Reviewed,
UniProtKB/Swiss-Prot Q8CIZ8 (VWF_MOUSE)
Last modified
January 19, 2010.
Version 71.
History...
Clusters with 100%,
90%,
50% identity |
Documents (3) |
Third-party data |
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Names and origin
| Protein names | Recommended name: von Willebrand factor Short name=vWF Cleaved into the following chain: 1- Recommended name: von Willebrand antigen 2 Alternative name(s): von Willebrand antigen II | ||
| Gene names |
| ||
| Organism | Mus musculus (Mouse) | ||
| Taxonomic identifier | 10090 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus |
Protein attributes
| Sequence length | 2813 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Important in the maintenance of hemostasis, it promotes adhesion of platelets to the sites of vascular injury by forming a molecular bridge between sub-endothelial collagen matrix and platelet-surface receptor complex GPIb-IX-V. Also acts as a chaperone for coagulation factor VIII, delivering it to the site of injury, stabilizing its heterodimeric structure and protecting it from premature clearance from plasma By similarity. UniProtKB P04275 |
| Subunit structure | Multimeric. Interacts with F8 By similarity. |
| Subcellular location | Secreted By similarity. Secreted › extracellular space › extracellular matrix By similarity. Note: Localized to storage granules By similarity. |
| Tissue specificity | Plasma. Expressed in liver. Ref.7 |
| Domain | The von Willebrand antigen 2 is required for multimerization of vWF and for its targeting to storage granules By similarity. |
| Post-translational modification | All cysteine residues are involved in intrachain or interchain disulfide bonds By similarity. UniProtKB P04275 N- and O-glycosylated By similarity. |
| Sequence similarities | Contains 1 CTCK (C-terminal cystine knot-like) domain. Contains 1 pacifastin repeat. Contains 4 TIL (trypsin inhibitory-like) domains. Contains 3 VWFA domains. Contains 3 VWFC domains. Contains 4 VWFD domains. |
Ontologies
Alternative products
| This entry describes 2 isoforms produced by alternative splicing. [Align] [Select] | ||||||
| Isoform 1 Ref.7 (identifier: Q8CIZ8-1) 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: Q8CIZ8-2) The sequence of this isoform differs from the canonical sequence as follows: 387-402: ECLVTGQSHFKSFDNR → RLGTFSPFLPVLCGEV 403-2813: Missing. | ||||||
| Note: No experimental confirmation available. |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||||||||||||||||||||||||||
Molecule processing | |||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 22 | 22 | By similarity UniProtKB P04275 | ||||||||||||||||||||||||||||||||
| Chain | 23 – 763 | 741 | von Willebrand antigen 2 UniProtKB P04275 | PRO_0000022684 | |||||||||||||||||||||||||||||||
| Chain | 764 – 2813 | 2050 | von Willebrand factor UniProtKB P04275 | PRO_0000022685 | |||||||||||||||||||||||||||||||
Regions | |||||||||||||||||||||||||||||||||||
| Domain | 34 – 240 | 207 | VWFD 1 | ||||||||||||||||||||||||||||||||
| Domain | 295 – 348 | 54 | TIL 1 | ||||||||||||||||||||||||||||||||
| Domain | 387 – 598 | 212 | VWFD 2 | ||||||||||||||||||||||||||||||||
| Domain | 652 – 707 | 56 | TIL 2 | ||||||||||||||||||||||||||||||||
| Domain | 804 – 827 | 24 | TIL 3 | ||||||||||||||||||||||||||||||||
| Repeat | 835 – 873 | 39 | Pacifastin | ||||||||||||||||||||||||||||||||
| Domain | 866 – 1074 | 209 | VWFD 3 | ||||||||||||||||||||||||||||||||
| Domain | 1146 – 1196 | 51 | TIL 4 | ||||||||||||||||||||||||||||||||
