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Q62009

- POSTN_MOUSE

UniProt

Q62009 - POSTN_MOUSE

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Protein

Periostin

Gene

Postn

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

Functioni

Induces cell attachment and spreading and plays a role in cell adhesion. May play a role in extracellular matrix mineralization. Enhances incorporation of BMP1 in the fibronectin matrix of connective tissues, and subsequent proteolytic activation of lysyl oxidase LOX.2 Publications

GO - Molecular functioni

  1. heparin binding Source: UniProtKB

GO - Biological processi

  1. cell adhesion Source: UniProtKB
  2. extracellular matrix organization Source: MGI
  3. regulation of Notch signaling pathway Source: MGI
  4. tissue development Source: MGI
Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Keywords - Ligandi

Heparin-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Periostin
Short name:
PN
Alternative name(s):
Osteoblast-specific factor 2
Short name:
OSF-2
Gene namesi
Name:Postn
Synonyms:Osf2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 3

Organism-specific databases

MGIiMGI:1926321. Postn.

Subcellular locationi

Golgi apparatus. Secretedextracellular spaceextracellular matrix
Note: Colocalizes with BMP1 in the Golgi.

GO - Cellular componenti

  1. proteinaceous extracellular matrix Source: UniProtKB
  2. trans-Golgi network Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Golgi apparatus, Secreted

Pathology & Biotechi

Disruption phenotypei

Reduced amount of collagen cross-linking in femur and periosteum.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323Sequence AnalysisAdd
BLAST
Chaini24 – 838815PeriostinPRO_0000008790Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi46 ↔ 82PROSITE-ProRule annotation
Disulfide bondi62 ↔ 71PROSITE-ProRule annotation
Disulfide bondi81 ↔ 94PROSITE-ProRule annotation
Modified residuei126 – 12614-carboxyglutamateSequence Analysis
Modified residuei127 – 12714-carboxyglutamateSequence Analysis
Modified residuei129 – 12914-carboxyglutamateSequence Analysis
Modified residuei142 – 14214-carboxyglutamateSequence Analysis
Modified residuei156 – 15614-carboxyglutamateSequence Analysis
Modified residuei162 – 16214-carboxyglutamateSequence Analysis
Modified residuei244 – 24414-carboxyglutamateSequence Analysis
Modified residuei246 – 24614-carboxyglutamateSequence Analysis
Modified residuei263 – 26314-carboxyglutamateSequence Analysis
Modified residuei279 – 27914-carboxyglutamateSequence Analysis
Modified residuei282 – 28214-carboxyglutamateSequence Analysis
Modified residuei290 – 29014-carboxyglutamateSequence Analysis
Modified residuei300 – 30014-carboxyglutamateSequence Analysis
Modified residuei315 – 31514-carboxyglutamateSequence Analysis
Modified residuei324 – 32414-carboxyglutamateSequence Analysis
Modified residuei327 – 32714-carboxyglutamateSequence Analysis
Modified residuei498 – 49814-carboxyglutamateSequence Analysis
Modified residuei519 – 51914-carboxyglutamateSequence Analysis
Modified residuei549 – 54914-carboxyglutamateSequence Analysis
Modified residuei550 – 55014-carboxyglutamateSequence Analysis
Modified residuei552 – 55214-carboxyglutamateSequence Analysis
Modified residuei580 – 58014-carboxyglutamateSequence Analysis
Glycosylationi601 – 6011N-linked (GlcNAc...)1 Publication

Post-translational modificationi

Gamma-carboxyglutamate residues are formed by vitamin K dependent carboxylation. These residues are essential for the binding of calcium.1 Publication

Keywords - PTMi

Disulfide bond, Gamma-carboxyglutamic acid, Glycoprotein

Proteomic databases

MaxQBiQ62009.
PaxDbiQ62009.
PRIDEiQ62009.

PTM databases

PhosphoSiteiQ62009.

Expressioni

Tissue specificityi

Preferentially expressed in periosteum and periodontal ligament. Also expressed in the developing and adult heart.2 Publications

Developmental stagei

In the heart, expressed from embryonic day 10.5. Continues to be strongly expressed throughout cardiac development and into adulthood.1 Publication

Inductioni

By TGF-beta.1 Publication

Gene expression databases

BgeeiQ62009.
CleanExiMM_POSTN.
GenevestigatoriQ62009.

