244:
221:
118:
143:
495:
250:
149:
1036:
gene family. The proteins encoded by this gene family are inhibitors of the matrix metalloproteinases, a group of peptidases involved in degradation of the extracellular matrix. The secreted, netrin domain-containing protein encoded by this gene is involved in regulation of platelet aggregation and
1533:"Utilization of a novel recombinant myoglobin fusion protein expression system to characterize the tissue inhibitor of metalloproteinase (TIMP)-4 and TIMP-2 C-terminal domain and tails by mutagenesis. The importance of acidic residues in binding the MMP-2 hemopexin C-domain"
1313:"Utilization of a novel recombinant myoglobin fusion protein expression system to characterize the tissue inhibitor of metalloproteinase (TIMP)-4 and TIMP-2 C-terminal domain and tails by mutagenesis. The importance of acidic residues in binding the MMP-2 hemopexin C-domain"
1209:
Olson TM, Hirohata S, Ye J, Leco K, Seldin MF, Apte SS (Sep 1998). "Cloning of the human tissue inhibitor of metalloproteinase-4 gene (TIMP4) and localization of the TIMP4 and Timp4 genes to human chromosome 3p25 and mouse chromosome 6, respectively".
1727:
Zhao YG, Xiao AZ, Park HI, et al. (2004). "Endometase/matrilysin-2 in human breast ductal carcinoma in situ and its inhibition by tissue inhibitors of metalloproteinases-2 and -4: a putative role in the initiation of breast cancer invasion".
1694:"Expression of matrix metalloproteinase-26 and tissue inhibitor of matrix metalloproteinase-3 and -4 in endometrium throughout the normal menstrual cycle and alteration in users of levonorgestrel implants who experience irregular uterine bleeding"
1367:"Specific, high affinity binding of tissue inhibitor of metalloproteinases-4 (TIMP-4) to the COOH-terminal hemopexin-like domain of human gelatinase A. TIMP-4 binds progelatinase A and the COOH-terminal domain in a similar manner to TIMP-2"
1264:"Specific, high affinity binding of tissue inhibitor of metalloproteinases-4 (TIMP-4) to the COOH-terminal hemopexin-like domain of human gelatinase A. TIMP-4 binds progelatinase A and the COOH-terminal domain in a similar manner to TIMP-2"
1609:
Troeberg L, Tanaka M, Wait R, et al. (2003). "E. coli expression of TIMP-4 and comparative kinetic studies with TIMP-1 and TIMP-2: insights into the interactions of TIMPs and matrix metalloproteinase 2 (gelatinase A)".
1400:
Pohar N, Godenschwege TA, Buchner E (1999). "Invertebrate tissue inhibitor of metalloproteinase: structure and nested gene organization within the synapsin locus is conserved from
Drosophila to human".
1845:"Total conversion of tissue inhibitor of metalloproteinase (TIMP) for specific metalloproteinase targeting: fine-tuning TIMP-4 for optimal inhibition of tumor necrosis factor-{alpha}-converting enzyme"
1944:
Koskivirta I, Rahkonen O, Mäyränpää M, et al. (2007). "Tissue inhibitor of metalloproteinases 4 (TIMP4) is involved in inflammatory processes of human cardiovascular pathology".
1459:
Huang W, Li WQ, Dehnade F, Zafarullah M (2002). "Tissue inhibitor of metalloproteinases-4 (TIMP-4) gene expression is increased in human osteoarthritic femoral head cartilage".
257:
156:
1498:"Expression of matrix metalloproteinase-26 and tissue inhibitor of metalloproteinase-4 in human normal cytotrophoblast cells and a choriocarcinoma cell line, JEG-3"
748:
79:
729:
1878:
Lizarraga F, Espinosa M, Maldonado V, Melendez-Zajgla J (2005). "Tissue inhibitor of metalloproteinases-4 is expressed in cervical cancer patients".
1430:
Hernandez-Barrantes S, Shimura Y, Soloway PD, et al. (2001). "Differential roles of TIMP-4 and TIMP-2 in pro-MMP-2 activation by MT1-MMP".
