wanglab/gogpt-training-data huggingface dataset:
Protein: 3-beta hydroxysteroid dehydrogenase/isomerase domain-containing protein (Q388N6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- NADH-ubiquinone oxidoreductase 20 kDa subunit, mitochondrial
- NADH dehydrogenase flavoprotein 1, mitochondrial
- NADH-ubiquinone oxidoreductase, mitochondrial, putative
- Electron transfer protein, putative
- Acyl carrier protein
- Reiske iron-sulfur protein, mitochondrial
- Cytochrome c1, heme protein, mitochondrial
- Mitochondrial processing peptidase alpha subunit, putative
- NADH dehydrogenase 1 beta subcomplex subunit 9
- NADH dehydrogenase 1 alpha subcomplex subunit 13
Sequence:
MLRRVGERVTGGIPCTVAPVVGPVRYFWDPYGHQPESMFLDRKDLEQMYPTRKPKTTGGEFGYERGPYWAAMLVPNPAVRLPHERRRLNPKPAKRVTVFGASGYLGGEIVREFCEHKDIEKVRATTRYPTLIPEGSDLDLLLQKYPEKIELHECDVTDRIQVNVAANGSDTLVFAVDYHAEYANNSHHDVFLTGSTNVSWTARSVRAERVIFCNGLDATFASESNYCDFRARAEDAVGANHPDATIIRFGPLYGKNYRYRGLGRYIYPACFPNSLVQPTWVVDAARAVVRCSMSRRAVRYKFDLGGPQTLTHVEAFRDIASHFDARLVVPCYRGIGRFFGKLLPWVVPNPWFDDNWIVTYELDQVNRRSTLFDRLASWERIAYAPHTIAEAAAIEKGKVKLPPLHELDVSYKALEAADKAAFDLEEENAKKFGIHRAKAEPGFGRTDGLEALAQEIYPGQQFRIRPLEGAKYPSNVKNPGPVAIH
Protein: CSD domain-containing protein (P91306)
Organism: Caenorhabditis elegans
Interaction partners:
- Chondroitin proteoglycan 1
- RNA-binding protein pos-1
- PUM-HD domain-containing protein
- LDL receptor repeat-containing protein egg-1
- ATP-dependent RNA helicase cgh-1
- Protein LSM14 homolog car-1
- Chitin-binding domain protein cbd-1
- EGF-like domain-containing protein
- CSD domain-containing protein
- CCCH-type zinc finger protein oma-2
Sequence:
MSDTANAAVEIGEEALEQKLEELSVQDKTTPSNSEEKMRKRRLPTAERIRLWEEEQKSKTAITTGLQGKVKWYSVLRRYGFISRNDGEKDIFVHQTAIAKSATEKFYLRTLGDDEEVLFDLVEGKNGPEAANVTGPNGDNVIGSRYRHKLLSRFRKNRKPRASVDGEESQSTDAKPQEMSADAEKKKPRKQRKNRNRKSKAQQKGAGDAADSSAVTESSESASDVASPDSKSCSKIITEEAGLSKVDRCDSALGEAGLGAQPIDAQI
Protein: Buddy of Hmr 2, isoform A (Buddy of Hmr 2, isoform B) (FI09336p) (Q9VKI2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Buddy of Hmr 1
- LD09786p
- Rab at 9D
Sequence:
MQQTNPASGGDALLPLRTCNTTGCKVATVVEKTKRKCSQFVSAPYIMPKPLVVNGHTSIFQVGGEMAHMGDIPALSKISDGGQLVYRIKPGTHAHVINYVIIDEGSDSLEKARSGDQEAMRLLLESQRDSAASKLQKFLTNHKGTPPSGYISSLILSRPVASVSTSAGTPAATGHVTTPQIHPNFSIASVEGAVPFRRAVPPLAVNPSAPAPVPSGPLPAVSAVQADSVDRLQAELVELRRTVARLEENSRR
Protein: 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase (EC 2.3.1.117) (Tetrahydrodipicolinate N-succinyltransferase) (THDP succinyltransferase) (THP succinyltransferase) (Tetrahydropicolinate succinylase) (P9WP21)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Catalyzes the conversion of the cyclic tetrahydrodipicolinate (THDP) into the acyclic N-succinyl-L-2-amino-6-oxopimelate using succinyl-CoA.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02122}.
