Reviewed,
UniProtKB/Swiss-Prot Q9UQ35 (SRRM2_HUMAN)
Last modified
May 5, 2009.
Version 59.
History...
Clusters with 100%,
90%,
50% identity |
Documents (5) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Serine/arginine repetitive matrix protein 2 Alternative name(s): Serine/arginine-rich splicing factor-related nuclear matrix protein of 300 kDa Short name=Ser/Arg-related nuclear matrix protein Short name=SR-related nuclear matrix protein of 300 kDa Splicing coactivator subunit SRm300 300 kDa nuclear matrix antigen | ||||||
| Gene names |
| ||||||
| Organism | Homo sapiens (Human) | ||||||
| Taxonomic identifier | 9606 [NCBI] | ||||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Protein attributes
| Sequence length | 2752 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Part of pre- and post-splicing multiprotein mRNP complexes. May be involved in pre-mRNA processing events. Binds to RNA. Ref.2 |
| Subunit structure | Component of the active spliceosome. Found in a pre-mRNA splicing complex with SFRS4, SFRS5, SNRP70, SNRPA1, SRRM1 and SRRM2. Identified in the spliceosome C complex, at least composed of AQR, ASCC3L1, C19orf29, CDC40, CDC5L, CRNKL1, DDX23, DDX41, DDX48, DDX5, DGCR14, DHX35, DHX38, DHX8, EFTUD2, FRG1, GPATC1, HNRPA1, HNRPA2B1, HNRPA3, HNRPC, HNRPF, HNRPH1, HNRPK, HNRPM, HNRPR, HNRPU, KIAA1160, KIAA1604, LSM2, LSM3, MAGOH, MORG1, PABPC1, PLRG1, PNN, PPIE, PPIL1, PPIL3, PPWD1, PRPF19, PRPF4B, PRPF6, PRPF8, RALY, RBM22, RBM8A, RBMX, SART1, SF3A1, SF3A2, SF3A3, SF3B1, SF3B2, SF3B3, SFRS1, SKIV2L2, SNRPA1, SNRPB, SNRPB2, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF, SNRPG, SNW1, SRRM1, SRRM2, SYF2, SYNCRIP, TFIP11, THOC4, U2AF1, WDR57, XAB2 and ZCCHC8. |
| Subcellular location | |
| Tissue specificity | Expressed in liver, placenta, and white blood cells. Ref.1 |
| Post-translational modification | Phosphorylated upon DNA damage, probably by ATM or ATR. Ref.1 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 |
| Sequence similarities | Belongs to the CWC21 family. |
| Sequence caution | The sequence AAF21439.1 differs from that shown. Reason: Frameshift at several positions. The sequence AAF28898.1 differs from that shown. Reason: Frameshift at positions 167, 175 and 179. The sequence AAH70050.1 differs from that shown. Reason: Miscellaneous discrepancy. Contaminating sequence. Potential poly-A sequence. |
Ontologies
| Keywords | |
|---|---|
| Biological process | mRNA processing mRNA splicing |
| Cellular component | Nucleus Spliceosome |
| Coding sequence diversity | Alternative splicing Polymorphism |
| Domain | Coiled coil |
| Ligand | RNA-binding |
| PTM | Acetylation Phosphoprotein |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | RNA splicing Inferred from electronic annotation. Source: UniProtKB-KW mRNA processingInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | nuclear speck Inferred from electronic annotation. Source: UniProtKB-SubCell spliceosomeInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | RNA binding Inferred from electronic annotation. Source: UniProtKB-KW protein bindingInferred from physical interaction. Source: IntAct |
| Complete GO annotation... | |
Binary interactions
With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| BAK1 | Q16611 | 1 | EBI-1050142,EBI-519866 | |
| RNPS1 | Q15287 | 1 | EBI-1050142,EBI-395959 | |
| YWHAB | P31946 | 1 | EBI-1050142,EBI-359815 | |
| YWHAG | P61981 | 1 | EBI-1050142,EBI-359832 |
Alternative products
| This entry describes 3 isoforms produced by alternative splicing. [Align] [Select] | ||||||
| Isoform 1 (identifier: Q9UQ35-1) This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. | ||||||
| Isoform 2 (identifier: Q9UQ35-2) The sequence of this isoform differs from the canonical sequence as follows: 2023-2440: Missing. | ||||||
