wanglab/gogpt-training-data huggingface dataset:
Protein: Small ribosomal subunit protein uS14 (40S ribosomal protein S29) (Q76P36)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- Small ribosomal subunit protein eS30
- Small ribosomal subunit protein eS10
- Small ribosomal subunit protein eS26
- Large ribosomal subunit protein eL33
- Small ribosomal subunit protein eS28
- Small ribosomal subunit protein uS13
- Small ribosomal subunit protein eS24
- Small ribosomal subunit protein uS3
- Small ribosomal subunit protein uS11
- Small ribosomal subunit protein eS25
Sequence:
MARELWLTHPRNFGPGSRTCRKCGNHHGIIRKYDLNMCRRCFRTDAEAIGFNKYR
Protein: Prohibitin 1 (Protein l(2)37Cc) (P24156)
Organism: Drosophila melanogaster (Fruit fly)
Function: Required for larval metabolism or for the progression of the larva into a pupa.
Interaction partners:
- Prohibitin
- Paraplegin, isoform A
- AFG3 like matrix AAA peptidase subunit 2, isoform A
- Mitochondrial-processing peptidase subunit alpha
- ATP-dependent zinc metalloprotease YME1L
- Heat shock 70 kDa protein cognate 5
- Eukaryotic translation initiation factor 5A
- IP15825p
- 14-3-3 protein zeta
- Small ribosomal subunit protein uS2
Sequence:
MAAQFFNRIGQMGLGVAVLGGVVNSALYNVEGGHRAVIFDRFTGIKENVVGEGTHFFIPWVQRPIIFDIRSQPRNVPVITGSKDLQNVNITLRILYRPIPDQLPKIYTILGQDYDERVLPSIAPEVLKAVVAQFDAGELITQREMVSQRVSQELTVRAKQFGFILDDISLTHLTFGREFTLAVEMKQVAQQEAEKARFVVEKAEQQKLASIISAEGDAEAAGLLAKSFGEAGDGLVELRRIEAAEDIAYQLSRSRGVAYLPSGQSTLLNLPSTIAQ
Protein: S-adenosylmethionine decarboxylase proenzyme (AdoMetDC) (SAMDC) (EC 4.1.1.50) [Cleaved into: S-adenosylmethionine decarboxylase alpha chain; S-adenosylmethionine decarboxylase beta chain] (P91931)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Spermidine synthase, isoform A
- S-adenosylmethionine synthase
- Ornithine decarboxylase 1
- Ornithine decarboxylase 2
- Arginase
- Probable deoxyhypusine synthase
- Eukaryotic translation initiation factor 5A
- Deoxyhypusine hydroxylase
- Trifunctional purine biosynthetic protein adenosine-3
- Nitrilase and fragile histidine triad fusion protein NitFhit
Sequence:
MLENGSHFFEGVEKLLEIWFEESSNGDDDLRNISRSDWENVLSNVNCQIISTSKNDIIDAFVLSESSMFVSKRRWILKTCGTTTPLKCLGQLLKLAEANGYNVVADLFYSRKNFTRPEAQITPHQGFTEEVTYLDSIFPNGRSYCLGSMNLECWYLYTFSRSDIKITPQLISDEKNVDSDPDQTIEILMQDLDPETMSIFYKNKFNDANGATVKSGIDTILPTMHIDDFLFDPCGYSMNGINDKGEYMTIHITPENQFSYVSFETNVALSNYRKLINQVINTFKPGKFIVTIFANKCSLAYETMKELEVEYSQGSHWKRTDMQCCNFPSYNLLFAQYSHSEKTGDYL
Protein: Musculin (Activated B-cell factor 1) (ABF-1) (Class A basic helix-loop-helix protein 22) (bHLHa22) (O60682)
Organism: Homo sapiens (Human)
Function: Transcription repressor capable of inhibiting the transactivation capability of TCF3/E47. May play a role in regulating antigen-dependent B-cell differentiation.
Subcellular location: Nucleus.