Interaction partners:
- Putative succinyl-diaminopimelate desuccinylase DapE
- Probable N-succinyldiaminopimelate aminotransferase DapC
- 4-hydroxy-tetrahydrodipicolinate reductase
- 4-hydroxy-tetrahydrodipicolinate synthase
- Diaminopimelate epimerase
- Acetylornithine aminotransferase
- Aspartate-semialdehyde dehydrogenase
- Aspartokinase
- Diaminopimelate decarboxylase
- UDP-N-acetylmuramate--L-alanine ligase
Sequence:
MSTVTGAAGIGLATLAADGSVLDTWFPAPELTESGTSATSRLAVSDVPVELAALIGRDDDRRTETIAVRTVIGSLDDVAADPYDAYLRLHLLSHRLVAPHGLNAGGLFGVLTNVVWTNHGPCAIDGFEAVRARLRRRGPVTVYGVDKFPRMVDYVVPTGVRIADADRVRLGAHLAPGTTVMHEGFVNYNAGTLGASMVEGRISAGVVVGDGSDVGGGASIMGTLSGGGTHVISIGKRCLLGANSGLGISLGDDCVVEAGLYVTAGTRVTMPDSNSVKARELSGSSNLLFRRNSVSGAVEVLARDGQGIALNEDLHAN
Protein: E3 ubiquitin ligase TRIM40 (EC 2.3.2.27) (Probable E3 NEDD8-protein ligase) (RING finger protein 35) (Q6P9F5)
Organism: Homo sapiens (Human)
Function: E3 ubiquitin-protein ligase that plays a role in the limitation of the innate immune response. Mediates inhibition of the RLR signaling pathway by ubiquitinating RIGI and IFIH1 receptors, leading to their proteasomal degradation. Promotes also the neddylation of IKBKG/NEMO, stabilizing NFKBIA, and thereby inhibiting of NF-kappa-B nuclear translocation and activation.
Interaction partners:
- NF-kappa-B essential modulator
- Ubiquitin-like protein NEDD8
- ELKS/Rab6-interacting/CAST family member 1
- Antiviral innate immune response receptor RIG-I
- Interferon-induced helicase C domain-containing protein 1
- Pyrin domain-containing protein 1
- Apoptosis-associated speck-like protein containing a CARD
Sequence:
MIPLQKDNQEEGVCPICQESLKEAVSTNCGHLFCRVCLTQHVEKASASGVFCCPLCRKPCSEEVLGTGYICPNHQKRVCRFCEESRLLLCVECLVSPEHMSHHELTIENALSHYKERLNRRSRKLRKDIAELQRLKAQQEKKLQALQFQVDHGNHRLEAGPESQHQTREQLGALPQQWLGQLEHMPAEAARILDISRAVTQLRSLVIDLERTAKELDTNTLKNAGDLLNRSAPQKLEVIYPQLEKGVSELLLQPPQKL
Protein: Vitamin K epoxide reductase complex subunit 1 (EC 1.17.4.4) (Vitamin K1 2,3-epoxide reductase subunit 1) (Q9BQB6)
Organism: Homo sapiens (Human)
Function: Involved in vitamin K metabolism. Catalytic subunit of the vitamin K epoxide reductase (VKOR) complex which reduces inactive vitamin K 2,3-epoxide to active vitamin K. Vitamin K is required for the gamma-carboxylation of various proteins, including clotting factors, and is required for normal blood coagulation, but also for normal bone development.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:14765194, ECO:0000269|PubMed:15716279, ECO:0000269|PubMed:16270630, ECO:0000269|PubMed:20978134, ECO:0000269|PubMed:22923610}; Multi-pass membrane protein {ECO:0000269|PubMed:14765194, ECO:0000269|PubMed:15716279, ECO:0000269|PubMed:16270630, ECO:0000269|PubMed:20696932, ECO:0000269|PubMed:20978134, ECO:0000269|PubMed:22923610, ECO:0000269|PubMed:33154105}.
Interaction partners:
- Vitamin K-dependent gamma-carboxylase
- Cytochrome P450 2C9
- Cytochrome P450 4F2
- Vitamin K epoxide reductase complex subunit 1-like protein 1
- NAD
- Cytochrome P450 2C19
- Vitamin K-dependent protein S
- Matrix Gla protein
- Prothrombin
- ATP-binding cassette sub-family C member 6
Sequence:
MGSTWGSPGWVRLALCLTGLVLSLYALHVKAARARDRDYRALCDVGTAISCSRVFSSRWGRGFGLVEHVLGQDSILNQSNSIFGCIFYTLQLLLGCLRTRWASVLMLLSSLVSLAGSVYLAWILFFVLYDFCIVCITTYAINVSLMWLSFRKVQEPQGKAKRH
Protein: Phycocyanobilin lyase CpcT (EC 4.-.-.-) (B1XI94)
Organism: Picosynechococcus sp. (strain ATCC 27264 / PCC 7002 / PR-6) (Agmenellum quadruplicatum)
Function: Attaches a phycocyanobilin (PCB) chromophore to 'Cys-153' of the C-phycocyanin beta subunit (PhcB). It does not attach chromophore to CpcA, ApcA or ApcB, the other phycobiliproteins.
