wanglab/gogpt-training-data huggingface dataset:
Protein: Nectin-3 (Nectin cell adhesion molecule 3) (Poliovirus receptor-related protein 3) (CD antigen CD113) (Q9JLB9)
Organism: Mus musculus (Mouse)
Function: Plays a role in cell-cell adhesion through heterophilic trans-interactions with nectins-like or other nectins, such as trans-interaction with NECTIN2 at Sertoli-spermatid junctions. Trans-interaction with PVR induces activation of CDC42 and RAC small G proteins through common signaling molecules such as SRC and RAP1. Also involved in the formation of cell-cell junctions, including adherens junctions and synapses. Induces endocytosis-mediated down-regulation of PVR from the cell surface, resulting in reduction of cell movement and proliferation. Plays a role in the morphology of the ciliary body.
Subcellular location: Cell membrane {ECO:0000269|PubMed:21798896}; Single-pass membrane protein {ECO:0000255}. Postsynaptic cell membrane {ECO:0000269|PubMed:11827984}; Single-pass type I membrane protein {ECO:0000255}. Cell junction, adherens junction {ECO:0000269|PubMed:15328010}. Note=In the auditory epithelium, specificaly localizes to the apical side of the lateral membranes of supporting cells. {ECO:0000269|PubMed:21798896}.
Interaction partners:
- Afadin
- T-cell immunoreceptor with Ig and ITIM domains
- Nectin-2
- Nectin-1
- Poliovirus receptor
- Cell adhesion molecule 1
- Partitioning defective 3 homolog
- Cell adhesion molecule 3
- Nectin-4
Sequence:
MARTPGPAPLCPGGGKAQLSSAFPPAAGLLLPAPTPPPLLLLLIPLLLFSRLCGALAGSIIVEPHVTAVWGKNVSLKCLIEVNETITQISWEKIHGKSTQTVAVHHPQYGFSVQGDYQGRVLFKNYSLNDATITLHNIGFSDSGKYICKAVTFPLGNAQSSTTVTVLVEPTVSLIKGPDSLIDGGNETVAAVCVAATGKPVAQIDWEGDLGEMESSTTSFPNETATIVSQYKLFPTRFARGRRITCVVKHPALEKDIRYSFILDIQYAPEVSVTGYDGNWFVGRKGVNLKCNADANPPPFKSVWSRLDGQWPDGLLASDNTLHFVHPLTVNYSGVYVCKVSNSLGQRSDQKVIYISDPPTTTTLQPTVQWHSSPADVQDIATEHKKLPFPLSTLATLKDDTIGTIIASVVGGALFLVLVSILAGVFCYRRRRTFRGDYFAKNYIPPSDMQKESQIDVLHQDELDSYPDSVKKENKNPVNNLIRKDYLEEPEKTQWNNVENLTRFERPMDYYEDLKMGMKFVSDERYNESEDGLVSHVDGSVISRREWYV
Protein: NADPH oxidase 1 (NOX-1) (EC 1.6.3.-) (Mitogenic oxidase 1) (MOX-1) (NADH/NADPH mitogenic oxidase subunit P65-MOX) (NOH-1) (Q9WV87)
Organism: Rattus norvegicus (Rat)
Function: Pyridine nucleotide-dependent oxidoreductase that generates superoxide and might conduct H(+) ions as part of its electron transport mechanism.
Subcellular location: Cell projection, invadopodium membrane {ECO:0000250|UniProtKB:Q9Y5S8}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:Q9Y5S8}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Cytochrome b-245 light chain
- Neutrophil cytosolic factor 1
- NADPH oxidase 4
- NADPH oxidase 2
- NADPH oxidase organizer 1
- NADPH oxidase activator 1
- NADPH oxidase 3
- Dual oxidase 1
- Neutrophil cytosol factor 4
- Ras-related C3 botulinum toxin substrate 1
Sequence:
MGNWLVNHWLSVLFLVSWLGLNIFLFVYVFLNYEKSDKYYYTREILGTALALARASALCLNFNSMVILIPVCRNLLSFLRGTCSFCNHTLRKPLDHNLTFHKLVAYMICIFTAIHIIAHLFNFERYSRSQQAMDGSLASVLSSLFHPEKEDSWLNPIQSPNVTVMYAAFTSIAGLTGVVATVALVLMVTSAMEFIRRNYFELFWYTHHLFIIYIICLGIHGLGGIVRGQTEESMSESHPRNCSYSFHEWDKYERSCRSPHFVGQPPESWKWILAPIAFYIFERILRFYRSRQKVVITKVVMHPCKVLELQMRKRGFTMGIGQYIFVNCPSISFLEWHPFTLTSAPEEEFFSIHIRAAGDWTENLIRTFEQQHSPMPRIEVDGPFGTVSEDVFQYEVAVLVGAGIGVTPFASFLKSIWYKFQRAHNKLKTQKIYFYWICRETGAFAWFNNLLNSLEQEMDELGKPDFLNYRLFLTGWDSNIAGHAALNFDRATDVLTGLKQKTSFGRPMWDNEFSRIATAHPKSVVGVFLCGPPTLAKSLRKCCRRYSSLDPRKVQFYFNKETF
Protein: 5-aminolevulinate synthase, non-specific, mitochondrial (ALAS-H) (EC 2.3.1.37) (5-aminolevulinic acid synthase 1) (Delta-ALA synthase 1) (Delta-aminolevulinate synthase 1) (P07997)
Organism: Gallus gallus (Chicken)
Function: Catalyzes the pyridoxal 5'-phosphate (PLP)-dependent condensation of succinyl-CoA and glycine to form aminolevulinic acid (ALA), with CoA and CO2 as by-products.
