wanglab/gogpt-training-data huggingface dataset:
Protein: Tubulin polyglutamylase TTLL7 (EC 6.3.2.-) (Testis development protein NYD-SP30) (Tubulin--tyrosine ligase-like protein 7) (Q6ZT98)
Organism: Homo sapiens (Human)
Function: Polyglutamylase which modifies tubulin, generating polyglutamate side chains of variable lengths on the gamma-carboxyl group of specific glutamate residues within the C-terminal tail of tubulin. Mediates both ATP-dependent initiation and elongation steps of the polyglutamylation reaction. Preferentially modifies the beta-tubulin tail over an alpha-tail. Competes with monoglycylase TTLL3 for modification site on beta-tubulin substrate, thereby creating an anticorrelation between glycylation and glutamylation reactions (By similarity). Required for neurite growth; responsible for the strong increase in tubulin polyglutamylation during postnatal neuronal maturation (By similarity).
Subcellular location: Cell projection, cilium {ECO:0000250|UniProtKB:A4Q9F0}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:A4Q9F0}. Cell projection, dendrite {ECO:0000250|UniProtKB:A4Q9F0}. Perikaryon {ECO:0000250|UniProtKB:A4Q9F0}. Note=In cells with primary cilia, found in both cilia and basal bodies. In neuronal cells, found in dendrites and perikaryon. {ECO:0000250|UniProtKB:A4Q9F0}.
Interaction partners:
Sequence:
MPSLPQEGVIQGPSPLDLNTELPYQSTMKRKVRKKKKKGTITANVAGTKFEIVRLVIDEMGFMKTPDEDETSNLIWCDSAVQQEKISELQNYQRINHFPGMGEICRKDFLARNMTKMIKSRPLDYTFVPRTWIFPAEYTQFQNYVKELKKKRKQKTFIVKPANGAMGHGISLIRNGDKLPSQDHLIVQEYIEKPFLMEGYKFDLRIYILVTSCDPLKIFLYHDGLVRMGTEKYIPPNESNLTQLYMHLTNYSVNKHNEHFERDETENKGSKRSIKWFTEFLQANQHDVAKFWSDISELVVKTLIVAEPHVLHAYRMCRPGQPPGSESVCFEVLGFDILLDRKLKPWLLEINRAPSFGTDQKIDYDVKRGVLLNALKLLNIRTSDKRRNLAKQKAEAQRRLYGQNSIKRLLPGSSDWEQQRHQLERRKEELKERLAQVRKQISREEHENRHMGNYRRIYPPEDKALLEKYENLLAVAFQTFLSGRAASFQRELNNPLKRMKEEDILDLLEQCEIDDEKLMGKTTKTRGPKPLCSMPESTEIMKRPKYCSSDSSYDSSSSSSESDENEKEEYQNKKREKQVTYNLKPSNHYKLIQQPSSIRRSVSCPRSISAQSPSSGDTRPFSAQQMISVSRPTSASRSHSLNRASSYMRHLPHSNDACSTNSQVSESLRQLKTKEQEDDLTSQTLFVLKDMKIRFPGKSDAESELLIEDIIDNWKYHKTKVASYWLIKLDSVKQRKVLDIVKTSIRTVLPRIWKVPDVEEVNLYRIFNRVFNRLLWSRGQGLWNCFCDSGSSWESIFNKSPEVVTPLQLQCCQRLVELCKQCLLVVYKYATDKRGSLSGIGPDWGNSRYLLPGSTQFFLRTPTYNLKYNSPGMTRSNVLFTSRYGHL
Protein: Colicin E3 (EC 4.6.1.-) (Colicin E3 A chain) (colE3) (Ribonuclease) (P00646)
Organism: Escherichia coli
Function: Inactivates ribosomes by hydrolyzing 16S RNA in 30S ribosomes at a specific site.
Subcellular location: Secreted {ECO:0000269|PubMed:4944624}.