Interaction partners:
- Transcription cofactor HES-6
- Aldo-keto reductase family 7 member A3
- Myogenic factor 5
- Transcription factor E2-alpha
- Myoblast determination protein 1
Sequence:
MSTGSVSDPEEMELRGLQREYPVPASKRPPLRGVERSYASPSDNSSAEEEDPDGEEERCALGTAGSAEGCKRKRPRVAGGGGAGGSAGGGGKKPLPAKGSAAECKQSQRNAANARERARMRVLSKAFSRLKTSLPWVPPDTKLSKLDTLRLASSYIAHLRQLLQEDRYENGYVHPVNLTWPFVVSGRPDSDTKEVSAANRLCGTTA
Protein: SEC14 cytosolic factor (Phosphatidylinositol/phosphatidylcholine transfer protein) (PI/PC TP) (P46250)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Required for transport of secretory proteins from the Golgi complex. Catalyzes the transfer of phosphatidylinositol and phosphatidylcholine between membranes in vitro (By similarity).
Subcellular location: Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
Interaction partners:
- Phosphatidylinositol transfer protein SFH5
- Prefoldin subunit 3
- Glycerophosphocholine phosphodiesterase GDE1
- Ras-related protein SEC4
Sequence:
MTTMTTEEILASYPQITAPTDQTGYTSNLTPEQKTTLDIFRQQLTELGYKDRLDDASLLRFLRARKFDIQKAIDMFVACEKWREDFGVNTILKDFHYEEKPIVAKMYPTYYHKTDKDGRPVYFEELGKVDLVKMLKITTQERMLKNLVWEYEAMCQYRLPACSRKAGYLVETSCTVLDLSGISVTSAYNVIGYVREASKIGQDYYPERMGKFYLINAPFGFSTAFKLFKPFLDPVTVSKIHILGYSYKKELLKQIPPQNLPVKFGGMSDVSDDDLLLKDVGPWRDPEFIGPEGECPRAYNI
Protein: Asparaginyl endopeptidase (R4TUW8)
Organism: Angiostrongylus cantonensis (Rat lungworm)
Interaction partners:
Sequence:
MAVLLWTFFFTLLCLGGAVEVQNAQSSANQKADIHVLLVAGSNGWWNYRHQADIAHAYHLMRNNGIPESNIIVMMYDDIANDPDNPYPGKLFNKPHGPDVYHGVKIDYKGDSVNPKNFLSVLQGKSNGVSGGNGRVLNSTANDRVFVYFADHGSDGLICFPNDIWSKHDLNKALQEMHEKKQYGQLVFYLEACESGSMFEGTLDKKMNIYAVTAANAVESSWGTYCYNDMNLPCLGDLFSVNWIEDSETHNINVETLMKQFDDVKKLTNLSHVMHYGNLKIATEPVRWFEGEVQTTVVPTTTTYDNVEGQYPKVSWPARDIELMHLQKLQETTNNALVSTALKQRITKIHEDRQKIEVVFKSLVANLLPNAEDRKQVMDGRNPVKDLKCHNDVVKAFDSICIDVNKFDYALKYIYMLNNLCVKVGDAEKIISSMHPTCSTIGDPYL
Protein: MADS-box transcription factor PHERES 2 (Agamous-like MADS-box protein AGL38) (Q7XJK8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable transcription factor involved in the development of gametophytes and seeds.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00251}.
Interaction partners:
- Agamous-like MADS-box protein AGL62
- Agamous-like MADS-box protein AGL28
- At2g13960
- Homeobox-leucine zipper protein HDG3
- MADS-box protein AGL73
- Homeodomain-like superfamily protein
- Agamous-like MADS-box protein AGL61
- Polycomb group protein FERTILIZATION-INDEPENDENT SEED 2
- At5g46950
- Histone-lysine N-methyltransferase MEDEA