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P22557}; Peripheral membrane protein {ECO:0000250|UniProtKB:P22557}. Note=Localizes to the matrix side of the mitochondrion inner membrane. {ECO:0000250|UniProtKB:P22557}.
Interaction partners:
- Delta-aminolevulinic acid dehydratase
- Sarcosine dehydrogenase.
- Ferrochelatase, mitochondrial
- Uncharacterized protein.
- Uroporphyrinogen decarboxylase.
- Uroporphyrinogen-III synthase
- Alanine--glyoxylate and serine--pyruvate aminotransferase.
- Pipecolic acid and sarcosine oxidase.
- Glycine dehydrogenase
- Serine hydroxymethyltransferase
Sequence:
MEAVVRRCPFLARVSQAFLQKAGPSLLFYAQHCPKMMEAAPPAAARGLATSASRGQQVEETPAAQPEAKKAKEVAQQNTDGSQPPAGHPPAAAVQSSATKCPFLAAQMNHKSSNVFCKASLELQEDVKEMQVDRKGKEFAKIPTNSVVRNTEAEGEEQSGLLKKFKDIMLKQRPESVSHLLQDNLPKSVSTFQYDQFFEKKIDEKKKDHTYRVFKTVNRKAQIFPMADDYSDSLITKKEVSVWCSNDYLGMSRHPRVCGAVMDTLKQHGAGAGGTRNISGTSKFHVDLEKELADLHGKDAALLFSSCFVANDSTLFTLAKMLPGCEIYSDSGNHASMIQGIRNSRVPKHIFRHNDVNHLRELLKKSDPSTPKIVAFETVHSMDGAVCPLEELCDVAHEHGAITFVDEVHAVGLYGARGGGIGDRDGVMHKMDIISGTLGKAFACVGGYISSTSALIDTVRSYAAGFIFTTSLPPMLLAGALESVRTLKSAEGQVLRRQHQRNVKLMRQMLMDAGLPVVHCPSHIIPIRVADAAKNTEICDKLMSQHSIYVQAINYPTVPRGEELLRIAPTPHHTPQMMSYFLEKLLATWKDVGLELKPHSSAECNFCRRPLHFEVMSERERSYFSGMSKLLSVSA
Protein: BRCA2 and CDKN1A-interacting protein (Q9CWI3)
Organism: Mus musculus (Mouse)
Function: During interphase, required for microtubule organizing and anchoring activities. During mitosis, required for the organization and stabilization of the spindle pole. May promote cell cycle arrest by enhancing the inhibition of CDK2 activity by CDKN1A. May be required for repair of DNA damage by homologous recombination in conjunction with BRCA2. May not be involved in non-homologous end joining (NHEJ) (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9P287}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:28394342}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:28394342}. Note=Colocalizes with BRCA2 in discrete nuclear foci (By similarity). In interphase, preferential localizes to the mother centriole (PubMed:28394342). Recruited to the spindle pole matrix and centrosome by microtubules and dynein/dynactin activity (By similarity). {ECO:0000250|UniProtKB:Q9P287, ECO:0000269|PubMed:28394342}.
Interaction partners:
- Breast cancer type 2 susceptibility protein homolog
- Cyclin-dependent kinase inhibitor 1
- Ribosome production factor 2 homolog
- Large ribosomal subunit protein uL14
- Ribosome biogenesis protein BRX1 homolog
- Cyclin-H
- Cyclin-dependent kinase 7
- Probable rRNA-processing protein EBP2
- MKI67 FHA domain-interacting nucleolar phosphoprotein
- Ribosome biogenesis protein WDR12
Sequence:
MASKAKKRAVGNGIQRPLGAPGQREEEEEEEDEVEDEEEDEDDSDEEEDEVDEIVDEEVNIEFEAYSISDNDYGGIKKLLQQLFLKAPVNTAELTNLLMQQNHIGSVIKQTDVSEDSDDEVDEDEIFGFISLLNLTERKGTQCAEQIKELVLSFCEKTCEQSMVEQLDKLLNDTSKPVGLLLSERFINVPPQIALPMHQQLQKELSEARRTNKPCGKCCFYLLISKTFMEAGKSSSRKRQDSLQQGALMFANAEEEFFYEKAILKFSYSVQGESDTRLGGRWSFDDVPMTPLRTVMVIPDDRMNEIMETLKDHLSV
Protein: Pathogenesis-related protein 10 (D4HR93)
Organism: Zea mays (Maize)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MASTNSWTVEIASPVAAPRLFRAAVMDWHTLAPKVTSHVVASAHPVEGEGGVGSVRQFNFTSAMPFGFVKERLEFLDVDKCECKSTLVEGGGIGVAIETAASHGVKVESAAGGCVVKVDSTYKLLPGVEVQDEITKAKESVTNIFKAAEAYLVANPEAYN
Protein: Defense against restriction protein B (EC 3.6.4.-) (DarB) (Q71TF8)
Organism: Escherichia phage P1 (Bacteriophage P1)
Function: Capsid internal protein that is probably ejected along with the viral DNA and prevents degradation of viral DNA by the host EcoB and EcoK restriction-modification antiviral defense systems.
