Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

O88783

- FA5_MOUSE

UniProt

O88783 - FA5_MOUSE

Protein

Coagulation factor V

Gene

F5

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 98 (01 Oct 2014)
      Sequence version 1 (01 Nov 1998)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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 – 1381CalciumBy similarity
    Metal bindingi139 – 1391CalciumBy similarity
    Sitei333 – 3342Cleavage; by activated protein CBy similarity
    Sitei532 – 5332Cleavage; by activated protein CBy similarity
    Sitei706 – 7072Cleavage; by activated protein CBy similarity
    Sitei736 – 7372Cleavage; by thrombinBy similarity
    Sitei1004 – 10052Cleavage; by activated protein CBy similarity
    Sitei1029 – 10302Cleavage; by thrombinBy similarity
    Sitei1533 – 15342Cleavage; by thrombinBy similarity
    Metal bindingi1802 – 18021CopperBy similarity
    Metal bindingi1804 – 18041CopperBy 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

    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

    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 – 1919Sequence AnalysisAdd
    BLAST
    Chaini20 – 21832164Coagulation factor VPRO_0000358718Add
    BLAST
    Chaini20 – 736717Coagulation factor V heavy chainBy similarityPRO_0000358719Add
    BLAST
    Propeptidei737 – 1533797Activation peptide (connecting region)By similarityPRO_0000358720Add
    BLAST
    Chaini1534 – 2183650Coagulation factor V light chainBy similarityPRO_0000358721Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi176 – 1761N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi238 – 2381N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi381 – 3811N-linked (GlcNAc...)Sequence Analysis
    Modified residuei638 – 6381PhosphothreonineBy similarity
    Modified residuei692 – 6921SulfotyrosineSequence Analysis
    Modified residuei725 – 7251SulfotyrosineSequence Analysis
    Glycosylationi841 – 8411N-linked (GlcNAc...)1 Publication
    Glycosylationi959 – 9591N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi972 – 9721N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1438 – 14381N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1811 – 18111N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1866 ↔ 2020PROSITE-ProRule annotation
    Disulfide bondi2025 ↔ 2180PROSITE-ProRule annotation

    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.By similarity

    Protein-protein interaction databases

    IntActiO88783. 1 interaction.
    MINTiMINT-4105665.

    Structurei

    3D structure databases

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

    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 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini2025 – 2180156F5/8 type C 2PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni691 – 1533843BBy 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

    Belongs to the multicopper oxidase family.Curated
    Contains 3 F5/8 type A domains.Curated
    Contains 2 F5/8 type C domains.PROSITE-ProRule annotation
    Contains 6 plastocyanin-like domains.Curated

    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

    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: October 1, 2014
    This is version 98 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