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O88783

- FA5_MOUSE

UniProt

O88783 - FA5_MOUSE

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Protein

Coagulation factor V

Gene
F5
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Central regulator of hemostasis. It serves as a critical cofactor for the prothrombinase activity of factor Xa that results in the activation of prothrombin to thrombin.

Enzyme regulationi

Inhibited by SERPINA5 By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi138 – 1381Calcium By similarity
Metal bindingi139 – 1391Calcium By similarity
Sitei333 – 3342Cleavage; by activated protein C By similarity
Sitei532 – 5332Cleavage; by activated protein C By similarity
Sitei706 – 7072Cleavage; by activated protein C By similarity
Sitei736 – 7372Cleavage; by thrombin By similarity
Sitei1004 – 10052Cleavage; by activated protein C By similarity
Sitei1029 – 10302Cleavage; by thrombin By similarity
Sitei1533 – 15342Cleavage; by thrombin By similarity
Metal bindingi1802 – 18021Copper By similarity
Metal bindingi1804 – 18041Copper By similarity

GO - Molecular functioni

  1. copper ion binding Source: InterPro
  2. serine-type endopeptidase activity Source: Ensembl

GO - Biological processi

  1. blood circulation Source: MGI
  2. blood coagulation Source: MGI
  3. cell adhesion Source: InterPro
Complete GO annotation...

Keywords - Biological processi

Blood coagulation, Hemostasis

Keywords - Ligandi

Calcium, Copper, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Coagulation factor V
Alternative name(s):
Activated protein C cofactor
Cleaved into the following 2 chains:
Gene namesi
Name:F5
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 1

Organism-specific databases

MGIiMGI:88382. F5.

Subcellular locationi

Secreted By similarity

GO - Cellular componenti

  1. extracellular space Source: MGI
  2. platelet alpha granule Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi333 – 3331R → Q: Does not affect pro-coagulant function. Partially resistant to inactivation by activated protein C. 1 Publication
Mutagenesisi532 – 5321R → Q: Does not affect pro-coagulant function. Partially resistant to inactivation by activated protein C. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919 Reviewed predictionAdd
BLAST
Chaini20 – 21832164Coagulation factor VPRO_0000358718Add
BLAST
Chaini20 – 736717Coagulation factor V heavy chain By similarityPRO_0000358719Add
BLAST
Propeptidei737 – 1533797Activation peptide (connecting region) By similarityPRO_0000358720Add
BLAST
Chaini1534 – 2183650Coagulation factor V light chain By similarityPRO_0000358721Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi176 – 1761N-linked (GlcNAc...) Reviewed prediction
Glycosylationi238 – 2381N-linked (GlcNAc...) Reviewed prediction
Glycosylationi381 – 3811N-linked (GlcNAc...) Reviewed prediction
Modified residuei638 – 6381Phosphothreonine By similarity
Modified residuei692 – 6921Sulfotyrosine Reviewed prediction
Modified residuei725 – 7251Sulfotyrosine Reviewed prediction
Glycosylationi841 – 8411N-linked (GlcNAc...)1 Publication
Glycosylationi959 – 9591N-linked (GlcNAc...) Reviewed prediction
Glycosylationi972 – 9721N-linked (GlcNAc...) Reviewed prediction
Glycosylationi1438 – 14381N-linked (GlcNAc...) Reviewed prediction
Glycosylationi1811 – 18111N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi1866 ↔ 2020 By similarity
Disulfide bondi2025 ↔ 2180 By similarity

Post-translational modificationi

Thrombin activates factor V proteolytically to the active cofactor, factor Va (formation of a heavy chain at the N-terminus and a light chain at the C-terminus) By similarity.
Sulfation is required for efficient thrombin cleavage and activation and for full procoagulant activity By similarity.
Activated protein C inactivates factor V and factor Va by proteolytic degradation By similarity.

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Sulfation, Zymogen

Proteomic databases

PaxDbiO88783.
PRIDEiO88783.

PTM databases

PhosphoSiteiO88783.

Expressioni

Gene expression databases

ArrayExpressiO88783.
BgeeiO88783.
GenevestigatoriO88783.

Interactioni

Subunit structurei

Factor Va, the activated form of factor V, is composed of a heavy chain and a light chain, non-covalently bound. The interaction between the two chains is calcium-dependent. Forms heterodimer with SERPINA5 By similarity.

Protein-protein interaction databases

IntActiO88783. 1 interaction.
MINTiMINT-4105665.

