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Protein

Serotransferrin

Gene

Tf

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

Functioni

Transferrins are iron binding transport proteins which can bind two Fe3+ ions in association with the binding of an anion, usually bicarbonate. It is responsible for the transport of iron from sites of absorption and heme degradation to those of storage and utilization. Serum transferrin may also have a further role in stimulating cell proliferation.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi82 – 821Iron 1PROSITE-ProRule annotation
Metal bindingi114 – 1141Iron 1PROSITE-ProRule annotation
Binding sitei139 – 1391Carbonate 1PROSITE-ProRule annotation
Binding sitei143 – 1431Carbonate 1PROSITE-ProRule annotation
Binding sitei145 – 1451Carbonate 1; via amide nitrogenPROSITE-ProRule annotation
Binding sitei146 – 1461Carbonate 1; via amide nitrogenPROSITE-ProRule annotation
Metal bindingi207 – 2071Iron 1PROSITE-ProRule annotation
Metal bindingi268 – 2681Iron 1PROSITE-ProRule annotation
Metal bindingi410 – 4101Iron 2PROSITE-ProRule annotation
Metal bindingi448 – 4481Iron 2PROSITE-ProRule annotation
Binding sitei474 – 4741Carbonate 2PROSITE-ProRule annotation
Binding sitei478 – 4781Carbonate 2PROSITE-ProRule annotation
Binding sitei480 – 4801Carbonate 2; via amide nitrogenPROSITE-ProRule annotation
Binding sitei481 – 4811Carbonate 2; via amide nitrogenPROSITE-ProRule annotation
Metal bindingi537 – 5371Iron 2PROSITE-ProRule annotation
Metal bindingi605 – 6051Iron 2PROSITE-ProRule annotation

GO - Molecular functioni

  1. ferric iron binding Source: InterPro

GO - Biological processi

  1. actin filament organization Source: DFLAT
  2. activation of JUN kinase activity Source: DFLAT
  3. cellular iron ion homeostasis Source: InterPro
  4. ERK1 and ERK2 cascade Source: DFLAT
  5. iron ion transport Source: MGI
  6. osteoclast differentiation Source: DFLAT
  7. positive regulation of bone resorption Source: DFLAT
  8. positive regulation of cell motility Source: DFLAT
  9. positive regulation of phosphorylation Source: DFLAT
  10. positive regulation of transcription, DNA-templated Source: DFLAT
  11. SMAD protein signal transduction Source: MGI
Complete GO annotation...

Keywords - Biological processi

Ion transport, Iron transport, Transport

Keywords - Ligandi

Iron, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_198515. Transferrin endocytosis and recycling.
REACT_205755. Iron uptake and transport.

Protein family/group databases

MEROPSiS60.977.

Names & Taxonomyi

Protein namesi
Recommended name:
Serotransferrin
Short name:
Transferrin
Alternative name(s):
Beta-1 metal-binding globulin
Siderophilin
Gene namesi
Name:Tf
Synonyms:Trf
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 9

Organism-specific databases

MGIiMGI:98821. Trf.

Subcellular locationi

GO - Cellular componenti

  1. apical plasma membrane Source: MGI
  2. basal part of cell Source: MGI
  3. basal plasma membrane Source: MGI
  4. blood microparticle Source: MGI
  5. cell surface Source: MGI
  6. coated pit Source: MGI
  7. cytoplasmic membrane-bounded vesicle Source: MGI
  8. dense body Source: MGI
  9. early endosome Source: MGI
  10. endocytic vesicle Source: MGI
  11. endosome Source: MGI
  12. extracellular space Source: MGI
  13. extracellular vesicular exosome Source: MGI
  14. late endosome Source: MGI
  15. perinuclear region of cytoplasm Source: MGI
  16. recycling endosome Source: MGI
  17. vesicle Source: MGI
  18. vesicle coat Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919By similarityAdd
BLAST
Chaini20 – 697678SerotransferrinPRO_0000035716Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi28 ↔ 67PROSITE-ProRule annotation
Disulfide bondi38 ↔ 58PROSITE-ProRule annotation
Modified residuei42 – 421Omega-N-methylated arginineBy similarity
Disulfide bondi137 ↔ 213PROSITE-ProRule annotation
Disulfide bondi156 ↔ 350PROSITE-ProRule annotation
Disulfide bondi177 ↔ 193PROSITE-ProRule annotation
Disulfide bondi180 ↔ 196PROSITE-ProRule annotation
Disulfide bondi190 ↔ 198PROSITE-ProRule annotation
Disulfide bondi246 ↔ 260PROSITE-ProRule annotation
Disulfide bondi363 ↔ 395PROSITE-ProRule annotation
Disulfide bondi373 ↔ 386PROSITE-ProRule annotation
Disulfide bondi420 ↔ 692PROSITE-ProRule annotation
Disulfide bondi435 ↔ 655PROSITE-ProRule annotation
Disulfide bondi472 ↔ 543PROSITE-ProRule annotation
Disulfide bondi496 ↔ 683PROSITE-ProRule annotation
Disulfide bondi506 ↔ 520PROSITE-ProRule annotation
Glycosylationi513 – 5131N-linked (GlcNAc...)1 Publication
Disulfide bondi517 ↔ 526PROSITE-ProRule annotation
Disulfide bondi583 ↔ 597PROSITE-ProRule annotation
Disulfide bondi633 ↔ 638PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Glycoprotein, Methylation

