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Protein

Sperm-specific antigen 2

Gene

SSFA2

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

Functioni

GO - Molecular functioni

  • actin filament binding Source: CACAO
Complete GO annotation...

Keywords - Ligandi

Actin-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Sperm-specific antigen 2
Alternative name(s):
Cleavage signal-1 protein
Short name:
CS-1
Ki-ras-induced actin-interacting protein
Gene namesi
Name:SSFA2
Synonyms:CS1, KIAA1927, KRAP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:11319. SSFA2.

Subcellular locationi

  • Cytoplasm 1 Publication

  • Note: Located near the plasma membrane. Associated with actin filaments. May also exist as a membrane-bound form with extracellular regions.

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA36143.

Polymorphism and mutation databases

BioMutaiSSFA2.
DMDMi134047924.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12591259Sperm-specific antigen 2PRO_0000072211Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei87 – 871PhosphothreonineCombined sources
Modified residuei92 – 921PhosphoserineCombined sources
Modified residuei111 – 1111PhosphoserineBy similarity
Modified residuei270 – 2701PhosphoserineCombined sources
Modified residuei330 – 3301PhosphoserineCombined sources
Modified residuei466 – 4661PhosphoserineCombined sources
Modified residuei644 – 6441PhosphoserineCombined sources
Modified residuei668 – 6681PhosphoserineCombined sources
Modified residuei737 – 7371PhosphoserineCombined sources
Modified residuei739 – 7391PhosphoserineCombined sources
Modified residuei746 – 7461PhosphoserineCombined sources
Modified residuei759 – 7591PhosphoserineCombined sources
Cross-linki808 – 808Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei869 – 8691PhosphoserineBy similarity
Modified residuei902 – 9021PhosphoserineCombined sources
Modified residuei1040 – 10401PhosphoserineBy similarity
Modified residuei1055 – 10551PhosphoserineBy similarity
Modified residuei1060 – 10601PhosphoserineBy similarity
Modified residuei1063 – 10631PhosphoserineCombined sources
Modified residuei1118 – 11181PhosphoserineCombined sources
Modified residuei1134 – 11341PhosphoserineCombined sources
Modified residuei1161 – 11611PhosphoserineCombined sources
Modified residuei1168 – 11681PhosphothreonineCombined sources

Post-translational modificationi

A 33 kDa peptide corresponding to the C-terminus of this protein is found in the testis and seems to be cleaved into 2 peptides of 14 kDa and 18 kDa found on the surface of mature sperm cells. This sperm surface antigen may be involved in some step of early cleavage of the fertilized oocyte.

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP28290.
MaxQBiP28290.
PaxDbiP28290.
PRIDEiP28290.

PTM databases

iPTMnetiP28290.
PhosphoSiteiP28290.

Expressioni

Tissue specificityi

Strongly expressed in pancreas and testis. Present in colon cancer cells (at protein level).1 Publication

Inductioni

Up-regulated by activated KRAS.1 Publication

Gene expression databases

BgeeiP28290.
ExpressionAtlasiP28290. baseline and differential.
GenevisibleiP28290. HS.

Organism-specific databases

HPAiHPA034665.
HPA039989.

Interactioni

GO - Molecular functioni

  • actin filament binding Source: CACAO

Protein-protein interaction databases

BioGridi112622. 56 interactions.
DIPiDIP-47271N.
IntActiP28290. 37 interactions.
MINTiMINT-1369766.
STRINGi9606.ENSP00000388731.

Structurei

3D structure databases

ProteinModelPortaliP28290.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili959 – 103779Sequence analysisAdd
BLAST

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG410IERU. Eukaryota.
ENOG410ZSFW. LUCA.
GeneTreeiENSGT00530000063345.
HOVERGENiHBG082646.
InParanoidiP28290.
OMAiQSTCSLH.
OrthoDBiEOG7S21X2.
PhylomeDBiP28290.
TreeFamiTF331566.