| Domain | 1277 – 1453 | 177 | VWFA 1; binding site for platelet glycoprotein Ib Ref.7 | ||||||||||||||||||||||||||||||||
| Domain | 1498 – 1665 | 168 | VWFA 2 | ||||||||||||||||||||||||||||||||
| Domain | 1691 – 1871 | 181 | VWFA 3; principal binding site for collagens type I and III Ref.7 | ||||||||||||||||||||||||||||||||
| Domain | 1949 – 2153 | 205 | VWFD 4 | ||||||||||||||||||||||||||||||||
| Domain | 2255 – 2328 | 74 | VWFC 1 | ||||||||||||||||||||||||||||||||
| Domain | 2429 – 2495 | 67 | VWFC 2 | ||||||||||||||||||||||||||||||||
| Domain | 2580 – 2645 | 66 | VWFC 3 | ||||||||||||||||||||||||||||||||
| Domain | 2724 – 2812 | 89 | CTCK | ||||||||||||||||||||||||||||||||
| Region | 764 – 787 | 24 | Amino-terminal | ||||||||||||||||||||||||||||||||
| Region | 788 – 833 | 46 | E1 | ||||||||||||||||||||||||||||||||
| Region | 826 – 853 | 28 | CX | ||||||||||||||||||||||||||||||||
| Region | 2216 – 2261 | 46 | E2 | ||||||||||||||||||||||||||||||||
| Motif | 2507 – 2509 | 3 | Cell attachment site By similarity UniProtKB P04275 | ||||||||||||||||||||||||||||||||
Amino acid modifications | |||||||||||||||||||||||||||||||||||
| Glycosylation | 99 | 1 | N-linked (GlcNAc...) Potential | ||||||||||||||||||||||||||||||||
| Glycosylation | 156 | 1 | N-linked (GlcNAc...) Potential | ||||||||||||||||||||||||||||||||
| Glycosylation | 666 | 1 | N-linked (GlcNAc...) Potential | ||||||||||||||||||||||||||||||||
| Glycosylation | 857 | 1 | N-linked (GlcNAc...) By similarity UniProtKB P04275 | ||||||||||||||||||||||||||||||||
| Glycosylation | 1005 | 1 | N-linked (GlcNAc...) Potential | ||||||||||||||||||||||||||||||||
| Glycosylation | 1147 | 1 | N-linked (GlcNAc...); atypical By similarity UniProtKB P04275 | ||||||||||||||||||||||||||||||||
| Glycosylation | 1231 | 1 | N-linked (GlcNAc...) By similarity UniProtKB P04275 | ||||||||||||||||||||||||||||||||
| Glycosylation | 1248 | 1 | O-linked (GalNAc...) By similarity | ||||||||||||||||||||||||||||||||
| Glycosylation | 1255 | 1 | O-linked (GalNAc...) By similarity | ||||||||||||||||||||||||||||||||
| Glycosylation | 1256 | 1 | O-linked (GalNAc...) By similarity | ||||||||||||||||||||||||||||||||
| Glycosylation | 1468 | 1 | O-linked (GalNAc...) By similarity | ||||||||||||||||||||||||||||||||
| Glycosylation | 1477 | 1 | O-linked (GalNAc...) By similarity | ||||||||||||||||||||||||||||||||
| Glycosylation | 1486 | 1 | O-linked (GalNAc...) By similarity | ||||||||||||||||||||||||||||||||
| Glycosylation | 1515 | 1 | N-linked (GlcNAc...) By similarity UniProtKB P04275 | ||||||||||||||||||||||||||||||||
| Glycosylation | 1574 | 1 | N-linked (GlcNAc...) By similarity UniProtKB P04275 | ||||||||||||||||||||||||||||||||
| Glycosylation | 1679 | 1 | O-linked (GalNAc...) By similarity | ||||||||||||||||||||||||||||||||
| Glycosylation | 2223 | 1 | N-linked (GlcNAc...) By similarity UniProtKB P04275 | ||||||||||||||||||||||||||||||||
| Glycosylation | 2290 | 1 | N-linked (GlcNAc...) By similarity UniProtKB P04275 | ||||||||||||||||||||||||||||||||
| Glycosylation | 2298 | 1 | O-linked (GalNAc...) By similarity | ||||||||||||||||||||||||||||||||
| Glycosylation | 2400 | 1 | N-linked (GlcNAc...) By similarity UniProtKB P04275 | ||||||||||||||||||||||||||||||||
| Glycosylation | 2546 | 1 | N-linked (GlcNAc...) By similarity UniProtKB P04275 | ||||||||||||||||||||||||||||||||
| Glycosylation | 2585 | 1 | N-linked (GlcNAc...) By similarity UniProtKB P04275 | ||||||||||||||||||||||||||||||||
| Glycosylation | 2790 | 1 | N-linked (GlcNAc...) By similarity UniProtKB P04275 | ||||||||||||||||||||||||||||||||