Proteomic databases

MaxQBiQ921I1.
PaxDbiQ921I1.
PRIDEiQ921I1.

2D gel databases

REPRODUCTION-2DPAGEIPI00139788.
Q921I1.

PTM databases

PhosphoSiteiQ921I1.

Expressioni

Tissue specificityi

Expressed by the liver and secreted in plasma.1 Publication

Gene expression databases

BgeeiQ921I1.
CleanExiMM_TRF.
ExpressionAtlasiQ921I1. baseline.
GenevestigatoriQ921I1.

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

BioGridi204313. 1 interaction.
IntActiQ921I1. 8 interactions.
MINTiMINT-1202663.

Structurei

3D structure databases

ProteinModelPortaliQ921I1.
SMRiQ921I1. Positions 20-694.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini25 – 347323Transferrin-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini360 – 682323Transferrin-like 2PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the transferrin family.PROSITE-ProRule annotation
Contains 2 transferrin-like domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiNOG87503.
GeneTreeiENSGT00390000001619.
HOVERGENiHBG000055.
InParanoidiQ921I1.
KOiK14736.
OrthoDBiEOG7D59N7.
PhylomeDBiQ921I1.
TreeFamiTF324013.

Family and domain databases

InterProiIPR016357. Transferrin.
IPR001156. Transferrin-like_dom.
IPR018195. Transferrin_Fe_BS.
[Graphical view]
PfamiPF00405. Transferrin. 2 hits.
[Graphical view]
PIRSFiPIRSF002549. Transferrin. 1 hit.
PRINTSiPR00422. TRANSFERRIN.
SMARTiSM00094. TR_FER. 2 hits.
[Graphical view]
PROSITEiPS00205. TRANSFERRIN_LIKE_1. 1 hit.
PS00206. TRANSFERRIN_LIKE_2. 2 hits.
PS00207. TRANSFERRIN_LIKE_3. 2 hits.
PS51408. TRANSFERRIN_LIKE_4. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q921I1-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MRLTVGALLA CAALGLCLAV PDKTVKWCAV SEHENTKCIS FRDHMKTVLP
60 70 80 90 100
PDGPRLACVK KTSYPDCIKA ISASEADAMT LDGGWVYDAG LTPNNLKPVA
110 120 130 140 150
AEFYGSVEHP QTYYYAVAVV KKGTDFQLNQ LEGKKSCHTG LGRSAGWVIP
160 170 180 190 200
IGLLFCKLSE PRSPLEKAVS SFFSGSCVPC ADPVAFPKLC QLCPGCGCSS
210 220 230 240 250
TQPFFGYVGA FKCLKDGGGD VAFVKHTTIF EVLPEKADRD QYELLCLDNT
260 270 280 290 300
RKPVDQYEDC YLARIPSHAV VARKNNGKED LIWEILKVAQ EHFGKGKSKD
310 320 330 340 350
FQLFSSPLGK DLLFKDSAFG LLRVPPRMDY RLYLGHNYVT AIRNQQEGVC
360 370 380 390 400
PEGSIDNSPV KWCALSHLER TKCDEWSIIS EGKIECESAE TTEDCIEKIV
410 420 430 440 450
NGEADAMTLD GGHAYIAGQC GLVPVMAEYY ESSNCAIPSQ QGIFPKGYYA
460 470 480 490 500
VAVVKASDTS ITWNNLKGKK SCHTGVDRTA GWNIPMGMLY NRINHCKFDE
510 520 530 540 550
FFSQGCAPGY EKNSTLCDLC IGPLKCAPNN KEEYNGYTGA FRCLVEKGDV
560 570 580 590 600
AFVKHQTVLD NTEGKNPAEW AKNLKQEDFE LLCPDGTRKP VKDFASCHLA
610 620 630 640 650
QAPNHVVVSR KEKAARVKAV LTSQETLFGG SDCTGNFCLF KSTTKDLLFR
660 670 680 690
DDTKCFVKLP EGTTPEKYLG AEYMQSVGNM RKCSTSRLLE ACTFHKH
Length:697
Mass (Da):76,724
Last modified:December 1, 2001 - v1
Checksum:i0996A0C3B64CB1B9
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti3 – 42LT → FA in AAL34533. 1 PublicationCurated
Sequence conflicti69 – 691K → R in AAA40488. (PubMed:3693348)Curated
Sequence conflicti71 – 744ISAS → HASG in AAH08559. (PubMed:15489334)Curated