Interaction partners:
- Phycocyanobilin lyase subunit alpha
- Phycocyanobilin lyase subunit CpcS
- C-phycocyanin subunit beta
- Phycocyanobilin lyase subunit CpcU
- Phycocyanobilin lyase subunit beta
- C-phycocyanin subunit alpha
- Allophycocyanin alpha subunit
- Allophycocyanin beta subunit
- Phycobilisome 32.3 kDa linker polypeptide, phycocyanin-associated, rod
- Phycobilisome rod-core linker polypeptide CpcG
Sequence:
MSHSTDAHTLARWMAGEFSNEAQALANPPLWAHIKVCMRPLPNQFFDGYGLYLEQAYSSDTSAPYRLRLFHIKPVDDHMELVHYKPKDDAKTKYMGAARNPAMMQHFDMADLDPMPGCDMIVTWSGTSFKGTVQAGKGCRVVRYNKESYLDNSFEITDNALISIDRGRDPVTNEILWGSLAGAFEFEKINNFSGEVQPH
Protein: Eukaryotic translation initiation factor 3 subunit L (eIF3l) (66 kDa tyrosine-rich heat shock protein) (67 kDa polymerase-associated factor) (Eukaryotic translation initiation factor 3 subunit 6-interacting protein) (Eukaryotic translation initiation factor 3 subunit E-interacting protein) (HSP-66Y) (PAF67) (Q8QZY1)
Organism: Mus musculus (Mouse)
Function: Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis. The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre-initiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation, including cell cycling, differentiation and apoptosis, and uses different modes of RNA stem-loop binding to exert either translational activation or repression.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03011}.
Interaction partners:
- Eukaryotic translation initiation factor 3 subunit I
- Eukaryotic translation initiation factor 3 subunit K
- Eukaryotic translation initiation factor 3 subunit E
- Eukaryotic translation initiation factor 3 subunit M
- Eukaryotic translation initiation factor 3 subunit B
- Eukaryotic translation initiation factor 3 subunit A
- Eukaryotic translation initiation factor 3 subunit F
- Eukaryotic translation initiation factor 3 subunit H
- Eukaryotic translation initiation factor 3 subunit D
- Eukaryotic translation initiation factor 3 subunit C
Sequence:
MSYPADDYESEAAYDPYAYPGDYDMHTGDPKQDLAYERQYEQQTYQVIPEVIKNFIQYFHKTVSDLIDQKVYELQASRVSSDVIDQKVYEIQDIYENSWTKLTERFFKNTPWPEAEAIAPQVGNDAVFLILYKELYYRHIYAKVSGGPSLEQRFESYYNYCNLFNYILNADGPAPLELPNQWLWDIIDEFIYQFQSFSQYRCKTAKKSEGEMDFLRSNPKVWNVHSVLNVLHSLVDKSNINRQLEVYTSGGDPESVAGEYGRHSLYKMLGYFSLVGLLRLHSLLGDYYQAIKVLENIELNKKSMYSRVPECQVTTYYYVGFAYLMMRRYQDAIRVFANILLYIQRTKSMFQRTTYKYEMINKQNEQMHALLAIALTMYPMRIDESIHLQLREKYGDKMLRMQKGDPQVYEELFSYACPKFLSPVVPNYDNVHPNYHKEPFLQQLKVFSDEVQQQAQLSTIRSFLKLYTTMPVAKLAGFLDLTEQEFRIQLLVFKHKMKNLVWTSGISALDGEFQSASEVDFYIDKDMIHIADTKVARRYGDFFIRQIHKFEELNRTLKKMGQRP
Protein: Uncharacterized protein (Q57VT1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Uncharacterized protein
- HMG box domain-containing protein
Sequence:
MMTLRSSTSLQSDLSRFIFPLARSLRHDKVSGAVTDASPVGSVTASGRHNAAEYVKPEGFCKSHQRTPGVRKTVTYFSPHMNALLNRPFGSTGTIDTNVPLYQCPICSCGSSAEGDIKRHMQPWMDPQEMTRHMSWLHASSGYTQSNFSIYNAGEMRRLCKSLPCSSADDPREETAMKPRVVLMLDVANIELSLEDVLIQLLTSEESILFFSRVACAIVCVHEVFIPHTSRPGHIFFQLSRLNALSDIFTLYAATRIESGDLLTAALMGELLFQDMRGCAPSIVLLTRDQQQKLCVSNMFSGVAGRGARVFLPRITAQSILCCLREANLASMGL
