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O76054

- S14L2_HUMAN

UniProt

O76054 - S14L2_HUMAN

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Protein

SEC14-like protein 2

Gene

SEC14L2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Carrier protein. Binds to some hydrophobic molecules and promotes their transfer between the different cellular sites. Binds with high affinity to alpha-tocopherol. Also binds with a weaker affinity to other tocopherols and to tocotrienols. May have a transcriptional activatory activity via its association with alpha-tocopherol. Probably recognizes and binds some squalene structure, suggesting that it may regulate cholesterol biosynthesis by increasing the transfer of squalene to a metabolic active pool in the cell.

GO - Molecular functioni

  1. phospholipid binding Source: UniProtKB
  2. transporter activity Source: InterPro
  3. vitamin E binding Source: UniProtKB

GO - Biological processi

  1. positive regulation of transcription, DNA-templated Source: UniProtKB
  2. regulation of cholesterol biosynthetic process Source: UniProtKB
  3. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Transcription, Transcription regulation, Transport

Keywords - Ligandi

Lipid-binding

Names & Taxonomyi

Protein namesi
Recommended name:
SEC14-like protein 2
Alternative name(s):
Alpha-tocopherol-associated protein
Short name:
TAP
Short name:
hTAP
Squalene transfer protein
Supernatant protein factor
Short name:
SPF
Gene namesi
Name:SEC14L2
Synonyms:C22orf6, KIAA1186, KIAA1658
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 22

Organism-specific databases

HGNCiHGNC:10699. SEC14L2.

Subcellular locationi

Cytoplasm. Nucleus
Note: Cytoplasmic in absence of alpha-tocopherol, and nuclear in presence of alpha-tocopherol.

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. extracellular vesicular exosome Source: UniProtKB
  3. integral component of membrane Source: InterPro
  4. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA35622.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 403403SEC14-like protein 2PRO_0000210755Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei51 – 511N6-succinyllysineBy similarity
Modified residuei253 – 2531N6-succinyllysineBy similarity
Modified residuei257 – 2571N6-succinyllysineBy similarity
Modified residuei393 – 3931N6-succinyllysineBy similarity

Proteomic databases

MaxQBiO76054.
PaxDbiO76054.
PeptideAtlasiO76054.
PRIDEiO76054.

PTM databases

PhosphoSiteiO76054.

Expressioni

Tissue specificityi

Widely expressed. Strong expression in liver, brain and prostate.1 Publication

Developmental stagei

Low expression in fetal tissues.

Gene expression databases

BgeeiO76054.
CleanExiHS_SEC14L2.
ExpressionAtlasiO76054. baseline and differential.
GenevestigatoriO76054.

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

BioGridi117085. 1 interaction.
IntActiO76054. 1 interaction.
MINTiMINT-3002196.
STRINGi9606.ENSP00000316203.

Structurei

Secondary structure

1
403
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi10 – 2314
Helixi24 – 296
Helixi35 – 4410
Turni45 – 473
Helixi49 – 6517
Helixi68 – 736
Helixi78 – 836
Beta strandi86 – 916
Beta strandi97 – 1026
Helixi108 – 1125
Helixi117 – 14226
Beta strandi149 – 1546
Helixi160 – 1634
Helixi165 – 18117
Beta strandi186 – 1938
Helixi198 – 2058
Helixi206 – 2083
Helixi211 – 2155
Beta strandi217 – 2193
Helixi224 – 2285
Turni229 – 2313
Helixi234 – 2363
Helixi239 – 2413
Beta strandi243 – 2453
Turni255 – 2573
Helixi266 – 2683
Beta strandi279 – 2846
Beta strandi289 – 2968
Beta strandi302 – 31211
Beta strandi314 – 3207
Beta strandi323 – 3264
Helixi330 – 3323
Beta strandi333 – 34210
Turni344 – 3463
Beta strandi349 – 3546
Beta strandi359 – 3668
Beta strandi374 – 38411
Helixi388 – 3958

