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Protein

SPRY domain-containing SOCS box protein 1

Gene

SPSB1

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

Functioni

Probable substrate recognition component of a SCF-like ECS (Elongin BC-CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins.1 Publication

Pathwayi: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Ubl conjugation pathway

Enzyme and pathway databases

ReactomeiR-HSA-983168. Antigen processing: Ubiquitination & Proteasome degradation.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
SPRY domain-containing SOCS box protein 1
Short name:
SSB-1
Gene namesi
Name:SPSB1
Synonyms:SSB1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:30628. SPSB1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi31 – 311Y → F: Loss of phosphorylation. 1 Publication
Mutagenesisi260 – 2634LPLP → AAAA: Abolishes interaction with RNF7 and CUL5. 1 Publication

Organism-specific databases

PharmGKBiPA142670871.

Polymorphism and mutation databases

BioMutaiSPSB1.
DMDMi74731225.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 273273SPRY domain-containing SOCS box protein 1PRO_0000238472Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei31 – 311Phosphotyrosine; by MET1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ96BD6.
PRIDEiQ96BD6.

PTM databases

iPTMnetiQ96BD6.
PhosphoSiteiQ96BD6.

Expressioni

Gene expression databases

BgeeiQ96BD6.
CleanExiHS_SPSB1.
ExpressionAtlasiQ96BD6. baseline and differential.
GenevisibleiQ96BD6. HS.

Organism-specific databases

HPAiHPA003296.

Interactioni

Subunit structurei

Component of the probable ECS(SPSB1) E3 ubiquitin-protein ligase complex which contains CUL5, RNF7/RBX2, Elongin BC complex and SPSB1. Interacts with CUL5, RNF7, TCEB1 and TCEB2. Directly interacts with MET tyrosine kinase domain in the presence and in the absence of HGF, however HGF treatment has a positive effect on this interaction. When phosphorylated, interacts with RASA1 without affecting its stability. Interacts, in complex with Elongin BC complex, with PAWR.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
KDM1AO603412EBI-2659201,EBI-710124
PAWRQ96IZ02EBI-2659201,EBI-595869
PRMT1Q998732EBI-2659201,EBI-78738
PRMT6Q96LA82EBI-2659201,EBI-912440
SNAI1O958633EBI-2659201,EBI-1045459
SUV39H1O434632EBI-2659201,EBI-349968
vasP090522EBI-2659201,EBI-134067From a different organism.

Protein-protein interaction databases

BioGridi123158. 22 interactions.
IntActiQ96BD6. 12 interactions.
MINTiMINT-6780046.
STRINGi9606.ENSP00000330221.

Structurei

Secondary structure

1
273
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi36 – 427Combined sources
Helixi48 – 536Combined sources
Beta strandi55 – 617Combined sources
Beta strandi65 – 684Combined sources
Beta strandi71 – 777Combined sources
Beta strandi83 – 908Combined sources
Beta strandi95 – 1039Combined sources
Helixi106 – 1083Combined sources
Beta strandi114 – 1185Combined sources
Beta strandi125 – 1295Combined sources
Beta strandi139 – 1435Combined sources
Turni144 – 1474Combined sources
Beta strandi148 – 1525Combined sources
Turni153 – 1553Combined sources
Beta strandi159 – 1624Combined sources
Beta strandi175 – 1828Combined sources
Turni183 – 1864Combined sources
Beta strandi187 – 1926Combined sources
Beta strandi195 – 2017Combined sources
Beta strandi209 – 2157Combined sources
Beta strandi221 – 23010Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2JK9X-ray1.79A24-233[»]
3F2OX-ray2.05A/B24-233[»]
ProteinModelPortaliQ96BD6.
SMRiQ96BD6. Positions 30-233.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ96BD6.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini33 – 231199B30.2/SPRYPROSITE-ProRule annotationAdd
BLAST
Domaini232 – 27342SOCS boxPROSITE-ProRule annotationAdd
BLAST

Domaini

The SOCS box domain mediates the interaction with the Elongin BC complex, an adapter module in different E3 ubiquitin ligase complexes (By similarity). The B30.2/SPRY domain is involved in MET binding.By similarity

Sequence similaritiesi

Belongs to the SPSB family.Curated
Contains 1 B30.2/SPRY domain.PROSITE-ProRule annotation
Contains 1 SOCS box domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG3953. Eukaryota.
ENOG410XQC1. LUCA.
GeneTreeiENSGT00390000009402.
HOGENOMiHOG000230524.
HOVERGENiHBG055793.
InParanoidiQ96BD6.
KOiK10343.
OMAiGMESECP.
OrthoDBiEOG72C513.
PhylomeDBiQ96BD6.
TreeFamiTF312822.