Sequence:
MKRKMKLSLIENSVSRKTTFTKRKKGMTKKLTELVTLCGVEACAVVYSPFNSIPEAWPSREGVEDVVSKFMELSVLDRTKKMVDQETFISQRIAKEKEQLQKLRDENHNSQIRELMFGCLKGETNVYNLDGRDLQDLSLYIDKYLNGLTRRIEILIENGESSSSLPLPIVANAAAPVGFDGPMFQYHNQNQQKPVQFQYQALYDFYDQIPKKIHGFNMNMNKDSNQSMVLDLNQNLNDGEDEGIPCMDNNNYHPEIDCLATVTTAPTDVCAPNITNDL
Protein: MAP2 RNA trans-acting protein 2 (Q2QC85)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MAELVQGQSAPVGLKAEDFVDALHRVRQIAAKIDSIPHLNNSTPLVDPSVYGYGVQKRPLDDGVGNQLGALVHQRAVITEEFKVPDKMVGFIIGRGGEQISRIQAESGCKIQIASESSGIPERPCVLTGTPESIEQAKRLLGQIVDRCRNGPGFHNDIDGNSTIQELLIPASKVGLVIGKGGETIKQLQERTGVKMVMIQDGPLPTGADKPLRITGDPFKVQQAREMVLEIIREKDQADFRGVRSDFTSRAGGGSIEVSVPRFVVGIVIGRNGEMIKKIQNGTGVRIQFKPDDGISPERAAQVMGPPDRCQHAARIINELILTAQEREILGGLTGTRGRGRGRGDWSVGTPGGIQEITYTVPADKCGLVIGKGGENIKSINQQSGAHVELQRNPPPNTDPNLRIFTIRGAPQQIEVARHLIDEKVGGASLGAPTAFGQSPFSQPPAAPHQNTFPPRAFPNIAAKVNGNPHSTPVSGPPAFLTQGWGSTYQAWQQPTQQVPSQQSQPQNSQPDYSKAWEDYYKKQGHTTSAAPQASSPPDYTMAWAEYYRQQAAFYGQTLGQAQAHSQEQ
Protein: Protein SOB FIVE-LIKE 2 (AtSOFL2) (Q9CA45)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in cytokinin-mediated development. Together with SOFL2, triggers the endogenous content of specific bioactive cytokinins derived from the biosynthetic intermediates trans-zeatin riboside monophosphate (tZRMP) and N(6)-(Delta(2)-isopentenyl)adenosine monophosphate (iPRMP) such as N-glucosides trans-zeatin 7-glucoside (tZ7G), cis-zeatin 7-glucoside (cZ7G) and N(6)-(Delta(2)-isopentenyl)adenine 7-glucoside (iP7G).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:29467189}. Nucleus {ECO:0000269|PubMed:29467189}.
Interaction partners:
- Protein SUPPRESSOR OF PHYTOCHROME B 5
- Uncharacterized protein
- Protein SOB FIVE-LIKE 4
- Protein SOB FIVE-LIKE 5
- Protein SOB FIVE-LIKE 3
- Transmembrane protein
- Putative F-box/FBD/LRR-repeat protein At1g66300
Sequence:
MESPRIHGGAEEKSSCESGWTMYIEDTFHGNHHSEVVYEEEDDGFSVKEVDDDGDGDEDDDDDDDDDSSNNESDDSMTSDASSWPSTHQPPRSTKNHAAAKNSNAKQVNNQTENRVRDRFSDEGEESELKARTRTTAASRVKVSKTK
Protein: Fatty acid-binding protein, intestinal (Intestinal fatty acid-binding protein) (Q8AX65)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MTFNGTWKVDRNENYEKFMEQMGVNMEKRKLAAHDNLKITLEQTGDKFNVKEVSTFRTLEINFTLGVTFDYSLADGTELTGSWVIEGDTLKGTFTRKDNGKVLTTVRTIVNGELVQSYSYDGVEAKRIFKRA