| Glycosylation | 2810 | 1 | N-linked (GlcNAc...) Potential | ||||||||||||||||||||||||||||||||
| Disulfide bond | 767 ↔ 808 | By similarity UniProtKB P04275 | |||||||||||||||||||||||||||||||||
| Disulfide bond | 776 ↔ 804 | By similarity UniProtKB P04275 | |||||||||||||||||||||||||||||||||
| Disulfide bond | 810 ↔ 821 | By similarity UniProtKB P04275 | |||||||||||||||||||||||||||||||||
| Disulfide bond | 889 ↔ 1031 | By similarity UniProtKB P04275 | |||||||||||||||||||||||||||||||||
| Disulfide bond | 898 ↔ 993 | By similarity UniProtKB P04275 | |||||||||||||||||||||||||||||||||
| Disulfide bond | 914 ↔ 921 | By similarity UniProtKB P04275 | |||||||||||||||||||||||||||||||||
| Disulfide bond | ? ↔ 996 | By similarity UniProtKB P04275 | |||||||||||||||||||||||||||||||||
| Disulfide bond | 1060 ↔ 1084 | By similarity UniProtKB P04275 | |||||||||||||||||||||||||||||||||
| Disulfide bond | 1071 ↔ 1111 | By similarity UniProtKB P04275 | |||||||||||||||||||||||||||||||||
| Disulfide bond | 1089 ↔ 1091 | By similarity UniProtKB P04275 | |||||||||||||||||||||||||||||||||
| Disulfide bond | 1126 ↔ 1130 | By similarity UniProtKB P04275 | |||||||||||||||||||||||||||||||||
| Disulfide bond | 1149 ↔ 1169 | By similarity UniProtKB P04275 | |||||||||||||||||||||||||||||||||
| Disulfide bond | 1153 ↔ 1165 | By similarity UniProtKB P04275 | |||||||||||||||||||||||||||||||||
| Disulfide bond | 1196 ↔ 1199 | By similarity UniProtKB P04275 | |||||||||||||||||||||||||||||||||
| Disulfide bond | 1234 ↔ 1237 | By similarity UniProtKB P04275 | |||||||||||||||||||||||||||||||||
| Disulfide bond | 1272 ↔ 1458 | By similarity UniProtKB P04275 | |||||||||||||||||||||||||||||||||
| Disulfide bond | 1669 ↔ 1670 | By similarity UniProtKB P04275 | |||||||||||||||||||||||||||||||||
| Disulfide bond | 1686 ↔ 1872 | By similarity UniProtKB P04275 | |||||||||||||||||||||||||||||||||
| Disulfide bond | 1879 ↔ 1904 | By similarity UniProtKB P04275 | |||||||||||||||||||||||||||||||||
| Disulfide bond | 1899 ↔ 1940 | Or C-1899 with C-1942 By similarity UniProtKB P04275 | |||||||||||||||||||||||||||||||||
| Disulfide bond | 1927 ↔ 2088 | By similarity UniProtKB P04275 | |||||||||||||||||||||||||||||||||
| Disulfide bond | 1950 ↔ 2085 | By similarity UniProtKB P04275 | |||||||||||||||||||||||||||||||||
| Disulfide bond | 1972 ↔ 2123 | By similarity UniProtKB P04275 | |||||||||||||||||||||||||||||||||
| Disulfide bond | 1993 ↔ 2001 | By similarity UniProtKB P04275 | |||||||||||||||||||||||||||||||||
| Disulfide bond | 2724 ↔ 2774 | By similarity UniProtKB P04275 | |||||||||||||||||||||||||||||||||
| Disulfide bond | 2739 ↔ 2788 | By similarity UniProtKB P04275 | |||||||||||||||||||||||||||||||||
| Disulfide bond | 2750 ↔ 2804 | By similarity UniProtKB P04275 | |||||||||||||||||||||||||||||||||
| Disulfide bond | 2754 ↔ 2806 | By similarity UniProtKB P04275 | |||||||||||||||||||||||||||||||||
| Disulfide bond | ? ↔ 2811 | By similarity UniProtKB P04275 | |||||||||||||||||||||||||||||||||
| Cross-link | 1720 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity | |||||||||||||||||||||||||||||||||
Natural variations | |||||||||||||||||||||||||||||||||||
| Alternative sequence | 387 – 402 | 16 | ECLVT…SFDNR → RLGTFSPFLPVLCGEV in isoform 2. | VSP_051618 | |||||||||||||||||||||||||||||||
| Alternative sequence | 403 – 2813 | 2411 | Missing in isoform 2. | VSP_051619 | |||||||||||||||||||||||||||||||
Experimental info | |||||||||||||||||||||||||||||||||||
| Mutagenesis | 1205 | 1 | R → H: Accelerated clearance of VWF from blood plasma. Ref.7 | ||||||||||||||||||||||||||||||||