| Note: No experimental confirmation available. | ||||||
| Isoform 3 (identifier: Q9UQ35-3) The sequence of this isoform differs from the canonical sequence as follows: 1-96: Missing. 394-407: PSEASPTRDRSPPK → SPQLFMFLKGILVF 408-2752: Missing. | ||||||
| Note: No experimental confirmation available. |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 2752 | 2752 | Serine/arginine repetitive matrix protein 2 | PRO_0000248154 | |||||
Regions | |||||||||
| Region | 197 – 259 | 63 | Sufficient for RNA-binding | ||||||
| Coiled coil | 60 – 92 | 33 | Potential | ||||||
| Compositional bias | 177 – 2731 | 2555 | Ser-rich | ||||||
| Compositional bias | 186 – 246 | 61 | Lys-rich | ||||||
| Compositional bias | 350 – 447 | 98 | Pro-rich | ||||||
| Compositional bias | 462 – 816 | 355 | Arg-rich | ||||||
| Compositional bias | 1666 – 2089 | 424 | Arg-rich | ||||||
| Compositional bias | 2182 – 2378 | 197 | Ala-rich | ||||||
| Compositional bias | 2673 – 2750 | 78 | Arg-rich | ||||||
Amino acid modifications | |||||||||
| Modified residue | 1 | 1 | N-acetylmethionine Ref.7 | ||||||
| Modified residue | 142 | 1 | Phosphoserine Ref.11 | ||||||
| Modified residue | 250 | 1 | Phosphoserine Ref.11 | ||||||
| Modified residue | 252 | 1 | Phosphothreonine Ref.11 | ||||||
| Modified residue | 274 | 1 | Phosphothreonine Ref.11 | ||||||
| Modified residue | 295 | 1 | Phosphoserine Ref.12 Ref.17 Ref.19 Ref.20 | ||||||
| Modified residue | 297 | 1 | Phosphoserine Ref.11 Ref.12 Ref.17 Ref.19 Ref.20 | ||||||
| Modified residue | 322 | 1 | Phosphoserine Ref.20 | ||||||
| Modified residue | 323 | 1 | Phosphoserine Ref.17 Ref.20 | ||||||
| Modified residue | 351 | 1 | Phosphoserine Ref.11 | ||||||
| Modified residue | 353 | 1 | Phosphoserine Ref.11 | ||||||
| Modified residue | 367 | 1 | Phosphothreonine Ref.11 Ref.14 | ||||||
| Modified residue | 377 | 1 | Phosphoserine Ref.17 Ref.18 | ||||||
| Modified residue | 383 | 1 | Phosphothreonine Ref.17 | ||||||
| Modified residue | 384 | 1 | Phosphothreonine Ref.17 | ||||||
| Modified residue | 387 | 1 | Phosphoserine Ref.17 Ref.18 | ||||||
| Modified residue | 395 | 1 | Phosphoserine Ref.17 | ||||||
| Modified residue | 398 | 1 | Phosphoserine Ref.17 Ref.18 | ||||||
| Modified residue | 400 | 1 | Phosphothreonine Ref.17 | ||||||
| Modified residue | 404 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 408 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 415 | 1 | Phosphoserine Ref.17 | ||||||
| Modified residue | 418 | 1 | Phosphoserine Ref.17 | ||||||
| Modified residue | 424 | 1 | Phosphoserine Ref.11 | ||||||
| Modified residue | 428 | 1 | Phosphothreonine Ref.17 | ||||||
| Modified residue | 435 | 1 | Phosphoserine Ref.17 | ||||||
| Modified residue | 436 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 437 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 440 | 1 | Phosphoserine Ref.17 | ||||||
| Modified residue | 534 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 536 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 755 | 1 | Phosphoserine Ref.17 | ||||||
| Modified residue | 759 | 1 | Phosphoserine Ref.17 | ||||||
| Modified residue | 761 | 1 | Phosphoserine Ref.17 | ||||||
| Modified residue | 763 | 1 | Phosphoserine Ref.17 | ||||||
| Modified residue | 764 | 1 | Phosphoserine Ref.17 | ||||||
| Modified residue | 774 | 1 | Phosphoserine Ref.17 | ||||||
| Modified residue | 778 | 1 | Phosphoserine Ref.14 Ref.17 | ||||||
| Modified residue | 780 | 1 | Phosphoserine Ref.14 Ref.17 | ||||||
| Modified residue | 783 | 1 | Phosphoserine Ref.14 Ref.17 | ||||||
| Modified residue | 820 | 1 | Phosphoserine Ref.11 | ||||||
| Modified residue | 846 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 848 | 1 | Phosphothreonine By similarity | ||||||