1033:
1150:
1983:"Endometrial TIMP-4 mRNA is expressed in the stroma, while TIMP-4 protein accumulates in the epithelium and is released to the uterine fluid"
1767:"Endometrial TIMP-4 mRNA is high at midcycle and in hyperplasia, but down-regulated in malignant tumours. Coordinated expression with MMP-26"
1132:
2043:
243:
963:
956:
1899:
Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network".
220:
1248:
1119:
1098:
1115:
142:
117:
1094:
59:
1046:
256:
155:
1311:
Kai HS, Butler
Georgina S, Morrison Charlotte J, King Angela E, Pelman Gayle R, Overall Christopher M (Dec 2002).
249:
148:
793:
67:
1802:"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)"
1568:"Identification, regulation and role of tissue inhibitor of metalloproteinases-4 (TIMP-4) in human platelets"
774:
1908:
1652:
131:
46:
939:
888:
1969:
1932:
1753:
1484:
91:
1641:"Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences"
935:
914:
884:
863:
2004:
1961:
1924:
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1866:
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1788:
1745:
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1680:
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39:
1994:
1953:
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1468:
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1410:
1378:
1324:
1275:
1219:
1181:
336:
267:
211:
166:
2028:
494:
87:
311:
1170:"Molecular cloning and characterization of human tissue inhibitor of metalloproteinase 4"
1912:
1656:
1037:
recruitment and may play role in hormonal regulation and endometrial tissue remodeling.
1592:
1567:
1826:
1801:
1710:
1693:
1675:
1640:
663:
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582:
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556:
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546:
541:
536:
2037:
523:
1973:
1757:
1488:
1936:
329:
108:
71:
1741:
95:
1155:
National Center for
Biotechnology Information, U.S. National Library of Medicine
1137:
National Center for
Biotechnology Information, U.S. National Library of Medicine
412:
1957:
228:
125:
75:
1514:
1497:
1383:
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1338:
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1186:
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1999:
1982:
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350:
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194:
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83:
2008:
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838:
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805:
760:
1623:
1472:
2024:
1019:
971:
715:
1168:
Greene J, Wang M, Liu YE, Raymond LA, Rosen C, Shi YE (Jan 1997).
1070:
1066:
1062:
1262:
Bigg HF, Shi Y E, Liu Y E, Steffensen B, Overall C M (Jun 1997).
678:
674:
1050:
1026:
63:
503:
634:
negative regulation of membrane protein ectodomain proteolysis
1639:
Strausberg RL, Feingold EA, Grouse LH, et al. (2003).
319:
1800:
Gerhard DS, Wagner L, Feingold EA, et al. (2004).
1566:
Radomski A, Jurasz P, Sanders EJ, et al. (2003).
1249:"Entrez Gene: TIMP4 TIMP metallopeptidase inhibitor 4"
2027:
online database for peptidases and their inhibitors:
484:
1981:
Pilka R, Noskova V, Domanski H, et al. (2006).
1765:
Pilka R, Domanski H, Hansson S, et al. (2005).
1531:
Kai HS, Butler GS, Morrison CJ, et al. (2003).
928:
907:
877:
856:
1111:
1109:
1107:
1090:
1088:
1086:
266:
165:
1692:Chegini N, Rhoton-Vlasak A, Williams RS (2003).
16:Protein-coding gene in the species Homo sapiens
1496:Zhang J, Cao YJ, Zhao YG, et al. (2003).
1116:GRCm38: Ensembl release 89: ENSMUSG00000030317
1365:Bigg HF, Shi YE, Liu YE, et al. (1997).
644:negative regulation of endopeptidase activity
8:
1095:GRCh38: Ensembl release 89: ENSG00000157150
50:, TIMP metallopeptidase inhibitor 4, TIMP-4
689:
519:
307:
206:
103:
1998:
1860:
1825:
1782:
1709:
1674:
1664:
1591:
1548:
1513:
1382:
1328:
1279:
1185:
639:negative regulation of catalytic activity
609:negative regulation of peptidase activity
1243:
1241:
1082:
557:metalloendopeptidase inhibitor activity
1034:tissue inhibitor of metalloproteinases
20:
271:
232:
227:
170:
129:
124:
7:
1843:Lee MH, Rapti M, Murphy G (2005).