Interactioni

Subunit structurei

Interacts with BMP1 and fibronectin.1 Publication

Protein-protein interaction databases

IntActiQ62009. 1 interaction.
MINTiMINT-4108229.

Structurei

3D structure databases

ProteinModelPortaliQ62009.
SMRiQ62009. Positions 124-238, 241-369, 500-632.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini42 – 9655EMIPROSITE-ProRule annotationAdd
BLAST
Domaini99 – 232134FAS1 1CuratedPROSITE-ProRule annotationAdd
BLAST
Domaini236 – 367132FAS1 2CuratedPROSITE-ProRule annotationAdd
BLAST
Domaini370 – 494125FAS1 3CuratedPROSITE-ProRule annotationAdd
BLAST
Domaini498 – 630133FAS1 4CuratedPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 EMI domain.PROSITE-ProRule annotation
Contains 4 FAS1 domains.CuratedPROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiCOG2335.
GeneTreeiENSGT00530000063860.
HOGENOMiHOG000220865.
HOVERGENiHBG000715.
InParanoidiQ62009.
OMAiHGEPIIK.
OrthoDBiEOG7N8ZV1.
PhylomeDBiQ62009.
TreeFamiTF316269.

Family and domain databases

Gene3Di2.30.180.10. 4 hits.
InterProiIPR011489. EMI_domain.
IPR000782. FAS1_domain.
IPR016666. TGFb-ind_bIGH3/osteoblast_fac2.
[Graphical view]
PfamiPF02469. Fasciclin. 4 hits.
[Graphical view]
PIRSFiPIRSF016553. BIGH3_OSF2. 1 hit.
SMARTiSM00554. FAS1. 4 hits.
[Graphical view]
SUPFAMiSSF82153. SSF82153. 4 hits.
PROSITEiPS51041. EMI. 1 hit.
PS50213. FAS1. 4 hits.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

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

This entry describes 5 isoformsi produced by alternative splicing. Align

Isoform 11 Publication (identifier: Q62009-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MVPLLPLYAL LLLFLCDINP ANANSYYDKV LAHSRIRGRD QGPNVCALQQ
60 70 80 90 100
ILGTKKKYFS SCKNWYQGAI CGKKTTVLYE CCPGYMRMEG MKGCPAVMPI
110 120 130 140 150
DHVYGTLGIV GATTTQHYSD VSKLREEIEG KGSYTYFAPS NEAWENLDSD
160 170 180 190 200
IRRGLENNVN VELLNALHSH MVNKRMLTKD LKHGMVIPSM YNNLGLFINH
210 220 230 240 250
YPNGVVTVNC ARVIHGNQIA TNGVVHVIDR VLTQIGTSIQ DFLEAEDDLS
260 270 280 290 300
SFRAAAITSD LLESLGRDGH FTLFAPTNEA FEKLPRGVLE RIMGDKVASE
310 320 330 340 350
ALMKYHILNT LQCSEAITGG AVFETMEGNT IEIGCEGDSI SINGIKMVNK
360 370 380 390 400
KDIVTKNGVI HLIDEVLIPD SAKQVIELAG KQQTTFTDLV AQLGLASSLK
410 420 430 440 450
PDGEYTLLAP VNNAFSDDTL SMDQRLLKLI LQNHILKVKV GLSDLYNGQI
460 470 480 490 500
LETIGGKQLR VFVYRTAICI ENSCMVRGSK QGRNGAIHIF REIIQPAEKS
510 520 530 540 550
LHDKLRQDKR FSIFLSLLEA ADLKDLLTQP GDWTLFAPTN DAFKGMTSEE
560 570 580 590 600
RELLIGDKNA LQNIILYHLT PGVYIGKGFE PGVTNILKTT QGSKIYLKGV
610 620 630 640 650
NETLLVNELK SKESDIMTTN GVIHVVDKLL YPADIPVGND QLLELLNKLI
660 670 680 690 700
KYIQIKFVRG STFKEIPMTV YTTKIITKVV EPKIKVIQGS LQPIIKTEGP
710 720 730 740 750
AMTKIQIEGD PDFRLIKEGE TVTEVIHGEP VIKKYTKIID GVPVEITEKQ
760 770 780 790 800
TREERIITGP EIKYTRISTG GGETGETLQK FLQKEVSKVT KFIEGGDGHL
810 820 830
FEDEEIKRLL QGDTPAKKIP ANKRVQGPRR RSREGRSQ
Length:838
Mass (Da):93,144
Last modified:February 2, 2004 - v2
Checksum:i907FEB37942EADEC
GO
Isoform 21 Publication (identifier: Q62009-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     672-699: TTKIITKVVEPKIKVIQGSLQPIIKTEG → R

Show »
Length:811
Mass (Da):90,255
Checksum:iDA5CE8F8B9380234
GO
Isoform 31 Publication (identifier: Q62009-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     785-812: Missing.