Protein: Repressor protein (Q8W0W7)
Organism: Oryza sativa (Rice)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MRKKLGTRFPAARIKKIMQADEDVGKIALAVPVLVSRALELFLQDLIDRTYEITLQSGAKTLNSFHLKQCVRRYSSFDFLTEVVNKVPDLGGADSCGDDRALPRRRKALPNGSDPENEESRSSKMAVRSANISPRGRGRGRGRGRGRPPTKRKEVGYVQFEDESSMFADQGEALPGEETVPETIHGTESVPPSTHPPAEAPSAAEIPAPNPKVEEAKNDDHQPDWPMPDAIGNIGVGPSGFGHLTVQVDEDEDYDNED
Protein: Calsequestrin-2 (Calsequestrin, cardiac muscle isoform) (O14958)
Organism: Homo sapiens (Human)
Function: Calsequestrin is a high-capacity, moderate affinity, calcium-binding protein and thus acts as an internal calcium store in muscle. Calcium ions are bound by clusters of acidic residues at the protein surface, especially at the interface between subunits. Can bind around 60 Ca(2+) ions. Regulates the release of lumenal Ca(2+) via the calcium release channel RYR2; this plays an important role in triggering muscle contraction. Plays a role in excitation-contraction coupling in the heart and in regulating the rate of heart beats.
Subcellular location: Sarcoplasmic reticulum lumen {ECO:0000250|UniProtKB:O09161}. Note=This isoform of calsequestrin occurs in the sarcoplasmic reticulum's terminal cisternae luminal spaces of cardiac and slow skeletal muscle cells. {ECO:0000250|UniProtKB:O09161}.
Interaction partners:
- Triadin
- Ryanodine receptor 2
- Aspartyl/asparaginyl beta-hydroxylase
- Ryanodine receptor 1
- Ryanodine receptor 3
- Calsequestrin-1
- Peptidyl-prolyl cis-trans isomerase FKBP1B
- Voltage-dependent L-type calcium channel subunit alpha-1C
- Phospholamban
- Inward rectifier potassium channel 2
Sequence:
MKRTHLFIVGIYFLSSCRAEEGLNFPTYDGKDRVVSLSEKNFKQVLKKYDLLCLYYHEPVSSDKVTQKQFQLKEIVLELVAQVLEHKAIGFVMVDAKKEAKLAKKLGFDEEGSLYILKGDRTIEFDGEFAADVLVEFLLDLIEDPVEIISSKLEVQAFERIEDYIKLIGFFKSEDSEYYKAFEEAAEHFQPYIKFFATFDKGVAKKLSLKMNEVDFYEPFMDEPIAIPNKPYTEEELVEFVKEHQRPTLRRLRPEEMFETWEDDLNGIHIVAFAEKSDPDGYEFLEILKQVARDNTDNPDLSILWIDPDDFPLLVAYWEKTFKIDLFRPQIGVVNVTDADSVWMEIPDDDDLPTAEELEDWIEDVLSGKINTEDDDEDDDDDDNSDEEDNDDSDDDDDE
Protein: Kinetoplast DNA-associated protein, putative (Q38A85)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MFRACLRFLAVSPFTLFMMDQKNNPALKGCAISKRGKLLSKMYKELSQNQRRELNMRAARHPNLGKRSKTEITDEKRSSRRKSKGTFATFVKNNYASVRGLNYRKRFAALSKLYNLSRPIQMEEVIKSMPKGHSLAALPGGKGSASVKAKEKEVVIAKAVQDASEMLRAAQKEGGKSDTSEKKPTRKGRGAPKKEEKPTQKEKKVTKKK
Protein: Nuclear GTPase SLIP-GC (EC 3.6.1.-) (Speckled-like pattern in the germinal center) (Q68CJ6)
Organism: Homo sapiens (Human)
Function: Nuclear GTPase found in germinal center B-cells, where it may inhibit function of the activation-induced cytidine deaminase AICDA. Reduces somatic hypermutation in B-cells which may enhance genome stability (By similarity).
Subcellular location: Nucleus speckle {ECO:0000269|PubMed:19734146}.