925:
904:
874:
853:
829:
810:
784:
765:
739:
720:
619:central nervous system development
489:
407:
345:
324:
14:
1022:that in humans is encoded by the
493:
439:lumbar subsegment of spinal cord
255:
248:
242:
219:
154:
147:
141:
116:
624:response to lipopolysaccharide
504:More reference expression data
473:More reference expression data
389:right hemisphere of cerebellum
1:
1742:10.1158/0008-5472.CAN-03-1932
1711:10.1016/S0015-0282(03)00797-0
1432:Biochem. Biophys. Res. Commun
1016:Metalloproteinase inhibitor 4
664:response to organic substance
451:tunica media of zone of aorta
240:
139:
1645:Proc. Natl. Acad. Sci. U.S.A
537:peptidase inhibitor activity
2044:Genes on human chromosome 3
614:response to peptide hormone
365:subcutaneous adipose tissue
2060:
1958:10.1007/s00418-006-0163-8
1151:"Mouse PubMed Reference:"
1133:"Human PubMed Reference:"
1032:This gene belongs to the
1002:
997:
993:
986:
970:
964:Chr 6: 115.22 – 115.23 Mb
951:
932:
911:
900:
881:
860:
849:
836:
832:
817:
813:
804:
791:
787:
772:
768:
759:
746:
742:
727:
723:
714:
699:
692:
688:
672:
542:enzyme inhibitor activity
522:
518:
501:
492:
483:
470:
419:
410:
393:Descending thoracic aorta
357:
348:
318:
310:
306:
289:
276:
239:
218:
209:
205:
188:
175:
138:
115:
106:
102:
57:
54:
44:
37:
32:
28:
23:
1384:10.1074/jbc.272.24.15496
1281:10.1074/jbc.272.24.15496
1187:10.1074/jbc.271.48.30375
1045:TIMP4 has been shown to
957:Chr 3: 12.15 – 12.16 Mb
604:Notch signaling pathway
423:interventricular septum
1862:10.1074/jbc.M500897200
1666:10.1073/pnas.242603899
1584:10.1038/sj.bjp.0704936
1550:10.1074/jbc.M209177200
1515:10.1093/molehr/8.7.659
1444:10.1006/bbrc.2001.4323
1415:10.1006/geno.1999.5776
1330:10.1074/jbc.M209177200
1224:10.1006/geno.1998.5362
447:deep cerebellar nuclei
2000:10.1093/molehr/gal055
1784:10.1093/molehr/gah092
1946:Histochem. Cell Biol
654:response to cytokine
588:extracellular matrix
578:extracellular region
459:brown adipose tissue
427:white adipose tissue
373:left coronary artery
273:6 E3|6 53.29 cM
234:Chromosome 6 (mouse)
132:Chromosome 3 (human)
1921:10.1038/nature04209
1913:2005Natur.437.1173R
1907:(7062): 1173–1178.
1657:2002PNAS...9916899M
1651:(26): 16899–16903.
1618:(50): 15025–15035.
1543:(50): 48696–48707.
1377:(24): 15496–15500.
1323:(50): 48696–48707.
1274:(24): 15496–15500.
1180:(48): 30375–30380.
649:response to hormone
583:extracellular space
1818:10.1101/gr.2596504
1812:(10B): 2121–2127.
794:ENSMUSG00000030317
659:biological process
597:Biological process
566:Cellular component
530:Molecular function
431:lobe of cerebellum
1624:10.1021/bi026454l
1473:10.1002/jcb.10138
1013:
1012:
1009:
1008:
982:
981:
947:
946:
922:
921:
896:
895:
871:
870:
845:
844:
826:
825:
800:
799:
781:
780:
755:
754:
736:
735:
684:
683:
547:metal ion binding
514:
513:
510:
509:
479:
478:
466:
465:
435:cerebellar vermis
404:
403:
302:
301:
201:
200:
96:TIMP4 - orthologs
2051:
2012:
2002:
1987:Mol. Hum. Reprod
1977:
1940:
1895:
1874:
1864:
1855:(16): 15967–75.