| Modified residue | 857 | 1 | Phosphoserine Ref.11 | ||||||
| Modified residue | 866 | 1 | Phosphothreonine Ref.11 | ||||||
| Modified residue | 871 | 1 | Phosphoserine Ref.14 | ||||||
| Modified residue | 875 | 1 | Phosphoserine Ref.19 | ||||||
| Modified residue | 876 | 1 | Phosphoserine Ref.14 | ||||||
| Modified residue | 883 | 1 | Phosphoserine Ref.17 | ||||||
| Modified residue | 885 | 1 | Phosphothreonine Ref.17 | ||||||
| Modified residue | 890 | 1 | Phosphoserine Ref.17 | ||||||
| Modified residue | 894 | 1 | Phosphoserine Ref.17 | ||||||
| Modified residue | 895 | 1 | Phosphoserine Ref.17 | ||||||
| Modified residue | 901 | 1 | Phosphoserine Ref.11 | ||||||
| Modified residue | 903 | 1 | Phosphothreonine Ref.11 | ||||||
| Modified residue | 908 | 1 | Phosphoserine Ref.11 | ||||||
| Modified residue | 914 | 1 | Phosphoserine Ref.11 | ||||||
| Modified residue | 924 | 1 | Phosphoserine Ref.12 | ||||||
| Modified residue | 950 | 1 | Phosphoserine Ref.17 | ||||||
| Modified residue | 952 | 1 | Phosphoserine Ref.14 Ref.17 | ||||||
| Modified residue | 954 | 1 | Phosphoserine Ref.14 Ref.17 Ref.19 | ||||||
| Modified residue | 972 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 973 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 974 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 983 | 1 | Phosphothreonine Ref.17 Ref.19 | ||||||
| Modified residue | 988 | 1 | Phosphoserine Ref.11 Ref.17 Ref.19 | ||||||
| Modified residue | 994 | 1 | Phosphoserine Ref.11 Ref.17 | ||||||
| Modified residue | 996 | 1 | Phosphotyrosine Ref.17 | ||||||
| Modified residue | 1003 | 1 | Phosphothreonine Ref.11 Ref.19 | ||||||
| Modified residue | 1014 | 1 | Phosphoserine Ref.19 | ||||||
| Modified residue | 1043 | 1 | Phosphothreonine Ref.11 Ref.19 | ||||||
| Modified residue | 1063 | 1 | Phosphothreonine Ref.17 | ||||||
| Modified residue | 1069 | 1 | Phosphoserine Ref.11 Ref.17 | ||||||
| Modified residue | 1071 | 1 | Phosphothreonine Ref.17 | ||||||
| Modified residue | 1072 | 1 | Phosphoserine Ref.14 Ref.17 | ||||||
| Modified residue | 1073 | 1 | Phosphoserine Ref.11 Ref.14 Ref.17 | ||||||
| Modified residue | 1079 | 1 | Phosphoserine Ref.11 | ||||||
| Modified residue | 1083 | 1 | Phosphoserine Ref.11 | ||||||
| Modified residue | 1099 | 1 | Phosphoserine Ref.17 | ||||||
| Modified residue | 1101 | 1 | Phosphoserine Ref.17 | ||||||
| Modified residue | 1103 | 1 | Phosphoserine Ref.11 Ref.17 | ||||||
| Modified residue | 1106 | 1 | Phosphothreonine Ref.17 Ref.19 | ||||||
| Modified residue | 1110 | 1 | Phosphoserine Ref.17 | ||||||
| Modified residue | 1112 | 1 | Phosphoserine Ref.17 Ref.19 | ||||||
| Modified residue | 1124 | 1 | Phosphoserine Ref.11 Ref.15 Ref.17 | ||||||
| Modified residue | 1129 | 1 | Phosphoserine Ref.17 | ||||||
| Modified residue | 1132 | 1 | Phosphoserine Ref.11 | ||||||
| Modified residue | 1179 | 1 | Phosphoserine Ref.11 | ||||||
| Modified residue | 1188 | 1 | Phosphoserine Ref.15 | ||||||
| Modified residue | 1205 | 1 | Phosphothreonine Ref.17 | ||||||
| Modified residue | 1208 | 1 | Phosphothreonine Ref.17 | ||||||
| Modified residue | 1214 | 1 | Phosphoserine Ref.11 | ||||||
| Modified residue | 1218 | 1 | Phosphoserine Ref.17 | ||||||
| Modified residue | 1219 | 1 | Phosphoserine Ref.11 Ref.17 | ||||||
| Modified residue | 1257 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1320 | 1 | Phosphoserine Ref.11 Ref.17 Ref.19 | ||||||
| Modified residue | 1326 | 1 | Phosphoserine Ref.11 | ||||||
| Modified residue | 1329 | 1 | Phosphoserine Ref.15 Ref.17 | ||||||
| Modified residue | 1348 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1378 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1382 | 1 | Phosphoserine Ref.12 | ||||||