Structurei

3D structure databases

ProteinModelPortaliO88783.
SMRiO88783. Positions 29-679, 1537-2183.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini30 – 328299F5/8 type A 1Add
BLAST
Domaini30 – 192163Plastocyanin-like 1Add
BLAST
Domaini202 – 328127Plastocyanin-like 2Add
BLAST
Domaini347 – 682336F5/8 type A 2Add
BLAST
Domaini347 – 524178Plastocyanin-like 3Add
BLAST
Domaini534 – 682149Plastocyanin-like 4Add
BLAST
Repeati892 – 911201-1Add
BLAST
Repeati1175 – 118392-1
Repeati1184 – 119292-2
Repeati1193 – 120192-3
Repeati1202 – 121092-4
Repeati1211 – 121992-5
Repeati1220 – 122892-6
Repeati1229 – 123792-7
Repeati1238 – 124692-8
Repeati1247 – 125592-9
Repeati1256 – 126492-10
Repeati1265 – 127392-11
Repeati1274 – 128292-12
Repeati1283 – 129192-13
Repeati1292 – 129982-14
Repeati1300 – 130892-15
Repeati1309 – 131682-16
Repeati1317 – 132592-17
Repeati1326 – 133492-18
Repeati1335 – 134172-19
Repeati1342 – 135092-20
Repeati1351 – 135992-21
Repeati1360 – 136892-22
Repeati1369 – 137792-23
Repeati1378 – 138692-24
Repeati1387 – 139592-25
Repeati1396 – 140492-26
Repeati1405 – 141392-27
Repeati1414 – 142292-28
Repeati1423 – 143192-29
Repeati1432 – 144092-30
Repeati1441 – 144992-31
Repeati1452 – 1461102-32
Domaini1538 – 1866329F5/8 type A 3Add
BLAST
Domaini1538 – 1711174Plastocyanin-like 5Add
BLAST
Domaini1721 – 1866146Plastocyanin-like 6Add
BLAST
Domaini1866 – 2020155F5/8 type C 1Add
BLAST
Domaini2025 – 2180156F5/8 type C 2Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni691 – 1533843B By similarityAdd
BLAST
Regioni892 – 908171 X 17 AA tandem repeatsAdd
BLAST
Regioni1175 – 146128732 X 9 AA approximate tandem repeats of [TNP]-L-S-P-D-L-S-Q-TAdd
BLAST

Domaini

Domain B contains 32 X 9 AA tandem repeats, and 1 X 17 AA repeats.

Sequence similaritiesi

Contains 3 F5/8 type A domains.
Contains 2 F5/8 type C domains.

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiNOG240444.
GeneTreeiENSGT00740000114988.
HOGENOMiHOG000082542.
HOVERGENiHBG005631.
InParanoidiQ3UV80.
KOiK03902.
OMAiPDLSHTT.
OrthoDBiEOG7ZWD1D.
PhylomeDBiO88783.
TreeFamiTF329807.

Family and domain databases

Gene3Di2.60.120.260. 2 hits.
2.60.40.420. 6 hits.
InterProiIPR000421. Coagulation_fac_5/8-C_type_dom.
IPR009271. Coagulation_factor_V_LSPD.
IPR011707. Cu-oxidase_3.
IPR002355. Cu_oxidase_Cu_BS.
IPR008972. Cupredoxin.
IPR008979. Galactose-bd-like.
[Graphical view]
PfamiPF07732. Cu-oxidase_3. 3 hits.
PF00754. F5_F8_type_C. 2 hits.
PF06049. LSPR. 22 hits.
[Graphical view]
SMARTiSM00231. FA58C. 2 hits.
[Graphical view]
SUPFAMiSSF49503. SSF49503. 6 hits.
SSF49785. SSF49785. 2 hits.
PROSITEiPS01285. FA58C_1. 2 hits.
PS01286. FA58C_2. 2 hits.
PS50022. FA58C_3. 2 hits.
PS00079. MULTICOPPER_OXIDASE1. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O88783-1 [UniParc]FASTAAdd to Basket

