Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q9H2V7

- SPNS1_HUMAN

UniProt

Q9H2V7 - SPNS1_HUMAN

(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)

Protein

Protein spinster homolog 1

Gene

SPNS1

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

Functioni

Sphingolipid transporter (By similarity). May be involved in necrotic or autophagic cell death.By similarity1 Publication

GO - Biological processi

  1. lipid transport Source: UniProtKB-KW
  2. transmembrane transport Source: InterPro
Complete GO annotation...

Keywords - Biological processi

Lipid transport, Transport

Protein family/group databases

TCDBi2.A.1.49.2. the major facilitator superfamily (mfs).

Names & Taxonomyi

Protein namesi
Recommended name:
Protein spinster homolog 1
Alternative name(s):
HSpin1
Spinster-like protein 1
Gene namesi
Name:SPNS1
Synonyms:SPIN1
ORF Names:PP20300
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 16

Organism-specific databases

HGNCiHGNC:30621. SPNS1.

Subcellular locationi

Mitochondrion inner membrane 1 Publication; Multi-pass membrane protein 1 Publication
Note: Colocalizes with SDHB.

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
  2. lysosomal membrane Source: UniProtKB
  3. mitochondrial inner membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162404561.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 528527Protein spinster homolog 1PRO_0000305039Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei518 – 5181Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9H2V7.
PaxDbiQ9H2V7.
PRIDEiQ9H2V7.

PTM databases

PhosphoSiteiQ9H2V7.

Expressioni

Gene expression databases

BgeeiQ9H2V7.
CleanExiHS_SPIN1.
HS_SPNS1.
ExpressionAtlasiQ9H2V7. baseline.
GenevestigatoriQ9H2V7.

Organism-specific databases

HPAiHPA041995.
HPA042988.

Interactioni

Subunit structurei

Interacts with BCL2 and BCL2L1.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
BCL2L1Q078173EBI-1386527,EBI-78035

Protein-protein interaction databases

BioGridi123836. 5 interactions.
IntActiQ9H2V7. 7 interactions.
MINTiMINT-2817616.

Structurei

3D structure databases

ProteinModelPortaliQ9H2V7.
SMRiQ9H2V7. Positions 416-441.
ModBaseiSearch...
MobiDBiSearch...

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei50 – 7021HelicalSequence AnalysisAdd
BLAST
Transmembranei98 – 11821HelicalSequence AnalysisAdd
BLAST
Transmembranei127 – 14721HelicalSequence AnalysisAdd
BLAST
Transmembranei160 – 18021HelicalSequence AnalysisAdd
BLAST
Transmembranei187 – 20721HelicalSequence AnalysisAdd
BLAST
Transmembranei218 – 23821HelicalSequence AnalysisAdd
BLAST
Transmembranei278 – 29821HelicalSequence AnalysisAdd
BLAST
Transmembranei323 – 34321HelicalSequence AnalysisAdd
BLAST
Transmembranei357 – 37721HelicalSequence AnalysisAdd
BLAST
Transmembranei381 – 40121HelicalSequence AnalysisAdd
BLAST
Transmembranei421 – 44121HelicalSequence AnalysisAdd
BLAST
Transmembranei465 – 48521HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0477.
GeneTreeiENSGT00390000005976.
HOVERGENiHBG055503.
InParanoidiQ9H2V7.
PhylomeDBiQ9H2V7.
TreeFamiTF314395.

Family and domain databases

InterProiIPR011701. MFS.
IPR020846. MFS_dom.
IPR016196. MFS_dom_general_subst_transpt.
[Graphical view]
PfamiPF07690. MFS_1. 1 hit.
[Graphical view]
SUPFAMiSSF103473. SSF103473. 1 hit.
PROSITEiPS50850. MFS. 1 hit.
[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 1 (identifier: Q9H2V7-1) [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
MAGSDTAPFL SQADDPDDGP VPGTPGLPGS TGNPKSEEPE VPDQEGLQRI
60 70 80 90 100
TGLSPGRSAL IVAVLCYINL LNYMDRFTVA GVLPDIEQFF NIGDSSSGLI
110 120 130 140 150
QTVFISSYMV LAPVFGYLGD RYNRKYLMCG GIAFWSLVTL GSSFIPGEHF
160 170 180 190 200
WLLLLTRGLV GVGEASYSTI APTLIADLFV ADQRSRMLSI FYFAIPVGSG
210 220 230 240 250
LGYIAGSKVK DMAGDWHWAL RVTPGLGVVA VLLLFLVVRE PPRGAVERHS
260 270 280 290 300
DLPPLNPTSW WADLRALARN PSFVLSSLGF TAVAFVTGSL ALWAPAFLLR
310 320 330 340 350
SRVVLGETPP CLPGDSCSSS DSLIFGLITC LTGVLGVGLG VEISRRLRHS
360 370 380 390 400
NPRADPLVCA TGLLGSAPFL FLSLACARGS IVATYIFIFI GETLLSMNWA
410 420 430 440 450
IVADILLYVV IPTRRSTAEA FQIVLSHLLG DAGSPYLIGL ISDRLRRNWP
460 470 480 490 500
PSFLSEFRAL QFSLMLCAFV GALGGAAFLG TAIFIEADRR RAQLHVQGLL
510 520
HEAGSTDDRI VVPQRGRSTR VPVASVLI
Length:528
Mass (Da):56,630
Last modified:March 1, 2001 - v1
Checksum:iF1B9D2EB3F9F1B48
GO
Isoform 2 (identifier: Q9H2V7-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     271-322: Missing.