| Modified residue | 1383 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1384 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1387 | 1 | Phosphoserine Ref.12 | ||||||
| Modified residue | 1397 | 1 | Phosphoserine Ref.11 Ref.17 | ||||||
| Modified residue | 1398 | 1 | Phosphoserine Ref.17 | ||||||
| Modified residue | 1403 | 1 | Phosphoserine Ref.17 | ||||||
| Modified residue | 1404 | 1 | Phosphoserine Ref.11 Ref.17 Ref.20 | ||||||
| Modified residue | 1413 | 1 | Phosphothreonine Ref.17 Ref.20 | ||||||
| Modified residue | 1415 | 1 | Phosphoserine Ref.17 | ||||||
| Modified residue | 1419 | 1 | Phosphoserine Ref.19 | ||||||
| Modified residue | 1420 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1421 | 1 | Phosphoserine Ref.11 | ||||||
| Modified residue | 1423 | 1 | Phosphoserine Ref.11 | ||||||
| Modified residue | 1424 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1441 | 1 | Phosphoserine Ref.11 | ||||||
| Modified residue | 1443 | 1 | Phosphoserine Ref.11 | ||||||
| Modified residue | 1444 | 1 | Phosphoserine Ref.11 | ||||||
| Modified residue | 1453 | 1 | Phosphothreonine Ref.11 | ||||||
| Modified residue | 1458 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1483 | 1 | Phosphoserine Ref.11 | ||||||
| Modified residue | 1492 | 1 | Phosphothreonine Ref.17 | ||||||
| Modified residue | 1497 | 1 | Phosphoserine Ref.12 Ref.17 | ||||||
| Modified residue | 1499 | 1 | Phosphoserine Ref.11 Ref.17 | ||||||
| Modified residue | 1501 | 1 | Phosphoserine Ref.11 Ref.12 Ref.17 | ||||||
| Modified residue | 1502 | 1 | Phosphoserine Ref.11 Ref.12 Ref.17 | ||||||
| Modified residue | 1511 | 1 | Phosphothreonine Ref.11 | ||||||
| Modified residue | 1517 | 1 | Phosphoserine Ref.11 | ||||||
| Modified residue | 1519 | 1 | Phosphoserine Ref.11 | ||||||
| Modified residue | 1522 | 1 | Phosphoserine Ref.11 | ||||||
| Modified residue | 1531 | 1 | Phosphothreonine Ref.16 | ||||||
| Modified residue | 1559 | 1 | Phosphoserine Ref.11 | ||||||
| Modified residue | 1571 | 1 | Phosphothreonine Ref.17 | ||||||
| Modified residue | 1579 | 1 | Phosphoserine Ref.11 Ref.17 | ||||||
| Modified residue | 1581 | 1 | Phosphoserine Ref.11 Ref.17 | ||||||
| Modified residue | 1582 | 1 | Phosphoserine Ref.11 Ref.17 | ||||||
| Modified residue | 1592 | 1 | Phosphoserine Ref.17 | ||||||
| Modified residue | 1596 | 1 | Phosphoserine Ref.17 | ||||||
| Modified residue | 1598 | 1 | Phosphoserine Ref.17 | ||||||
| Modified residue | 1600 | 1 | Phosphoserine Ref.11 Ref.12 Ref.17 | ||||||
| Modified residue | 1601 | 1 | Phosphoserine Ref.11 Ref.12 Ref.17 | ||||||
| Modified residue | 1616 | 1 | Phosphoserine Ref.12 Ref.17 | ||||||
| Modified residue | 1618 | 1 | Phosphoserine Ref.11 Ref.17 | ||||||
| Modified residue | 1620 | 1 | Phosphoserine Ref.12 Ref.17 | ||||||
| Modified residue | 1621 | 1 | Phosphoserine Ref.11 Ref.12 Ref.17 | ||||||
| Modified residue | 1636 | 1 | Phosphoserine Ref.17 | ||||||
| Modified residue | 1638 | 1 | Phosphoserine Ref.17 | ||||||
| Modified residue | 1640 | 1 | Phosphoserine Ref.17 | ||||||
| Modified residue | 1641 | 1 | Phosphoserine Ref.17 | ||||||
| Modified residue | 1657 | 1 | Phosphoserine Ref.17 | ||||||
| Modified residue | 1658 | 1 | Phosphoserine Ref.17 | ||||||
| Modified residue | 1682 | 1 | Phosphoserine Ref.17 | ||||||
| Modified residue | 1684 | 1 | Phosphothreonine Ref.17 | ||||||
| Modified residue | 1690 | 1 | Phosphoserine Ref.17 | ||||||
| Modified residue | 1691 | 1 | Phosphoserine Ref.17 | ||||||
| Modified residue | 1693 | 1 | Phosphoserine Ref.17 | ||||||
| Modified residue | 1694 | 1 | Phosphoserine Ref.17 | ||||||
| Modified residue | 1842 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1844 | 1 | Phosphothreonine By similarity | ||||||
| Modified residue | 1876 | 1 | Phosphoserine Ref.17 | ||||||