Sequence conflicti72 – 721S → A in AAA40488. (PubMed:3693348)Curated
Sequence conflicti85 – 851W → L in AAA40488. (PubMed:3693348)Curated
Sequence conflicti104 – 1041Y → C in AAA40488. (PubMed:3693348)Curated
Sequence conflicti113 – 1131Y → S in AAA40488. (PubMed:3693348)Curated
Sequence conflicti123 – 1242GT → ER in AAA40488. (PubMed:3693348)Curated
Sequence conflicti135 – 1351K → E in BAE29847. (PubMed:16141072)Curated
Sequence conflicti283 – 2831W → L in AAB28966. (PubMed:8248032)Curated
Sequence conflicti307 – 3071P → L in AAB28966. (PubMed:8248032)Curated
Sequence conflicti350 – 3512CP → SA in AAA39438. (PubMed:3611056)Curated
Sequence conflicti487 – 4871G → C in AAA40490. (PubMed:3693348)Curated
Sequence conflicti527 – 5271A → D in AAA40491. (PubMed:3693348)Curated
Sequence conflicti529 – 5291N → S in BAE29847. (PubMed:16141072)Curated
Sequence conflicti575 – 5751K → N in AAA40491. (PubMed:3693348)Curated
Sequence conflicti697 – 6971H → S in AAL34533. 1 PublicationCurated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF440692 mRNA. Translation: AAL34533.1.
AK085754 mRNA. Translation: BAC39532.1.
AK142599 mRNA. Translation: BAE25124.1.
AK146549 mRNA. Translation: BAE27253.1.
AK149559 mRNA. Translation: BAE28960.1.
AK149595 mRNA. Translation: BAE28981.1.
AK150782 mRNA. Translation: BAE29847.1.
AK168419 mRNA. Translation: BAE40332.1.
AK168938 mRNA. Translation: BAE40747.1.
BC008559 mRNA. Translation: AAH08559.1.
BC012313 mRNA. Translation: AAH12313.1.
BC022986 mRNA. Translation: AAH22986.1.
BC092046 mRNA. Translation: AAH92046.1.
AF027336 Genomic DNA. Translation: AAB84034.1.
M23013 mRNA. Translation: AAA40488.1.
M23014 mRNA. Translation: AAA40489.1.
M23015 mRNA. Translation: AAA40490.1.
M23016 mRNA. Translation: AAA40491.1.
S67217 mRNA. Translation: AAB28966.2.
J03299 mRNA. Translation: AAA39438.1.
CCDSiCCDS23451.1.
PIRiA28446.
RefSeqiNP_598738.1. NM_133977.2.
UniGeneiMm.37214.

Genome annotation databases

EnsembliENSMUST00000035158; ENSMUSP00000035158; ENSMUSG00000032554.
ENSMUST00000112645; ENSMUSP00000108264; ENSMUSG00000032554.
GeneIDi22041.
KEGGimmu:22041.
UCSCiuc009rgi.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF440692 mRNA. Translation: AAL34533.1.
AK085754 mRNA. Translation: BAC39532.1.
AK142599 mRNA. Translation: BAE25124.1.
AK146549 mRNA. Translation: BAE27253.1.
AK149559 mRNA. Translation: BAE28960.1.
AK149595 mRNA. Translation: BAE28981.1.
AK150782 mRNA. Translation: BAE29847.1.
AK168419 mRNA. Translation: BAE40332.1.
AK168938 mRNA. Translation: BAE40747.1.
BC008559 mRNA. Translation: AAH08559.1.
BC012313 mRNA. Translation: AAH12313.1.
BC022986 mRNA. Translation: AAH22986.1.
BC092046 mRNA. Translation: AAH92046.1.
AF027336 Genomic DNA. Translation: AAB84034.1.
M23013 mRNA. Translation: AAA40488.1.
M23014 mRNA. Translation: AAA40489.1.
M23015 mRNA. Translation: AAA40490.1.
M23016 mRNA. Translation: AAA40491.1.
S67217 mRNA. Translation: AAB28966.2.
J03299 mRNA. Translation: AAA39438.1.
CCDSiCCDS23451.1.
PIRiA28446.
RefSeqiNP_598738.1. NM_133977.2.
UniGeneiMm.37214.