« Hide

MLLVCPCFFL LVVLGTRWAG WGSHQAEAAQ LRQFYVAAQG ILWNYHPEPT     50
DPSLNSIPSF KKIVYREYEQ YFKKEKPRSS NSGLLGPTLY AEVGDVIKVH 100
FRNKADKPLS IHPQGIKYSK FSEGASYADH TFPAERKDDA VAPGEEYTYE 150
WIVSEDSGPT PDDPPCLTHI YYSYENLTQD FNSGLIGPLL ICKKGTLTED 200
GTQKMFDKQH VLLFAVFDES KSRSQSPSLM YTINGFVNKT MPDITVCAHD 250
HVSWHLIGMS SGPELFSIHF NGQVLEQNQH KVSTVTLVSA TSTTANMTMS 300
PEGRWIVSSL IPKHYQAGMQ AYIDIKNCPK KTRSPKTLTR EQRRYMKRWE 350
YFIAAEEVIW NYAPVIPANM DKIYRSQHLD NFSNQIGKHY KKVIYRQYEE 400
ETFTKRTDNP SIKQSGILGP VIRAQVRDTL KIVFKNMASR PYSIYPHGVT 450
FSPYEDGINS SSTSGSHTTI RPVQPGETFT YKWNILEFDE PTENDAQCLT 500
RPYYSDVDVT RDIASGLIGL LLICKSRSLD QRGVQRVADI EQQAVFAVFD 550
ENKSWYIEDN INKFCENPDE VKRDDPKFYE SNIMSTINGY VPESISTLGF 600
CFDDTVQWHF CSVGTHDDIL TIHFTGHSFI YGRRHEDTLT LFPMRGESVT 650
VTMDNVGTWM LTTMNSNPKR RNLRLRFRDV KCNRDYDNED SYEIYEPPAP 700
TSMTTRRIHD SLENEFGIDN EDDDYQYLLA SSLGIRSFKN SSLNPEENEF 750
NLTALALENS SEFISPSTDR VVDSNSSRIL SKIINNNLKD FQRTLPGSGA 800
TVAGTLLRNL IGLDENFVLN SSTEHRSSSY HENDMENPQS NITMVYLLPL 850
GPKGSGNREQ DKPKTIKTGR PHMMKHRFSW MKAPAGKTGR HSNPKNSYSG 900
MKSEEDIPSE LIPLKQKITS KFLNRRWRVA SEKGSYEIIA ANGEDTDVDK 950
LTNSPQNQNI TVPRGESTSH TNTTRKPSDL PTFSGVGHKS PHVRQEEENS 1000
GFQKRQLFIR TRKKKKNKKL ALHSPLSPRG FDPLRGHNHS PFPDRRLLNH 1050
SLLLHKSNET ALSPDLNQTS PSMSTDRSLP DYNQYSKNDT EQMSSSLDLY 1100
QSVPAEEHSP TFPAQDPDQT HSTTDPSYRS SPPELSQGLD YDLSHDFYPD 1150
DIGLTSFFPD QSQKSSFSSD DDQAIPSSDL SLFTISPELD QTIIYPDLDQ 1200
LLLSPEDNQK TSSPDLGQVP LSPDDNQKTS SPDLGQVSLS PDDNQKTSSP 1250
DLGQVPLSLD DNQKTTSPDL GQVPLSPDDN QMITSPDLGQ VPLSSDNQKT 1300
SSPDLGQVPL FPEDNQNYFL DLSQVPLSSD QNQETSSTDL LTLSPDFGQT 1350
VLSPDLDQLP LPSDNSQVTV SPDLSLLTLS PDFNEIILAP DLGQVTLSPD 1400
LIQTNPALNH GHKASSADPD QASYPPDSGQ ASSLPELNRT LPHPDLTHIP 1450
PPSPSPTLNN TSLSRKFNPL VVVGLSRVDG DDVEIVPSEE PERIDEDYAE 1500
DDFVTYNDPY RTDTRTDVNS SRNPDTIAAW YLRGHGGHKK FYYIAAEEIT 1550
WNYAEFAQSE MDHEDTGHTP KDTTYKKVVF RKYLDSTFTS RDPRAEYEEH 1600
LGILGPVIRA EVDDVIQVRF KNLASRPYSL HAHGLSYEKS SEGKTYEDES 1650
PEWFQEDDAV QPNSSYTYVW HATKRSGPEN PGSACRAWAY YSAVNVERDI 1700
HSGLIGPLLI CRKGTLHMER NLPMDMREFV LLFMVFDEKK SWYYEKSKGS 1750
RRIESPEEKN AHKFYAINGM IYNLPGLRMY EQEWVRLHLL NMGGSRDIHV 1800
VHFHGQTLLD NRTKQHQLGV WPLLPGSFKT LEMKASKPGW WLLDTEVGEN 1850
QVAGMQTPFL IIDKECKMPM GLSTGVISDS QIKASEYLTY WEPRLARLNN 1900
AGSYNAWSIE KTALDFPIKP WIQVDMQKEV VVTGIQTQGA KHYLKSCFTT 1950
EFQVAYSSDQ TNWQIFRGKS GKSVMYFTGN SDGSTIKENR LDPPIVARYI 2000
RIHPTKSYNR PTLRLELQGC EVNGCSTPLG LEDGRIQDKQ ITASSFKKSW 2050
WGDYWEPSLA RLNAQGRVNA WQAKANNNKQ WLQVDLLKIK KVTAIVTQGC 2100
KSLSSEMYVK SYSIQYSDQG VAWKPYRQKS SMVDKIFEGN SNTKGHMKNF 2150
FNPPIISRFI RIIPKTWNQS IALRLELFGC DIY 2183
Length:2,183
Mass (Da):247,230
Last modified:November 1, 1998 - v1
Checksum:iBF0A8AA723F60317
GO