Show »
Length:476
Mass (Da):51,333
Checksum:i99272BB60BA81889
GO
Isoform 3 (identifier: Q9H2V7-3) [UniParc]FASTAAdd to Basket

Also known as: CRA_d

The sequence of this isoform differs from the canonical sequence as follows:
     81-102: Missing.
     271-322: Missing.

Show »
Length:454
Mass (Da):49,013
Checksum:i4A393F34239B87CF
GO
Isoform 4 (identifier: Q9H2V7-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-73: Missing.

Note: No experimental confirmation available.

Show »
Length:455
Mass (Da):49,139
Checksum:i63B25A8A61A99C30
GO
Isoform 5 (identifier: Q9H2V7-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     223-528: TPGLGVVAVL...TRVPVASVLI → SLVLAWG

Note: No experimental confirmation available.

Show »
Length:229
Mass (Da):24,594
Checksum:i07FF7E3B57DF8B8A
GO

Sequence cautioni

The sequence AAQ15259.1 differs from that shown. Reason: Frameshift at position 97.
The sequence AAQ15259.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti230 – 2301A → P.1 Publication
Corresponds to variant rs17855956 [ dbSNP | Ensembl ].
VAR_035157

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 7373Missing in isoform 4. 1 PublicationVSP_028194Add
BLAST
Alternative sequencei81 – 10222Missing in isoform 3. 1 PublicationVSP_028195Add
BLAST
Alternative sequencei223 – 528306TPGLG…ASVLI → SLVLAWG in isoform 5. 1 PublicationVSP_036389Add
BLAST
Alternative sequencei271 – 32252Missing in isoform 2 and isoform 3. 2 PublicationsVSP_028196Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF212371 mRNA. Translation: AAG43830.1.
AK095677 mRNA. Translation: BAC04603.1.
AK289787 mRNA. Translation: BAF82476.1.
AF370423 mRNA. Translation: AAQ15259.1. Sequence problems.
AL390215 mRNA. Translation: CAB99229.1.
AC109460 Genomic DNA. No translation available.
CH471267 Genomic DNA. Translation: EAW52018.1.
CH471267 Genomic DNA. Translation: EAW52019.1.
BC006156 mRNA. Translation: AAH06156.1.
BC008325 mRNA. Translation: AAH08325.1.
BC038961 mRNA. Translation: AAH38961.1.
BC047741 mRNA. Translation: AAH47741.1.
BC065235 mRNA. Translation: AAH65235.1.
CCDSiCCDS10646.1. [Q9H2V7-1]
CCDS45452.1. [Q9H2V7-2]
CCDS45453.1. [Q9H2V7-3]
CCDS45454.1. [Q9H2V7-4]
RefSeqiNP_001135920.1. NM_001142448.1. [Q9H2V7-1]
NP_001135921.1. NM_001142449.1. [Q9H2V7-3]
NP_001135922.1. NM_001142450.1. [Q9H2V7-4]
NP_001135923.1. NM_001142451.1. [Q9H2V7-2]
NP_114427.1. NM_032038.2. [Q9H2V7-1]
UniGeneiHs.617449.

Genome annotation databases

EnsembliENST00000311008; ENSP00000309945; ENSG00000169682. [Q9H2V7-1]
ENST00000323081; ENSP00000318228; ENSG00000169682. [Q9H2V7-4]
ENST00000334536; ENSP00000335494; ENSG00000169682. [Q9H2V7-2]
ENST00000352260; ENSP00000306050; ENSG00000169682. [Q9H2V7-3]
GeneIDi83985.
KEGGihsa:83985.
UCSCiuc002drx.2. human. [Q9H2V7-1]
uc002dry.2. human. [Q9H2V7-5]
uc002drz.2. human. [Q9H2V7-2]
uc010byp.2. human. [Q9H2V7-3]