Interaction partners:
Sequence:
MAETKDVFGQEPHPVEDDLYKERTRKRRKSDRDQRFRAFPSMEQSALKEYEKLESRTRRVLSNTYQKLIQSVFLDDSIPNGVKYLINRLLALIEKPTVDPIYIALFGSTGAGKSSLINAIIQQAMFLPVSGESICTSCIVQVSSGCCVQYEAKIHLLSDQEWREELKNLTKLLHRTEELSREEADAWNRDEAVEEATWKLQMIYGNGAESKNYEELLRAKPKRKIPTSRVITLKAEEAEELSIKLDPYIRTQRRDWDGEAAEMRIWPLIKHVEVTLPKSDLIPEGVVLVDIPGTGDFNSKRDEMWKKTIDKCSVIWVISDIERVSGGQAHEDLLNESIKACQRGFCRDVALVVTKMDKLHLPEYLRERKAGNQAIQSQREAVLERNEMIKLQRTRILKEKLKRKLPADFKVLEASDLVYTVSAQEYWQQALLTEEETEIPKLREYIRKSLLDKKKRTVTKYVTEAFGLLLLTDSFNSTQNLPNEHLHMSVLRRFAEEKVELLEKAIAQCFACMEQPLQEGVRTARTSYRCILRACLVRSKGNQGFHQTLKAVCLKNGIYASRTLARIDLNEALTQPVYDQIDPVFGSIFRTGKPTGSALMPHIDAFKQSLQEKMTEIGIRSGWKYDSCKKNFLIQEISAILGGLEDHILRRKRRIYESLTASVQSDLKLCYEEAAQITGKKACERMKDAIRRGVDRQVAEGMFERAQERMQHQFQQLKTGIVEKVKGSITTMLALASSQGDGLYKELADVGSEYKEMEKLHRSLREVAENARLRKGMQEFLLRASPSKAGPPGTSL
Protein: Beta-crystallin B1 (Beta-B1 crystallin) (P53674)
Organism: Homo sapiens (Human)
Function: Crystallins are the dominant structural components of the vertebrate eye lens.
Interaction partners:
- Phakinin
- Gap junction alpha-8 protein
- Gap junction alpha-3 protein
- Beta-crystallin A3
- Alpha-crystallin A2
- Filensin
- Alpha-crystallin B chain
- Pituitary homeobox 3
- Transmembrane protein 114
- Lens fiber membrane intrinsic protein
Sequence:
MSQAAKASASATVAVNPGPDTKGKGAPPAGTSPSPGTTLAPTTVPITSAKAAELPPGNYRLVVFELENFQGRRAEFSGECSNLADRGFDRVRSIIVSAGPWVAFEQSNFRGEMFILEKGEYPRWNTWSSSYRSDRLMSFRPIKMDAQEHKISLFEGANFKGNTIEIQGDDAPSLWVYGFSDRVGSVKVSSGTWVGYQYPGYRGYQYLLEPGDFRHWNEWGAFQPQMQSLRRLRDKQWHLEGSFPVLATEPPK
Protein: Late embryogenesis abundant protein D-113 (LEA D-113) (P09441)
Organism: Gossypium hirsutum (Upland cotton) (Gossypium mexicanum)
Function: LEA proteins are late embryonic proteins abundant in higher plant seed embryos. There are two subsets of LEA proteins (5a and 5b), the first ones are expressed when the cotyledon weight reach 80 mg and the second set are expressed above 100 mg. The function of those proteins is not known.
Interaction partners:
Sequence:
MQSMKDAAASAKAGMEKAKASMQEKVDQMKTRDPNEKEMARERKEERQEDAELRKQEARHHNATAGHVGGGGIGGTGYTTAGYNIGDTGGYGGTGGHDNRGYPTAGSGYDTGRQDDLSSMGFGGDTEGAYGTTGNQDFPNAASNNAGTRRNTRGGTQDDPYYRSY
Protein: Tau-tubulin kinase 2 (EC 2.7.11.1) (Protein bartleby) (Q3UVR3)
Organism: Mus musculus (Mouse)
Function: Serine/threonine kinase that acts as a key regulator of ciliogenesis: controls the initiation of ciliogenesis by binding to the distal end of the basal body and promoting the removal of CCP110, which caps the mother centriole, leading to the recruitment of IFT proteins, which build the ciliary axoneme. Has some substrate preference for proteins that are already phosphorylated on a Tyr residue at the +2 position relative to the phosphorylation site. Able to phosphorylate tau on serines in vitro. Phosphorylates MPHOSPH9 which promotes its ubiquitination and proteasomal degradation, loss of MPHOSPH9 facilitates the removal of the CP110-CEP97 complex (a negative regulator of ciliogenesis) from the mother centrioles, promoting the initiation of ciliogenesis (By similarity).
