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Protein

SH3-containing GRB2-like protein 3-interacting protein 1

Gene

Sgip1

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

Functioni

May function in clathrin-mediated endocytosis. Has both a membrane binding/tubulating activity and the ability to recruit proteins essential to the formation of functional clathrin-coated pits. Has a preference for membranes enriched in phosphatidylserine and phosphoinositides and is required for the endocytosis of the transferrin receptor. May also bind tubulin. May play a role in the regulation of energy homeostasis.2 Publications

GO - Molecular functioni

  • microtubule binding Source: UniProtKB
  • phospholipid binding Source: UniProtKB
  • SH3 domain binding Source: MGI
  • tubulin binding Source: UniProtKB

GO - Biological processi

  • endocytosis Source: UniProtKB-KW
  • membrane tubulation Source: MGI
  • positive regulation of energy homeostasis Source: UniProtKB
  • positive regulation of feeding behavior Source: UniProtKB
  • positive regulation of receptor-mediated endocytosis Source: UniProtKB
  • response to dietary excess Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Endocytosis

Names & Taxonomyi

Protein namesi
Recommended name:
SH3-containing GRB2-like protein 3-interacting protein 1
Alternative name(s):
Endophilin-3-interacting protein
Gene namesi
Name:Sgip1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:1920344. Sgip1.

Subcellular locationi

GO - Cellular componenti

  • AP-2 adaptor complex Source: UniProtKB
  • clathrin-coated vesicle Source: UniProtKB
  • coated pit Source: MGI
  • cytoplasm Source: UniProtKB
  • plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Coated pit, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 806806SH3-containing GRB2-like protein 3-interacting protein 1PRO_0000248396Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei78 – 781PhosphoserineCombined sources
Modified residuei104 – 1041PhosphoserineBy similarity
Modified residuei105 – 1051PhosphoserineBy similarity
Modified residuei107 – 1071PhosphoserineBy similarity
Modified residuei149 – 1491PhosphoserineCombined sources
Modified residuei151 – 1511PhosphoserineCombined sources
Modified residuei156 – 1561PhosphoserineCombined sources
Modified residuei169 – 1691PhosphoserineBy similarity
Modified residuei180 – 1801PhosphothreonineCombined sources
Modified residuei182 – 1821PhosphothreonineCombined sources
Modified residuei236 – 2361PhosphoserineBy similarity
Modified residuei247 – 2471PhosphothreonineCombined sources
Modified residuei259 – 2591PhosphothreonineCombined sources
Modified residuei265 – 2651PhosphoserineCombined sources
Modified residuei287 – 2871PhosphoserineCombined sources
Modified residuei289 – 2891PhosphoserineCombined sources
Modified residuei300 – 3001PhosphoserineCombined sources
Modified residuei316 – 3161PhosphoserineCombined sources
Modified residuei319 – 3191PhosphoserineCombined sources
Modified residuei324 – 3241PhosphothreonineCombined sources
Modified residuei328 – 3281PhosphothreonineCombined sources
Modified residuei335 – 3351PhosphothreonineBy similarity
Modified residuei371 – 3711PhosphoserineCombined sources
Modified residuei398 – 3981PhosphoserineCombined sources
Modified residuei409 – 4091PhosphothreonineCombined sources
Modified residuei484 – 4841PhosphoserineCombined sources
Isoform 2 (identifier: Q8VD37-2)
Modified residuei243 – 2431PhosphoserineCombined sources
Isoform 3 (identifier: Q8VD37-3)
Modified residuei274 – 2741PhosphoserineCombined sources
Modified residuei338 – 3381PhosphoserineCombined sources
Isoform 4 (identifier: Q8VD37-4)
Modified residuei274 – 2741PhosphoserineCombined sources
Isoform 7 (identifier: Q8VD37-8)
Modified residuei505 – 5051PhosphoserineCombined sources
Isoform 6 (identifier: Q8VD37-6)
Modified residuei533 – 5331PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ8VD37.
PaxDbiQ8VD37.
PRIDEiQ8VD37.