Family and domain databases

InterProiIPR029325. IP3R-bd.
IPR026648. SSFA2.
IPR029326. SSFA2_C.
[Graphical view]
PANTHERiPTHR17469:SF11. PTHR17469:SF11. 3 hits.
PfamiPF14722. KRAP_IP3R_bind. 1 hit.
PF14723. SSFA2_C. 1 hit.
[Graphical view]
SMARTiSM01257. KRAP_IP3R_bind. 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: P28290-1) [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
MDRPLSSSAE AEEELEWQVA SRRRKAWAKC RSSWQASETE DLSTEATTQD
60 70 80 90 100
EEEDEEEDLP GAQLPAAGGR GNVPNEKIAI WLKDCRTPLG ASLDEQSSST
110 120 130 140 150
LKGVLVRNGG SFEDDLSLGA EANHLHESDA QIENCNNILA KERRLQFHQK
160 170 180 190 200
GRSMNSTGSG KSSGTVSSVS ELLELYEEDP EEILYNLGFG RDEPDIASKI
210 220 230 240 250
PSRFFNSSSF AKGIDIKVFL SAQMQRMEVE NPNYALTSRF RQIEVLTTVA
260 270 280 290 300
NAFSSLYSQV SGTPLQRIGS MSSVTSNKET DPPPPLTRSN TANRLMKTLS
310 320 330 340 350
KLNLCVDKTE KGESSSPSPS AEKGKILNVS VIEESGNKND QKSQKIMKKK
360 370 380 390 400
ESSSMLATVK EEVSGSSAAV TENADSDRIS DEANSNFNQG TENEQSKETQ
410 420 430 440 450
SHESKLGEES GIVESKLDSD FNISSHSELE NSSELKSVHI STPEKEPCAP
460 470 480 490 500
LTIPSIRNIM TQQKDSFEME EVQSTEGEAP HVPATYQLGL TKSKRDHLLR
510 520 530 540 550
TASQHSDSSG FAEDSTDCLS LNHLQVQESL QAMGSSADSC DSETTVTSLG
560 570 580 590 600
EDLATPTAQD QPYFNESEEE SLVPLQKGLE KAAAVADKRK SGSQDFPQCN
610 620 630 640 650
TIENTGTKQS TCSPGDHIIE ITEVEEDLFP AETVELLREA SAESDVGKSS
660 670 680 690 700
ESEFTQYTTH HILKSLASIE AKCSDMSSEN TTGPPSSMDR VNTALQRAQM
710 720 730 740 750
KVCSLSNQRM GRSLLKSKDL LKQRYLFAKA GYPLRRSQSL PTTLLSPVRV
760 770 780 790 800
VSSVNVRLSP GKETRCSPPS FTYKYTPEEE QELEKRVMEH DGQSLVKSTI
810 820 830 840 850
FISPSSVKKE EAPQSEAPRV EECHHGRTPT CSRLAPPPMS QSTCSLHSIH
860 870 880 890 900
SEWQERPLCE HTRTLSTHSV PNISGATCSA FASPFGCPYS HRHATYPYRV
910 920 930 940 950
CSVNPPSAIE MQLRRVLHDI RNSLQNLSQY PMMRGPDPAA APYSTQKSSV
960 970 980 990 1000
LPLYENTFQE LQVMRRSLNL FRTQMMDLEL AMLRQQTMVY HHMTEEERFE
1010 1020 1030 1040 1050
VDQLQGLRNS VRMELQDLEL QLEERLLGLE EQLRAVRMPS PFRSSALMGM
1060 1070 1080 1090 1100
CGSRSADNLS CPSPLNVMEP VTELMQEQSY LKSELGLGLG EMGFEIPPGE
1110 1120 1130 1140 1150
SSESVFSQAT SESSSVCSGP SHANRRTGVP STASVGKSKT PLVARKKVFR
1160 1170 1180 1190 1200
ASVALTPTAP SRTGSVQTPP DLESSEEVDA AEGAPEVVGP KSEVEEGHGK
1210 1220 1230 1240 1250
LPSMPAAEEM HKNVEQDELQ QVIREIKESI VGEIRREIVS GLLAAVSSSK

ASNSKQDYH
Length:1,259
Mass (Da):138,386
Last modified:March 20, 2007 - v3
Checksum:iD5843D9D6D5414D7
GO
Isoform 2 (identifier: P28290-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-153: Missing.

Show »
Length:1,106
Mass (Da):121,453
Checksum:iF262E608310E9AB0
GO
Isoform 3 (identifier: P28290-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1226-1251: IKESIVGEIRREIVSGLLAAVSSSKA → VGMDPISCVILELSMICTGGGVICALEDTCC
     1252-1259: Missing.