Subcellular location: Cell projection, cilium {ECO:0000269|PubMed:23141541}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:23141541, ECO:0000269|PubMed:29038301}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:23141541, ECO:0000269|PubMed:29038301}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q6IQ55}. Nucleus {ECO:0000250|UniProtKB:Q6IQ55}. Note=Localizes at the transition zone, a region between the basal body and the ciliary axoneme (PubMed:29038301). May also be present in cytosol and, at lower level in the nucleus (By similarity). {ECO:0000250|UniProtKB:Q6IQ55, ECO:0000269|PubMed:29038301}.
Interaction partners:
- Centrosomal protein of 164 kDa
- Centrosomal protein of 83 kDa
- Fas-binding factor 1
- Centriolar coiled-coil protein of 110 kDa
- Rab-3A-interacting protein
- Sodium channel and clathrin linker 1
- Centrosomal protein of 97 kDa
Sequence:
MSGGGEQPDILSVGILVKERWKVLRKIGGGGFGEIYDALDMLTRENVALKVESAQQPKQVLKMEVAVLKKLQGKDHVCRFIGCGRNDRFNYVVMQLQGRNLADLRRSQSRGTFTISTTLRLGKQILESIESIHSVGFLHRDIKPSNFAMGRFPSTCRKCFMLDFGLARQFTNSCGDVRPPRAVAGFRGTVRYASINAHRNREMGRHDDLWSLFYMLVEFVVGQLPWRKIKDKEQVGSIKERYDHRLMLKHLPPEFSTFLDHISSLDYFTKPDYQLLTSVFDNSIKTFGVIESDPFDWEKSGTDGSLTTTTTSATPQLHTRLTPAAIGIANATPIPGDLLRENTDEVFPDEQLSDGENGIPVGVSPDKLPGSLGHPRPQEKDVWEEMDINKNKIKLGICKAATEEENSHGQVNGILNAPSLGSPIRVRSEITQPDRDVPLVRKLRSIHSFELEKRLTLEPKPDTDKFLETCMEKMQKDSSAGKEPVPPALPHKPCVPVVTHTDHIWHYDDEYLPDASKPASANTPEQADGGGSNGFIAVNLSSCKQEVDSKEWVIVDKEQDLQDFRTNEVLGHKTTGSPSDEEPEVLQVLEGSPQDEKIQVGPWTDNHHLKKESSGVVLALSAECPATAASELYTDRLDLQAGAASQFITVTPTSPMEAQAEGPLTAITIPRPSVASTQSTSGSFHYGPQPEKKDLQPLEPTVELYSPRENFSGLVVTEGELASGGSRVDLGLQIDHTGHDMLPNMRDGDTSQDLGPKDPPDHNRLAVKEFEHLPGETEERSLLLGSENEDERLSKGQHCIEVSSPGELVTAERAQLAATEPLHVSETQNCSVLPNQDKTHEIMKLLAVGTSEISPQAIDPHAEGQIGQMAAMQKNKLFKDDGIQSESLPRQQGDLSAFLHQEGKREKVVPRNGELYHCVSENEHGPPTRKDMLRSSFVTRHSRIPVLAQEIDSTFESSSAISAKEKLLQKKAYQPEIVKLLVEKRQFKSFLGDLSSASDKLIEEKLAAVPVPFSEEEVFAPFSRLAADSHLSRSVEDSFLSPIISQARKSKIPRPVSWVSTDQINGSASPQFLPRPPPGKPPVRPGVEARLRRYKVLGSSNSDSDLFSRLAQILQNGSQKSRSTTQCKSPGSPHNPKTPPKSPVVPRRSPSASPRSSSLPRTSSSSPSRAGRPHHDQRSSSPHLGRSKSPPSHSGSSSSRRSCQQEHCKPSKNGPKGSGSLHHHSTSSKTPPGKSKPASKLSR
Protein: Vitronectin (VN) (S-protein) (Serum-spreading factor) (P48819)
Organism: Sus scrofa (Pig)
Function: Vitronectin is a cell adhesion and spreading factor found in serum and tissues. Vitronectin interact with glycosaminoglycans and proteoglycans. Is recognized by certain members of the integrin family and serves as a cell-to-substrate adhesion molecule. Inhibitor of the membrane-damaging effect of the terminal cytolytic complement pathway (By similarity).
Subcellular location: Secreted, extracellular space.
Interaction partners:
- Plasminogen activator inhibitor 1
- Integrin beta
- Plasminogen activator, urokinase receptor.