1839:
1829:
1796:
1786:
1771:Mol. Hum. Reprod
1761:
1723:
1713:
1688:
1678:
1668:
1635:
1605:
1595:
1578:(8): 1330–1338.
1572:Br. J. Pharmacol
1562:
1552:
1527:
1517:
1502:Mol. Hum. Reprod
1492:
1461:J. Cell. Biochem
1455:
1426:
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1159:
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1147:
1141:
1140:
1129:
1123:
1113:
1102:
1092:
995:
994:
966:
959:
942:
926:
917:
905:
901:RefSeq (protein)
891:
875:
866:
854:
830:
811:
785:
766:
740:
721:
690:
552:protease binding
520:
506:
497:
490:
475:
455:substantia nigra
415:
413:Top expressed in
408:
397:popliteal artery
353:
351:Top expressed in
346:
325:
308:
298:
285:
274:
259:
252:
246:
235:
223:
207:
197:
184:
173:
158:
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120:
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98:
49:
42:
21:
2059:
2058:
2054:
2053:
2052:
2050:
2049:
2048:
2034:
2033:
2020:
2015:
1980:
1943:
1898:
1877:
1842:
1799:
1764:
1726:
1691:
1638:
1608:
1565:
1530:
1495:
1458:
1429:
1399:
1364:
1360:
1358:Further reading
1355:
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1149:
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1130:
1126:
1114:
1105:
1093:
1084:
1079:
1059:
1043:
1004:View/Edit Mouse
999:View/Edit Human
962:
955:
952:Location (UCSC)
938:
934:
913:
887:
883:
862:
775:ENSG00000157150
668:
629:ovulation cycle
592:
561:
502:
471:
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453:
449:
445:
441:
437:
433:
429:
425:
411:
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391:
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379:
377:ascending aorta
375:
371:
367:
363:
349:
293:
280:
272:
262:
261:
260:
253:
233:
210:Gene location (
192:
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159:
152:
130:
107:Gene location (
58:
45:
38:
17:
12:
11:
5:
2057:
2055:
2047:
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2036:
2035:
2032:
2031:
2019:
2018:External links
2016:
2014:
2013:
1993:(8): 497–503.
1978:
1952:(3): 335–342.
1941:
1896:
1880:Anticancer Res
1875:
1840:
1797:
1777:(9): 641–650.
1762:
1736:(2): 590–598.
1724:
1704:(3): 564–570.
1698:Fertil. Steril
1689:
1636:
1606:
1563:
1528:
1508:(7): 659–666.
1493:
1467:(2): 295–303.
1456:
1438:(1): 126–130.
1427:
1409:(2): 293–296.
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385:synovial joint
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369:thoracic aorta
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312:RNA expression
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1886:(1B): 623–7.
