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Protein

SEC14-like protein 2

Gene

SEC14L2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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

  • phospholipid binding Source: UniProtKB
  • transporter activity Source: InterPro
  • vitamin E binding Source: UniProtKB

GO - Biological processi

  • positive regulation of transcription, DNA-templated Source: UniProtKB
  • regulation of cholesterol biosynthetic process Source: UniProtKB
  • 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 Componenti: 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

  • cytoplasm Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • integral component of membrane Source: InterPro
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA35622.

Chemistry

DrugBankiDB00163. Vitamin E.

Polymorphism and mutation databases

BioMutaiSEC14L2.

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.
GenevisibleiO76054. HS.

Organism-specific databases

HPAiHPA064466.

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 – 2314Combined sources
Helixi24 – 296Combined sources
Helixi35 – 4410Combined sources
Turni45 – 473Combined sources
Helixi49 – 6517Combined sources
Helixi68 – 736Combined sources
Helixi78 – 836Combined sources
Beta strandi86 – 916Combined sources
Beta strandi97 – 1026Combined sources
Helixi108 – 1125Combined sources
Helixi117 – 14226Combined sources
Beta strandi149 – 1546Combined sources
Helixi160 – 1634Combined sources
Helixi165 – 18117Combined sources
Beta strandi186 – 1938Combined sources
Helixi198 – 2058Combined sources
Helixi206 – 2083Combined sources
Helixi211 – 2155Combined sources
Beta strandi217 – 2193Combined sources
Helixi224 – 2285Combined sources
Turni229 – 2313Combined sources
Helixi234 – 2363Combined sources
Helixi239 – 2413Combined sources
Beta strandi243 – 2453Combined sources
Turni255 – 2573Combined sources
Helixi266 – 2683Combined sources
Beta strandi279 – 2846Combined sources
Beta strandi289 – 2968Combined sources
Beta strandi302 – 31211Combined sources
Beta strandi314 – 3207Combined sources
Beta strandi323 – 3264Combined sources
Helixi330 – 3323Combined sources
Beta strandi333 – 34210Combined sources
Turni344 – 3463Combined sources
Beta strandi349 – 3546Combined sources
Beta strandi359 – 3668Combined sources
Beta strandi374 – 38411Combined sources
Helixi388 – 3958Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1O6UX-ray2.05A/C/E1-403[»]
1OLMX-ray1.95A/C/E1-403[»]
4OMJX-ray1.60A/B1-275[»]
4OMKX-ray1.75A/B1-275[»]
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.
OMAiARKWNLE.
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. AlignAdd to basket

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. Curated

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1O6UX-ray2.05A/C/E1-403[»]
1OLMX-ray1.95A/C/E1-403[»]
4OMJX-ray1.60A/B1-275[»]
4OMKX-ray1.75A/B1-275[»]
ProteinModelPortaliO76054.
SMRiO76054. Positions 1-397.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Chemistry

DrugBankiDB00163. Vitamin E.

PTM databases

PhosphoSiteiO76054.

Polymorphism and mutation databases

BioMutaiSEC14L2.

Proteomic databases

MaxQBiO76054.
PaxDbiO76054.
PeptideAtlasiO76054.
PRIDEiO76054.

Protocols and materials databases

DNASUi23541.
Structural Biology KnowledgebaseSearch...

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]

Organism-specific databases

CTDi23541.
GeneCardsiGC22P030792.
HGNCiHGNC:10699. SEC14L2.
HPAiHPA064466.
MIMi607558. gene.
neXtProtiNX_O76054.
PharmGKBiPA35622.
HUGEiSearch...
Search...
GenAtlasiSearch...

Phylogenomic databases

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

Miscellaneous databases

ChiTaRSiSEC14L2. human.
EvolutionaryTraceiO76054.
GeneWikiiSEC14L2.
GenomeRNAii23541.
NextBioi46048.
PROiO76054.
SOURCEiSearch...

Gene expression databases

BgeeiO76054.
CleanExiHS_SEC14L2.
ExpressionAtlasiO76054. baseline and differential.
GenevisibleiO76054. HS.

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]
ProtoNetiSearch...

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. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  12. "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: June 24, 2015
This is version 144 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

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.