| Modified residue | 1878 | 1 | Phosphoserine Ref.14 Ref.17 Ref.19 | ||||||
| Modified residue | 1880 | 1 | Phosphothreonine Ref.11 Ref.14 Ref.17 Ref.19 | ||||||
| Modified residue | 1958 | 1 | Phosphoserine Ref.17 | ||||||
| Modified residue | 1960 | 1 | Phosphoserine Ref.17 | ||||||
| Modified residue | 1962 | 1 | Phosphothreonine Ref.11 Ref.17 | ||||||
| Modified residue | 1975 | 1 | Phosphoserine Ref.16 | ||||||
| Modified residue | 2011 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 2018 | 1 | Phosphoserine Ref.17 | ||||||
| Modified residue | 2020 | 1 | Phosphoserine Ref.17 | ||||||
| Modified residue | 2022 | 1 | Phosphothreonine Ref.17 | ||||||
| Modified residue | 2030 | 1 | Phosphoserine Ref.17 | ||||||
| Modified residue | 2032 | 1 | Phosphoserine Ref.14 Ref.15 Ref.17 | ||||||
| Modified residue | 2034 | 1 | Phosphothreonine Ref.14 Ref.17 | ||||||
| Modified residue | 2042 | 1 | Phosphoserine Ref.17 | ||||||
| Modified residue | 2044 | 1 | Phosphoserine Ref.11 Ref.14 Ref.15 Ref.17 | ||||||
| Modified residue | 2046 | 1 | Phosphoserine Ref.11 Ref.14 Ref.17 Ref.19 | ||||||
| Modified residue | 2067 | 1 | Phosphoserine Ref.15 Ref.17 | ||||||
| Modified residue | 2069 | 1 | Phosphothreonine Ref.17 | ||||||
| Modified residue | 2071 | 1 | Phosphoserine Ref.11 Ref.17 | ||||||
| Modified residue | 2092 | 1 | Phosphothreonine Ref.11 | ||||||
| Modified residue | 2100 | 1 | Phosphoserine Ref.12 Ref.19 | ||||||
| Modified residue | 2102 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 2104 | 1 | Phosphothreonine Ref.11 | ||||||
| Modified residue | 2121 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 2132 | 1 | Phosphoserine Ref.19 | ||||||
| Modified residue | 2272 | 1 | Phosphoserine Ref.11 Ref.14 Ref.15 Ref.17 Ref.20 | ||||||
| Modified residue | 2289 | 1 | Phosphothreonine Ref.14 | ||||||
| Modified residue | 2291 | 1 | Phosphothreonine Ref.14 | ||||||
| Modified residue | 2316 | 1 | Phosphothreonine Ref.14 | ||||||
| Modified residue | 2335 | 1 | Phosphoserine Ref.11 | ||||||
| Modified residue | 2382 | 1 | Phosphoserine Ref.11 Ref.14 | ||||||
| Modified residue | 2397 | 1 | Phosphothreonine Ref.19 | ||||||
| Modified residue | 2398 | 1 | Phosphoserine Ref.11 Ref.19 Ref.20 | ||||||
| Modified residue | 2407 | 1 | Phosphoserine Ref.11 Ref.17 Ref.20 | ||||||
| Modified residue | 2409 | 1 | Phosphothreonine Ref.11 Ref.17 Ref.20 | ||||||
| Modified residue | 2426 | 1 | Phosphoserine Ref.11 | ||||||
| Modified residue | 2436 | 1 | Phosphoserine Ref.18 | ||||||
| Modified residue | 2449 | 1 | Phosphoserine Ref.11 Ref.14 | ||||||
| Modified residue | 2453 | 1 | Phosphoserine Ref.18 | ||||||
| Modified residue | 2581 | 1 | Phosphoserine Ref.11 Ref.19 | ||||||
| Modified residue | 2583 | 1 | Phosphothreonine By similarity | ||||||
| Modified residue | 2675 | 1 | Phosphoserine Ref.13 Ref.21 | ||||||
| Modified residue | 2677 | 1 | Phosphoserine Ref.13 Ref.21 | ||||||
| Modified residue | 2684 | 1 | Phosphoserine Ref.13 | ||||||
| Modified residue | 2688 | 1 | Phosphoserine Ref.13 Ref.20 | ||||||
| Modified residue | 2690 | 1 | Phosphoserine Ref.21 | ||||||
| Modified residue | 2692 | 1 | Phosphoserine Ref.11 Ref.14 Ref.15 Ref.21 | ||||||
| Modified residue | 2693 | 1 | Phosphotyrosine By similarity | ||||||
| Modified residue | 2694 | 1 | Phosphoserine Ref.11 Ref.14 Ref.15 Ref.19 Ref.20 Ref.21 | ||||||
| Modified residue | 2702 | 1 | Phosphoserine Ref.13 | ||||||
| Modified residue | 2706 | 1 | Phosphoserine Ref.13 | ||||||
| Modified residue | 2714 | 1 | Phosphoserine Ref.11 | ||||||
| Modified residue | 2738 | 1 | Phosphothreonine Ref.13 | ||||||
| Modified residue | 2740 | 1 | Phosphoserine Ref.13 | ||||||
Natural variations | |||||||||
| Alternative sequence | 1 – 96 | 96 | Missing in isoform 3. | VSP_020184 | |||||