Interaction partners:
Sequence:
MSGGDGRGHNTGAHSTSGNINGGPTGLGVGGGASDGSGWSSENNPWGGGSGSGIHWGGGSGHGNGGGNGNSGGGSGTGGNLSAVAAPVAFGFPALSTPGAGGLAVSISAGALSAAIADIMAALKGPFKFGLWGVALYGVLPSQIAKDDPNMMSKIVTSLPADDITESPVSSLPLDKATVNVNVRVVDDVKDERQNISVVSGVPMSVPVVDAKPTERPGVFTASIPGAPVLNISVNNSTPAVQTLSPGVTNNTDKDVRPAGFTQGGNTRDAVIRFPKDSGHNAVYVSVSDVLSPDQVKQRQDEENRRQQEWDATHPVEAAERNYERARAELNQANEDVARNQERQAKAVQVYNSRKSELDAANKTLADAIAEIKQFNRFAHDPMAGGHRMWQMAGLKAQRAQTDVNNKQAAFDAAAKEKSDADAALSSAMESRKKKEDKKRSAENNLNDEKNKPRKGFKDYGHDYHPAPKTENIKGLGDLKPGIPKTPKQNGGGKRKRWTGDKGRKIYEWDSQHGELEGYRASDGQHLGSFDPKTGNQLKGPDPKRNIKKYL
Protein: Sulfhydryl oxidase (EC 1.8.3.2) (Q54R76)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
Sequence:
MKKINLFYLNLIIFIIFLNFIYGSSEIRSKRIQIQQSSFHFLSATGYRASLTDQEWCEEYQVKTGRDYYWSDFRSMAINYLDLYIALQFDVECEAQLIEFRKFFIENINQPPPFSKNSTIWDTTYLQLALNAFTCGFNGSKIEDFEFVSSDLRTNFNSEPLKQKVWFIIGDYIHSEYKQRENSNRRMDYDSGLYIPFLDKYTGTDYTADQQIRAGYPSYMGRSLWFIFHTVAQRISDSQCENDSNSKEIYNQLTQKVKNFITSFLYQHPCPICREHQISRIFVNDRYAKDPIDNEAIRYYPIEHLLMGGIRGDTYGKLSTLIPTDKKSIAAFFWKLHNAITASVDNGCQCFSEEYEDKSPYKCVFDYKLQIQPQFPRQQRLFPFGKRFEFFLSPDHNYTLFDEIRSQFIPMVTEINQLDSFALRKELFQYWSQGISISKKSQNTINQLLSLISNMTTQFMNSNVLSASYSYQSDLPLQCNLILEKLNASTHSLSTPTIKDAFPPSVCNPYLQPSVCDQQYLYRYFTQPPVTSPPKSTKNVEPINSTIATTTTTTTNNNNNSYILKINFILILILSLFSLI
Protein: 16S rRNA aminocarboxypropyltransferase (EC 2.5.1.157) (20S S rRNA accumulation protein 3 homolog) (VdTsr3) (E1QU22)
Organism: Vulcanisaeta distributa (strain DSM 14429 / JCM 11212 / NBRC 100878 / IC-017)
Function: Aminocarboxypropyltransferase that catalyzes the aminocarboxypropyl transfer on pseudouridine corresponding to position 914 in M.jannaschii 16S rRNA. It constitutes the last step in biosynthesis of the hypermodified N1-methyl-N3-(3-amino-3-carboxypropyl) pseudouridine (m1acp3-Psi).
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01116}.
Interaction partners:
- Small ribosomal subunit protein uS2
Sequence:
MIPRVFIYRLPQDDPRKNTAIKLVRFGFAQLVDSIKALPSGSIILDPTVKTPLTPSDRVIAESRGLSLIDCSWKRAVDVHTKFIRGKFIRRRLPLLIAANPTHYGKPYILSTIEAVAAALYIMGFKDEAMEVLRLYKWGPNFIIINQKYLERYAAGDLSPERELLGVDDVDNGLEQLMRVLTNGD
Protein: Ral guanine nucleotide dissociation stimulator-like 2 (RalGDS-like 2) (RalGDS-like factor) (Ras-associated protein RAB2L) (O15211)
Organism: Homo sapiens (Human)
Function: Probable guanine nucleotide exchange factor. Putative effector of Ras and/or Rap. Associates with the GTP-bound form of Rap 1A and H-Ras in vitro (By similarity).