PTM databases

iPTMnetiQ8VD37.
PhosphoSiteiQ8VD37.

Expressioni

Tissue specificityi

Detected in brain, spinal cord and cerebellum.1 Publication

Inductioni

Up-regulated in the hypothalamus of obese mice.1 Publication

Gene expression databases

BgeeiQ8VD37.
ExpressionAtlasiQ8VD37. baseline and differential.
GenevisibleiQ8VD37. MM.

Interactioni

Subunit structurei

Interacts with proteins essential or regulating the formation of functional clathrin-coated pits (By similarity). Interacts with CANX. Interacts with AP2A1. Interacts with EPS15. Interacts with SH3GL3 (By similarity). Interacts with AMPH (By similarity). Interacts with ITSN1 (via SH3 domains) (By similarity). Interacts with and REPS1 (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
A7BFV94EBI-776269,EBI-6095043From a different organism.
CanxP355643EBI-776269,EBI-738422

GO - Molecular functioni

  • microtubule binding Source: UniProtKB
  • SH3 domain binding Source: MGI
  • tubulin binding Source: UniProtKB

Protein-protein interaction databases

IntActiQ8VD37. 7 interactions.
MINTiMINT-4119735.
STRINGi10090.ENSMUSP00000079553.

Structurei

3D structure databases

ProteinModelPortaliQ8VD37.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini537 – 805269MHDPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni627 – 806180Necessary and sufficient to mediate interaction with CANXAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi106 – 1127Poly-Glu
Compositional biasi229 – 497269Pro-richAdd
BLAST

Sequence similaritiesi

Contains 1 MHD (mu homology) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG2398. Eukaryota.
ENOG410XTCY. LUCA.
GeneTreeiENSGT00510000046419.
HOGENOMiHOG000231544.
HOVERGENiHBG081524.
InParanoidiQ8VD37.
OMAiIDWDRYN.
OrthoDBiEOG712TVK.
TreeFamiTF328986.

Family and domain databases

InterProiIPR028565. MHD.
IPR018808. Muniscin_C.
[Graphical view]
PfamiPF10291. muHD. 1 hit.
[Graphical view]
SUPFAMiSSF49447. SSF49447. 1 hit.
PROSITEiPS51072. MHD. 1 hit.
[Graphical view]

Sequences (7)i

Sequence statusi: Complete.

This entry describes 7 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8VD37-1) [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
MMEGLKKRTR KAFGIRKKEK DTDSTGSPDR DGMQPSPHEP PYHSKAECAR
60 70 80 90 100
EGGKKASKKS NGAPNGFYAE IDWERYNSPE LDEEGYSIRP EEPGSTKGKH
110 120 130 140 150
FYSSSESEEE EESHKKFNIK IKPLQSKDVL KNAATVDELK ASIGNIALSP
160 170 180 190 200
SPVRKSPRRS PGAIKRNLSS EEVARPRRST PTPELTSKKP LDDTLALAPL
210 220 230 240 250
FGPPLESAFD EQKTEVLLDQ PEIWGSGQPM NPSTESPELA RPFPTGTPPP
260 270 280 290 300
LPPKTVPATP PRTGSPLTVA TGNDQAATEA KIEKLPSISD LDSIFGPVLS
310 320 330 340 350
PKSVAVNTEE KWVHFSDASP EHVTPELTPR EQVVTPPAAS DIPADSPAPA
360 370 380 390 400
PPGPTGSAGP PGPPGPRHVP SPLNLEEVQK KVAEQTFIKD DYLETLSSPK
410 420 430 440 450
ECGLGQRATP PPPPPPTYRT VVSSPGPGSG SGTGTTSGAS SPARPATPLV
460 470 480 490 500
PCSTTPPPPP PRPPSRPKLP PGKPGVGDVS RPFSPPIHSS SPPPIAPLAR
510 520 530 540 550
AESTSSISST NSLSAATTPT VGSSRGPSPL TMGAQDTLPV AAAFTETVNA
560 570 580 590 600
YFKGADPSKC IVKITGEMVL SFPAGITRHF ANNPSPAALT FRVVNSSRLE
610 620 630 640 650
HVLPNPQLLC CDNTQNDANT KEFWVNMPNL MTHLKKVSEQ KPQATYYNVD
660 670 680 690 700
MLKYQVSAQG IQSTPLNLAV NWRCEPASTD LRIDYKYNTD AMSTAVALNN
710 720 730 740 750
VQFLVPIDGG VTKLQAVLPP AVWNAEQQRI LWKIPDISQK SENGGVGSLL
760 770 780 790 800
ARFQLSEGPS KPSPLVVQFT SEGSTLSGCD IELVGAGYRF SLIKKRFAAG