Family and domain databases

InterProiIPR001870. B30.2/SPRY.
IPR013320. ConA-like_dom.
IPR001496. SOCS_box.
IPR003877. SPRY_dom.
[Graphical view]
PfamiPF07525. SOCS_box. 1 hit.
PF00622. SPRY. 1 hit.
[Graphical view]
SMARTiSM00969. SOCS_box. 1 hit.
SM00449. SPRY. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 1 hit.
PROSITEiPS50188. B302_SPRY. 1 hit.
PS50225. SOCS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q96BD6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGQKVTGGIK TVDMRDPTYR PLKQELQGLD YCKPTRLDLL LDMPPVSYDV
60 70 80 90 100
QLLHSWNNND RSLNVFVKED DKLIFHRHPV AQSTDAIRGK VGYTRGLHVW
110 120 130 140 150
QITWAMRQRG THAVVGVATA DAPLHSVGYT TLVGNNHESW GWDLGRNRLY
160 170 180 190 200
HDGKNQPSKT YPAFLEPDET FIVPDSFLVA LDMDDGTLSF IVDGQYMGVA
210 220 230 240 250
FRGLKGKKLY PVVSAVWGHC EIRMRYLNGL DPEPLPLMDL CRRSVRLALG
260 270
RERLGEIHTL PLPASLKAYL LYQ
Length:273
Mass (Da):30,942
Last modified:December 1, 2001 - v1
Checksum:iF93D5690A32403DF
GO

Sequence cautioni

The sequence BAD92796.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti14 – 141M → L in BAD92796 (Ref. 3) Curated
Sequence conflicti73 – 731L → P in BAB15335 (PubMed:14702039).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF403026 mRNA. Translation: AAL57345.1.
AK026046 mRNA. Translation: BAB15335.1.
AB209559 mRNA. Translation: BAD92796.1. Different initiation.
AL358252, AL008734 Genomic DNA. Translation: CAI14376.2.
AL008734, AL358252 Genomic DNA. Translation: CAM12843.1.
CH471130 Genomic DNA. Translation: EAW71617.1.
BC005852 mRNA. Translation: AAH05852.2.
BC015711 mRNA. Translation: AAH15711.1.
CCDSiCCDS102.1.
RefSeqiNP_079382.2. NM_025106.3.
UniGeneiHs.738680.
Hs.8261.

Genome annotation databases

EnsembliENST00000328089; ENSP00000330221; ENSG00000171621.
ENST00000357898; ENSP00000350573; ENSG00000171621.
ENST00000377399; ENSP00000366616; ENSG00000171621.
GeneIDi80176.
KEGGihsa:80176.
UCSCiuc001apv.4. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF403026 mRNA. Translation: AAL57345.1.
AK026046 mRNA. Translation: BAB15335.1.
AB209559 mRNA. Translation: BAD92796.1. Different initiation.
AL358252, AL008734 Genomic DNA. Translation: CAI14376.2.
AL008734, AL358252 Genomic DNA. Translation: CAM12843.1.
CH471130 Genomic DNA. Translation: EAW71617.1.
BC005852 mRNA. Translation: AAH05852.2.
BC015711 mRNA. Translation: AAH15711.1.
CCDSiCCDS102.1.
RefSeqiNP_079382.2. NM_025106.3.
UniGeneiHs.738680.
Hs.8261.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2JK9X-ray1.79A24-233[»]
3F2OX-ray2.05A/B24-233[»]
ProteinModelPortaliQ96BD6.
SMRiQ96BD6. Positions 30-233.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi123158. 22 interactions.
IntActiQ96BD6. 12 interactions.
MINTiMINT-6780046.
STRINGi9606.ENSP00000330221.