Interaction partners:
- Ras-related protein Ral-A
- GTPase HRas
- Ras-related protein Ral-B
- GTPase KRas
- GTPase NRas
- Ras-related protein R-Ras
- Ras-related protein M-Ras
- Ras-related protein R-Ras2
- Prefoldin subunit 6
- Small ribosomal subunit protein uS13
Sequence:
MLPRPLRLLLDTSPPGGVVLSSFRSRDPEEGGGPGGLVVGGGQEEEEEEEEEAPVSVWDEEEDGAVFTVTSRQYRPLDPLVPMPPPRSSRRLRAGTLEALVRHLLDTRTSGTDVSFMSAFLATHRAFTSTPALLGLMADRLEALESHPTDELERTTEVAISVLSTWLASHPEDFGSEAKGQLDRLESFLLQTGYAAGKGVGGGSADLIRNLRSRVDPQAPDLPKPLALPGDPPADPTDVLVFLADHLAEQLTLLDAELFLNLIPSQCLGGLWGHRDRPGHSHLCPSVRATVTQFNKVAGAVVSSVLGATSTGEGPGEVTIRPLRPPQRARLLEKWIRVAEECRLLRNFSSVYAVVSALQSSPIHRLRAAWGEATRDSLRVFSSLCQIFSEEDNYSQSRELLVQEVKLQSPLEPHSKKAPRSGSRGGGVVPYLGTFLKDLVMLDAASKDELENGYINFDKRRKEFAVLSELRRLQNECRGYNLQPDHDIQRWLQGLRPLTEAQSHRVSCEVEPPGSSDPPAPRVLRPTLVISQWTEVLGSVGVPTPLVSCDRPSTGGDEAPTTPAPLLTRLAQHMKWPSVSSLDSALESSPSLHSPADPSHLSPPASSPRPSRGHRRSASCGSPLSGGAEEASGGTGYGGEGSGPGASDCRIIRVQMELGEDGSVYKSILVTSQDKAPSVISRVLKKNNRDSAVASEYELVQLLPGERELTIPASANVFYAMDGASHDFLLRQRRRSSTATPGVTSGPSASGTPPSEGGGGSFPRIKATGRKIARALF
Protein: Plexin A1 (Plexin-A1b) (A8IYK2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
Interaction partners:
Sequence:
MWPPQGPQCIISPKTVVLLGLLTICNSPHHSEGALEPFRSFTPPDWGLTHLAIHNKTGDVYVGAVNWIYKLSSNLTKLRSHVTGPVVDNEKCYPPPSVQSCPHDLSPNSNVNKLLLIDYPQNRLIACGSTSQGICQFLRLDDLFKLGEPHHRKEHYLSSVVESGTMSGVIISEGHLSKLFIGTPIDGKSEYFPTLSSRKLMANEEDADMFSFVHQDEFVSSQLKIPSDTLSKFPAFDIYYIYSFSSEQFVYYLTLQLDTQLTSPDASGEQFFTSKIVRLCIDDPRFYSYVEFPIGCTKDGVEYRLIQDAYLSKPGRQLANSLGVSEQEDILFTVFSQGQKNRVKPPRESALCLFTLTKIKEKIKERIQSCYRGEGRLSLPWLLNKELPCINSPLQIDDNFCGQDFNQPLGGTKTIEGTPLFIDKDDGMTSVAAYDYRGNTVVFAGTRNGRMKKILINSVSPSRPALLYESVAVSEGSPLLRDMLFSPDLQFIYTLTDKQVTRVPVERCSQYSTCSECLSSRDPHCGWCVLHNICSRRDRCERADEPQRFASRVDQCVELTVQPNNISVTMAEVQLVLQARNVPDLSAGVDCSFEDYTQTEGTIHGSRIYCLSPTAKELVPITRLQRDTHVLKLYLKSRETGQKFASVDFTFYNCSIHRSCLSCVNGSFPCHWCKYRHLCTQNANDCSFQEGRVNMSEDCPQILPSTEIYIPVGVPKPITLSARNLPQPQSGQRNYECVFHIQGETHSVTALRFNSSSIQCQKTTYNYEGSDISDLPVDLSVVWNGNFIIDNPYNIQAHLYKCYALRESCGLCLKADPSFECGWCVQDRKCSLRQECAQPENTWMHATAGNSRCTHPRITKLSPETGPRQGGTRLTISGENLGLQFKDIQNGVRIGKVSCQPIEEEYISAEQIVCRLADATGYRVQEAHVEVCVRDCLQDYRAVSPKVFTFVSPYFTRVVPSYGPISGGTRITIYGSHLNAGSAVSIKIGLNTCQFERRSAREIVCVTPAGLGSGGTPVMVDINAAELRNPEVKFNYTDDPTILKIEPDWSIASGGTPLTVTGVNLATVREPKMRAKYGTISSVNNCTVLNNTVMVCAVPSVAGSERGFSEVGNAPDEIGFIMDHVQMLLVVNESFSFYPDPVFEAFGPAMLELKPGSPLILKGKNLIPSAAGNYRLNYTVLIGDKQCVLTVSETQLLCESPNLTGQHKVTVLAGGFRFSPGTLQIYSDSLLTLPAIIGIGGGGGLLLLVIIIILIAYKRKSRDADRTLKRLQMQMHNLESRVALECKEAFAELQTDIHELTQDLDGSGIPFLDYRTYAMRVLFPGIEDHPVLKEMEVPANVEKALTLFGQLLNKKHFLLTFIRTLEAQRSFSMRDRGNVASLIMSGLQGEMEYATGVLKQLLADLIDKNLESKNHPKLLLRRTESVAEKMLTNWFTFLLYKFLKECAGEPLFMLYCAIKQQMEKGPIDSITGEARYSLSEDKLIRQQIDYKTLTLHCINPENENAAEVMVKCLNCDTVTQVKEKLLDAVFKGTPYSQRPKVGDMDLEWRQGRMARIILQDEDVTTKIDNDWKRLNTLAHYQVTDGSLIALVPKQNSAYNISNSSTFTKSLSRYESMLRTSSPDSLRSRTPMITPDLESGTKLWHLVKNHDHTDQREVDRGSKMVSEIYLTRLLATKGTLQKFVDDLFETIFSTAHRGSALPLAIKYMFDFLDEQADRHMISDPDVRHTWKSNCLPLRFWVNVIKNPQFVFDIHKNSITDACLSVVAQTFMDSCSTSEHKLGKDSPSNKLLYAKDIPNYKNWVERYYSDISRMSAISDQDMSAYLAEQSRLHLNQFNSMSALHEIFSYITKYKDEILSALERDEQSRRQRLRAKLEQVIDTMALPS