Show »
Length:1,256
Mass (Da):137,860
Checksum:iEF4E3976E7A73534
GO

Sequence cautioni

The sequence AAB00773.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence AAH12947.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAB67820.2 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAC05308.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti292 – 2921A → V in CAH18314 (PubMed:17974005).Curated
Sequence conflicti353 – 3531S → P in BAC05027 (PubMed:14702039).Curated
Sequence conflicti405 – 4051K → E in BAC05027 (PubMed:14702039).Curated
Sequence conflicti513 – 5131E → G in CAH18314 (PubMed:17974005).Curated
Sequence conflicti993 – 9931M → L in AAB00773 (PubMed:1555770).Curated
Sequence conflicti1056 – 10561A → T in AAB00773 (PubMed:1555770).Curated
Sequence conflicti1108 – 11103QAT → KQR in AAB00773 (PubMed:1555770).Curated
Sequence conflicti1116 – 11161V → I in AAB00773 (PubMed:1555770).Curated
Sequence conflicti1193 – 11931E → ESE in AAB00773 (PubMed:1555770).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti817 – 8171A → V.
Corresponds to variant rs16867510 [ dbSNP | Ensembl ].
VAR_056998
Natural varianti833 – 8331R → W.1 Publication
Corresponds to variant rs13419020 [ dbSNP | Ensembl ].
VAR_031186
Natural varianti836 – 8361P → L.2 Publications
Corresponds to variant rs17647806 [ dbSNP | Ensembl ].
VAR_031187
Natural varianti1258 – 12581Y → N.
Corresponds to variant rs2303554 [ dbSNP | Ensembl ].
VAR_059724

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 153153Missing in isoform 2. 2 PublicationsVSP_023865Add
BLAST
Alternative sequencei1226 – 125126IKESI…SSSKA → VGMDPISCVILELSMICTGG GVICALEDTCC in isoform 3. 1 PublicationVSP_023866Add
BLAST
Alternative sequencei1252 – 12598Missing in isoform 3. 1 PublicationVSP_023867

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB116937 mRNA. Translation: BAC81767.1.
AB067514 mRNA. Translation: BAB67820.2. Different initiation.
AK091197 mRNA. Translation: BAC03607.1.
AK097375 mRNA. Translation: BAC05027.1.
AK098455 mRNA. Translation: BAC05308.1. Different initiation.
AK291745 mRNA. Translation: BAF84434.1.
CR749488 mRNA. Translation: CAH18314.1.
AC009962 Genomic DNA. Translation: AAY14913.1.
CH471058 Genomic DNA. Translation: EAX10980.1.
BC012947 mRNA. Translation: AAH12947.1. Different initiation.
BC028706 mRNA. Translation: AAH28706.1.
BC052581 mRNA. Translation: AAH52581.1.
BC064499 mRNA. Translation: AAH64499.1.
M61199 mRNA. Translation: AAB00773.1. Different initiation.
CCDSiCCDS2284.1. [P28290-3]
CCDS46467.1. [P28290-1]
RefSeqiNP_001123917.1. NM_001130445.2. [P28290-1]
NP_001274432.1. NM_001287503.1.
NP_001274433.1. NM_001287504.1.
NP_006742.2. NM_006751.6. [P28290-3]
UniGeneiHs.196983.

Genome annotation databases

EnsembliENST00000320370; ENSP00000314669; ENSG00000138434. [P28290-3]
ENST00000431877; ENSP00000388731; ENSG00000138434. [P28290-1]
GeneIDi6744.
KEGGihsa:6744.
UCSCiuc002uoh.5. human. [P28290-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB116937 mRNA. Translation: BAC81767.1.
AB067514 mRNA. Translation: BAB67820.2. Different initiation.
AK091197 mRNA. Translation: BAC03607.1.
AK097375 mRNA. Translation: BAC05027.1.
AK098455 mRNA. Translation: BAC05308.1. Different initiation.
AK291745 mRNA. Translation: BAF84434.1.
CR749488 mRNA. Translation: CAH18314.1.
AC009962 Genomic DNA. Translation: AAY14913.1.
CH471058 Genomic DNA. Translation: EAX10980.1.
BC012947 mRNA. Translation: AAH12947.1. Different initiation.
BC028706 mRNA. Translation: AAH28706.1.
BC052581 mRNA. Translation: AAH52581.1.
BC064499 mRNA. Translation: AAH64499.1.
M61199 mRNA. Translation: AAB00773.1. Different initiation.
CCDSiCCDS2284.1. [P28290-3]
CCDS46467.1. [P28290-1]
RefSeqiNP_001123917.1. NM_001130445.2. [P28290-1]
NP_001274432.1. NM_001287503.1.
NP_001274433.1. NM_001287504.1.
NP_006742.2. NM_006751.6. [P28290-3]
UniGeneiHs.196983.

