Knowledge (XXG)

ELMO (protein)

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549: 108: 590: 500:"An alpha-helical extension of the ELMO1 pleckstrin homology domain mediates direct interaction to DOCK180 and is critical in Rac signaling" 435: 291: 173: 410: 306:). The Dock180-ELMO interaction requires the ELMO PH domain and also involves binding of the ELMO proline-rich motif to the Dock180 128: 177: 354:"The C. elegans PH domain protein CED-12 regulates cytoskeletal reorganization via a Rho/Rac GTPase signaling pathway" 583: 609: 436:"CED-12/ELMO, a novel member of the CrkII/Dock180/Rac pathway, is required for phagocytosis and cell migration" 116: 434:
Gumienny TL, Brugnera E, Tosello-Trampont AC, Kinchen JM, Haney LB, Nishiwaki K, et al. (October 2001).
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Komander D, Patel M, Laurin M, Fradet N, Pelletier A, Barford D, Côté JF (November 2008).
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which can regulate the activity of other proteins through their ability to mediate
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Lu M, Ravichandran KS (2006). "Dock180–ELMO Cooperation in Rac Activation".
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and extend around two thirds of the way along the protein, as well as a
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This family contains members in all animals. In humans there are three
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The ELMO domain was first characterized in the CED-12 proteins of
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Zhou Z, Caron E, Hartwieg E, Hall A, Horvitz HR (October 2001).
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Regulators and Effectors of Small GTPases: Rho Family
122: 102: 84: 79: 63: 51: 39: 31: 26: 21: 222:, which is a homolog to the ELMO protein found in 584: 8: 168:networks. These proteins have no intrinsic 591: 577: 76: 523: 369: 318: 242:Structure and function of ELMO proteins 290:-related proteins to form a bipartite 18: 7: 545: 543: 263:. All isoforms contain a series of 238:, and cytoskeletal rearrangements. 563:. You can help Knowledge (XXG) by 292:guanine nucleotide exchange factor 14: 172:activity and instead function as 547: 226:. This protein is involved in 1: 504:Molecular Biology of the Cell 455:10.1016/S0092-8674(01)00520-7 403:10.1016/S0076-6879(06)06028-9 371:10.1016/s1534-5807(01)00058-2 282:. They function as part of a 80:Available protein structures: 178:protein-protein interactions 232:apoptotic cell phagocytosis 161:(~82 kDa) involved in 631: 542: 278:-rich motif and a central 157:) is a family of related 75: 248:evolutionarily conserved 516:10.1091/mbc.E08-04-0345 219:Drosophila melanogaster 559:-related article is a 213:Caenorhabditis elegans 267:, which begin at the 246:The ELMO family are 332:The Interactive Fly 358:Developmental Cell 22:ELMO/CED-12 family 572: 571: 298:(a member of the 265:armadillo repeats 148:ngulfment and Cel 138: 137: 134: 133: 129:structure summary 622: 610:Protein families 593: 586: 579: 551: 544: 538: 537: 527: 495: 489: 488: 486: 485: 479: 473:. Archived from 440: 431: 425: 424: 390: 384: 383: 373: 349: 343: 342: 340: 338: 323: 77: 19: 630: 629: 625: 624: 623: 621: 620: 619: 600: 599: 598: 597: 541: 510:(11): 4837–51. 