Subcellular location: Virion {ECO:0000269|PubMed:28509398, ECO:0000269|PubMed:3029954}. Note=Internal capsid protein. DarA is required for DarB incorporation into the virions. {ECO:0000269|PubMed:28509398}.
Interaction partners:
Sequence:
MNKLSMGVFRCSSVSEILKYIRAITSHRAPIKYGVEKVEGKSYDRLRREANQKAIDLLNSLVDGATLTDEQRQILAGYTGEGGIGGSVSEYYTPKPIAEGVWEIMKLYGADVGNTLEPSAGTGVFNETKPVGTVMTATEISSVSGRINQLLHPEDSVQISPFEQLAVSTPNDSFDHVVGNVPFGGRDNTRNIDKPYAEETDMGSYFMLRMLDKIKPGGFMCVIVPPSIVSGSNMKRLRLRLSRKAEFLGAHRLPTGTFDANGTSTVVDVVLMRKHPAEMAEKIPLVHESTLESANVLWPTFISGKWFEKDGRRFVHGTQEKGFQGRIEVRADGQIDNQALKAKLIHCFESRIDWYLLDMAEPSPTADVVDEGEMRLINGVWQKYAGGRWIESDAGKELKIDVASYGADSWEALQRNLTTTEGRLGMTFTQMANVRDKYTTSISDDMVQLVDWINSQPEKYRERLYRGAMIGRMLIEYQDMKAAGHSAEQIEQQRLSLVSRLQAEIDRFGNPGRGPIAKLSGSGARAWFAFRGAIKLDGTISDELTGKLVTHDSSASYDSTSYQDTLRYLYSDLTRDPIQLDDFRLAFTGELPASDDELLNLLASTPGIAVSPYGGIVPFARATSGDINEIVAPKQEFLATLTDGPVKNNVLNQLAAIEEKRIKTPAENIRFKLNSRWFDRSVILEFLQENGYPDLRYVQSVQLEGDEMVSDTYHGGDGLFVGHRYGVVQRKDKETGEIRYEWDRKSGENATGFPAQLEKYLNGARIGGKDSATANGYREQMALLEDQFNKWIKTHDRYDELVAKYNDVFNSNIPYEHSGDPLGLKGLSGKRQPFDYQNSEVRRLSEDGRGILGFGTGLGKTTTALALEAFNYENGRSTRTAYVVPKSVLENWYYEAKEFLSEEAFSNYLFVGLDVLMDGDQIRQVPVLDENGKPVLGTDGTPVMRDALKLADEATITARMNAIPHSNYRAVVFTKEQYARIPLRDDTVDEHAQDMLYDFVAAGRVASAMDSDSHRKEAARRRVLSEYSDTGTEKAEKYPYFEDMGFDSVIADEGHNYRNSYKNGREASQLAYLPTSAVAQSARDMAIKNAYLMKKNGGRGPVLLTATPVVNTPIDAYNMLSHVLPKEYWQKMGIYGPDDFVKFFGKTRLETVQKISGEVEEKMALVGFENLDALRGIFHRWTTLKTAEDVKDTVEIPELDEHQQDAPLTEEQLAAYEELRQQAEAAAKANNGVTTSVNEDGVIEHEKARPIFSIIRDMDRVCTDMDLYYRRITYRFLPEYADAVQQLADSLPKQATSEDDDSDDSITQQSQYSLIDKGEFIQLQVPEAFEQEVNKRLARFGIDEQTVTHPVTPKYAKLIATLKEFFPEGKQIIFTDEKTQHQKLKRIICNALNLEPSKVGILNAQTVAEAGKTGKKLKAVKPPKELPDEPTDAQIAKYNEQMALYDAYIAQQNEMSLGGLEKIAADFQEGRTPIIICNKKAEVGINLHRGTTDIHHLTLPWTPASIAQRNGRGARVGSNRASVRVHYYCGKGSFDEYRLKTLKRKAGWISDILRSDKSEMENADANDMIEMQMYTAKDDGERLAMMQVQMDKAKAAQRARQKEQATIDLQNYIKAQHAAGEDVEVLTAELERSKAELEKTTAEVAKFKQAVMAKAADNADWKARWGSVHHTDRMLLAQYRASLKSAIQRKANISQAISPYEKLLNRTQKAATDIKRLRPLVEDAINKGILDVDPDLVNHASEFLVIGDRSWRVGQYYDCAGDIVRIKSLDFDSQRADVEIIFTFKGTKSGNWDVKTLDKQVDVTPDEDAVMQKISGGVSIAGINDIISCDDFYRFQQRGMIKITDSYGVQTTESGYSIDFVGTYTDPLKHAVYPDRRDGALKSSIAKWVLGMMSEGNNRQVRLAEVFLTELFGSNYGDVIASYGDTLSPEAIQEKIADAIARMPEKTSQGATRNGDSELEVTNAIFGTHEFRASDYEITTAQFGTIGIYSNKAEIKQAMDAASARIAAEREANLNHAVAALTQSWVTAIREAATTGKITPAIADVVNDGSKFMDAYKMDAVQLPSAYGQLSYRMTYNLVSMFSDLAILGLVDLNEVTPELLSMRKNHVEILQRINTVLAGRTDEEKQADADRINLALGNITEEEIAARNEKQEELSSIQGDATSIAQSLGLNYRVSTADLKMMYAPKFAAGEVFGLQEASGMKGVLFRAKDAIKTKFGARWLPAKAKNSDFPGNWWIIETKHNVADVLAVIQQYA
Protein: Serine/threonine-protein phosphatase 2B catalytic subunit (EC 3.1.3.16) (Calmodulin-dependent calcineurin A subunit) (P48457)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Calcium-dependent, calmodulin-stimulated protein phosphatase. This subunit may have a role in the calmodulin activation of calcineurin.