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1O6UX-ray2.05A/C/E1-403[»]
1OLMX-ray1.95A/C/E1-403[»]
ProteinModelPortaliO76054.
SMRiO76054. Positions 1-397.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO76054.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini76 – 249174CRAL-TRIOPROSITE-ProRule annotationAdd
BLAST
Domaini275 – 383109GOLDPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 CRAL-TRIO domain.PROSITE-ProRule annotation
Contains 1 GOLD domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG309458.
GeneTreeiENSGT00550000074580.
HOGENOMiHOG000232201.
HOVERGENiHBG055336.
InParanoidiO76054.
OMAiKXPKLFP.
OrthoDBiEOG7N8ZVD.
PhylomeDBiO76054.
TreeFamiTF313988.

Family and domain databases

Gene3Di3.40.525.10. 1 hit.
InterProiIPR001071. CRAL-bd_toc_tran.
IPR001251. CRAL-TRIO_dom.
IPR011074. CRAL/TRIO_N_dom.
IPR009038. GOLD.
[Graphical view]
PfamiPF00650. CRAL_TRIO. 1 hit.
PF03765. CRAL_TRIO_N. 1 hit.
[Graphical view]
PRINTSiPR00180. CRETINALDHBP.
SMARTiSM01100. CRAL_TRIO_N. 1 hit.
SM00516. SEC14. 1 hit.
[Graphical view]
SUPFAMiSSF101576. SSF101576. 1 hit.
SSF46938. SSF46938. 1 hit.
SSF52087. SSF52087. 1 hit.
PROSITEiPS50191. CRAL_TRIO. 1 hit.
PS50866. GOLD. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O76054-1) [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
MSGRVGDLSP RQKEALAKFR ENVQDVLPAL PNPDDYFLLR WLRARSFDLQ
60 70 80 90 100
KSEAMLRKHV EFRKQKDIDN IISWQPPEVI QQYLSGGMCG YDLDGCPVWY
110 120 130 140 150
DIIGPLDAKG LLFSASKQDL LRTKMRECEL LLQECAHQTT KLGRKVETIT
160 170 180 190 200
IIYDCEGLGL KHLWKPAVEA YGEFLCMFEE NYPETLKRLF VVKAPKLFPV
210 220 230 240 250
AYNLIKPFLS EDTRKKIMVL GANWKEVLLK HISPDQVPVE YGGTMTDPDG
260 270 280 290 300
NPKCKSKINY GGDIPRKYYV RDQVKQQYEH SVQISRGSSH QVEYEILFPG
310 320 330 340 350
CVLRWQFMSD GADVGFGIFL KTKMGERQRA GEMTEVLPNQ RYNSHLVPED
360 370 380 390 400
GTLTCSDPGI YVLRFDNTYS FIHAKKVNFT VEVLLPDKAS EEKMKQLGAG

TPK
Length:403
Mass (Da):46,145
Last modified:November 1, 1998 - v1
Checksum:iD846747EC8D1513E
GO
Isoform 2 (identifier: O76054-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     361-403: YVLRFDNTYSFIHAKKVNFTVEVLLPDKASEEKMKQLGAGTPK → CKYLCLGNALKPHVQLSACEVPLPPWIFGSEC

Note: No experimental confirmation available.

Show »
Length:392
Mass (Da):44,748
Checksum:i11A833345968FE5A
GO
Isoform 3 (identifier: O76054-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     58-140: Missing.

Note: No experimental confirmation available.