Polymorphism databases

DMDMi74733566.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF212371 mRNA. Translation: AAG43830.1 .
AK095677 mRNA. Translation: BAC04603.1 .
AK289787 mRNA. Translation: BAF82476.1 .
AF370423 mRNA. Translation: AAQ15259.1 . Sequence problems.
AL390215 mRNA. Translation: CAB99229.1 .
AC109460 Genomic DNA. No translation available.
CH471267 Genomic DNA. Translation: EAW52018.1 .
CH471267 Genomic DNA. Translation: EAW52019.1 .
BC006156 mRNA. Translation: AAH06156.1 .
BC008325 mRNA. Translation: AAH08325.1 .
BC038961 mRNA. Translation: AAH38961.1 .
BC047741 mRNA. Translation: AAH47741.1 .
BC065235 mRNA. Translation: AAH65235.1 .
CCDSi CCDS10646.1. [Q9H2V7-1 ]
CCDS45452.1. [Q9H2V7-2 ]
CCDS45453.1. [Q9H2V7-3 ]
CCDS45454.1. [Q9H2V7-4 ]
RefSeqi NP_001135920.1. NM_001142448.1. [Q9H2V7-1 ]
NP_001135921.1. NM_001142449.1. [Q9H2V7-3 ]
NP_001135922.1. NM_001142450.1. [Q9H2V7-4 ]
NP_001135923.1. NM_001142451.1. [Q9H2V7-2 ]
NP_114427.1. NM_032038.2. [Q9H2V7-1 ]
UniGenei Hs.617449.

3D structure databases

ProteinModelPortali Q9H2V7.
SMRi Q9H2V7. Positions 416-441.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 123836. 5 interactions.
IntActi Q9H2V7. 7 interactions.
MINTi MINT-2817616.

Protein family/group databases

TCDBi 2.A.1.49.2. the major facilitator superfamily (mfs).

PTM databases

PhosphoSitei Q9H2V7.

Polymorphism databases

DMDMi 74733566.

Proteomic databases

MaxQBi Q9H2V7.
PaxDbi Q9H2V7.
PRIDEi Q9H2V7.

Protocols and materials databases

DNASUi 83985.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000311008 ; ENSP00000309945 ; ENSG00000169682 . [Q9H2V7-1 ]
ENST00000323081 ; ENSP00000318228 ; ENSG00000169682 . [Q9H2V7-4 ]
ENST00000334536 ; ENSP00000335494 ; ENSG00000169682 . [Q9H2V7-2 ]
ENST00000352260 ; ENSP00000306050 ; ENSG00000169682 . [Q9H2V7-3 ]
GeneIDi 83985.
KEGGi hsa:83985.
UCSCi uc002drx.2. human. [Q9H2V7-1 ]
uc002dry.2. human. [Q9H2V7-5 ]
uc002drz.2. human. [Q9H2V7-2 ]
uc010byp.2. human. [Q9H2V7-3 ]

Organism-specific databases

CTDi 83985.
GeneCardsi GC16P028986.
HGNCi HGNC:30621. SPNS1.
HPAi HPA041995.
HPA042988.
MIMi 612583. gene.
neXtProti NX_Q9H2V7.
PharmGKBi PA162404561.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0477.
GeneTreei ENSGT00390000005976.
HOVERGENi HBG055503.
InParanoidi Q9H2V7.
PhylomeDBi Q9H2V7.
TreeFami TF314395.

Miscellaneous databases

GenomeRNAii 83985.
NextBioi 73114.
PROi Q9H2V7.
SOURCEi Search...

Gene expression databases

Bgeei Q9H2V7.
CleanExi HS_SPIN1.
HS_SPNS1.
ExpressionAtlasi Q9H2V7. baseline.
Genevestigatori Q9H2V7.

Family and domain databases

InterProi IPR011701. MFS.
IPR020846. MFS_dom.
IPR016196. MFS_dom_general_subst_transpt.
[Graphical view ]
Pfami PF07690. MFS_1. 1 hit.
[Graphical view ]
SUPFAMi SSF103473. SSF103473. 1 hit.
PROSITEi PS50850. MFS. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Mutations in the novel membrane protein spinster interfere with programmed cell death and cause neural degeneration in Drosophila melanogaster."
    Nakano Y., Fujitani K., Kurihara J., Ragan J., Usui-Aoki K., Shimoda L., Lukacsovich T., Suzuki K., Sezaki M., Sano Y., Ueda R., Awano W., Kaneda M., Umeda M., Yamamoto D.
    Mol. Cell. Biol. 21:3775-3788(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "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 5).
    Tissue: Brain.
  3. "Large-scale cDNA transfection screening for genes related to cancer development and progression."
    Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.
    , Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.
    Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    Tissue: Mammary cancer.
  5. "The sequence and analysis of duplication-rich human chromosome 16."
    Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
    , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
    Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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] (ISOFORMS 1 AND 2), VARIANT PRO-230.
    Tissue: Blood, Brain, Pancreas and Skin.
  8. "HSpin1, a transmembrane protein interacting with Bcl-2/Bcl-xL, induces a caspase-independent autophagic cell death."
    Yanagisawa H., Miyashita T., Nakano Y., Yamamoto D.
    Cell Death Differ. 10:798-807(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH BCL2 AND BCL2L1.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-518, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  11. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiSPNS1_HUMAN
AccessioniPrimary (citable) accession number: Q9H2V7
Secondary accession number(s): B5MDM9
, Q6P182, Q71RB5, Q7L541, Q86VU7, Q8N953, Q8TCS5, Q9BRN5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: March 1, 2001
Last modified: October 29, 2014
This is version 108 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3