KYLADN
Length:806
Mass (Da):86,063
Last modified:March 1, 2002 - v1
Checksum:i4909A6D1DACCC775
GO
Isoform 2 (identifier: Q8VD37-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     35-58: Missing.
     154-161: Missing.
     272-437: Missing.

Show »
Length:608
Mass (Da):65,462
Checksum:i01294472E1F814D2
GO
Isoform 3 (identifier: Q8VD37-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     34-34: Missing.
     272-437: Missing.
     521-521: V → VENEQPSLVWFDRGKFYLTFE

Note: No experimental confirmation available.Combined sources
Show »
Length:659
Mass (Da):71,361
Checksum:i4A2F2788CF03E9F7
GO
Isoform 4 (identifier: Q8VD37-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     34-34: Missing.
     272-437: Missing.

Note: No experimental confirmation available.Combined sources
Show »
Length:639
Mass (Da):68,873
Checksum:i8EB81B8C8E8331B3
GO
Isoform 5 (identifier: Q8VD37-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     154-188: RKSPRRSPGAIKRNLSSEEVARPRRSTPTPELTSK → VKKLQDPGVPPQLQNLQARSLWMTLWPLLPSLVHH
     189-806: Missing.

Show »
Length:188
Mass (Da):21,052
Checksum:i869202C079926C05
GO
Isoform 6 (identifier: Q8VD37-6) [UniParc]FASTAAdd to basket

Also known as: SGIP1alpha

The sequence of this isoform differs from the canonical sequence as follows:
     33-33: M → MQGKKKAQKTQLLLTSCFWLRALSLTLSQ
     521-521: V → VENEQPSLVWFDRGKFYLTFE

Note: The N-terminal domain (1-97) of this isoform mediates binding to and tubulation of membranes.Combined sources
Show »
Length:854
Mass (Da):91,725
Checksum:i9FB1695AA4A47D8D
GO
Isoform 7 (identifier: Q8VD37-8) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     521-521: V → VENEQPSLVWFDRGKFYLTFE

Show »
Length:826
Mass (Da):88,551
Checksum:i706459A1A5A74CB5
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti100 – 1001H → Q in BAC27870 (PubMed:16141072).Curated
Sequence conflicti250 – 2501P → H in BAE28466 (PubMed:16141072).Curated
Sequence conflicti355 – 3551T → P in BAF74784 (PubMed:17626015).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei33 – 331M → MQGKKKAQKTQLLLTSCFWL RALSLTLSQ in isoform 6. 1 PublicationVSP_043987
Alternative sequencei34 – 341Missing in isoform 3 and isoform 4. 1 PublicationVSP_020279
Alternative sequencei35 – 5824Missing in isoform 2. 1 PublicationVSP_020280Add
BLAST
Alternative sequencei154 – 18835RKSPR…ELTSK → VKKLQDPGVPPQLQNLQARS LWMTLWPLLPSLVHH in isoform 5. 1 PublicationVSP_020281Add
BLAST
Alternative sequencei154 – 1618Missing in isoform 2. 1 PublicationVSP_020282
Alternative sequencei189 – 806618Missing in isoform 5. 1 PublicationVSP_020283Add
BLAST
Alternative sequencei272 – 437166Missing in isoform 2, isoform 3 and isoform 4. 1 PublicationVSP_020284Add
BLAST
Alternative sequencei521 – 5211V → VENEQPSLVWFDRGKFYLTF E in isoform 3, isoform 6 and isoform 7. 2 PublicationsVSP_020285