Protein: Glutathione peroxidase (W8W106)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Interaction partners:
Sequence:
MSGSEFYNMTAKLISGDFFKFSSLGGKVVLIENVASLUGTTTRDYTQMNELHERYADKGLVILGVPCNQFGHQENCNNEEILMSLKYVRPGNGFEPNFQLLEKVDVNGKHAHPLFVYLKEKLQFPSDDPMALMNDPKCIIWSPVGRNDIAWNFEKFLIGPDGEPFKRYSRRFPTIDIEGDIKKLLNTAN
Protein: HTH-type transcriptional repressor BluR (P75989)
Organism: Escherichia coli (strain K12)
Function: Controls the expression of several small proteins that may play a role in biofilm maturation. Binds to and represses the operator of the ycgZ-ymgA-ariR-ymgC operon and also regulates ynaK. Binding is antagonized by BluF upon blue light (470 nm) irradiation. Blue light may increase the affinity of BluF for BluR, allowing it to be released from its operator.
Interaction partners:
- Blue light- and temperature-regulated antirepressor BluF
- Probable two-component-system connector protein YmgA
- Probable two-component-system connector protein AriR
- Probable two-component-system connector protein YcgZ
- Uncharacterized protein YcgX
Sequence:
MAYYSIGDVAERCGINPVTLRAWQRRYGLLKPQRSEGGHRLFDEEDIQRIEEIKRWISNGVPVGKVKALLETTSQDTEDDWSRLQEEMMSILRMANPAKLRARIISLGREYPVDQLINHVYLPVRQRLVLDHNTSRIMSSMFDGALIEYAATSLFEMRRKPGKEAILMAWNVEERARLWLEAWRLSLSGWHISVLADPIESPRPELFPTQTLIVWTGMAPTRRQNELLQHWGEQGYKVIFHAP
Protein: 1-phosphatidylinositol-3-phosphate 5-kinase (EC 2.7.1.150) (Q6FM73)
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 D complete sequence
- Candida glabrata strain CBS138 chromosome H complete sequence
- Phosphatidylinositol 3-kinase VPS34
- 1-phosphatidylinositol 4-kinase
- 1-phosphatidylinositol 4-kinase
- Candida glabrata strain CBS138 chromosome C complete sequence
- Candida glabrata strain CBS138 chromosome K complete sequence
- phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase
- CDP-diacylglycerol--inositol 3-phosphatidyltransferase
- Phosphoinositide phospholipase C
Sequence:
MAIGQGTLPKDDQIEYNNEAGGTSTISEPIDLITRTGLVPKTTTTTEITTEDILSNDITVPRVNDKSSNQLINDEMENHSYKESLSVNKLPHELNDNADHMDIKSKNIEPINTIVIPDTSNFLPISNDIDKQEYISDPTSDKEEPPVESNTFLRSERNGEITSNDLRSELRVDKNIQLRASPNQNKTLLFALANDMNSKRSSTYASKSTVKAIPIRNHSSHSMARGFNSYYDNDDVSSLKSRSSSMAASFSKGFLLGFYNNRNKHANNQKVVLSKEYWMKDESARECFTCGKRFNTFRRKHHCRICGQIFCKNCTLIINGERFGYDRSLRVCQNCYKHADNYQDSSDEEYYEEENSVITREPSTNLMNEHLSKKEEQDSMNDFNIQEEGDSSIFNTPNKNNEVLFIHDDDVHSIITSKQDSKLFISTPPPPPKMAIPATKQGESLEIAFNNNLVNRNSNKTISHDGNNEKITIRDLDDPTSYKPNEKKNPNSTPSLRRSLFQYMGKTNRDQANNHMPSNPLPDSSLLNNRNFQFKFNFRPELYNERRKSFGADKFNSNENKNAINVSQSPKLSLEYDNNDLEDEASMSLYSSLHGSIPTDKPIGFVRTSSKSDQRAMASLHRIRHKRTGKSKSISMTYPSNLDSDFISQSSPNLLSVVSDELPLPQPTSILYRTGWDKASTGTNNAWKRHSSLTSVRPSAEPKPELNKVAQIHLNSLLDQVLGDQDIADKELWKNKLLSLLSQIQNIILSAKDLNTLDYRQNYLKIKRITGGSIDASEYINGIVFSKNLPNKHMSRKIENPRILLLMFPVEYERSENKFLSIDSVIAQEKEYLNKLVSRILSLSPDIIYVGANVSGYALDLFCNAGIVIQYNMKPQVLERIAKYTDADIALSIEKLATNIKMGECQLFEVKSYLYDKHISKTYTFLRGCEPTLGGTILLRGANETVLRKIKQIVEFMVYATFSLKLESSFFNDNFLQLSVEHYLLAKTESKNQQPEGYYSDFVEKFNNRLLSVSPTVSFPLPFLLKQARNLERELRLLEDQESTVHAAKEEYQIGLLSDISNKLTKMELVNLGRYIMEKEIQDLKNEYKKRARQWEVYYSLTRNMLGTGSHQSITVLYSMVSIKTATPCIGPQLMTIDYFWDSDISVGQFIENIVSTAWHPCKQGCNTYLFDHYRSYVHGDGKVDVMLERFETKLPKLRDIILTWSYCKKCGCSTPILQISQKTWNYSFGKYLEIMFWSERHSLLGVGKCGHEFTKDHVKYFSYNDLVVRLEYSDLEIHELITPSRRIRWKPNRDIIMKVELYYGILDKINYFYSNVSERLDRIKLDGLVVDKMEPGKQKLNEMKIMLENNKRNLLEKLEKQYKDTPGTEHLHLNSILRSLYNQTNFWNNEFKEFGETYLPSENDITRITTSQLKKIFGEPKKPDLIPESTHLNVSDRSNELERISESQSFISESKEDSVDNNRAAERINALREHTKKPSISTSMINLSKHDQPSFIEHSVPPTTYNDSGYDSRVGKLTNFFDQLHFDALTKEFELERELQKLQLNKSKSRKFRLQNSTPIVEIYKDVKDAVDEPLHNDEKIQNDDSNEVESVDYSNSSKAHRSTQQKKVSEMLESELKNSINRWGEAYINSDSNLASMEHLEKKGETDITKDNNKILDTDQKSVEVAPQPEKSTLMKTLATFWADRSAYLWKPFSFPIGANEHVFTDSDVIIREDEPSSLIAFCLSTSDYNNKMASIKDDTDVAPVEKVVNNQDHKKSSNQQNISDSSEKTHANSNIESVNETSSVLTEEKASVSDKYFDPAKNLEAIMTKKTAIHLRYQFEDGLVVMSCKVFFAEHFEAFRKICNCDENFIQSLSRCVKWHSNGGKSGSGFLKTLDNRFVIKELTHSEVDSFIKFTPSYFEYMAQAMFHDLPTTLAKVFGFFQIQVKNPISGSKNYKMNVIIMENLFYNKKTSRIFDLKGSMRNRHVEQTGKANEVLLDENMVEYIFESPIHVREYDKKLLRASLWNDTLFLAKMNVMDYSLVVGINNDDYTLTVGIIDFIRTFTWDKKLESWVKEKGLVGGGNSIMKQPTVVTPKQYKNRFREAMERYILMVPDPWYQDTN
Protein: Dynactin subunit 2 (A0A384MDU9)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MADPKYADLPGIARNEPDVYETSDLPEDDQAEFDAEELTSTSVEHIIVNPNAAYDKFKDKRVGTKGLDFSDRIGKTKRTGYESGEYEMLGEGLGVKETPQQKYQRLLHEVQELTTEVEKIKTTVKESATEEKLTPVLLAKQLAALKQQLVASHLEKLLGPDAAINLTDPDGALAKRLLLQLEATKNSKGGSGGKTTGTPPDSSLVTYELHSRPEQDKFSQAAKVAELEKRLTELETAVRCDQDAQNPLSAGLQGACLMETVELLQAKVSALDLAVLDQVEARLQSVLGKVNEIAKHKASVEDADTQSKVHQLYETIQRWSPIASTLPELVQRLVTIKQLHEQAMQFGQLLTHLDTTQQMIANSLKDNTTLLTQVQTTMRENLATVEGNFASIDERMKKLGK
Protein: Mammaglobin-A (Mammaglobin-1) (Secretoglobin family 2A member 2) (Q13296)
Organism: Homo sapiens (Human)
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Secretoglobin family 1D member 2
- Mucin-like protein 1
- Mammaglobin-B
- Uteroglobin
- Prolactin-inducible protein
- Secretoglobin family 1D member 1
Sequence:
MKLLMVLMLAALSQHCYAGSGCPLLENVISKTINPQVSKTEYKELLQEFIDDNATTNAIDELKECFLNQTDETLSNVEVFMQLIYDSSLCDLF
Protein: C-X-C motif chemokine 5 (Cytokine LIX) (Small-inducible cytokine B5) [Cleaved into: GCP-2(1-78); GCP-2(9-78)] (P50228)
Organism: Mus musculus (Mouse)
Function: May participate in the recruitment of inflammatory cells by injured or infected tissue. GCP-2(1-78) and, more potent, GCP-2(9-78) attract neutrophils and are involved in neutrophil activation.