- Albumin
- Urokinase-type plasminogen activator
- Plasminogen
- Integrin alpha-V
- Integrin beta
- Clusterin
- Inter-alpha-trypsin inhibitor heavy chain H2
Sequence:
MAPLRPLLMLALLAWVALADQESCKGRCTDGFIAERKCQCDELCSYYQSCCTDYVAECKPQVTRGDVFLQPDDEYRAYDYHEETRHNTSVQEEQRIPVLLAKTEETPVLKPEEEAPPPGPQTDDLGVPEEELCSGKPFDAFTNLKNGSVFAFRGLYCYELDEKAVRPGYPKLIQDVWGIKGPIDAAFTRINCQGKTYLFKGSQYWRFDDGVLDPNYPREISEGFKGIPDDVDAALALPAHSYSGRERVYFFKGKQYWEYVFQQQPSREECEGSSPSDVFAHFALMQRDSWEDIFRLLFWSHSFGGAIEPRVISQDWLGLPEQVDAAMAGQIYISGSALKPSQPKMTKSARRSGKRYRSRRGRGRGRGHSRSQKSHRQSRSTWLPWFSSEETGPGGYNYDDYKMDWLVPATCEPIQSVYFFSGEEYYRVNLRTQRVDTVTPPYPRSIAQYWLGCPVPDQK
Protein: Actin Act1 (Q4WDH2)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Interaction partners:
- Actin-related protein 4
- Chromatin remodeling complex subunit
- Arp2/3 complex subunit
- Fimbrin
- Arp2/3 complex subunit
- Helicase swr1
- Profilin
- Chromatin-remodeling ATPase INO80
- Cytokinesis protein SepA/Bni1
- Cofilin
Sequence:
MSLCRLSPGECVNRCPCVRLDNPIPGGFLSLNHHARQLNLDNETLTCEIASIVGRPRHHGIMIGMGQKDSYVGDEAQSKRGILTLRYPIEHGVVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPINPKSNREKMTQIVFETFNAPAFYVSIQAVLSLYASGRTTGIVLDSGDGVTHVVPIYEGFALPHAISRVDMAGRDLTDYLMKILAERGYTFSTTAEREIVRDIKEKLCYVALDFEQEIQTASQSSSLEKSYELPDGQVITIGNERFRAPEALFQPSVLGLESGGIHVTTFNSIMKCDVDVRKDLYGNIVMSGGTTMYPGISDRMQKEITALAPSSMKVKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIVHRKCF
Protein: Prokaryotic-type class I peptide chain release factors domain-containing protein (Q38CG3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MHRQRRLVRGLLSNSSSQMLGCRPFFGMSGRGSGGAGGRGDSGKEGEVGGKGWSGLFSGAGGLPPGFDEQRLKAVQEIFNKQSPEKQAELMKKALEFQKVFGKVPGIGKMAQKNIEMLEKVVINNSSQQQQQTPPKANGIRSMSGAAERENKAKIKSSNESTAAGSARISGGAAGPTIDELKKINLGPEIEELFAELSSIRAKKNSYRSKFLAAETDLEKLRKEVEQLRETDASLRSKLRRVEQDVMLLNSENMELKEHEKEWRQVRHKNEKLTDAVQRLQHDNAAQDRQLSEALQVQLKEKDDMLRSLQRKLDRLRKRDPLLQFSLLCSDVARLCDTEQNAAKDAAEDAFNMLQGIHQQKQDAAWKSAMLQDGAAAKAFMAVVRRFYLSRVPHANYDALVAVDDAEALRPLVSEMGFTLEHVAAGRYVIVAPSVEVPKTFIGPYGLCAALYLAGKSVEGEKMFSFKLTVVYPHVSSTLFGNTCRTGVQYDTARSSGPGGQAVNVSETQIIAKLSIDGDAAYTAEAQDSRSALNNREAATEKLAKTRRQHYNEQLAKQHKPEGLERELVAVVQSTLNGNGSSGSDGMVGPVPKEIVELVNDTVAKKLLPGAELGLLYGMLYLFREAAAAASS