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB262964 mRNA. Translation: BAF74784.1.
AK014022 mRNA. Translation: BAB29118.1.
AK032439 mRNA. Translation: BAC27870.1.
AK043018 mRNA. Translation: BAC31435.1.
AK148043 mRNA. Translation: BAE28309.1.
AK148302 mRNA. Translation: BAE28466.1.
BC017596 mRNA. Translation: AAH17596.1.
CCDSiCCDS18404.1. [Q8VD37-1]
CCDS71429.1. [Q8VD37-3]
CCDS71430.1. [Q8VD37-4]
RefSeqiNP_001272788.1. NM_001285859.1. [Q8VD37-3]
NP_001272789.1. NM_001285860.1. [Q8VD37-4]
NP_001272791.1. NM_001285862.1.
NP_659155.1. NM_144906.2. [Q8VD37-1]
XP_006503491.1. XM_006503428.2. [Q8VD37-8]
UniGeneiMm.238094.
Mm.446273.
Mm.54201.

Genome annotation databases

EnsembliENSMUST00000066824; ENSMUSP00000063712; ENSMUSG00000028524. [Q8VD37-3]
ENSMUST00000072481; ENSMUSP00000072301; ENSMUSG00000028524. [Q8VD37-4]
ENSMUST00000080728; ENSMUSP00000079553; ENSMUSG00000028524. [Q8VD37-1]
ENSMUST00000106882; ENSMUSP00000102495; ENSMUSG00000028524. [Q8VD37-8]
ENSMUST00000183855; ENSMUSP00000139337; ENSMUSG00000028524. [Q8VD37-5]
GeneIDi73094.
KEGGimmu:73094.
UCSCiuc008two.2. mouse. [Q8VD37-1]
uc008twq.2. mouse. [Q8VD37-6]
uc008twr.2. mouse. [Q8VD37-3]
uc008tws.2. mouse. [Q8VD37-4]
uc008twt.2. mouse. [Q8VD37-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB262964 mRNA. Translation: BAF74784.1.
AK014022 mRNA. Translation: BAB29118.1.
AK032439 mRNA. Translation: BAC27870.1.
AK043018 mRNA. Translation: BAC31435.1.
AK148043 mRNA. Translation: BAE28309.1.
AK148302 mRNA. Translation: BAE28466.1.
BC017596 mRNA. Translation: AAH17596.1.
CCDSiCCDS18404.1. [Q8VD37-1]
CCDS71429.1. [Q8VD37-3]
CCDS71430.1. [Q8VD37-4]
RefSeqiNP_001272788.1. NM_001285859.1. [Q8VD37-3]
NP_001272789.1. NM_001285860.1. [Q8VD37-4]
NP_001272791.1. NM_001285862.1.
NP_659155.1. NM_144906.2. [Q8VD37-1]
XP_006503491.1. XM_006503428.2. [Q8VD37-8]
UniGeneiMm.238094.
Mm.446273.
Mm.54201.

3D structure databases

ProteinModelPortaliQ8VD37.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ8VD37. 7 interactions.
MINTiMINT-4119735.
STRINGi10090.ENSMUSP00000079553.

PTM databases

iPTMnetiQ8VD37.
PhosphoSiteiQ8VD37.