Protein: SCART2 splice variant B (Scavenger receptor family member expressed on T cells 2) (B3F5L5)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MAFSFLRLWPLLLLTCWTLVPDLALENFVSFLGGDNKCEGQVRLRNGGQWGLMCADGLGMQEASVICRELGCGSVKFMPRYVLTPEEMRQPWLYDAQCHGNESTFLECRLGSWGTISGCKCQCVAVITCSGGTTLQMGLVDGGSPCAGTAQATGASNFALRCDLHEKEAGVVCRQLECGTALQWSRAHDGTNGNQEQKYLTCQGTETNILQCLINVNVLEQCDLLTYTQVVCTGHVEARLLGGVHPCEGRLEVLRGLTWGTVCHDDLDLPMAHVVCRELGCGTAVSILGSSHFGYGSGPLWTEAFRCMGNESLLFHCLREPGHQCGHDQDAALICSGEKFRLVNGSSRCEGRVELLVQDAWQPLCAANWDLADATVLCHQLNCGYAVATPQGGHFGNVEGPIRTDVFHCVGTEPHLLSCPTSTLGAQACALGNSASALCSGLQDALRLREGQSHCDGRVEVFLDGTWGRVLDSAWDLRDAAVVCRQLGCGEAQLAYDAPAPGHKTIPVGLSLVHCLGSETHLTQCNVSASLLVHAGTLRDAGVVCSGSLHIRLAAGKNRCAGRVEVFYQGTWGTVCDDAWDLQDAHVVCRQLGCGHALSAPRAAHFGAGTGRIWMDELGCMGEEAALWECQSGGWGQQDCGHKEDAGVICSEFIDVRLQEHSQPCTGRLEVFYNGTWGGVCQSLNAASLRVLCEHLGCGSQGQLLARPRGSSTIETVWLKSIQCRDKHDMSLWQCPSEPWNRHSCLRGEEAWLACAEKTEVSQDMEQIANCSSTLSCPEEGALRVLGGENGCSGRVELWHGGSWGTVCDDSWDLADAEVVCRQLGCGPAIAALQNAAFGPGSGPVWLDEVGCRGSELSLGACQAEPWGYGDCSHKEDAGVRCLGIPGTMASGNSSAPPPVPEFWTMPEIACLVLGCLLGIVFLVLAVQWCHSRAIGLGSGAVAELPSEVVYECIETVPMDEKEEPAASQSPVQDEDYDDAEEPKDSPGEDMEAGHH
Protein: Chloride channel CLIC-like protein 1 (Q9XVW6)
Organism: Caenorhabditis elegans
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- EOG090X04TT
- Torsin-like protein
- Cytochrome c oxidase assembly protein COX11
- Torsin-1B
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
- GEX Interacting protein
- Protoheme IX farnesyltransferase, mitochondrial
- Cytochrome c oxidase subunit 1
- Thioredoxin domain-containing protein
Sequence:
MKIIWVTLLLLVPQLFATQDIDEEFTHENVWKDPNDPTSGESPPASKRLLSVRNQVQKFQPDQSLRLILRQLLHETKIDYHLEGSIKKDVQIKISRHSMSVLSKYLKNDEADLAEEREAVRSALSNIFSVKPPAPDRTWQDTFVTLQPFIFTLNIFILPAAAFVVLRSIVRPRNFWILVLSTALLVSMYSGYSKKYQEAESRRFAQFQEHAHDSCATEGLLSRMVEILASPFQYRQKSKCLKYIESQTISIFHEISIIEVFSETISGGFFAFFSGSAKHFNLFFRNLYDGAPLIAQIVMTIFLVLMLGAIRTPFFSYEPIWLNFCSSSIGKIAGWLDGEPPQQPAPQLLITAKEMKRLEQARNKKPEMISYPTSEREDVVSGSENGNEKKSDNEREESMKMEEDSAPVESSLEDDLSLLGESSEDEDEEKVNESPAKIDSTTLSESSF
Protein: 5'-nucleotidase (EC 3.1.3.5) (X6RM59)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|RuleBase:RU361276}.
Interaction partners:
Sequence:
MDRAAVARVGAVASASVCALVAGVVLAQYIFTLKRKTGRKTKIIEMMPEFQKSSVRIKNPTRVEEIICGLIKGGAAKLQIITDFDMTLSRFSYKGKRCPTCHNIIDNCKLVTDECRKKLLQLKEKYYAIEVDPVLTVEEKYPYMVEWYTKSHGLLVQQALPKAKLKEIVAESDVMLKEGYENFFDKLQQHSIPVFIFSAGIGDVLEEVIRQAGVYHPNVKVVSNFMDFDETGVLKGFKGELIHVFNKHDGALRNTEYFNQLKDNSNIILLGDSQGDLRMADGVANVEHILKIGYLNDRVDELLEKYMDSYDIVLVQDESLEVANSILQKIL
Protein: Ras guanine nucleotide exchange factor M (RasGEF domain-containing protein M) (Q8SSQ3)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Promotes the exchange of Ras-bound GDP by GTP.