Protein: TBC1 domain family, member 4 (A0A8I6ABF1)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MESPSCIQDEPFPHPLEPEPIALAQPGATKPGDKRFRLWYVGGSCLDRRTTLPMLPWLMAEIRRRSLKPEAGGCGAPAAREVLLVLSAPFLRCVPAPGVGVGGGAGSGAVQPNTGVFIFEHKAQHISRFIHNSHDLTYFAYLIKAQPDDPESQMACHVFRATDPNQVPDVISSIRQLSKAAMKEDAKPSKDNEDAFYNSQKFEVLYCGRVIVTHKKAPSSLIDDCKDKFSLHEQQRLKLQGERGGDPGDGDEMGVLEAESPVSPDDGLPEKPDGLVNCPRALPSLASLPALASQPALASSRVCFPERILEDCGFDEQQEFRSRCSSVTGVMQKKVHENNQKTQPRRRHASAPSHVQPSDSEKNRTMLFQVGRFEINLISPDTKSVVLEKNFKDISSCSQGIKHVDHFGFICRESLEPGLSQYICYVFQCANESLVDEVMLTLKQAFSTAAALQSAKTQIKLCEACPMHSLHKLCERIEGLYPPRAKLVIQRHLSSLTDNEQADIFERVQKMKPISDQEENELVILHLRQLCEAKQKTHVHIGEGQAIISNSTIPENSTSGGRFKLDVLKNKAKRSLTSSLENIFSRGANRMRGRLGSVDSFERSNSLASEKDFSPGGSPPGTPPASPLSSAWHTFPEEDSDSPQFRRRAHTFSHPPSSSRRKLNLQDGKAHGLRSPLLRQNSSEQCSVLPSARRMCKESNSSSSLPSLHTSFSAPSFTASSFLKSFYQSSDRCARTSSTCSNESLSAGGTPVTPRRISWRQRIFLRVASPVNKSPSAMQQQKDGLDRTELLPLSPLSPTMEEEPLVIFLSGDEDTEKVEEKKKSKEIKSLWKKAIHQQILLLRMEKENQKLEARRDELQSRKVKLDYEEVGTCQKEVLIAWDKKLLNCRTKIRCDMEDIHTSLKEGVPKSRRGEIWQFLALQYRLRHRLPNKHQPPDTSYKELLKQLTAQQHAILVDLGRTFPTQPYFSVQLGAGQLSLFNLLKAYSLLDKEVGYCQGISFVAGVLLLHMSEEQAFEMLKFLMYDLGFRKQYRPDMMSLQIQMYQLSRLLHDYHRDLYNHLEENEISPSLYAAPWFLTLFASQFPLGFVARVFDIIFLQGTEVIFKVALSLLSSQEALVMECENFENIVEFLKSTLPDMNTTEMEKIITQVFEMDISKQLHAYEVEYHVLQDELLESSYACEDNESLEKLERANNQLKRQNMDLLEKLQVAHAKIQALESNLETLLTRETKMKALIRTLEQDKMAYQKTVEQIRKLLPADALANCELLLKDLSYPTNDKAKAGNKP
Protein: Cathepsin H (E9PKT6)
Organism: Homo sapiens (Human)
Subcellular location: Lysosome {ECO:0000256|ARBA:ARBA00004371}.
Interaction partners:
Sequence:
MSKHRKTYSTEEYHHRLQTFASNWRKINAHNNGNHTFKMALNQFSDMSFAEIKHKYLWSEPQNCSATKSNYLRGTGPYPPSVDWRKKGNFVSPVKNQGACGSCWTFSTTGALESAIAIATGKMLSLAEQQLVDCAQDFNNHGCQGGLPSQAFEYILYNKGIMGEDTYPYQGKDGYCKFQPGKAIGFVKDVANITIYDEEAMVEAVALYNPVSFAFEVTQDFMMYRTGIYSSTSCHKTPDKVNHAVLAVGYGEKNGIPYWIVKNSWGPQWGMNGYFLIERGKNMCGLAACASYPIPLV
Protein: ATP synthase subunit c, chloroplastic (ATP synthase F(0) sector subunit c) (ATPase subunit III) (F-type ATPase subunit c) (F-ATPase subunit c) (Lipid-binding protein) (P56760)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000255|HAMAP-Rule:MF_01396}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01396}.
Interaction partners:
- ATP synthase subunit b, chloroplastic
- ATP synthase subunit a, chloroplastic
- ATP synthase subunit alpha, chloroplastic
- ATP synthase epsilon chain, chloroplastic
- ATP synthase subunit beta, chloroplastic
- ATP synthase subunit alpha
- ATP synthase subunit alpha
- V-type proton ATPase subunit D
- ATP synthase subunit delta, chloroplastic
- ATP synthase gamma chain 1, chloroplastic
Sequence:
MNPLVSAASVIAAGLAVGLASIGPGVGQGTAAGQAVEGIARQPEAEGKIRGTLLLSLAFMEALTIYGLVVALALLFANPFV