3D structure databases

ProteinModelPortaliQ921I1.
SMRiQ921I1. Positions 20-694.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi204313. 1 interaction.
IntActiQ921I1. 8 interactions.
MINTiMINT-1202663.

Protein family/group databases

MEROPSiS60.977.

PTM databases

PhosphoSiteiQ921I1.

2D gel databases

REPRODUCTION-2DPAGEIPI00139788.
Q921I1.

Proteomic databases

MaxQBiQ921I1.
PaxDbiQ921I1.
PRIDEiQ921I1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000035158; ENSMUSP00000035158; ENSMUSG00000032554.
ENSMUST00000112645; ENSMUSP00000108264; ENSMUSG00000032554.
GeneIDi22041.
KEGGimmu:22041.
UCSCiuc009rgi.1. mouse.

Organism-specific databases

CTDi22041.
MGIiMGI:98821. Trf.

Phylogenomic databases

eggNOGiNOG87503.
GeneTreeiENSGT00390000001619.
HOVERGENiHBG000055.
InParanoidiQ921I1.
KOiK14736.
OrthoDBiEOG7D59N7.
PhylomeDBiQ921I1.
TreeFamiTF324013.

Enzyme and pathway databases

ReactomeiREACT_198515. Transferrin endocytosis and recycling.
REACT_205755. Iron uptake and transport.

Miscellaneous databases

NextBioi301824.
PROiQ921I1.
SOURCEiSearch...

Gene expression databases

BgeeiQ921I1.
CleanExiMM_TRF.
ExpressionAtlasiQ921I1. baseline.
GenevestigatoriQ921I1.

Family and domain databases

InterProiIPR016357. Transferrin.
IPR001156. Transferrin-like_dom.
IPR018195. Transferrin_Fe_BS.
[Graphical view]
PfamiPF00405. Transferrin. 2 hits.
[Graphical view]
PIRSFiPIRSF002549. Transferrin. 1 hit.
PRINTSiPR00422. TRANSFERRIN.
SMARTiSM00094. TR_FER. 2 hits.
[Graphical view]
PROSITEiPS00205. TRANSFERRIN_LIKE_1. 1 hit.
PS00206. TRANSFERRIN_LIKE_2. 2 hits.
PS00207. TRANSFERRIN_LIKE_3. 2 hits.
PS51408. TRANSFERRIN_LIKE_4. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Construction of a robust CHO cell-line for biopharmaceutical production."
    Lai D.-Z.
    Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: BALB/c.
    Tissue: Liver.
  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].
    Strain: C57BL/6J.
    Tissue: Amnion, Bone marrow, Liver and Mammary gland.
  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].
    Strain: FVB/N.
    Tissue: Liver and Mammary tumor.
  4. "Comparative sequence analysis of the mouse and human transferrin promoters: hormonal regulation of the transferrin promoter in Sertoli cells."
    Chaudhary J., Skinner M.K.
    Mol. Reprod. Dev. 50:273-283(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-11.
    Strain: BALB/c.
  5. "Transferrin mRNA level in the mouse mammary gland is regulated by pregnancy and extracellular matrix."
    Chen L.-H., Bissell M.J.
    J. Biol. Chem. 262:17247-17250(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 66-131; 277-337; 462-496 AND 526-575.
  6. "Transferrin gene expression in maternal liver, fetal liver and placenta during pregnancy in the mouse."
    Kasik J.W., Rice E.J.
    Placenta 14:365-371(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 268-307.
    Tissue: Placenta.
  7. "Lactotransferrin is the major estrogen inducible protein of mouse uterine secretions."
    Pentecost B.T., Teng C.T.
    J. Biol. Chem. 262:10134-10139(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 282-412.
  8. Lubec G., Klug S., Kang S.U.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 332-343 AND 659-667, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6.
    Tissue: Brain and Hippocampus.
  9. "Expression from the transferrin gene promoter in transgenic mice."
    Idzerda R.L., Behringer R.R., Theisen M., Huggenvik J.I., McKnight G.S., Brinster R.L.
    Mol. Cell. Biol. 9:5154-5162(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  10. "Enhanced analysis of the mouse plasma proteome using cysteine-containing tryptic glycopeptides."
    Bernhard O.K., Kapp E.A., Simpson R.J.
    J. Proteome Res. 6:987-995(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-513.
    Strain: C57BL/6.
    Tissue: Plasma.

Entry informationi

Entry nameiTRFE_MOUSE
AccessioniPrimary (citable) accession number: Q921I1
Secondary accession number(s): O35421
, Q3UBW7, Q58E69, Q61803, Q62357, Q62358, Q62359, Q63915, Q64515, Q8VII5, Q922C0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 6, 2002
Last sequence update: December 1, 2001
Last modified: February 4, 2015
This is version 132 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, Direct protein sequencing, 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

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.