| Alternative sequence | 394 – 407 | 14 | PSEAS…RSPPK → SPQLFMFLKGILVF in isoform 3. | VSP_020185 | |||||
| Alternative sequence | 408 – 2752 | 2345 | Missing in isoform 3. | VSP_020186 | |||||
| Alternative sequence | 2023 – 2440 | 418 | Missing in isoform 2. | VSP_020187 | |||||
| Natural variant | 804 | 1 | P → T: dbSNP rs2240140. Ref.3 | VAR_027259 | |||||
| Natural variant | 856 | 1 | T → R: dbSNP rs12185191. | VAR_048868 | |||||
| Natural variant | 883 | 1 | S → C: dbSNP rs17136053. | VAR_027260 | |||||
Experimental info | |||||||||
| Sequence conflict | 157 | 1 | A → V in AAF28898. Ref.8 | ||||||
| Sequence conflict | 178 – 179 | 2 | SS → NN in AAF21439. Ref.2 | ||||||
| Sequence conflict | 195 | 1 | D → K in AAH07752. Ref.6 | ||||||
| Sequence conflict | 314 | 1 | G → S in AAF21439. Ref.2 | ||||||
| Sequence conflict | 321 | 1 | P → A in AAF21439. Ref.2 | ||||||
| Sequence conflict | 1474 | 1 | S → F in BAA83716. Ref.1 | ||||||
| Sequence conflict | 1474 | 1 | S → F in BAA83718. Ref.1 | ||||||
Sequences
| ||||||||||||||||||||||||||||||
References
| « Hide 'large scale' references | |
| [1] | "Cloning and characterization of a novel RNA-binding protein SRL300 with RS domains." Sawada Y., Miura Y., Umeki K., Tamaoki T., Fujinaga K., Ohtaki S. Biochim. Biophys. Acta 1492:191-195(2000) [PubMed: 11004489] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), RNA-BINDING, TISSUE SPECIFICITY, PHOSPHORYLATION. Tissue: Cervix carcinoma. |
| [2] | "The SRm160/300 splicing coactivator subunits." Blencowe B.J., Bauren G., Eldridge A.G., Issner R., Nickerson J.A., Rosonina E., Sharp P.A. RNA 6:111-120(2000) [PubMed: 10668804] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), PROTEIN SEQUENCE OF 1223-1226 AND 2587-2597, FUNCTION. |
| [3] | "Prediction of the coding sequences of unidentified human genes. VII. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro." Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O. DNA Res. 4:141-150(1997) [PubMed: 9205841] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT THR-804. Tissue: Brain. |
| [4] | "The sequence and analysis of duplication-rich human chromosome 16." Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J. Pennacchio L.A.Nature 432:988-994(2004) [PubMed: 15616553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
| [5] | Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. Venter J.C.Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
| [6] | "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1018 AND 2555-2752. Tissue: Blood, Embryonic testis carcinoma, Placenta, Retinoblastoma and Rhabdomyosarcoma. |
| [7] | Bienvenut W.V., Heiserich L., Boulahbel H., Gottlieb E. Submitted (JUL-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 1-11; 44-51; 116-130; 137-155; 357-401; 1001-1013; 1041-1058; 1101-1111; 1119-1128; 1138-1158; 1224-1277; 1316-1352; 1394-1412; 1539-1556; 2104-2113; 2120-2129; 2132-2163; 2181-2221; 2232-2392; 2431-2460 AND 2690-2698, ACETYLATION AT MET-1, MASS SPECTROMETRY. Tissue: Colon carcinoma. |
| [8] | "Human partial CDS from CD34+ stem cells." Ye M., Zhang Q.-H., Zhou J., Shen Y., Wu X.-Y., Guan Z.Q., Wang L., Fan H.-Y., Mao Y.-F., Dai M., Huang Q.-H., Chen S.-J., Chen Z. Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 88-185. Tissue: Umbilical cord blood. |
| [9] | "A coactivator of pre-mRNA splicing." Blencowe B.J., Issner R., Nickerson J.A., Sharp P.A. Genes Dev. 12:996-1009(1998) [PubMed: 9531537] [Abstract] Cited for: IDENTIFICATION IN A PRE-MRNA SPLICING COMPLEX WITH SFRS4; SFRS5; SNRP70; SNRPA1 AND SRRM1. |
| [10] | "Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis." Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J. RNA 8:426-439(2002) [PubMed: 11991638] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE SPICEOSOMAL C COMPLEX. |