Subcellular location: Secreted.
Interaction partners:
- C-X-C chemokine receptor type 2
- C-X-C chemokine receptor type 1
- C-X-C motif chemokine 14
- C-X-C chemokine receptor type 4
- Eotaxin
- C-X-C motif chemokine 10
- Growth-regulated alpha protein
- C-X-C motif chemokine 13
- C-C motif chemokine 5
- C-X-C chemokine receptor type 3
Sequence:
MSLQLRSSARIPSGSISPFMRMAPLAFLLLFTLPQHLAEAAPSSVIAATELRCVCLTVTPKINPKLIANLEVIPAGPQCPTVEVIAKLKNQKEVCLDPEAPVIKKIIQKILGSDKKKAKRNALAVERTASVQ
Protein: RPGR interacting protein 1 (A0A8I6GGU8)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MLKLCSKDAGAYSFEESSDTVPGVFSMLESSHQPLESSHQPHWNRELMAEQLPQQVCPLLDQVGAELEETKVLLQVTNQVAQDEQLTFQVTSILCQHKQEEENLQSTATIPLFPEELFELAVQPTLLAQTVQRESSEPRVQEESSLSQVLNELQVSHAETALELEKTRDMLLLQRKINLCYQEELEATLTKADKENRDHEETMERLTHLLDFKNSRIMQLEGILRSHVQIR
Protein: Uncharacterized protein (Q5BG05)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
Sequence:
MDLTKIVVITGANTGIGFETVKSLLRSNQRYYIFLGGRNLEKAQAASKQLFSESAHHVLEPFQVDVESDESIEAAFKHIASKYNRIDCLINNAGACFDAYIDKDMATRQAWNKSWDVNVTGAHIMTTTFLPLLLNSQDPRLLFITSGLSSLQAASDTTDPKNVIPAAGLPKQLPFVGYRSAKVGLNMLMVEWTKALKKDGVKVWAVAPGLLATSLGGSTELLKKLGAQDPSIGGNTIRRVVEGERDADVGNVVREYGSPIQPW
Protein: Conserved oligomeric Golgi complex subunit 1 (COG complex subunit 1) (Complexed with DOR1 protein 3) (Component of oligomeric Golgi complex 1) (Protein SEC36) (P53079)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Acts as essential component of the peripheral membrane COG complex that is involved in intra-Golgi protein trafficking. COG is located at the cis-Golgi, and regulates tethering of retrograde intra-Golgi vesicles and possibly a number of other membrane trafficking events.