Interaction partners:
Sequence:
MWQKPSLTKSMMNEVSSNSPKSPTLTSSPSTQSFANRVLPGRNLDGGGGGSNRLIFGGSGGGSGGGSLPSSPVSSPVNPFNLNGGGGGKSSRRRGVTVAAGSEQVETRRKILLGNSRPFRRRARSMEILNSWDFIPYQKKPSDDEQGQVDQYIQGENDEDLTSYESYITNNNTTTTTNTNNSNNNNSNNDGSGSGSGAGGSFIGTTTSAKTTSTTSTSAATTTTTTTTSSSSSSPSSSSPSSTSPTIASNNDNNNKIEPPQPSKIANSVPPLTLSQSQTQQQQQQKVKPPPPSPRFSTNSSGSQSPPVPPRSSKSLGLSNDFSISLSSSMSSNSLLISGSINTLPTSSSSSSSVGGSGASAASASISSSSSLSSSSLSVSKLIYENNEENKFVVVSGPKDQLVEYLCNKNKLDFSFVNSFILSFRYFIEPEELFNHLMVKYETKVQTTSSIKVSKQFEEIQDRIRQNILIIISVWVDCNYSDFEDNLSLHKRLFKLVQDTPHAVFLRDSIDRQKVSKIPILDLYEKLKDELLLSLSPRGSLSGSGGISNNNNGSDLKNSNNGNNSSNNNNSSSNSSSSSSSSDIKNIKNSFFSLTTMMDWLMNHLSIGYATADSILKKLFKLKVIGSLGSGGGFTNISSSHTNSNSKSSKEELYFFTSTKSIINKEIYSRSFMDYSPQDIAKQLTLIEFKLFQSVKMKELYHKSWTISKSKFENSPNIMSLITMSNKIANWVATEVVTTPHPKKRVEVLKRFISVAEHCKKINNFNTLMEVISGLSNSAVSRLKETWKSLPTRYVNSFNSLQNFLKTDENWKSYRQTLKTKETPCLPYLGLFLQDINFIEDGNSNLSSENDWVNFKKMNLLTSVFTEIQYFQRHPYFSFSTHQNIQTYFEKDIVILPEKELYAFSKFIESPSNPLFRLSKSKNQSIFNI
Protein: UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase (EC 6.3.2.13) (Meso-A2pm-adding enzyme) (Meso-diaminopimelate-adding enzyme) (UDP-MurNAc-L-Ala-D-Glu:meso-diaminopimelate ligase) (UDP-MurNAc-tripeptide synthetase) (UDP-N-acetylmuramyl-tripeptide synthetase) (P22188)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan. Is also able to use many meso-diaminopimelate analogs as substrates, although much less efficiently, but not L-lysine.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- UDP-N-acetylmuramate--L-alanine ligase
- UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase
- UDP-N-acetylglucosamine--N-acetylmuramyl-
- Peptidoglycan D,D-transpeptidase FtsI
- UDP-N-acetylmuramoylalanine--D-glutamate ligase
- Phospho-N-acetylmuramoyl-pentapeptide-transferase
- Probable peptidoglycan glycosyltransferase FtsW
- UDP-N-acetylglucosamine 1-carboxyvinyltransferase
- D-alanine--D-alanine ligase B
- UDP-N-acetylenolpyruvoylglucosamine reductase
Sequence:
MADRNLRDLLAPWVPDAPSRALREMTLDSRVAAAGDLFVAVVGHQADGRRYIPQAIAQGVAAIIAEAKDEATDGEIREMHGVPVIYLSQLNERLSALAGRFYHEPSDNLRLVGVTGTNGKTTTTQLLAQWSQLLGEISAVMGTVGNGLLGKVIPTENTTGSAVDVQHELAGLVDQGATFCAMEVSSHGLVQHRVAALKFAASVFTNLSRDHLDYHGDMEHYEAAKWLLYSEHHCGQAIINADDEVGRRWLAKLPDAVAVSMEDHINPNCHGRWLKATEVNYHDSGATIRFSSSWGDGEIESHLMGAFNVSNLLLALATLLALGYPLADLLKTAARLQPVCGRMEVFTAPGKPTVVVDYAHTPDALEKALQAARLHCAGKLWCVFGCGGDRDKGKRPLMGAIAEEFADVAVVTDDNPRTEEPRAIINDILAGMLDAGHAKVMEGRAEAVTCAVMQAKENDVVLVAGKGHEDYQIVGNQRLDYSDRVTVARLLGVIA
Protein: Gibberellin 2-beta-dioxygenase 8 (EC 1.14.11.13) (GA 2-oxidase 8) (Gibberellin 2-beta-hydroxylase 8) (Gibberellin 2-oxidase 8) (O49561)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the 2-beta-hydroxylation of gibberellins (GA) precursors, rendering them unable to be converted to active GAs. Hydroxylates the C20-GA GA12 and GA53, but is not active on C19-GAs, like GA1, GA4, GA9 and GA20.