Proteomic databases

MaxQBiQ8VD37.
PaxDbiQ8VD37.
PRIDEiQ8VD37.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000066824; ENSMUSP00000063712; ENSMUSG00000028524. [Q8VD37-3]
ENSMUST00000072481; ENSMUSP00000072301; ENSMUSG00000028524. [Q8VD37-4]
ENSMUST00000080728; ENSMUSP00000079553; ENSMUSG00000028524. [Q8VD37-1]
ENSMUST00000106882; ENSMUSP00000102495; ENSMUSG00000028524. [Q8VD37-8]
ENSMUST00000183855; ENSMUSP00000139337; ENSMUSG00000028524. [Q8VD37-5]
GeneIDi73094.
KEGGimmu:73094.
UCSCiuc008two.2. mouse. [Q8VD37-1]
uc008twq.2. mouse. [Q8VD37-6]
uc008twr.2. mouse. [Q8VD37-3]
uc008tws.2. mouse. [Q8VD37-4]
uc008twt.2. mouse. [Q8VD37-2]

Organism-specific databases

CTDi84251.
MGIiMGI:1920344. Sgip1.

Phylogenomic databases

eggNOGiKOG2398. Eukaryota.
ENOG410XTCY. LUCA.
GeneTreeiENSGT00510000046419.
HOGENOMiHOG000231544.
HOVERGENiHBG081524.
InParanoidiQ8VD37.
OMAiIDWDRYN.
OrthoDBiEOG712TVK.
TreeFamiTF328986.

Miscellaneous databases

NextBioi337465.
PROiQ8VD37.
SOURCEiSearch...

Gene expression databases

BgeeiQ8VD37.
ExpressionAtlasiQ8VD37. baseline and differential.
GenevisibleiQ8VD37. MM.

Family and domain databases

InterProiIPR028565. MHD.
IPR018808. Muniscin_C.
[Graphical view]
PfamiPF10291. muHD. 1 hit.
[Graphical view]
SUPFAMiSSF49447. SSF49447. 1 hit.
PROSITEiPS51072. MHD. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "SGIP1alpha is an endocytic protein that directly interacts with phospholipids and Eps15."
    Uezu A., Horiuchi A., Kanda K., Kikuchi N., Umeda K., Tsujita K., Suetsugu S., Araki N., Yamamoto H., Takenawa T., Nakanishi H.
    J. Biol. Chem. 282:26481-26489(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6), FUNCTION IN ENDOCYTOSIS, LIPID-BINDING, SUBCELLULAR LOCATION, INTERACTION WITH AP2A1 AND EPS15.
  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] (ISOFORMS 2; 3; 4 AND 5).
    Strain: C57BL/6J.
    Tissue: Cerebellum, Embryonic head, Melanoma and Olfactory bulb.
  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] (ISOFORM 1).
    Tissue: Retina.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic brain.
  5. "Src homology 3-domain growth factor receptor-bound 2-like (endophilin) interacting protein 1, a novel neuronal protein that regulates energy balance."
    Trevaskis J., Walder K., Foletta V., Kerr-Bayles L., McMillan J., Cooper A., Lee S., Bolton K., Prior M., Fahey R., Whitecross K., Morton G.J., Schwartz M.W., Collier G.R.
    Endocrinology 146:3757-3764(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  6. "Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
    Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
    Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-300, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-78; SER-149; SER-151; SER-156; THR-180; THR-182; THR-247; THR-259; SER-265; SER-287; SER-289; SER-300; SER-316; SER-319; THR-324; THR-328; SER-371; SER-398; THR-409 AND SER-484, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-243 (ISOFORM 2), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-338 (ISOFORM 3), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-274 (ISOFORMS 3 AND 4), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-533 (ISOFORM 6), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-505 (ISOFORM 7), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue and Lung.
  8. "Enhanced clathrin-dependent endocytosis in the absence of calnexin."
    Li H.D., Liu W.X., Michalak M.
    PLoS ONE 6:E21678-E21678(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ALTERNATIVE SPLICING (ISOFORM 7), INTERACTION WITH CANX, TISSUE SPECIFICITY.

Entry informationi

Entry nameiSGIP1_MOUSE
AccessioniPrimary (citable) accession number: Q8VD37
Secondary accession number(s): A7BFW0
, Q3UFU3, Q3UGA0, Q8BXX4, Q8C034, Q9CXT2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 5, 2006
Last sequence update: March 1, 2002
Last modified: May 11, 2016
This is version 101 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, 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

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.