Interaction partners:
- Calcineurin subunit B
- FK506-binding protein 1A
- Calmodulin
- FK506-binding protein 1B
- Calcineurin binding protein, putative
- Calmodulin
- Protein phosphatase PP2A regulatory subunit B
- Protein phosphotase 2a 65kd regulatory sububit
- Secreted thaumatin-like protein calA
- Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit
Sequence:
MDRNLARAVADKQPVPEIDFTLHVMEDGTQVSTLERVVKEVQAPALNKPSDDQFWDPEEPTKPNLQFLKQHFYREGRLTEDQALWIIQAGTQILKSEPNLLEMDAPITVCGDVHGQYYDLMKLFEVGGDPAETRYLFLGDYVDRGYFSIECVLYLWALKIWYPNTLWLLRGNHECRHLTDYFTFKLECKHKYSERIYEACIESFCALPLAAVMNKQFLCIHGGLSPELHTLEDIKSIDRFREPPTHGLMCDILWADPLEDFGQEKTGDYFIHNSVRGCSYFFSYPAACAFLEKNNLLSVIRAHEAQDAGYRMYRKTRTTGFPSVMTIFSAPNYLDVYNNKAAVLKYENNVMNIRQFNCTPHPYWLPNFMDVFTWSLPFVGEKITDMLIAILNTCSKEELEDETPSTISPAEPSPPMPMDTVDTESTEFKRRAIKNKILAIGRLSRVFQVLREESERVTELKTAAGGRLPAGTLMLGAEGIKQAITNFEDARKVDLQNERLPPSHDEVVRRSEEERRIALDRAQHEADNDTGLATVARRISMKIPSTTRR
Protein: Uncharacterized protein P4G3.03 (Q9P7U7)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
Sequence:
MSYNGKDLGELQLKCHQSMLQAGAVFENCTFVNGDVLLEIPSFFIESLQFHYLINQSEKISLKLIFWNELVYLLGLNDTSKASATTSFQQGQIETKPDLTLFINELLTTKKEHKKLDNDNRESEIPFSDTRFHDEFDRESRACLHRSEFPKNPHAFLAQDLPHGLPHRRAALPCEALGFHPNVGDYFDWYPHRPNHFGGKFDGHSRGRGAGRGGFCGRHGRGGFGKRSGLHGCREEFWMQV
Protein: Unconventional myosin-Ie (Myosin-Ic) (Unconventional myosin 1E) (Q12965)
Organism: Homo sapiens (Human)
Function: Actin-based motor molecule with ATPase activity. Unconventional myosins serve in intracellular movements. Their highly divergent tails bind to membranous compartments, which are then moved relative to actin filaments. Binds to membranes containing anionic phospholipids via its tail domain. Involved in clathrin-mediated endocytosis and intracellular movement of clathrin-coated vesicles. Required for normal morphology of the glomerular basement membrane, normal development of foot processes by kidney podocytes and normal kidney function. In dendritic cells, may control the movement of class II-containing cytoplasmic vesicles along the actin cytoskeleton by connecting them with the actin network via ARL14EP and ARL14.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:E9Q634}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:E9Q634}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:E9Q634}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000269|PubMed:36316095}. Cell junction {ECO:0000269|PubMed:36316095}. Note=Colocalizes with F-actin (By similarity). In cultured podocytes, it localizes close to and is associated with the cytoplasmic membrane, with enrichment at the lamellipodia tips. Colocalizes with cytoplasmic vesicles, including endocytic clathrin-coated vesicles. Colocalizes with dynamin at cytoplasmic vesicles. {ECO:0000250}.