| Sequence conflict | 103 | 1 | M → T in AAP41950. Ref.1 | ||||||||||||||||||||||||||||||||
| Sequence conflict | 122 | 1 | L → R in AAP41950. Ref.1 | ||||||||||||||||||||||||||||||||
| Sequence conflict | 799 | 1 | R → C in AAP41950. Ref.1 | ||||||||||||||||||||||||||||||||
| Sequence conflict | 867 | 1 | R → C in AAP41950. Ref.1 | ||||||||||||||||||||||||||||||||
| Sequence conflict | 895 | 1 | Y → Q in AAP41950. Ref.1 | ||||||||||||||||||||||||||||||||
| Sequence conflict | 1007 | 1 | S → F in AAP41950. Ref.1 | ||||||||||||||||||||||||||||||||
| Sequence conflict | 1245 | 1 | A → V in CAB86200. Ref.4 | ||||||||||||||||||||||||||||||||
| Sequence conflict | 1421 | 1 | S → D in AAA82929. Ref.5 | ||||||||||||||||||||||||||||||||
| Sequence conflict | 1485 – 1486 | 2 | IS → TL in AAA82929. Ref.5 | ||||||||||||||||||||||||||||||||
| Sequence conflict | 2361 | 1 | D → A in AAP41950. Ref.1 | ||||||||||||||||||||||||||||||||
Secondary structure | |||||||||||||||||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||||||||||||||||
| Beta strand | 1274 – 1283 | 10 | |||||||||||||||||||||||||||||||||
| Beta strand | 1285 – 1288 | 4 | |||||||||||||||||||||||||||||||||
| Helix | 1290 – 1304 | 15 | |||||||||||||||||||||||||||||||||
| Beta strand | 1311 – 1329 | 19 | |||||||||||||||||||||||||||||||||
| Helix | 1337 – 1345 | 9 | |||||||||||||||||||||||||||||||||
| Helix | 1357 – 1366 | 10 | |||||||||||||||||||||||||||||||||
| Turn | 1367 – 1369 | 3 | |||||||||||||||||||||||||||||||||
| Beta strand | 1377 – 1385 | 9 | |||||||||||||||||||||||||||||||||
| Helix | 1391 – 1394 | 4 | |||||||||||||||||||||||||||||||||
| Helix | 1397 – 1406 | 10 | |||||||||||||||||||||||||||||||||
| Beta strand | 1409 – 1420 | 12 | |||||||||||||||||||||||||||||||||
| Helix | 1422 – 1430 | 9 | |||||||||||||||||||||||||||||||||
| Beta strand | 1438 – 1442 | 5 | |||||||||||||||||||||||||||||||||
| Helix | 1443 – 1458 | 16 | |||||||||||||||||||||||||||||||||
Sequences
| ||||||||||||||||||||||||
References
| « Hide 'large scale' references | |
| [1] | "Cloning of full-length murine von Willebrand factor cDNA." Chitta M.S., Duhe R.J., Kermode J.C. Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Strain: C57BL/6. Tissue: Lung. |
| [2] | "Murine von Willebrand factor." Lenting P.J., Westein E., de Groot P.G., Denis C.V. Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Strain: BALB/c. |
| [3] | "The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. Hayashizaki Y.Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Strain: C57BL/6J. Tissue: Hippocampus. |
| [4] | "Variance of molecular datings, evolution of rodents and the phylogenetic affinities between Ctenodactylidae and Hystricognathi." Huchon D., Catzeflis F.M., Douzery E.J.P. Proc. R. Soc. B 267:393-402(2000) [PubMed: 10722222] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1238-1658 (ISOFORM 1). |
| [5] | "von Willebrand disease in the RIIIS/J mouse is caused by a defect outside of the von Willebrand factor gene." Nichols W.C., Cooney K.A., Mohlke K.L., Ballew J.D., Yang A., Bruck M.E., Reddington M., Novak E.K., Swank R.T., Ginsburg D. Blood 83:3225-3231(1994) [PubMed: 8193357] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1298-1684 (ISOFORM 1). Strain: BALB/c. |
| [6] | Erratum Nichols W.C., Cooney K.A., Mohlke K.L., Ballew J.D., Yang A., Bruck M.E., Reddington M., Novak E.K., Swank R.T., Ginsburg D. Blood 86:2461-2461(1995) [PubMed: 7662996] [Abstract] |