497: 496: 492: 483: 481: 477: 438: 433: 432: 428: 413: 392: 391: 387: 351: 350: 346: 336: 334: 326:Brody, Thomas. 325: 324: 320: 316: 284:protein complex 244: 17: 12: 11: 5: 628: 626: 618: 617: 612: 602: 601: 596: 595: 588: 581: 573: 570: 569: 552: 540: 539: 490: 426: 411: 385: 344: 317: 315: 312: 243: 240: 236:cell migration 208: 207: 202: 197: 136: 135: 132: 131: 126: 120: 119: 106: 100: 99: 89: 82: 81: 73: 72: 67: 61: 60: 55: 49: 48: 43: 37: 36: 33: 29: 28: 24: 23: 16:Protein family 15: 13: 10: 9: 6: 4: 3: 2: 627: 616: 615:Protein stubs 613: 611: 608: 607: 605: 594: 589: 587: 582: 580: 575: 574: 568: 566: 562: 558: 553: 550: 546: 535: 531: 526: 521: 517: 513: 509: 505: 501: 494: 491: 480:on 2021-09-22 476: 472: 468: 464: 460: 456: 452: 448: 444: 437: 430: 427: 422: 418: 414: 412:9780121828110 408: 404: 400: 396: 389: 386: 381: 377: 372: 367: 364:(4): 477–89. 363: 359: 355: 348: 345: 333: 329: 322: 319: 313: 311: 309: 305: 301: 297: 293: 289: 285: 281: 277: 274: 270: 266: 262: 258: 257: 252: 249: 241: 239: 237: 233: 229: 225: 221: 220: 215: 214: 206: 203: 201: 198: 196: 193: 192: 191: 189: 186: 181: 179: 175: 171: 167: 164: 163:intracellular 160: 156: 154: 151: 147: 142: 130: 127: 125: 121: 118: 114: 110: 107: 105: 101: 97: 93: 90: 87: 83: 78: 74: 71: 68: 66: 62: 59: 56: 54: 50: 47: 44: 42: 38: 34: 30: 25: 20: 565:expanding it 554: 507: 503: 493: 482:. Retrieved 475:the original 449:(1): 27–41. 446: 442: 429: 394: 388: 361: 357: 347: 337:November 11, 335:. Retrieved 331: 321: 254: 245: 230:activation, 217: 211: 209: 182: 152: 149: 145: 144: 140: 139: 27:Identifiers 604:Categories 484:2020-06-06 314:References 308:SH3 domain 304:G proteins 300:Rho family 273:C-terminal 269:N-terminus 256:C. elegans 228:Rac-GTPase 185:paralogous 166:signalling 92:structures 35:ELMO_CED12 302:of small 280:PH domain 251:orthologs 170:catalytic 70:PDOC51335 58:IPR006816 534:18768751 471:15232864 463:11595183 421:16472672 380:11703939 328:"Ced-12" 259:protein 188:isoforms 174:adaptors 159:proteins 109:RCSB PDB 53:InterPro 557:protein 525:2575150 288:Dock180 276:proline 253:of the 224:mammals 65:PROSITE 46:PF04727 532:  522:  469:  461:  419:  409:  378:  261:CED-12 155:tility 124:PDBsum 98:  88:  32:Symbol 555:This 478:(PDF) 467:S2CID 439:(PDF) 286:with 205:ELMO3 200:ELMO2 195:ELMO1 561:stub 530:PMID 459:PMID 443:Cell 417:PMID 407:ISBN 376:PMID 339:2015 294:for 216:and 141:ELMO 117:PDBj 113:PDBe 96:ECOD 86:Pfam 41:Pfam 520:PMC 512:doi 451:doi 447:107 399:doi 366:doi 296:Rac 104:PDB 606:: 528:. 518:. 508:19 506:. 502:. 465:. 457:. 445:. 441:. 415:. 405:. 374:. 360:. 356:. 330:. 310:. 234:, 190:: 180:. 153:Mo 115:; 111:; 94:/ 592:e 585:t 578:v 567:. 536:. 514:: 487:. 453:: 423:. 401:: 382:. 368:: 362:1 341:. 150:l 146:E 143:(

Index

Pfam
PF04727
InterPro
IPR006816
PROSITE
PDOC51335
Pfam
structures
ECOD
PDB
RCSB PDB
PDBe
PDBj
PDBsum
structure summary
proteins
intracellular
signalling
catalytic
adaptors
protein-protein interactions
paralogous
isoforms
ELMO1
ELMO2
ELMO3
Caenorhabditis elegans
Drosophila melanogaster
mammals
Rac-GTPase

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