Interaction partners:
- Actin nucleation-promoting factor WAS
- Actin nucleation-promoting factor WASL
- Inverted formin-2
- WAS/WASL-interacting protein family member 2
- Alpha-actinin-4
- Anillin
- Actin, cytoplasmic 1
- Osteoclast-stimulating factor 1
- Actin, cytoplasmic 2
Sequence:
MGSKGVYQYHWQSHNVKHSGVDDMVLLSKITENSIVENLKKRYMDDYIFTYIGSVLISVNPFKQMPYFGEKEIEMYQGAAQYENPPHIYALADNMYRNMIIDRENQCVIISGESGAGKTVAAKYIMSYISRVSGGGTKVQHVKDIILQSNPLLEAFGNAKTVRNNNSSRFGKYFEIQFSPGGEPDGGKISNFLLEKSRVVMRNPGERSFHIFYQLIEGASAEQKHSLGITSMDYYYYLSLSGSYKVDDIDDRREFQETLHAMNVIGIFAEEQTLVLQIVAGILHLGNISFKEVGNYAAVESEEFLAFPAYLLGINQDRLKEKLTSRQMDSKWGGKSESIHVTLNVEQACYTRDALAKALHARVFDFLVDSINKAMEKDHEEYNIGVLDIYGFEIFQKNGFEQFCINFVNEKLQQIFIELTLKAEQEEYVQEGIRWTPIEYFNNKIVCDLIENKVNPPGIMSILDDVCATMHAVGEGADQTLLQKLQMQIGSHEHFNSWNQGFIIHHYAGKVSYDMDGFCERNRDVLFMDLIELMQSSELPFIKSLFPENLQADKKGRPTTAGSKIKKQANDLVSTLMKCTPHYIRCIKPNETKKPRDWEESRVKHQVEYLGLKENIRVRRAGYAYRRIFQKFLQRYAILTKATWPSWQGEEKQGVLHLLQSVNMDSDQFQLGRSKVFIKAPESLFLLEEMRERKYDGYARVIQKSWRKFVARKKYVQMREEASDLLLNKKERRRNSINRNFIGDYIGMEEHPELQQFVGKREKIDFADTVTKYDRRFKGVKRDLLLTPKCLYLIGREKVKQGPDKGLVKEVLKRKIEIERILSVSLSTMQDDIFILHEQEYDSLLESVFKTEFLSLLAKRYEEKTQKQLPLKFSNTLELKLKKENWGPWSAGGSRQVQFHQGFGDLAVLKPSNKVLQVSIGPGLPKNSRPTRRNTTQNTGYSSGTQNANYPVRAAPPPPGYHQNGVIRNQYVPYPHAPGSQRSNQKSLYTSMARPPLPRQQSTSSDRVSQTPESLDFLKVPDQGAAGVRRQTTSRPPPAGGRPKPQPKPKPQVPQCKALYAYDAQDTDELSFNANDIIDIIKEDPSGWWTGRLRGKQGLFPNNYVTKI
Protein: L-type lectin-domain containing receptor kinase IV.3 (LecRK-IV.3) (EC 2.7.11.1) (O81292)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
Interaction partners:
- non-specific serine/threonine protein kinase
Sequence:
MFFKLFTIFFFFIILLSKPLNSSSQSLNFTYNSFHRPPTNISIQGIATVTSNGILKLTDKTVISTGHAFYTEPIRFKDSPNDTVSSFSTTFVIGIYSGIPTISGHGMAFFIAPNPVLSSAMASQYLGLFSSTNNGNDTNHILAVEFDTIMNPEFDDTNDNHVGININSLTSVKSSLVGYWDEINQFNNLTLISRKRMQVWVDYDDRTNQIDVTMAPFGEVKPRKALVSVVRDLSSVFLQDMYLGFSAATGYVLSEHFVFGWSFMVKGKTAPPLTLSKVPKFPRVGPTSLQRFYKNRMPLFSLLLIPVLFVVSLIFLVRFIVRRRRKFAEEFEDWETEFGKNRLRFKDLYYATKGFKDKDLLGSGGFGRVYRGVMPTTKKEIAVKRVSNESRQGLKEFVAEIVSIGRMSHRNLVPLLGYCRRRDELLLVYDYMPNGSLDKYLYDCPEVTLDWKQRFNVIIGVASGLFYLHEEWEQVVIHRDIKASNVLLDAEYNGRLGDFGLARLCDHGSDPQTTRVVGTWGYLAPDHVRTGRATTATDVFAFGVLLLEVACGRRPIEIEIESDESVLLVDSVFGFWIEGNILDATDPNLGSVYDQREVETVLKLGLLCSHSDPQVRPTMRQVLQYLRGDATLPDLSPLDFRGSGKMLGMNHRFSESCTFSSGSSIAYSIVSGGR
Protein: Copper-translocating P-type ATPase (EC 3.6.3.4) (B7J8K5)
Organism: Acidithiobacillus ferrooxidans (strain ATCC 23270 / DSM 14882 / CIP 104768 / NCIMB 8455) (Ferrobacillus ferrooxidans (strain ATCC 23270))
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MDHARHQEHGMGTAHPGAHGGHNHAAMIADFRRRFWVSLALTIPILLLSPLIQHLLRLEAALAFTGSSYVLFALSSAVYFYGGWPFLKGLFAELKTRKPAMMTLIALAISVAYFYSSAVVFGVQGEVFFWELATLIDVMLLGHWIEMKSVMGASGALEKLVQMMPSEAHLVAPEGMKDVPVANLQRGDRVLVKPGEKIPTDGRVIEGRTTVNQAMLTGESQPVEKGGGDEVIGGSVNGESSITVEVHKTGSETYLSQVIEMVRRAQESRSRTQDLADRAALVLTLTALSVGGLTLAIWLVLGQHFEFALARMVTVMVIACPHALGLAIPLVVAVSTALAAQHGLLIRDRSAFERARQLQAVVFDKTGTLTEGRFGVTDVVVLGGYAEDEVVRLAAALESQSEHPIAAGIVAYAKAKDIGFEPPKEFKAIPGKGAQALVNGRNVKVVSPGYLEEHGLDVSDERIAALASQGKTVVYLLIDEKPAGAVALADIIRAESREALARLKGMGVQVMMLTGDSAAVARWVAQEMGLDDYFAEVLPGQKAEKIKAVQARGLRVAMVGDGVNDAPALVEADVGIAIGAGTDVAIESADIVLVRSDPRDVAAILELSRATYRKMIQNLWWGAGYNIVAIPLAAGVAYSIGLVLSPAVGAALMSVSTVIVAINAKLLQRVRLTA
Protein: Interleukin 18 binding protein (F7F5P4)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Interleukin-18
- Interferon gamma
Sequence:
MTMRHCGCAADPSPWWVLLLYVHVVILARATSAPLTTATVLTRSSKDPCSSWSPAVPTKQYPTLDVIWPEKEVPLNGTLTLSCTACSRFPNFSILYWLGNGSFIEHLPGRLREGHTSREQRNASTWLHRALVLEELSPSLLSTNFSCLFVDPGQVAQYHVILAQLWVRNLKEGIQGWEELHYLGKKGLAFPMQPDGLKTAPSPSQETLSSHSPGPRSAGPGAP
Protein: P130CAS, isoform E (B7Z0H1)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MSSPRQNASGSEFETYDIPKPATPVPLNYDSPRSGLPKASNSTTTSSSSLGTRFETLKSVAASIAEESYDVPRPLILGSNQLQQQMSQMTPSSSASSLLTSDSLSLSFSSSNRSSLANMPDYDIPRRNPLPVRRQQSGLTYDFPLPPLQEQVPRVLCTPSTVTTTKELPLELSSALETLAKLQLQTTAAINRLLSFVVPNWRTRAQLEPAIMDLKLAALRLRTTLHDLAEFGEGALGNATRSEDRNLALKLRPLVRALRDANKLIHDSSESLDAQGAWSIDQLARSDEKHGCRPPDALDQLMVCAQTLTEDVRSTTSFIQGNASLLFKRQLTVGHNGGSGTGVLEGSRGSAEWLEDYDYVAFESKDAAARKNEALREAIPADLKTQFDTVIRTAESSAMGAGSGSIPTTPTARTTPTTPCKSPEMTDKDKKLVRYYAQQISTHMGNLMQAIDSFLETVEKNQPPKFFIAYGKFVVVSAHNLVTIGDNVYRNISKEALREKILRCTNALSDALKTCVLKSKKAAAHFPSGSAVQEMVDSVVHINNLARDLKSVMLQAVHLSTAAGVGA
Protein: Filamin-A (FLN-A) (Actin-binding protein 280) (ABP-280) (Filamin-1) (Filamin1) (Q9VEN1)
Organism: Drosophila melanogaster (Fruit fly)
Function: Involved in the germline ring canal formation. May tether actin microfilament within the ovarian ring canal to the cell membrane. Contributes to actin microfilaments organization.
Subcellular location: Cytoplasm, cytoskeleton. Cell membrane. Note=Localizes to intercellular bridges corresponding to ring canals that connect cytoplasm of nurse cells to the developing oocyte. Localizes to nurse cell plasma membranes. Detected in both the inner and outer rims of the ring canal.