| [7] | "An experimental model to study the in vivo survival of von Willebrand factor. Basic aspects and application to the R1205H mutation." Lenting P.J., Westein E., Terraube V., Ribba A.-S., Huizinga E.G., Meyer D., de Groot P.G., Denis C.V. J. Biol. Chem. 279:12102-12109(2004) [PubMed: 14613933] [Abstract] Cited for: MUTAGENESIS OF ARG-1205, TISSUE SPECIFICITY. Strain: C57BL/6J. |
| [8] | "von Willebrand factor, platelets and endothelial cell interactions." Ruggeri Z.M. J. Thromb. Haemost. 1:1335-1342(2003) [PubMed: 12871266] [Abstract] Cited for: REVIEW. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | AY208897 mRNA. Translation: AAP41950.1. AY162409 mRNA. Translation: AAN73055.1. AF539800 mRNA. Translation: AAN07781.2. AK083237 mRNA. Translation: BAC38822.1. Different initiation. AJ238390 Genomic DNA. Translation: CAB86200.1. U27810 Genomic DNA. Translation: AAA82929.1. | ||||||||||||
| IPI | IPI00798576. IPI00830789. | ||||||||||||
| RefSeq | NP_035838.3. | ||||||||||||
| UniGene | Mm.22339 | ||||||||||||
3D structure databases | |||||||||||||
| PDBe RCSB PDB PDBj |
| ||||||||||||
| SMR | Q8CIZ8. Positions 293-361, 650-719, 1684-1873. | ||||||||||||
| ModBase | Search... | ||||||||||||
Protein-protein interaction databases | |||||||||||||
| STRING | Q8CIZ8. | ||||||||||||
Protein family/group databases | |||||||||||||
| MEROPS | I08.950. I08.954. | ||||||||||||
PTM databases | |||||||||||||
| PhosphoSite | Q8CIZ8. | ||||||||||||
Proteomic databases | |||||||||||||
| PRIDE | Q8CIZ8. | ||||||||||||
Genome annotation databases | |||||||||||||
| Ensembl | ENSMUST00000001995; ENSMUSP00000001995; ENSMUSG00000001930; Mus musculus. [Genome view] ENSMUST00000112254; ENSMUSP00000107873; ENSMUSG00000001930; Mus musculus. [Genome view] ENSMUST00000112262; ENSMUSP00000107881; ENSMUSG00000001930; Mus musculus. [Genome view] | ||||||||||||
| GeneID | 22371. | ||||||||||||
| KEGG | mmu:22371. | ||||||||||||
Organism-specific databases | |||||||||||||
| CTD | 22371. | ||||||||||||
| MGI | MGI:98941. Vwf. | ||||||||||||
Phylogenomic databases | |||||||||||||
| HOGENOM | HBG444837. | ||||||||||||
| HOVERGEN | Q8CIZ8. | ||||||||||||
| InParanoid | Q8CIZ8. | ||||||||||||
Gene expression databases | |||||||||||||
| ArrayExpress | Q8CIZ8. | ||||||||||||
| Bgee | Q8CIZ8. | ||||||||||||
| CleanEx | MM_VWF. | ||||||||||||
| Genevestigator | Q8CIZ8. | ||||||||||||
| GermOnline | ENSMUSG00000001930. Mus musculus. | ||||||||||||
Family and domain databases | |||||||||||||
| InterPro | IPR014853. Conserved-cysteine-rich_domain. IPR006207. Cys_knot_C. IPR002919. Prot_Inh_CR_TIL. IPR018453. Prot_Inh_CR_TIL_sg. IPR001846. von_Willebrand_fac_D. IPR012011. VWF. IPR002035. VWF_A. IPR001007. VWF_C. [Graphical view] | ||||||||||||
| Pfam | PF08742. C8. 4 hits. PF01826. TIL. 5 hits. PF00092. VWA. 3 hits. PF00093. VWC. 2 hits. PF00094. VWD. 4 hits. [Graphical view] | ||||||||||||
| PIRSF | PIRSF002495. VWF. 1 hit. | ||||||||||||
| SMART | SM00832. C8. 4 hits. SM00041. CT. 1 hit. SM00327. VWA. 3 hits. SM00214. VWC. 5 hits. SM00216. VWD. 4 hits. [Graphical view] | ||||||||||||
| PROSITE | PS01185. CTCK_1. 1 hit. PS01225. CTCK_2. 1 hit. PS50234. VWFA. 3 hits. PS01208. VWFC_1. 3 hits. PS50184. VWFC_2. 3 hits. PS51233. VWFD. 4 hits. [Graphical view] | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Other Resources | |||||||||||||
| NextBio | 302707. | ||||||||||||
| SOURCE | Search... | ||||||||||||
Entry information
| Entry name | VWF_MOUSE | ||||||||
| Accession | Primary (citable) accession number: Q8CIZ8 Secondary accession number(s): Q60863 Q9JK16 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
Relevant documents
| MGD cross-references Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with