3D structure databases

ProteinModelPortaliP28290.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112622. 56 interactions.
DIPiDIP-47271N.
IntActiP28290. 37 interactions.
MINTiMINT-1369766.
STRINGi9606.ENSP00000388731.

PTM databases

iPTMnetiP28290.
PhosphoSiteiP28290.

Polymorphism and mutation databases

BioMutaiSSFA2.
DMDMi134047924.

Proteomic databases

EPDiP28290.
MaxQBiP28290.
PaxDbiP28290.
PRIDEiP28290.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000320370; ENSP00000314669; ENSG00000138434. [P28290-3]
ENST00000431877; ENSP00000388731; ENSG00000138434. [P28290-1]
GeneIDi6744.
KEGGihsa:6744.
UCSCiuc002uoh.5. human. [P28290-1]

Organism-specific databases

CTDi6744.
GeneCardsiSSFA2.
HGNCiHGNC:11319. SSFA2.
HPAiHPA034665.
HPA039989.
MIMi118990. gene.
neXtProtiNX_P28290.
PharmGKBiPA36143.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IERU. Eukaryota.
ENOG410ZSFW. LUCA.
GeneTreeiENSGT00530000063345.
HOVERGENiHBG082646.
InParanoidiP28290.
OMAiQSTCSLH.
OrthoDBiEOG7S21X2.
PhylomeDBiP28290.
TreeFamiTF331566.

Miscellaneous databases

ChiTaRSiSSFA2. human.
GeneWikiiSSFA2.
GenomeRNAii6744.
NextBioi26306.
PROiP28290.
SOURCEiSearch...

Gene expression databases

BgeeiP28290.
ExpressionAtlasiP28290. baseline and differential.
GenevisibleiP28290. HS.

Family and domain databases

InterProiIPR029325. IP3R-bd.
IPR026648. SSFA2.
IPR029326. SSFA2_C.
[Graphical view]
PANTHERiPTHR17469:SF11. PTHR17469:SF11. 3 hits.
PfamiPF14722. KRAP_IP3R_bind. 1 hit.
PF14723. SSFA2_C. 1 hit.
[Graphical view]
SMARTiSM01257. KRAP_IP3R_bind. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Deregulated expression of KRAP, a novel gene encoding actin-interacting protein, in human colon cancer cells."
    Inokuchi J., Komiya M., Baba I., Naito S., Sasazuki T., Shirasawa S.
    J. Hum. Genet. 49:46-52(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INDUCTION BY KRAS.
  2. "Prediction of the coding sequences of unidentified human genes. XXI. The complete sequences of 60 new cDNA clones from brain which code for large proteins."
    Nagase T., Kikuno R., Ohara O.
    DNA Res. 8:179-187(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT LEU-836.
    Tissue: Brain.
  3. "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] (ISOFORMS 1 AND 2), VARIANTS TRP-833 AND LEU-836.
    Tissue: Mammary gland, Placenta and Tongue.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Liver.
  5. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [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 3).
    Tissue: Pancreas, Prostate and Testis.
  8. "Human cleavage signal-1 protein; cDNA cloning, transcription and immunological analysis."
    Javed A.A., Naz R.K.
    Gene 112:205-211(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 991-1259 (ISOFORM 1).
    Tissue: Testis.
  9. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-87; SER-92; SER-668; SER-737; SER-739; SER-746 AND SER-1134, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92 AND SER-330, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  13. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92; SER-270; SER-737; SER-746 AND SER-759, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-87; SER-92; SER-270; SER-466; SER-644; SER-737; SER-739; SER-746; SER-902; SER-1063; SER-1118; SER-1134; SER-1161 AND THR-1168, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  15. "Uncovering global SUMOylation signaling networks in a site-specific manner."
    Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M., Vertegaal A.C.
    Nat. Struct. Mol. Biol. 21:927-936(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-808, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiSSFA2_HUMAN
AccessioniPrimary (citable) accession number: P28290
Secondary accession number(s): A8K6T0
, Q68DA6, Q7Z7L2, Q8N1L3, Q8N263, Q8N7H2, Q8NEN5, Q96E36, Q96PW1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: March 20, 2007
Last modified: May 11, 2016
This is version 137 of the entry and version 3 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 2
    Human chromosome 2: 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

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.