Interaction partners:
- Zyx102 protein
- Vinculin
- Integrin beta-PS
- non-specific serine/threonine protein kinase
- Cdc42 homolog
- Breast cancer type 2 susceptibility protein homolog
- Rhea, isoform B
- Paxillin, isoform F
- Integrin beta-nu
- Actin-interacting protein 1
Sequence:
MEAERDLAEDAQWKKIQQNTFTRWANEHLKTIDRSINNLETDLSDGLRLIALIEVLSQKRMPKYNKRPTFRSQKLENVSVALKFLQDEGIKIVNIDSSDIVDCKLKLILGLIWTLILHYSISMPMWDGEDDKQLNGSGHTPKQRLLNWIHAKIPDLPINNFTNDWTTGKAVGALVDACAPGLCPDWELWDPKDAVQNASEAMGLADDWLNVRQLIKPEELVNPNVDEQSMMTYLSQYPNSKLKTGAPLRPKTNPNRVRAYGPGIEPIGPVVGAPANFTVETFSAGKGSVDVDIQGPNGEIEKADVRFNNDKNLTYTVSYIPKSEGSHKVAVKFSGRDIPKSPFPVKVEGHAGDASKVKVTGPGIQPNGVTIKKPTFFDILAKDAGRGVPEVIIIDPANHKTSVAAKVRQLENDTWRCEYVTALQGLHSVNVFYAGTPIPNSPFPVKVAPLSDARKVRASGRGLQATGVRVGDDADFKIYTEGAGEGEPEVRVIGPGGMNQNVMQSKVDGNTYECHYYPTKEGRYVIMVTFAGQEVAKSPFEVKVGPKKESSIVAYGPGLSSGVIGYPAAFVVETNGETGALGFTVAGPSQAEIECHDNGDGSALVKYHPTAVGEYAVHILCDNEDIPKSPFIAQILPRTDFHPELVKASGPGLEKNGVTINQPTSFTVDPSKAGNAPLDVVVQDVFGTKLPVELKNNPDGTKKVTYTPTSGVPHTVEVNYGGVSTPNSPHRVYVGVPVDAAKVQAFGPWLQPGVRPNAATHFNVDAREAGDAELKVKIIHEETKIEVPCRIIDNEDNTYSVEVIPPSKGAYTTTMTYGGQRVPLGEKVVVEQTVDVSKIKVDGLEPSVIMNAATDFMVDMSKVGSNIDSGKLSCAIFDPMGHVLPSKIVQGPTDDIFRIMYTPFEAGRHTIELMYDNIPVPGSPFVVNVKSGCDPARCKAYGPGLEKGLTNQKNKFTVETKGAGNGGLSLAIEGPSEAKMTCTDNRDGSCDVDYLATDPGEYDITIRFADKHIPGSPFRVLVEETVDPSKVKVYGPGIEHGQVRESVPTFFNVDVGEAGPGRIAVKLTNSEGIPVDNLRVEDKGNCIYAVHYVPPKAGSVLTCQVKFSEVEVPCSPFVMTVFPKSEPTKVKVKGVNEKKKTPASLPAEFEIDTKQAGQADINVAIKNPKGKAMQPRLEEVSTGTYVVSFVPDECGTYQCSIKYGDKEIEGSPFKLEAFPTGEAKKCKLVEQAPKIQTSGSQSHLKVDAREAGDGAVTCKITNKAGSEIVDIDVIEKDGFFDILYALNDPGDYDINVKFGGKDIPNGSFSIKAVESIEQYSHSEYIEEHTTKVVQQTTQSELVNGKSEITYRSVAFEKLPLPTTGGNVTAEVRMPSGKVDKPVIQDNRDGTVSVKYDPREEGSHELVVKYNGEPVQGSPFKFHVDSITSGYVTAYGPGLTHGVTGEPANFTISTKGASAGGLTMAVEGPSKADINYHDNKDGTVSVQYLPTAPGEYQVSVRFGDKHIKGSPYFAKITGEGRKRNQISVGSCSEVTMPGDITDDDLRALNASIQAPSGLEEPCFLKRMPTGNIGISFTPREIGEHLVSVKRLGKHINNSPFKVTVCEREVGDAKKVKVSGTGLKEGQTHADNIFSVDTRNAGFGGLSVSIEGPSKAEIQCTDKDDGTLNISYKPTEPGYYIVNLKFADHHVEGSPFTVKVAGEGSNRKREKIQRERDAVPITEIGSQCKLTFKMPGITSFDLAACVTSPSNVTEDAEIQEVEDGLYAVHFVPKELGVHTVSVRYSEMHIPGSPFQFTVGPLRDSGSHLVKAGGSGLERGVVGEAAEFNVWTREAGGGSLAISVEGPSKADIEFKDRKDGSCDVSYKVTEPGEYRVGLKFNDRHIPDSPFKVYVSPDAGDAHKLEVQQFPQGNIQADAPYQFMVRKNGAKGELDAKIVAPSGTDDDCFIQVIDGEMYSVRFYPRENGIHAIHVKFNGVHIPDSPFRIKVGKDVADPAAVHASGNGLDEVKTGHKADFIINTCNAGVGTLAVSIDGPSKVAMDCTEVEEGYKVRYTPLLPGEHYITVKYNNMHIVGSPFKVNATGDKLADEGAQETSTVIVETVQKVAKGGKNTGVHLPTFKSDASKVVSKGMGLKKAYIGKQNQFSISATDAGNNILYVGMYGPKGPCEEFHVKHAGHNNYNVQYLVRDRGQYVLLIKWGEEHIPGSPFQIDV
Protein: MutT/nudix family protein (O33199)
Organism: Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Interaction partners:
Sequence:
MAEHDFETISSETLHTGAIFALRRDQVRMPGGGIVTREVVEHFGAVAIVAMDDNGNIPMVYQYRHTYGRRLWELPAGLLDVAGEPPHLTAARELREEVGLQASTWQVLVDLDTAPGFSDESVRVYLATGLREVGRPEAHHEEADMTMGWYPIAEAARRVLRGEIVNSIAIAGVLAVHAVTTGFAQPRPLDTEWIDRPTAFAARRAER
Protein: Hemoglobin subunit alpha-A (Alpha-A-globin) (Hemoglobin alpha-A chain) (P21871)
Organism: Columba livia (Rock dove)
Function: Involved in oxygen transport from the lung to the various peripheral tissues.
Interaction partners:
Sequence:
MVLSANDKSNVKAVFAKIGGQAGDLGGEALERLFITYPQTKTYFPHFDLSHGSAQIKGHGKKVAEALVEAANHIDDIAGALSKLSDLHAQKLRVDPVNFKLLGHCFLVVVAVHFPSLLTPEVHASLDKFVLAVGTVLTAKYR
Protein: Liprin-alpha-3 (Protein tyrosine phosphatase receptor type f polypeptide-interacting protein alpha-3) (PTPRF-interacting protein alpha-3) (Q91Z79)
Organism: Rattus norvegicus (Rat)
Function: May regulate the disassembly of focal adhesions. May localize receptor-like tyrosine phosphatases type 2A at specific sites on the plasma membrane, possibly regulating their interaction with the extracellular environment and their association with substrates.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:23124857}. Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000269|PubMed:23124857}. Note=Also detected in epididymosome. {ECO:0000269|PubMed:23124857}.
Interaction partners:
- Receptor-type tyrosine-protein phosphatase delta
- Receptor-type tyrosine-protein phosphatase S
- Receptor-type tyrosine-protein phosphatase F
- ELKS/Rab6-interacting/CAST family member 1
- Regulating synaptic membrane exocytosis protein 1
- Ras-related protein Rab-3A
- Peripheral plasma membrane protein CASK
- Synapsin-1
- PPFIA binding protein 1
- PPFIA binding protein 2
Sequence:
MMCEVMPTISEDGRRGSALGPDDAGGELERLMVTMLTERERLLETLREAQDGLATAQLRLRELGHEKDSLQRQLSIALPQEFAALTKELNLCREQLLEREEEIAELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSPGGVSSEVEVLKALKSLFEHHKALDEKVRERLRMALERVAVLEEELELSNQEALNLRDQLSRRRSGLEEPGKDGDGQTLANGLGPVGESSRRTAELEEALERQRAEVCQLRERLAVLCRQMSQLEEELGTAHRELGKAEEANSKLQRDLKEALAQREDMEERITTLEKRYLSAQREATSLHDANDKLENELASKESLYRQSEEKSRQLAEWLDDAKQKLQQTLQKAETLPEIEAQLAQRVAALNKAEERHGNFEERLRQLEAQLEEKNQELQRARQREKMNDDHNKRLSETVDKLLSESNERLQLHLKERMGALEEKNSLSEEIANMKKLQDELLLNKEQLLAEMERMQMEIDQLRGRPPSYSRSLPGSALELRYSQAPTLPSGAPLDPYGAGSGRAGKRGRWSGAKDESSKDWDRSTPAGSIPPPFPGELDGSDEEETEGMFGAELLSPSGQADVQTLAIMLQEQLEAINKEIKLIQEEKETTEQRAEELESRVSSSGLDSLGRYRSSCSLPPSLTTSTLASPSPPSSGHSTPRLAPPSPARETDKTNHVPKDEAGVPRGEGPAIPGDTPPPTPRSARLERMTQALALQAGSLEDGAPPRGSESTPDSLHKAPKRKSIKSSIGRLFGKKEKGRMGPPGRESVSLAGTPSDETLATDPLGLAKLTGPGDKDRRNKRKHELLEEACRQGLPFAAWDGPTVVSWLELWVGMPAWYVAACRANVKSGAIMANLSDTEIQREIGISNPLHRLKLRLAIQEMVSLTSPSAPASSRTPTGNVWMTHEEMESLTAATKPETKEISWEQILAYGDMNHEWVGNDWLPSLGLPQYRSYFMESLVDARMLDHLNKKELREQLKMVDSFHRVSLHYGIMCLKRLNYDRKDLERRREESQTQIRDVMVWSNERVMGWVSGLGLKEFATNLTESGVHGALLALDETFDYSDLALLLQIPTQNAQARQLLEKEFSNLISLGTDRRLDEDSAKSFSRSPSWRKMFREKDLRGVTPDSAEMLPPNFRSAAAGALGSPGLPLRKLQPEGQTSGSSRADGVSVRTYSC