Show »
Length:320
Mass (Da):36,636
Checksum:i64CCC92D4A8149C7
GO

Sequence cautioni

The sequence BAA86500.2 differs from that shown. Reason: Erroneous initiation.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti36 – 361Y → H(PubMed:11444841)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti11 – 111R → K.2 Publications
Corresponds to variant rs757660 [ dbSNP | Ensembl ].
VAR_024626

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei58 – 14083Missing in isoform 3. 1 PublicationVSP_045880Add
BLAST
Alternative sequencei361 – 40343YVLRF…AGTPK → CKYLCLGNALKPHVQLSACE VPLPPWIFGSEC in isoform 2. 1 PublicationVSP_042021Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AL096881 mRNA. Translation: CAB51405.1.
AB033012 mRNA. Translation: BAA86500.2. Different initiation.
CR456571 mRNA. Translation: CAG30457.1.
AK303751 mRNA. Translation: BAH14037.1.
AK223587 mRNA. Translation: BAD97307.1.
AC004832 Genomic DNA. Translation: AAF19256.1.
BC058915 mRNA. Translation: AAH58915.1.
CCDSiCCDS13876.1. [O76054-1]
CCDS46685.1. [O76054-4]
CCDS56228.1. [O76054-5]
PIRiJC7708.
RefSeqiNP_001191133.1. NM_001204204.2. [O76054-5]
NP_036561.1. NM_012429.4. [O76054-1]
NP_203740.1. NM_033382.2. [O76054-4]
UniGeneiHs.335614.

Genome annotation databases

EnsembliENST00000402592; ENSP00000383882; ENSG00000100003. [O76054-5]
ENST00000405717; ENSP00000385186; ENSG00000100003. [O76054-4]
ENST00000615189; ENSP00000478755; ENSG00000100003. [O76054-1]
GeneIDi23541.
KEGGihsa:23541.
UCSCiuc003ahq.3. human. [O76054-4]
uc003ahr.3. human. [O76054-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AL096881 mRNA. Translation: CAB51405.1 .
AB033012 mRNA. Translation: BAA86500.2 . Different initiation.
CR456571 mRNA. Translation: CAG30457.1 .
AK303751 mRNA. Translation: BAH14037.1 .
AK223587 mRNA. Translation: BAD97307.1 .
AC004832 Genomic DNA. Translation: AAF19256.1 .
BC058915 mRNA. Translation: AAH58915.1 .
CCDSi CCDS13876.1. [O76054-1 ]
CCDS46685.1. [O76054-4 ]
CCDS56228.1. [O76054-5 ]
PIRi JC7708.
RefSeqi NP_001191133.1. NM_001204204.2. [O76054-5 ]
NP_036561.1. NM_012429.4. [O76054-1 ]
NP_203740.1. NM_033382.2. [O76054-4 ]
UniGenei Hs.335614.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1O6U X-ray 2.05 A/C/E 1-403 [» ]
1OLM X-ray 1.95 A/C/E 1-403 [» ]
ProteinModelPortali O76054.
SMRi O76054. Positions 1-397.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 117085. 1 interaction.
IntActi O76054. 1 interaction.
MINTi MINT-3002196.
STRINGi 9606.ENSP00000316203.

Chemistry

DrugBanki DB00163. Vitamin E.

PTM databases

PhosphoSitei O76054.

Proteomic databases

MaxQBi O76054.
PaxDbi O76054.
PeptideAtlasi O76054.
PRIDEi O76054.

Protocols and materials databases

DNASUi 23541.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000402592 ; ENSP00000383882 ; ENSG00000100003 . [O76054-5 ]
ENST00000405717 ; ENSP00000385186 ; ENSG00000100003 . [O76054-4 ]
ENST00000615189 ; ENSP00000478755 ; ENSG00000100003 . [O76054-1 ]
GeneIDi 23541.
KEGGi hsa:23541.
UCSCi uc003ahq.3. human. [O76054-4 ]
uc003ahr.3. human. [O76054-1 ]

Organism-specific databases

CTDi 23541.
GeneCardsi GC22P030792.
HGNCi HGNC:10699. SEC14L2.
MIMi 607558. gene.
neXtProti NX_O76054.
PharmGKBi PA35622.
HUGEi Search...
Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG309458.
GeneTreei ENSGT00550000074580.
HOGENOMi HOG000232201.
HOVERGENi HBG055336.
InParanoidi O76054.
OMAi KXPKLFP.
OrthoDBi EOG7N8ZVD.
PhylomeDBi O76054.
TreeFami TF313988.

Miscellaneous databases

ChiTaRSi SEC14L2. human.
EvolutionaryTracei O76054.
GeneWikii SEC14L2.
GenomeRNAii 23541.
NextBioi 46048.
PROi O76054.
SOURCEi Search...

Gene expression databases

Bgeei O76054.
CleanExi HS_SEC14L2.
ExpressionAtlasi O76054. baseline and differential.
Genevestigatori O76054.

Family and domain databases

Gene3Di 3.40.525.10. 1 hit.
InterProi IPR001071. CRAL-bd_toc_tran.
IPR001251. CRAL-TRIO_dom.
IPR011074. CRAL/TRIO_N_dom.
IPR009038. GOLD.
[Graphical view ]
Pfami PF00650. CRAL_TRIO. 1 hit.
PF03765. CRAL_TRIO_N. 1 hit.
[Graphical view ]
PRINTSi PR00180. CRETINALDHBP.
SMARTi SM01100. CRAL_TRIO_N. 1 hit.
SM00516. SEC14. 1 hit.
[Graphical view ]
SUPFAMi SSF101576. SSF101576. 1 hit.
SSF46938. SSF46938. 1 hit.
SSF52087. SSF52087. 1 hit.
PROSITEi PS50191. CRAL_TRIO. 1 hit.
PS50866. GOLD. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "A novel human tocopherol-associated protein: cloning, in vitro expression, and characterization."
    Zimmer S., Stocker A., Sarbolouki M.N., Spycher S.E., Sassoon J., Azzi A.
    J. Biol. Chem. 275:25672-25680(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, CHARACTERIZATION.
  2. "Tocopherol-associated protein is a ligand-dependent transcriptional activator."
    Yamauchi J., Iwamoto T., Kida S., Masushige S., Yamada K., Esashi T.
    Biochem. Biophys. Res. Commun. 285:295-299(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CHARACTERIZATION.
    Tissue: Liver.
  3. "Supernatant protein factor, which stimulates the conversion of squalene to lanosterol, is a cytosolic squalene transfer protein and enhances cholesterol biosynthesis."
    Shibata N., Arita M., Misaki Y., Dohmae N., Takio K., Ono T., Inoue K., Arai H.
    Proc. Natl. Acad. Sci. U.S.A. 98:2244-2249(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CHARACTERIZATION.
    Tissue: Liver.
  4. "Characterization of cDNA clones selected by the GeneMark analysis from size-fractionated cDNA libraries from human brain."
    Hirosawa M., Nagase T., Ishikawa K., Kikuno R., Nomura N., Ohara O.
    DNA Res. 6:329-336(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Brain.
  5. Ohara O., Nagase T., Kikuno R.
    Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  7. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), VARIANT LYS-11.
    Tissue: Liver.
  8. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
    Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT LYS-11.
    Tissue: Kidney.
  9. "The DNA sequence of human chromosome 22."
    Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
    , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
    Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  10. "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 2).
    Tissue: Brain.
  11. "Crystal structure of the human supernatant protein factor."
    Stocker A., Tomizaki T., Schulze-Briese C., Baumann U.
    Structure 10:1533-1540(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).

Entry informationi

Entry nameiS14L2_HUMAN
AccessioniPrimary (citable) accession number: O76054
Secondary accession number(s): B7Z8Q1
, F5H3U4, Q53EQ2, Q6PD61, Q9ULN4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 20, 2002
Last sequence update: November 1, 1998
Last modified: October 29, 2014
This is version 138 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 22
    Human chromosome 22: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3