Sequence cautioni

The sequence BAE23393.1 differs from that shown. Reason: Erroneous initiation.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U52925 mRNA. Translation: AAC99553.1.
AK137521 mRNA. Translation: BAE23393.1. Different initiation.
AK139240 mRNA. Translation: BAE23928.1.
CCDSiCCDS35754.1.
PIRiT42764.
RefSeqiNP_032002.1. NM_007976.2.
UniGeneiMm.12900.

Genome annotation databases

EnsembliENSMUST00000086040; ENSMUSP00000083204; ENSMUSG00000026579.
GeneIDi14067.
KEGGimmu:14067.
UCSCiuc007dic.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U52925 mRNA. Translation: AAC99553.1 .
AK137521 mRNA. Translation: BAE23393.1 . Different initiation.
AK139240 mRNA. Translation: BAE23928.1 .
CCDSi CCDS35754.1.
PIRi T42764.
RefSeqi NP_032002.1. NM_007976.2.
UniGenei Mm.12900.

3D structure databases

ProteinModelPortali O88783.
SMRi O88783. Positions 29-679, 1537-2183.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi O88783. 1 interaction.
MINTi MINT-4105665.

PTM databases

PhosphoSitei O88783.

Proteomic databases

PaxDbi O88783.
PRIDEi O88783.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000086040 ; ENSMUSP00000083204 ; ENSMUSG00000026579 .
GeneIDi 14067.
KEGGi mmu:14067.
UCSCi uc007dic.1. mouse.

Organism-specific databases

CTDi 2153.
MGIi MGI:88382. F5.

Phylogenomic databases

eggNOGi NOG240444.
GeneTreei ENSGT00740000114988.
HOGENOMi HOG000082542.
HOVERGENi HBG005631.
InParanoidi Q3UV80.
KOi K03902.
OMAi PDLSHTT.
OrthoDBi EOG7ZWD1D.
PhylomeDBi O88783.
TreeFami TF329807.

Miscellaneous databases

ChiTaRSi F5. mouse.
NextBioi 285052.
PROi O88783.
SOURCEi Search...

Gene expression databases

ArrayExpressi O88783.
Bgeei O88783.
Genevestigatori O88783.

Family and domain databases

Gene3Di 2.60.120.260. 2 hits.
2.60.40.420. 6 hits.
InterProi IPR000421. Coagulation_fac_5/8-C_type_dom.
IPR009271. Coagulation_factor_V_LSPD.
IPR011707. Cu-oxidase_3.
IPR002355. Cu_oxidase_Cu_BS.
IPR008972. Cupredoxin.
IPR008979. Galactose-bd-like.
[Graphical view ]
Pfami PF07732. Cu-oxidase_3. 3 hits.
PF00754. F5_F8_type_C. 2 hits.
PF06049. LSPR. 22 hits.
[Graphical view ]
SMARTi SM00231. FA58C. 2 hits.
[Graphical view ]
SUPFAMi SSF49503. SSF49503. 6 hits.
SSF49785. SSF49785. 2 hits.
PROSITEi PS01285. FA58C_1. 2 hits.
PS01286. FA58C_2. 2 hits.
PS50022. FA58C_3. 2 hits.
PS00079. MULTICOPPER_OXIDASE1. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The structure and function of murine factor V and its inactivation by protein C."
    Yang T.L., Cui J., Rehumtulla A., Yang A., Moussalli M., Kaufman R.J., Ginsburg D.
    Blood 91:4593-4599(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], CLEAVAGE BY ACTIVATED PROTEIN C, MUTAGENESIS OF ARG-333 AND ARG-532.
    Strain: C57BL/6J.
    Tissue: Bone marrow.
  2. "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.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1012.
    Strain: C57BL/6J.
    Tissue: Bone, Cerebellum and Olfactory bulb.
  3. "Proteome-wide characterization of N-glycosylation events by diagonal chromatography."
    Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J., Gevaert K.
    J. Proteome Res. 5:2438-2447(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-841.
    Strain: C57BL/6.
    Tissue: Plasma.

Entry informationi

Entry nameiFA5_MOUSE
AccessioniPrimary (citable) accession number: O88783
Secondary accession number(s): Q3UTQ2, Q3UV80
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: November 1, 1998
Last modified: July 9, 2014
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi