRVPGLLLEAMKVAVKKQRRKIKAKMLGTPEEAESSEDEDGSWLLLSNDKEDVPLVPESRIQNFFGLWYRGETEAPEAETSNPASSSLQKGEETPQQPHLQPVNSPPAPNS
Protein: Large ribosomal subunit protein uL29 (60S ribosomal protein L35) (P17078)
Organism: Rattus norvegicus (Rat)
Function: Component of the large ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P42766}.
Interaction partners:
- Large ribosomal subunit protein uL5
- Large ribosomal subunit protein uL4
- Large ribosomal subunit protein eL18
- Large ribosomal subunit protein uL18
- Large ribosomal subunit protein eL30
- Large ribosomal subunit protein eL32
- Large ribosomal subunit protein uL14
- Large ribosomal subunit protein eL15
- Large ribosomal subunit protein eL24
- Large ribosomal subunit protein eL20
Sequence:
MAKIKARDLRGKKKEELLKQLDDLKVELSQLRVAKVTGGAASKLSKIRVVRKSIARVLTVINQTQKENLRKFYKGKKYKPLDLRPKKTRAMRRRLTKHEEKLKTKKQQRKERLYPLRKYAVKA
Protein: SEC14 like lipid binding 2 (C9JZI9)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MLRKHVEFRKQKDIDNIISWQPPEVIQQYLSGGMCGYDLDGCPVWYDIIGPLDAKGLLFSASKQDLLRTKMRECELLLQECAHQTTKLGRKVETITIIYDCEGLGLKHLWKPAVEAYGEFLCMFEENYPETLKRLFVVKAPKLFPVAYNLIKPFLSEDTRKKIMVLGANWKEVLLKHISPDQVPVEYGGTMTDPDGNPKCKSK
Protein: E3 ubiquitin-protein ligase ZNRF4 (EC 2.3.2.27) (Nixin) (RING finger protein 204) (RING-type E3 ubiquitin transferase ZNRF4) (Zinc/RING finger protein 4) (Q8WWF5)
Organism: Homo sapiens (Human)
Function: E3 ubiquitin-protein ligase that acts as a negative regulator of NOD2 signaling by mediating ubiquitination and degradation of RIPK2. Also catalyzes ubiquitination and proteasomal degradation of CANX within the endoplasmic reticulum. Could have a role in spermatogenesis (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:21205830, ECO:0000269|PubMed:24387786, ECO:0000269|PubMed:28656966}; Single-pass type I membrane protein {ECO:0000255}.
Interaction partners:
- Receptor-type tyrosine-protein phosphatase S
- E3 ubiquitin-protein ligase RNF4
- PDZ domain-containing protein GIPC3
Sequence:
MPLCRPEHLMPRASRVPVAASLPLSHAVIPTQLPSRPGHRPPGRPRRCPKASCLPPPVGPSSTQTAKRVTMGWPRPGRALVAVKALLVLSLLQVPAQAVVRAVLEDNSSSVDFADLPALFGVPLAPEGIRGYLMEVKPANACHPIEAPRLGNRSLGAIVLIRRYDCTFDLKVLNAQRAGFEAAIVHNVHSDDLVSMTHVYEDLRGQIAIPSVFVSEAASQDLRVILGCNKSAHALLLPDDPPCHDLGCHPVLTVSWVLGCTLALVVSAFFVLNHLWLWAQACCSHRRPVKTSTCQKAQVRTFTWHNDLCAICLDEYEEGDQLKILPCSHTYHCKCIDPWFSQAPRRSCPVCKQSVAATEDSFDSTTYSFRDEDPSLPGHRPPIWAIQVQLRSRRLELLGRASPHCHCSTTSLEAEYTTVSSAPPEAPGQ
Protein: Putative uric acid sigma-54-dependent transcriptional regulator UacR (Uric acid regulator) (Q46802)
Organism: Escherichia coli (strain K12)
Function: Essential for both formate-dependent and formate-independent uric acid degradation. May be directly involved in the transcription of uacF in response to hypoxanthine, xanthine, and uric acid.