Show »
Length:810
Mass (Da):89,987
Checksum:i7CF602BDD3BAB995
GO
Isoform 41 Publication (identifier: Q62009-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     759-812: Missing.

Show »
Length:784
Mass (Da):87,166
Checksum:i915027B89E47A6C3
GO
Isoform 5Curated (identifier: Q62009-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     672-699: TTKIITKVVEPKIKVIQGSLQPIIKTEG → R
     785-812: Missing.

Note: No experimental confirmation available.Curated

Show »
Length:783
Mass (Da):87,099
Checksum:i24B93AB348C9A7FE
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti346 – 3461K → R in BAC27122. (PubMed:16141072)Curated
Sequence conflicti541 – 5411D → N in BAC27122. (PubMed:16141072)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei672 – 69928TTKII…IKTEG → R in isoform 2 and isoform 5. 3 PublicationsVSP_050666Add
BLAST
Alternative sequencei759 – 81254Missing in isoform 4. 1 PublicationVSP_050667Add
BLAST
Alternative sequencei785 – 81228Missing in isoform 3 and isoform 5. 3 PublicationsVSP_050668Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D13664 mRNA. Translation: BAA02835.1.
AK030756 mRNA. Translation: BAC27122.1.
BC031449 mRNA. Translation: AAH31449.1.
CCDSiCCDS17351.1. [Q62009-2]
CCDS57211.1. [Q62009-3]
CCDS57212.1. [Q62009-5]
PIRiS36109.
RefSeqiNP_001185694.1. NM_001198765.1. [Q62009-3]
NP_001185695.1. NM_001198766.1. [Q62009-5]
NP_056599.1. NM_015784.3. [Q62009-2]
XP_006501716.1. XM_006501653.1. [Q62009-1]
XP_006501717.1. XM_006501654.1. [Q62009-4]
UniGeneiMm.236067.

Genome annotation databases

EnsembliENSMUST00000073012; ENSMUSP00000072773; ENSMUSG00000027750. [Q62009-2]
ENSMUST00000081564; ENSMUSP00000080276; ENSMUSG00000027750. [Q62009-1]
ENSMUST00000107985; ENSMUSP00000103619; ENSMUSG00000027750. [Q62009-3]
ENSMUST00000117373; ENSMUSP00000112735; ENSMUSG00000027750. [Q62009-5]
GeneIDi50706.
KEGGimmu:50706.
UCSCiuc008pfh.2. mouse. [Q62009-2]
uc008pfi.2. mouse. [Q62009-3]
uc008pfj.2. mouse. [Q62009-5]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D13664 mRNA. Translation: BAA02835.1 .
AK030756 mRNA. Translation: BAC27122.1 .
BC031449 mRNA. Translation: AAH31449.1 .
CCDSi CCDS17351.1. [Q62009-2 ]
CCDS57211.1. [Q62009-3 ]
CCDS57212.1. [Q62009-5 ]
PIRi S36109.
RefSeqi NP_001185694.1. NM_001198765.1. [Q62009-3 ]
NP_001185695.1. NM_001198766.1. [Q62009-5 ]
NP_056599.1. NM_015784.3. [Q62009-2 ]
XP_006501716.1. XM_006501653.1. [Q62009-1 ]
XP_006501717.1. XM_006501654.1. [Q62009-4 ]
UniGenei Mm.236067.

3D structure databases

ProteinModelPortali Q62009.
SMRi Q62009. Positions 124-238, 241-369, 500-632.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q62009. 1 interaction.
MINTi MINT-4108229.

PTM databases

PhosphoSitei Q62009.