PTM databases

iPTMnetiQ96BD6.
PhosphoSiteiQ96BD6.

Polymorphism and mutation databases

BioMutaiSPSB1.
DMDMi74731225.

Proteomic databases

PaxDbiQ96BD6.
PRIDEiQ96BD6.

Protocols and materials databases

DNASUi80176.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000328089; ENSP00000330221; ENSG00000171621.
ENST00000357898; ENSP00000350573; ENSG00000171621.
ENST00000377399; ENSP00000366616; ENSG00000171621.
GeneIDi80176.
KEGGihsa:80176.
UCSCiuc001apv.4. human.

Organism-specific databases

CTDi80176.
GeneCardsiSPSB1.
HGNCiHGNC:30628. SPSB1.
HPAiHPA003296.
MIMi611657. gene.
neXtProtiNX_Q96BD6.
PharmGKBiPA142670871.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3953. Eukaryota.
ENOG410XQC1. LUCA.
GeneTreeiENSGT00390000009402.
HOGENOMiHOG000230524.
HOVERGENiHBG055793.
InParanoidiQ96BD6.
KOiK10343.
OMAiGMESECP.
OrthoDBiEOG72C513.
PhylomeDBiQ96BD6.
TreeFamiTF312822.

Enzyme and pathway databases

UniPathwayiUPA00143.
ReactomeiR-HSA-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Miscellaneous databases

ChiTaRSiSPSB1. human.
EvolutionaryTraceiQ96BD6.
GeneWikiiSPSB1.
GenomeRNAii80176.
PROiQ96BD6.
SOURCEiSearch...

Gene expression databases

BgeeiQ96BD6.
CleanExiHS_SPSB1.
ExpressionAtlasiQ96BD6. baseline and differential.
GenevisibleiQ96BD6. HS.

Family and domain databases

InterProiIPR001870. B30.2/SPRY.
IPR013320. ConA-like_dom.
IPR001496. SOCS_box.
IPR003877. SPRY_dom.
[Graphical view]
PfamiPF07525. SOCS_box. 1 hit.
PF00622. SPRY. 1 hit.
[Graphical view]
SMARTiSM00969. SOCS_box. 1 hit.
SM00449. SPRY. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 1 hit.
PROSITEiPS50188. B302_SPRY. 1 hit.
PS50225. SOCS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "SOCS box proteins."
    Friedel E.J., Nicholson S.E., Nicola N.A., Kile B.T., Hilton D.J.
    Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  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].
  3. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
    Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  4. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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].
    Tissue: Melanoma.
  7. "VHL-box and SOCS-box domains determine binding specificity for Cul2-Rbx1 and Cul5-Rbx2 modules of ubiquitin ligases."
    Kamura T., Maenaka K., Kotoshiba S., Matsumoto M., Kohda D., Conaway R.C., Conaway J.W., Nakayama K.I.
    Genes Dev. 18:3055-3065(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN AN E3 UBIQUITIN-PROTEIN LIGASE COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH CUL5; RNF7; TCEB1 AND TCEB2, MUTAGENESIS OF 260-LEU--PRO-263.
  8. "The SPRY domain-containing SOCS box protein 1 (SSB-1) interacts with MET and enhances the hepatocyte growth factor-induced Erk-Elk-1-serum response element pathway."
    Wang D., Li Z., Messing E.M., Wu G.
    J. Biol. Chem. 280:16393-16401(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MET AND RASA1, PHOSPHORYLATION AT TYR-31, MUTAGENESIS OF TYR-31.
  9. "Structural basis for protein recognition by B30.2/SPRY domains."
    Woo J.S., Suh H.Y., Park S.Y., Oh B.H.
    Mol. Cell 24:967-976(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ELONGIN BC COMPLEX AND PAWR.

Entry informationi

Entry nameiSPSB1_HUMAN
AccessioniPrimary (citable) accession number: Q96BD6
Secondary accession number(s): A2A275
, Q59FA1, Q5TIH9, Q9BRY9, Q9H6C5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: December 1, 2001
Last modified: June 8, 2016
This is version 122 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 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. SIMILARITY comments
    Index of protein domains and families

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 one 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.