Interaction partners:
- RNA polymerase sigma-54 factor
- Ribosome hibernation promoting factor
Sequence:
MELATTQSVLMQIQPTIQRFARMLASVLQLEVEIVDENLCRVAGTGAYGKFLGRQLSGNSRLLRHVLETKTEKVVTQSRFDPLCEGCDSKENCREKAFLGTPVILQDRCVGVISLIAVTHEQQEHISDNLREFSDYVRHISTIFVSKLLEDQGPGDNISKIFATMIDNMDQGVLVVDDENRVQFVNQTALKTLGVVQNNIIGKPIRFRPLTFESNFTHGHMQHIVSWDDKSELIIGQLHNIQGRQLFLMAFHQSHTSFSVANAPDEPHIEQLVGECRVMRQLKRLISRIAPSPSSVMVVGESGTGKEVVARAIHKLSGRRNKPFIAINCAAIPEQLLESELFGYVKGAFTGASANGKTGLIQAANTGTLFLDEIGDMPLMLQAKLLRAIEAREILPIGASSPIQVDIRIISATNQNLAQFIAEGKFREDLFYRLNVIPITLPPLRERQEDIELLVHYFLHLHTRRLGSVYPGIAPDVVEILRKHRWPGNLRELSNLMEYLVNVVPSGEVIDSTLLPPNLLNNGTTEQSDVTEVSEAHLSLDDAGGTALEEMEKQMIREALSRHNSKKQVADELGIGIATLYRKIKKYELLNT
Protein: adenylate cyclase (EC 4.6.1.1) (ATP pyrophosphate-lyase) (Adenylyl cyclase) (Q583I0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Phosphodiesterase
- Phosphodiesterase
- 3', 5'-cyclic nucleotide phosphodiesterase, putative
Sequence:
MIYHSETDGPHTPAASKSAGYAVWHCRLSTVMALLLFSNVLPAHSEGNIKVKVYSFIYSPYVEYRLVEAINAGLNASFAARQWTVAPNVTVQVVPPPPNNVEVVDALQRVATTEKGLFVVFGPLSDRRTVLLLPLLKREDLVAFAPSTGSSIVRGWNPNIYFIRVSPTAELIALVRHAVSQLRLLRIGFMYLQNASFGDSEYKHAVELFSHMGRELCGVFTKNIDDEGLYGSHNFDFLWNDFALTEPQGVILFAPPGKDSIQFMKKMVADKRTRDAYVLAPSALEFSIVGAWREALEAAGAPLKFGQVILTGTNPLAADIRYQAIRRFQDHMRSYLSANPGVTVFNGTDNFDHDDVDGRLMVYGWIAGEVLSQALSSREWLTSRKAFMESLYNQRRYVIDDLVIGDFGGDCKGGAGERGAACNCNQGGSVVYINVIGSSYRLFPVNGGVTIFDSKKCYINKPRIPSPMSILSLTLFDTALPVDTYASMSAALHSPISEKDSVLSRQLFFHSMASSSAESARTLQHQLDTRSVTAVFGVVDDAMLSIAEVAFVDPVMLTPRLHHRGKNVIQLSPTLEQQLFVVVGYVTNTSASAPMSAIVRGADATIIEVALRKIVWMHGGTLQTVAVLDDNATLVGRLPNRGNAFVIGLAPGDPSLLAAHLDRNPDVRVLIPFFDVALMYDELVSAFNGNPNAERVQFATSLPHWADANTSSEIVREFHTALPDSSAWKPLPLLGYAAARFAQAVLPRMEYVTPKTLLDTIYMQSIITADEMRYGPFEEEEEKECFTANDPVPEQGEVCVVNYGATRISMWSLARALNASVPPLTSPVTPLIRYADPNAIKLSSAQLAGVIVGSLVALALFAAPLVVVLYVLRRGARDNDSAPKEPVEPVTLIFTDIESSTAQWAAHPELMPDAVSTHHRLIRSLIVQYGCYEVKTVGDSFMIACKKPFAAAQLASDLQRCFLCHEWGTTAFDDSYREFERQRADDDNEYKAPSARLDPEVYRQLWNGLRVRVGVHTGLCDIRHDEVTKGYDYYGRTSNMAARTESVANGGQVLLTRAAYLSLSNSERGQLDVTALGSMSLRGVPEPVEMYQLNAVVGRSFAALRLDHEVVEDGDLSSTSFSDTGSLRGVLSGTSQMIDSCLHAVFGTVPLSQRQKLLMPLCERWQVSLPPSSKATWNEEYCEGVIRRIAVKVGRVVDHCAAVGSEHSVSTLRSASLIIISNHGLERELHGN