Subcellular location: Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
Interaction partners:
- Conserved oligomeric Golgi complex subunit 3
- Conserved oligomeric Golgi complex subunit 4
- Conserved oligomeric Golgi complex subunit 2
- Conserved oligomeric Golgi complex subunit 5
- Conserved oligomeric Golgi complex subunit 6
- Conserved oligomeric Golgi complex subunit 7
- Conserved oligomeric Golgi complex subunit 8
Sequence:
MDEVLPLFRDSHIPQIKDYQLELQNDLTKTNEAFQKNLLKNYNKILSLTDSVNDLSLNLKNVDQDFKSLCFNDEKFQLNKLTPLPYQTTTHISPPRDEEKVSIPSQNILVISNWTISINNFCNRIVTSTTPSRIFDELLLNFHELSLIPVPSKFEALVKDKCCRLQKFLVDSMKTLNLTLLQWVKLYNLLNTEFSSKWDDDLLSIFNESLFETLFNDNVQALLISSANSKDHQYHSNQQYKDAIVVDFVNSSTFRDHLIRRTVKEINTHLDTLSTLRAKLKEPETLHKLDIFHDNDTNLNDGTVSPLDDDALKQYIDTAVFYSKGLTNDTTLQIYQTVQPTIEILQNLELYKCPQETLTDLRNKLITQLQEFKTQISSRLPSPLENSTSVVDDFITSYNNHNLLQLVIDQITQLRQQ
Protein: BTB/POZ domain-containing protein KCTD5 (Q8VC57)
Organism: Mus musculus (Mouse)
Function: Its interaction with CUL3 suggests that it may act as a substrate adapter in some E3 ligase complex (By similarity). Does not affect the function of Kv channel Kv2.1/KCNB1, Kv1.2/KCNA2, Kv4.2/KCND2 and Kv3.4/KCNC4 (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9NXV2}. Cytoplasm {ECO:0000250|UniProtKB:Q9NXV2}. Nucleus {ECO:0000250|UniProtKB:Q9NXV2}. Note=Predominantly cytoplasmic, translocated to the nucleus upon interaction with Rep proteins. {ECO:0000250|UniProtKB:Q9NXV2}.
Interaction partners:
- Cullin-3
- Potassium channel tetramerisation domain containing 17
- BTB/POZ domain-containing protein KCTD2
- BTB/POZ domain-containing adapter for CUL3-mediated RhoA degradation protein 1
Sequence:
MAENHCELLPPAPSGLGAGLGGGLCRRCSAGMGALAQRPGGVSKWVRLNVGGTYFLTTRQTLCRDPKSFLYRLCQADPDLDSDKDETGAYLIDRDPTYFGPVLNYLRHGKLVINKDLAEEGVLEEAEFYNITSLIKLVKDKIRERDSRISQMPVKHVYRVLQCQEEELTQMVSTMSDGWKFEQLVSIGSSYNYGNEDQAEFLCVVSKELHNTPYGTTSEPSEKAKILQERGSRM
Protein: Possible transcriptional regulatory protein (Probably TetR-family) (P95100)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Probable short chain alcohol dehydrogenase/reductase
- Putative cytochrome P450 136
- Possible transcriptional regulatory protein
Sequence:
MTSHAADEKQAAPPMRRRGDRHRQAILRAARELLEETPFAELSVRAISLRAGVARSGFYFYFDSKYSVLAQILAEATEELEEASQHFSARQPGESPEQFVNRMIGSVAAVYANNDPVLRACNAARQSDMEIRDILERQFQVLLRETIGVFEAEVKAGTAHPISEDLPTLVRTLAATTALMLTGDALLVGPDSDAARRVRVLEQMWLNALWGGGKAP
Protein: Divalent metal cation transporter MntH (Q89K67)
Organism: Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110)
Function: H(+)-stimulated, divalent metal cation uptake system.
Subcellular location: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_00221}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00221}.
Interaction partners:
- ABC transporter substrate-binding protein
- Blr3815 protein
- Magnesium-transporting ATPase, P-type 1
- Blr4043 protein
- Magnesium/cobalt transport protein
- ABC transporter permease protein
Sequence:
MDARSPDLTTDAAGWRTDVPTTKSLAEVNASVALPTAGVWWRRLLAFVGPGYLVSVGYMDPGNWATDLAGGSKFGYTLLSVILLSNLMAILLQSLAARLGIVTDRDLAQACRATYSPAVNFLLWLACEAAIIACDLAEVIGTAIALKLLFGIPLIGGALIAALDAFLLLLLMNRGFRFLEAFVIALLAVIAVCFAVQIVAAAPPVAEVLHGFMPKSEIFTNPEMLYIAIGIIGATVMPHNLYLHSSIVQTRAYERNETGRREAIKWATTDSTIALMLALFINAAILVVAAATFHKSGHSDVAEIGQAFELLSPLLGLGIASTLFAIALLASGLNSTVTATLAGQIVMEGFLDLRLPSWARRLLTRGIAIIPVIIVTAIYGERGTADLLVFSQVVLSMQLPFAVIPLVRFVSDRRKMGKFAISPYVAAIAWIVAGVIVVLNLKLLADTLLG
Protein: Protein kinase family protein (C6ZRY5)
Organism: Glycine max (Soybean) (Glycine hispida)
Interaction partners:
- non-specific serine/threonine protein kinase
Sequence:
MKEESTGLIIGISIGVVIGVGLAISALFCLRYHRKRSQIGNSSSRRAHTIPIRENGVDSCNILSDSTLGPESPVRSGRNGMSLWLDGFKKSSNMVSASGIPEYSYKDLQKATYNFTTLIGQGAFGPVYKAQMSTGETVAVKVLATNSKQGEKEFQTEVMLLGRLHHRNLVNLVGYCAEKGQHMLVYVYMSKGSLASHLYSEENGALGWDLRVHIALDVARGIEYLHDGAVPPVIHRDIKSSNILLDQSMRARVADFGLSREEMVDKHAAIRGTFGYLDPEYISSGTFTKKSDVYSFGVLLFELIAGRNPQQGLMEYVELAAMNTEGKVGWEEIVDSRLEGKCDFQELNQVAALAYKCINRAPKKRPSMRDIVQVFTRILKSRYQRNHHHKKSLSATVDEVSIDVDQLETKSSVTDHRREESIDSTADIYDL
Protein: CNH domain-containing protein (Q387Z5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Vacuolar protein sorting complex subunit, putative
- RING-type domain-containing protein
- Pep3/Vps18/deep orange beta-propeller domain-containing protein
- Vacuolar assembly protein vps41, putative
- Vacuolar protein sorting 33, putative
- RING-type domain-containing protein
- Ras-related protein Rab-7b
- Vesicle transport v-SNARE N-terminal domain-containing protein
- Vesicle-associated membrane protein, putative
Sequence:
MLAVKYLLKLYETPPENGHISAFDTYGNTVFAGTDSGVLMRFVVEGATSPEIVPTEGSLSGDARDRHISGGNSARSAEAGGVGEEQQAHEEMHADDFHAVSQLEKIYTTLVHHVVVSETQRRVERIQHSRTHNILFVLCEHRLLVLNSITFEHIYTVSDYVGTFFVSDSRQTSSQRVGRHVICTTEPHGRELRVYEFDIAQNKHVRPMAPHKVMLHEQAQTLVTYGNMVCVGMRRGGYRLLSLPDGNTCSVLPLSGDMQPLLAVGDGEVFMRYDHSIFSVSMRSMPSGRVLGRTIQLEDEVRHMIARHPFLFAFTESYCDVYSLYDDDVSERLPMSGCLFGSQLGGGDFLYAASATKIWMAGLHPLRHQLADLVERFKVEEAFHLLSTQRSRNSLDWQAIELELHVMVGFAYLHRCRPKEAMLHFNDHIDPRDLLLLLPECIPPGPDEYSSELRGLLKGDCVGETRTSSDGVDFASKDEDVVNVPVGGNNVEPLLAKCGPDIGCWDGGFWEEWSGCCPYNTYIGELEKAWLETFETFPTVPRSTDQADGVIHRQVMEWGCITAEGFLERSWEALKDELVVYFRSRLDQASPVHARPMEYALLVLALEARDHREAYQIVVKSSSLSVEDCYDLLCSLHEYRLLACLLYCRGYTQDADRLLRQRVCVSSLLPPWLPGRCNNSKQSPAYMNVPAALHSQLTRLLTPLPKNECLVVADLSSPRGAHSPNDVDETHTINLPLSLSLPMYLVSHLNIPALQELLAEDPDAAVITDEEGCTLLHVLFSLFISVRDLTEGEAMTKGSALVGLVLSCAVLLLDHGADVAAPNVHGITCLDVLAIAAGGVFFDIVVSALLADRDVRKAAAFTNKDDNTLVNGFIPIA
Protein: Transcription factor MYB1 (Myb-related protein 1) (A0A2R6S148)
Organism: Actinidia chinensis var. chinensis (Chinese soft-hair kiwi)
Function: Transcription activator involved in the regulation of anthocyanin biosynthesis in red-fleshed kiwifruit varieties. Activates the transcription of genes involved in anthocyanin biosynthesis, such as dihydroflavonol reductase (DFR), anthocyanidin synthase (ANS) and UDP flavonoid glycosyltransferase (UFGT).
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625, ECO:0000269|PubMed:28919902, ECO:0000269|PubMed:29203778}.
Interaction partners:
Sequence:
MESVTLGVRKGAWTEEEDKLLKKCIEKYGEGKWHQVPLRSGLNRCRKSCRMRWLNYLRPNINRGNFTADEVDLIIRLHKLLGNRWSLIAGRLPGRTSNDVKNYWNTHLQKKLITYPRAQPIPKTQKTIVPKGTEAQPRAHPKSPPRPSPPSNNEILWWDNKTVSPQIDNIGIHWSIDGSIFEEPILGNLQSAGDSFLQQNQSDWSDIFLEDVNLWDLLGDD