Interaction partners:
- Gibberellin 3-beta-dioxygenase 1
- Gibberellin 3-beta-dioxygenase 3
- Ent-kaur-16-ene synthase, chloroplastic
- Gibberellin 3-beta-dioxygenase 2
- Gibberellin 3-beta-dioxygenase 4
- Gibberellin 20 oxidase 4
- Gibberellin 20 oxidase 1
- Gibberellin 20 oxidase 2
- Gibberellin 20 oxidase 3
- Ent-kaurenoic acid oxidase 2
Sequence:
MDPPFNEIYNNLLYNQITKKDNDVSEIPFSFSVTAVVEEVELPVIDVSRLIDGAEEEREKCKEAIARASREWGFFQVINHGISMDVLEKMRQEQIRVFREPFDKKSKSEKFSAGSYRWGTPSATSIRQLSWSEAFHVPMTDISDNKDFTTLSSTMEKFASESEALAYMLAEVLAEKSGQNSSFFKENCVRNTCYLRMNRYPPCPKPSEVYGLMPHTDSDFLTILYQDQVGGLQLIKDNRWIAVKPNPKALIINIGDLFQAWSNGMYKSVEHRVMTNPKVERFSTAYFMCPSYDAVIECSSDRPAYRNFSFREFRQQVQEDVKKFGFKVGLPRFLNHVY
Protein: Serine/threonine kinase 19 (B7ZLI8)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MLVCASPPPLPALTGLRDDKLTLLSSSPGLGGTPGETVRHCSAPEDPIFRFSSLHSYPFPGTIKSRDMSWKRHHLIPETFGVKRRRKRGPVESDPLRGEPGSARAAVSELMQLFPRGLFEDALPPIVLRSQVYSLVPDRTVADRQLKELQEQGEIRIVQLGFDLDAHGIIFTEDYRTRVLKACDGRPYAGAVQKFLASVLPACGDLSFQQDQMTQTFGFRDSEITHLVNAGVLTVRDAGSWWLAVPGAGRFIKYFVKGRQAVLSMVRKAKYRELLLSELLGRRAPVVVRLGLTYHVHDLIGAQLVDCISTTSGTLLRLPET
Protein: BBSome complex member BBS5 (Bardet-Biedl syndrome 5 protein homolog) (Q9CZQ9)
Organism: Mus musculus (Mouse)
Function: The BBSome complex is thought to function as a coat complex required for sorting of specific membrane proteins to the primary cilia. The BBSome complex is required for ciliogenesis but is dispensable for centriolar satellite function. This ciliogenic function is mediated in part by the Rab8 GDP/GTP exchange factor, which localizes to the basal body and contacts the BBSome. Rab8(GTP) enters the primary cilium and promotes extension of the ciliary membrane. Firstly the BBSome associates with the ciliary membrane and binds to RAB3IP/Rabin8, the guanosyl exchange factor (GEF) for Rab8 and then the Rab8-GTP localizes to the cilium and promotes docking and fusion of carrier vesicles to the base of the ciliary membrane. The BBSome complex, together with the LTZL1, controls SMO ciliary trafficking and contributes to the sonic hedgehog (SHH) pathway regulation. Required for BBSome complex ciliary localization but not for the proper complex assembly (By similarity).
Subcellular location: Cell projection, cilium membrane {ECO:0000250}. Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:15137946}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriolar satellite {ECO:0000250}. Note=Localizes to basal bodies.
Interaction partners:
- BBSome complex member BBS4
- BBSome complex member BBS2
- Tetratricopeptide repeat protein 8
- BBSome complex member BBS1
- BBSome complex member BBS7
- Protein PTHB1
- BBSome interacting protein 1
- Leucine zipper transcription factor-like protein 1
- BBSome complex assembly protein BBS10
- Chaperonin-containing T-complex member BBS12
Sequence:
MSVLDVLWEDRDVRFDVSSQQMKTRPGEVLIDCLDSIEDTKGNNGDRGRLLVTNLRIIWHSLALPRVNLSIGYNCILNITTRTANSKLRGQTEALYILTKCNTTRFEFIFTNLVPGSPRLFTSVIAVHRAYETSKMYRDFKLRSAVIQNKQLRLLPQEHVYDKINGVWNLSSDQGNLGTFFITNVRIVWHANMNDSFNVSIPYLQIRSIKIRDSKFGLALVIESSQQSGGYVLGFKIDPVEKLQESVKEINSLHKVYSASPIFGVNYEMEEKPQPLEALTVEQIQDDVEIDSDDHTDAFVAYFADGNKQQDREPVFSEELGLAIEKLKDGFTLQGLWEVMS
Protein: Transcription factor IIIA (TFIIIA) (Q8VHT7)
Organism: Mus musculus (Mouse)
Function: Involved in ribosomal large subunit biogenesis. Binds the approximately 50 base pairs internal control region (ICR) of 5S ribosomal RNA genes. It is required for their RNA polymerase III-dependent transcription and may also maintain the transcription of other genes (By similarity). Also binds the transcribed 5S RNA's (By similarity).