Protein: Flavin reductase like domain-containing protein (Q581Y7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MLSWNPESYVSEAVSRILAEEAKQGRGGAIPSYYDAVTSHLEAHELSKSIKVALEEQRRQNIGISCDIGGNVLEILFNPVDIEDAGVAEERVKKCVADIGCLFGNVSDELNSLNGKSGLVAVSEDVLDILHHLQSMGLLTNFRFNPVSEKLGCILSATDRSSILKSMVLYNSQVEWPKGMTLNFTDYMKAWLVDRVAARLEVLNEHRGCLIRLEDFARVFGTSRGSSVWKYGVSVSDLDGEQKFIGCLELDALRPTAAAHAVEDPFFDHLGMQSCVACCRTTTTSYCLANALSVCSHGEKALFFVREWREVNGPESKDSLLSFTLYFGYGKPISDEGDVRIGENDDKRIYLHSEKDQIVRTYKQMGDVKRYESHVETVIANSKNADLFHNISGYIGETTCENLERAMSLFPRMCVVASCIGNENAVCVSVLKAADVLRGDATFVFCISQRSPLFNHVFAPRSQVTLNFLFDNAQAVCQAINDTYPLWINETGNEPVVFESESRTYVTTKALMDISKQVAFETAESFLVGEEVLVVGRCLDSIPSTVVINVKNTLVLQDHVPPQEFYPFLFTIVHKIYGTVGFVGYGCQLCSLSPLTMYIYSPIESSQFALDEVYTGPKCNLTFLSSFGAPIFDGKDFEELGCGMPMAASSVSSLPQQNIYFQVEGMLIRIVRDISDKYVICVVAANECRFNQTDPCKLLVRPDDERLIPA
Protein: Fatty acid metabolism regulator protein (P0A8V6)
Organism: Escherichia coli (strain K12)
Function: Multifunctional regulator of fatty acid metabolism. Represses transcription of at least eight genes required for fatty acid transport and beta-oxidation including fadA, fadB, fadD, fadL and fadE. Activates transcription of at least three genes required for unsaturated fatty acid biosynthesis: fabA, fabB and iclR, the gene encoding the transcriptional regulator of the aceBAK operon encoding the glyoxylate shunt enzymes.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00696}.
Interaction partners:
- HTH-type transcriptional repressor FabR
- 3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase
- Acyl-coenzyme A dehydrogenase
- Long-chain-fatty-acid--CoA ligase
- 3-oxoacyl-[acyl-carrier-protein] synthase 1
- HTH-type transcriptional regulator GntR
- Met repressor
- Putative L-lactate dehydrogenase operon regulatory protein
- Long-chain fatty acid transport protein
- Fatty acid oxidation complex subunit alpha
Sequence:
MVIKAQSPAGFAEEYIIESIWNNRFPPGTILPAERELSELIGVTRTTLREVLQRLARDGWLTIQHGKPTKVNNFWETSGLNILETLARLDHESVPQLIDNLLSVRTNISTIFIRTAFRQHPDKAQEVLATANEVADHADAFAELDYNIFRGLAFASGNPIYGLILNGMKGLYTRIGRHYFANPEARSLALGFYHKLSALCSEGAHDQVYETVRRYGHESGEIWHRMQKNLPGDLAIQGR