| [11] | "Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-142; SER-250; THR-252; THR-274; SER-297; SER-351; SER-353; THR-367; SER-424; SER-820; SER-857; THR-866; SER-901; THR-903; SER-908; SER-914; SER-988; SER-994; THR-1003; THR-1043; SER-1069; SER-1073; SER-1079; SER-1083; SER-1103; SER-1124; SER-1132; SER-1179; SER-1214; SER-1219; SER-1320; SER-1326; SER-1397; SER-1404; SER-1421; SER-1423; SER-1441; SER-1443; SER-1444; THR-1453; SER-1483; SER-1499; SER-1501; SER-1502; THR-1511; SER-1517; SER-1519; SER-1522; SER-1559; SER-1579; SER-1581; SER-1582; SER-1600; SER-1601; SER-1618; SER-1621; THR-1880; THR-1962; SER-2044; SER-2046; SER-2071; THR-2092; THR-2104; SER-2272; SER-2335; SER-2382; SER-2398; SER-2407; THR-2409; SER-2426; SER-2449; SER-2581; SER-2692; SER-2694 AND SER-2714, MASS SPECTROMETRY. Tissue: Epithelium. |
| [12] | "Global phosphoproteome of HT-29 human colon adenocarcinoma cells." Kim J.-E., Tannenbaum S.R., White F.M. J. Proteome Res. 4:1339-1346(2005) [PubMed: 16083285] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295; SER-297; SER-924; SER-1382; SER-1387; SER-1497; SER-1501; SER-1502; SER-1600; SER-1601; SER-1616; SER-1620; SER-1621 AND SER-2100, MASS SPECTROMETRY. |
| [13] | "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2675; SER-2677; SER-2684; SER-2688; SER-2702; SER-2706; THR-2738 AND SER-2740, MASS SPECTROMETRY. Tissue: Epithelium. |
| [14] | "A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed: 16964243] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-367; SER-778; SER-780; SER-783; SER-871; SER-876; SER-952; SER-954; SER-1072; SER-1073; SER-1878; THR-1880; SER-2032; THR-2034; SER-2044; SER-2046; SER-2272; THR-2289; THR-2291; THR-2316; SER-2382; SER-2449; SER-2692 AND SER-2694, MASS SPECTROMETRY. Tissue: Epithelium. |
| [15] | "Phosphoproteome analysis of the human mitotic spindle." Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R. Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006) [PubMed: 16565220] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1124; SER-1188; SER-1329; SER-2032; SER-2044; SER-2067; SER-2272; SER-2692 AND SER-2694, MASS SPECTROMETRY. Tissue: Epithelium. |
| [16] | "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra." Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D. J. Proteome Res. 6:4150-4162(2007) [PubMed: 17924679] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1531 AND SER-1975, MASS SPECTROMETRY. Tissue: Epithelium. |
| [17] | "Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry." Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A. Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295; SER-297; SER-323; SER-377; THR-383; THR-384; SER-387; SER-395; SER-398; THR-400; SER-415; SER-418; THR-428; SER-435; SER-440; SER-755; SER-759; SER-761; SER-763; SER-764; SER-774; SER-778; SER-780; SER-783; SER-883; THR-885; SER-890; SER-894; SER-895; SER-950; SER-952; SER-954; THR-983; SER-988; SER-994; TYR-996; THR-1063; SER-1069; THR-1071; SER-1072; SER-1073; SER-1099; SER-1101; SER-1103; THR-1106; SER-1110; SER-1112; SER-1124; SER-1129; THR-1205; THR-1208; SER-1218; SER-1219; SER-1320; SER-1329; SER-1397; SER-1398; SER-1403; SER-1404; THR-1413; SER-1415; THR-1492; SER-1497; SER-1499; SER-1501; SER-1502; THR-1571; SER-1579; SER-1581; SER-1582; SER-1592; SER-1596; SER-1598; SER-1600; SER-1601; SER-1616; SER-1618; SER-1620; SER-1621; SER-1636; SER-1638; SER-1640; SER-1641; SER-1657; SER-1658; SER-1682; THR-1684; SER-1690; SER-1691; SER-1693; SER-1694; SER-1876; SER-1878; THR-1880; SER-1958; SER-1960; THR-1962; SER-2018; SER-2020; THR-2022; SER-2030; SER-2032; THR-2034; SER-2042; SER-2044; SER-2046; SER-2067; THR-2069; SER-2071; SER-2272; SER-2407 AND THR-2409, MASS SPECTROMETRY. |