Proteomic databases

MaxQBi Q62009.
PaxDbi Q62009.
PRIDEi Q62009.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000073012 ; ENSMUSP00000072773 ; ENSMUSG00000027750 . [Q62009-2 ]
ENSMUST00000081564 ; ENSMUSP00000080276 ; ENSMUSG00000027750 . [Q62009-1 ]
ENSMUST00000107985 ; ENSMUSP00000103619 ; ENSMUSG00000027750 . [Q62009-3 ]
ENSMUST00000117373 ; ENSMUSP00000112735 ; ENSMUSG00000027750 . [Q62009-5 ]
GeneIDi 50706.
KEGGi mmu:50706.
UCSCi uc008pfh.2. mouse. [Q62009-2 ]
uc008pfi.2. mouse. [Q62009-3 ]
uc008pfj.2. mouse. [Q62009-5 ]

Organism-specific databases

CTDi 10631.
MGIi MGI:1926321. Postn.

Phylogenomic databases

eggNOGi COG2335.
GeneTreei ENSGT00530000063860.
HOGENOMi HOG000220865.
HOVERGENi HBG000715.
InParanoidi Q62009.
OMAi HGEPIIK.
OrthoDBi EOG7N8ZV1.
PhylomeDBi Q62009.
TreeFami TF316269.

Miscellaneous databases

NextBioi 307557.
PROi Q62009.
SOURCEi Search...

Gene expression databases

Bgeei Q62009.
CleanExi MM_POSTN.
Genevestigatori Q62009.

Family and domain databases

Gene3Di 2.30.180.10. 4 hits.
InterProi IPR011489. EMI_domain.
IPR000782. FAS1_domain.
IPR016666. TGFb-ind_bIGH3/osteoblast_fac2.
[Graphical view ]
Pfami PF02469. Fasciclin. 4 hits.
[Graphical view ]
PIRSFi PIRSF016553. BIGH3_OSF2. 1 hit.
SMARTi SM00554. FAS1. 4 hits.
[Graphical view ]
SUPFAMi SSF82153. SSF82153. 4 hits.
PROSITEi PS51041. EMI. 1 hit.
PS50213. FAS1. 4 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Osteoblast-specific factor 2: cloning of a putative bone adhesion protein with homology with the insect protein fasciclin I."
    Takeshita S., Kikuno R., Tezuka K., Amann E.
    Biochem. J. 294:271-278(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Strain: C57BL/61 Publication.
    Tissue: Calvaria1 Publication.
  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] (ISOFORM 3).
    Strain: C57BL/6J.
  3. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
    Tissue: Mammary glandImported.
  4. "Identification and characterization of a novel protein, periostin, with restricted expression to periosteum and periodontal ligament and increased expression by transforming growth factor beta."
    Horiuchi K., Amizuka N., Takeshita S., Takamatsu H., Katsuura M., Ozawa H., Toyama Y., Bonewald L.F., Kudo A.
    J. Bone Miner. Res. 14:1239-1249(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL NUCLEOTIDE SEQUENCE (ISOFORMS 1; 2; 3 AND 4), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION.
  5. "Expression and characterization of murine osteoblast-specific factor 2 (OSF-2) in a baculovirus expression system."
    Sugiura T., Takamatsu H., Kudo A., Amann E.
    Protein Expr. Purif. 6:305-311(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: HEPARIN-BINDING ACTIVITY, GLYCOSYLATION.
  6. "Periostin (an osteoblast-specific factor) is expressed within the embryonic mouse heart during valve formation."
    Kruzynska-Frejtag A., Machnicki M., Rogers R., Markwald R.R., Conway S.J.
    Mech. Dev. 103:183-188(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
  7. "Periostin, a member of a novel family of vitamin K-dependent proteins, is expressed by mesenchymal stromal cells."
    Coutu D.L., Wu J.H., Monette A., Rivard G.-E., Blostein M.D., Galipeau J.
    J. Biol. Chem. 283:17991-18001(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: GAMMA-CARBOXYGLUTAMATION.
  8. "Interaction between periostin and BMP-1 promotes proteolytic activation of lysyl oxidase."
    Maruhashi T., Kii I., Saito M., Kudo A.
    J. Biol. Chem. 285:13294-13303(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH BMP1 AND FIBRONECTIN, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiPOSTN_MOUSE
AccessioniPrimary (citable) accession number: Q62009
Secondary accession number(s): Q8BMJ6, Q8K1K0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 26, 2004
Last sequence update: February 2, 2004
Last modified: October 29, 2014
This is version 115 of the entry and version 2 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