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- TATA-box-binding protein
- General transcription factor 3C polypeptide 1
- General transcription factor 3C polypeptide 5
- General transcription factor IIIC, polypeptide 3
- Transcription factor IIIB 90 kDa subunit
- Transcription factor TFIIIB component B'' homolog
Sequence:
MEPRVSVAEAVSSLTIADAFVGACEGPAPPRPALPSRFICSFPDCSASYNKAWKLDAHLCKHTGERPFVCDYEGCGKAFIRDYHLSRHVLIHTGEKPFVCADDGCNQKFNTKSNLKKHIERKHGNPQKQYVCSYEGCKKAFKKHQQLRTHQCQHTSEPLFRCTHEGCGKHFASPSRLKRHGKVHEGYLCQKGCSFMGKTWTELLKHMREAHKEDITCNVCQRMFKRRDYLKQHMKTHAPERDVYRCPRQGCGRTYTTVFNLQSHILSFHEEKRPFVCEHAGCGKTFAMKQSLMRHSVVHDPDKKRMKLKVRAPRERRSLASRLSGYFPPKRKQEPDYSLPNASAESSSSPEAQLPPPAALLTVC
Protein: Antileukoproteinase (ALP) (BLPI) (HUSI-1) (Mucus proteinase inhibitor) (MPI) (Protease inhibitor WAP4) (Secretory leukocyte protease inhibitor) (Seminal proteinase inhibitor) (WAP four-disulfide core domain protein 4) (P03973)
Organism: Homo sapiens (Human)
Function: Acid-stable proteinase inhibitor with strong affinities for trypsin, chymotrypsin, elastase, and cathepsin G. Modulates the inflammatory and immune responses after bacterial infection, and after infection by the intracellular parasite L.major. Down-regulates responses to bacterial lipopolysaccharide (LPS) (By similarity). Plays a role in regulating the activation of NF-kappa-B and inflammatory responses. Has antimicrobial activity against mycobacteria, but not against salmonella. Contributes to normal resistance against infection by M.tuberculosis. Required for normal resistance to infection by L.major. Required for normal wound healing, probably by preventing tissue damage by limiting protease activity (By similarity). Together with ELANE, required for normal differentiation and proliferation of bone marrow myeloid cells.
Subcellular location: Secreted {ECO:0000269|PubMed:2039600, ECO:0000269|PubMed:24352879, ECO:0000269|PubMed:3462719, ECO:0000269|PubMed:3485543}.
Interaction partners:
- Neutrophil elastase
- Progranulin
- Neutrophil gelatinase-associated lipocalin
- Cathepsin G
- Beta-defensin 103
- Lactotransferrin
- Chymotrypsinogen B2
- Chymotrypsinogen B
- Tubulin beta-1 chain
- Elafin
Sequence:
MKSSGLFPFLVLLALGTLAPWAVEGSGKSFKAGVCPPKKSAQCLRYKKPECQSDWQCPGKKRCCPDTCGIKCLDPVDTPNPTRRKPGKCPVTYGQCLMLNPPNFCEMDGQCKRDLKCCMGMCGKSCVSPVKA
Protein: Phosphoserine phosphatase RsbX (EC 3.1.3.3) (Sigma-B negative effector) (P17906)
Organism: Bacillus subtilis (strain 168)
Function: Negative regulator of sigma-B activity. Dephosphorylates RsbS. Plays a role both in maintaining low sigma-B activity during growth and in reestablishing prestress sigma-B activity after induction. Could have a negative feedback role by indirectly communicating sigma-B protein levels.