| [18] | "ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 316:1160-1166(2007) [PubMed: 17525332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-377; SER-387; SER-398; SER-2436 AND SER-2453, MASS SPECTROMETRY. |
| [19] | "Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column." Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y. Anal. Sci. 24:161-166(2008) [PubMed: 18187866] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295; SER-297; SER-875; SER-954; THR-983; SER-988; THR-1003; SER-1014; THR-1043; THR-1106; SER-1112; SER-1320; SER-1419; SER-1878; THR-1880; SER-2046; SER-2100; SER-2132; THR-2397; SER-2398; SER-2581 AND SER-2694, MASS SPECTROMETRY. |
| [20] | "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis." Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III J. Proteome Res. 7:1346-1351(2008) [PubMed: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295; SER-297; SER-322; SER-323; SER-1404; THR-1413; SER-2272; SER-2398; SER-2407; THR-2409; SER-2688 AND SER-2694, MASS SPECTROMETRY. |
| [21] | "A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2675; SER-2677; SER-2690; SER-2692 AND SER-2694, MASS SPECTROMETRY. |
| [22] | Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY. |
Cross-references
Sequence databases | |
|---|---|
| AB015644 mRNA. Translation: BAA34957.1. AB016087 mRNA. Translation: BAA83713.1. AB016089 mRNA. Translation: BAA83715.1. AB016090 mRNA. Translation: BAA83716.1. AB016091 mRNA. Translation: BAA83717.1. AB016092 mRNA. Translation: BAA83718.1. AF201422 mRNA. Translation: AAF21439.1. Frameshift. AB002322 mRNA. Translation: BAA20782.3. Different initiation. AC092117 Genomic DNA. No translation available. CH471112 Genomic DNA. Translation: EAW85478.1. BC007752 mRNA. Translation: AAH07752.1. BC009062 mRNA. Translation: AAH09062.1. BC032416 mRNA. Translation: AAH32416.1. BC041155 mRNA. Translation: AAH41155.1. BC070050 mRNA. Translation: AAH70050.1. Sequence problems. AF161338 mRNA. Translation: AAF28898.1. Frameshift. | |
| IPI | IPI00782992. IPI00784560. IPI00785023. |
| RefSeq | NP_057417.3. |
| UniGene | Hs.712559 |
3D structure databases | |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | Q9UQ35. 10 interactions. |
PTM databases | |
| PhosphoSite | Q9UQ35. |
Proteomic databases | |
| PRIDE | Q9UQ35. |
Genome annotation databases | |
| Ensembl | ENSG00000167978. Homo sapiens. [Contig view] |
| GeneID | 23524. |
| KEGG | hsa:23524. |
| NMPDR | fig|9606.3.peg.11582. |
Organism-specific databases | |
| GeneCards | GC16P002742. |
| HGNC | HGNC:16639. SRRM2. |
| MIM | 606032. gene. |
| PharmGKB | PA38178. |
| HUGE | Search... |
| GenAtlas | Search... |
Phylogenomic databases | |
| HOVERGEN | Q9UQ35. |
| OMA | Q9UQ35. TSPAPWK. |
Gene expression databases | |
| ArrayExpress | Q9UQ35. |
| Bgee | Q9UQ35. |
| GermOnline | ENSG00000167978. Homo sapiens. |
Family and domain databases | |
| InterPro | IPR013170. mRNA_splic_Cwf21. [Graphical view] |
| Pfam | PF08312. cwf21. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| NextBio | 45984. |
| SOURCE | Search... |
Entry information
| Entry name | SRRM2_HUMAN | ||||||||
| Accession | Primary (citable) accession number: Q9UQ35 Secondary accession number(s): A6NKB9 Q9UQ40 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
Relevant documents
| Human chromosome 16 Human chromosome 16: entries, gene names and cross-references to MIM |
| Human entries with polymorphisms or disease mutations List of human entries with polymorphisms or disease mutations |
| Human polymorphisms and disease mutations Index of human polymorphisms and disease mutations |
| MIM cross-references Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot |
| SIMILARITY comments Index of protein domains and families |

Clusters with