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1849:J. Biol. Chem
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1371:J. Biol. Chem
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1317:J. Biol. Chem
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1269:
1268:J. Biol. Chem
1265:
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931:
927:
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918:
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906:
903:
899:
892:
890:
886:
880:
876:
873:
867:
865:
859:
855:
852:
850:RefSeq (mRNA)
848:
841:
840:
835:
831:
828:
822:
821:
816:
812:
809:
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803:
796:
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524:Gene ontology
521:
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469:
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388:
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381:apex of heart
380:
376:
372:
368:
364:
361:abdominal fat
360:
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196:
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137:
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119:
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110:
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97:
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85:
81:
77:
73:
69:
65:
61:
53:
48:
41:
36:
31:
27:
22:
19:
1990:
1986:
1949:
1945:
1904:
1900:
1883:
1879:
1852:
1848:
1809:
1805:
1774:
1770:
1733:
1729:
1701:
1697:
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1612:Biochemistry
1611:
1575:
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1540:
1536:
1505:
1501:
1464:
1460:
1435:
1431:
1406:
1402:
1374:
1370:
1320:
1316:
1306:
1271:
1267:
1257:
1215:
1211:
1204:
1177:
1173:
1163:
1154:
1145:
1136:
1127:
1044:
1041:Interactions
1031:
1023:
1015:
1014:
940:NP_001343335
933:
912:
889:NM_001356406
882:
861:
837:
818:
792:
773:
747:
728:
708:
703:
443:motor neuron
335:
328:
294:115,229,166
281:115,218,853
55:External IDs
18:
1174:J Biol Chem
193:12,158,912
180:12,153,068
33:Identifiers
1806:Genome Res
1730:Cancer Res
1122:, May 2017
1101:, May 2017
1077:References
339:(ortholog)
76:HomoloGene
1339:0021-9258
1290:0021-9258
936:NP_542370
915:NP_003247
885:NM_080639
864:NM_003256
694:Orthologs
573:sarcomere
84:GeneCards
2038:Category
2009:16809379
1974:10581957
1966:16521002
1929:16189514
1892:15816637
1871:15713681
1836:15489334
1793:15273280
1758:15342778
1750:14744773
1720:12969699
1685:12477932
1632:12475252
1602:12466243
1559:12374789
1524:12087081
1489:43053515
1481:11948685
1452:11178970
1423:10198170
1403:Genomics
1347:12374789
1212:Genomics
1118:–
1097:–
1057:See also
1047:interact
988:Wikidata
673:Sources:
2029:I35.004
1937:4427026
1909:Bibcode
1653:Bibcode
1593:1573597
1393:9182583
1298:9182583
1232:9693046
1196:8939999
1120:Ensembl
1099:Ensembl
806:UniProt
761:Ensembl
700:Species
679:QuickGO
314:pattern
40:Aliases
2025:MEROPS
2007:
1972:
1964:
1935:
1927:
1901:Nature
1890:
1869:
1834:
1827:528928
1824:
1791:
1756:
1748:
1718:
1683:
1676:139241
1673:
1630:
1600:
1590:
1557:
1522:
1487:
1479:
1450:
1421:
1391:
1345:
1337:
1296:
1288:
1230:
1194:
1020:enzyme
1018:is an
974:search
972:PubMed
839:Q9JHB3
820:Q99727
749:110595
716:Entrez
485:BioGPS
172:3p25.2
72:109125
64:601915
1970:S2CID
1933:S2CID
1754:S2CID
1485:S2CID
1071:TIMP3
1067:TIMP2
1063:TIMP1
1049:with
1024:TIMP4
709:Mouse
704:Human
675:Amigo
337:Mouse
330:Human
277:Start
212:Mouse
176:Start
109:Human
88:TIMP4
80:37748
47:TIMP4
24:TIMP4
2023:The
2005:PMID
1962:PMID
1925:PMID
1888:PMID
1867:PMID
1832:PMID
1789:PMID
1746:PMID
1716:PMID
1681:PMID
1628:PMID
1598:PMID
1555:PMID
1520:PMID
1477:PMID
1448:PMID
1419:PMID
1389:PMID
1343:PMID
1335:ISSN
1294:PMID
1286:ISSN
1228:PMID
1192:PMID
1051:MMP2
1027:gene
730:7079
320:Bgee
268:Band
229:Chr.
167:Band
126:Chr.
60:OMIM
1995:doi
1954:doi
1950:126
1917:doi
1905:437
1857:doi
1853:280
1822:PMC
1814:doi
1779:doi
1738:doi
1706:doi
1671:PMC
1661:doi
1620:doi
1588:PMC
1580:doi
1576:137
1545:doi
1541:277
1510:doi
1469:doi
1440:doi
1436:281
1411:doi
1379:doi
1375:272
1325:doi
1321:277
1276:doi
1272:272
1220:doi
1182:doi
1178:271
290:End
189:End
92:OMA
68:MGI
2040::
2003:.
1991:12
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1176:.
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1106:^
1085:^
1069:,
1065:,
1053:.
1029:.
677:/
296:bp
283:bp
195:bp
182:bp
90:;
86::
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78::
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1997::
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94::
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