Interaction partners:
- RNA polymerase sigma-B factor
- Serine/threonine-protein kinase RsbT
- Serine-protein kinase RsbW
- RsbT antagonist protein RsbS
- Anti-sigma-B factor antagonist
- RsbT co-antagonist protein RsbRA
- Phosphoserine phosphatase RsbU
- RsbT co-antagonist protein RsbRB
- RsbT co-antagonist protein RsbRD
- RsbT co-antagonist protein RsbRC
Sequence:
MIQVEENEHIQTLVYQLNKEGKSICGDSFFMKADDKELICAVADGLGSGSLANESSAAIKDLVENYASEDVESIIERCNQAMKNKRGATASILKINFEQRQFTYCSVGNVRFILHSPSGESFYPLPISGYLSGKPQKYKTHTATYEKGSKFIIHTDGLNVPDIRSHLKKGQSVEEISNSLKMYTTSRKDDLTYILGQLS
Protein: Probable methylxanthine N7-demethylase NdmC (EC 1.14.13.128) (7-methylxanthine demethylase) (F0E1K6)
Organism: Pseudomonas sp. (strain TJI-51)
Function: Involved in the caffeine degradation, which is the essential first step for assimilating the carbon and nitrogen in caffeine. Probably catalyzes the N7-demethylation of 7-methylxanthine to produce xanthine and formaldehyde.
Interaction partners:
Sequence:
MHAENSFVIDDWYPVGALAETVSGRKYHTRILGTEIWYQLADGTVSAGLADNTAELASKSIYGLLWVSLSDNPRDVIAIPEFAEADRRVVSAGSIRVATSGLRVIENFLDMAHFPFVHTDILGAEPLTEVAAYDVEIDEAADEIRAVNCRFPQPKGSAAASEPVEMQYVYRIARPFIAILYKTCVIDANRLDVLGLFVQPVDQESSIAHTIMCYLDDINTDKQLRDFQQRIFGQDIMILINQVPKALPLNPRHETPVRADALSSAYRRWLNDRNVTFGTTRG
Protein: Dystroglycan 1 (Dystroglycan) (Dystrophin-associated glycoprotein 1) (Q8JHU7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane, sarcolemma {ECO:0000256|ARBA:ARBA00004135}. Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}. Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}. Nucleus, nucleoplasm {ECO:0000256|ARBA:ARBA00004642}. Postsynaptic cell membrane {ECO:0000256|ARBA:ARBA00034100}. Secreted, extracellular space {ECO:0000256|ARBA:ARBA00004239}.
Interaction partners:
Sequence:
MRNKLREFRDGGRPMLGQWDRTLVVLLMALALTVTDVQASWDQMEVLGDVKLEASMHSAVLSDIREAEAVVAAVSQPSGFPDSSAVVGRVFRLQVPIKAKDSGSIVKITEASKDVLPAWLHWDAESGTLQGLPLETDKGVHYISVSVSNESKVSQSPDVFSIEVHPEEHAETDPFQLAIQQSASNDAQPFICGNEEPVTVLTVILDADLTKMSSKQRVELLAKMKKFSGMGLQHMKILPVVNNRLFDMSAFMAGPGNAKKVVENGALLSWKLGCSLDQSSIPDISSVQVPAKEGTMSAQLGYPVVGWHIANKKPHVPKRVRRQLNNTPTPIPSLLPPTTYPEPPIRIVPTPTSPSIAPTSESSAPPVRGPVPLPVKPTIRNRDSAPSTPTLGPPLPTRVMVTTSTIAIQPTMTRPVYVGASVTPATPTTRKPTKRPPKKPKTTPIPREPKTTTTKPPRRSTPAVIGDSNIKPELRNPIDQVNAYVGTYFEVKVPSDTFFDKEDGTTDKLRLTLRKGNDVVADDSWIQFNSTSQLLYGLPDQEHAGKHEYFMQATDKGGLYAMDAFEVRVSMWGNSVKPPVLFTAVFDGDARTVTNDIHKKILLVKKLSQSFGDRNSSTITLKSITKGSIIVEWTNNSLQQSPCPKDQIQQLSKKISDPEGKPSSIFKFTMEPDFRPSNITVRGTASCRNYMFVPLGEIPDPTPSPGTPAVGAGRQSTDDVYLHTVIPAVVVAAILLIAGIIAMICYRKKRKGKLTIEDQATFIKKGVPIIFADELDDSKPPPSSSMPLILQEEKPPLPPPEYPNMATPETTPLNQDLLGEYTPLHDEDPNAPPYQPPPPFSTPMEGKGSRPKNMTPYRSPPPYVPP